|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
6-1094 |
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: 883.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 6 TTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKLFSSLRSKTATF 85
Cdd:TIGR00957 412 STVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKS 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 86 TDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVTFTTYVLL--GSVI 163
Cdd:TIGR00957 492 KDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVdeNNIL 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 164 TASRVFVAVTLYGAVRLTVTLFfPSAIERVSEAIVSIRRIQTFLLLDEI---SQRNRQLPSDGKKMVHVQDFTAFWDKaS 240
Cdd:TIGR00957 572 DAEKAFVSLALFNILRFPLNIL-PMVISSIVQASVSLKRLRIFLSHEELepdSIERRTIKPGEGNSITVHNATFTWAR-D 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSQQPWVFSGTLRSNILFGKKYEKER 320
Cdd:TIGR00957 650 LPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKY 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 321 YEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQ--I 398
Cdd:TIGR00957 730 YQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPegV 809
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 399 LHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSGIDFGSLLKK--------DNEES----------EQPPV 460
Cdd:TIGR00957 810 LKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTyapdeqqgHLEDSwtalvsgegkEAKLI 889
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 461 PGTPTLRN-------RTFSESSVWSQQSSRPSLKDGALESQDTENVPVTLSEENRSE-GKVGFQAYKNYFRAGAHWIVF- 531
Cdd:TIGR00957 890 ENGMLVTDvvgkqlqRQLSASSSDSGDQSRHHGSSAELQKAEAKEETWKLMEADKAQtGQVELSVYWDYMKAIGLFITFl 969
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 532 -IFLILLNTAAQVAyvlQDWWLSYWANkQSMLNVTVNgggNVTEKLDLNWYLGIYSGLTVatvlFGIARSLLVFYVLvnS 610
Cdd:TIGR00957 970 sIFLFVCNHVSALA---SNYWLSLWTD-DPMVNGTQN---NTSLRLSVYGALGILQGFAV----FGYSMAVSIGGIQ--A 1036
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 611 SQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQTLLQVVGVVSVAVAVIPWIAIPLVPLGI 690
Cdd:TIGR00957 1037 SRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGL 1116
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 691 IFIFLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLD 770
Cdd:TIGR00957 1117 LYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLE 1196
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 771 AICAMFVIIVAFGSLILAKTLDAGQVGLALSYALTLMGMFQWCVRQSAEVENMMISVERVIEYTDLEKEAPWEYQK-RPP 849
Cdd:TIGR00957 1197 CVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQEtAPP 1276
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 850 PAWPHEGVIIFDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLH 928
Cdd:TIGR00957 1277 SGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESaEGEIIIDGLNIAKIGLH 1356
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 929 DLRKKMSIIPQEPVLFTGTMRKNLDPFNEHTDEELWNALQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAI 1008
Cdd:TIGR00957 1357 DLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARAL 1436
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1009 LRKNQILIIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNKeSLFYK 1088
Cdd:TIGR00957 1437 LRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQR-GIFYS 1515
|
....*.
gi 2217293410 1089 MVQQLG 1094
Cdd:TIGR00957 1516 MAKDAG 1521
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
5-1094 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 880.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 5 KTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKLFSSLRSKTAT 84
Cdd:PLN03130 394 KFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQ 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 85 FTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNlaSFFSASkIIVFVT---FTTYVLLGS 161
Cdd:PLN03130 474 RTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFN--SFILNS-IPVLVTvvsFGVFTLLGG 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 162 VITASRVFVAVTLYGAVRLTvtLF-FPSAIERVSEAIVSIRRIQTFLLLDE-ISQRNRQLPSdGKKMVHVQDFTAFWDKA 239
Cdd:PLN03130 551 DLTPARAFTSLSLFAVLRFP--LFmLPNLITQAVNANVSLKRLEELLLAEErVLLPNPPLEP-GLPAISIKNGYFSWDSK 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 240 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAP-SHGLVSVHGRIAYVSQQPWVFSGTLRSNILFGKKYEK 318
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDP 707
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 319 ERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQI 398
Cdd:PLN03130 708 ERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDE 787
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 399 LHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSGIDFGSLLKKDNEESEQPPVPGTPTLRNrtfsESSVWS 478
Cdd:PLN03130 788 LRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAGKMEEYVEENGEEEDDQ----TSSKPV 863
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 479 QQSSRPSL-KDGALESQDTENVPVTLSEENRSEGKVGFQAYKNYFRA-GAHWIVFIfLILLNTAAQVAYVLQDWWLSYWA 556
Cdd:PLN03130 864 ANGNANNLkKDSSSKKKSKEGKSVLIKQEERETGVVSWKVLERYKNAlGGAWVVMI-LFLCYVLTEVFRVSSSTWLSEWT 942
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 557 NKQSmlnvtvngggnvTEKLDLNWYLGIYSGLTVATVLFGIARSllvfYVLVNSS----QTLHNKMFESILKAPVLFFDR 632
Cdd:PLN03130 943 DQGT------------PKTHGPLFYNLIYALLSFGQVLVTLLNS----YWLIMSSlyaaKRLHDAMLGSILRAPMSFFHT 1006
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 633 NPIGRILNRFSKDIGHLDDLLPL---TFLDFIQTLLQVVGVVSVAVAVIPWIAIPLVplgIIFIFLRRYFLETSRDVKRL 709
Cdd:PLN03130 1007 NPLGRIINRFAKDLGDIDRNVAVfvnMFLGQIFQLLSTFVLIGIVSTISLWAIMPLL---VLFYGAYLYYQSTAREVKRL 1083
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 710 ESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICA-MFVIIVAFGSLILA 788
Cdd:PLN03130 1084 DSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGlMIWLTASFAVMQNG 1163
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 789 KTLD----AGQVGLALSYALTLMGMFQWCVRQSAEVENMMISVERVIEYTDLEKEAPWEYQ-KRPPPAWPHEGVIIFDNV 863
Cdd:PLN03130 1164 RAENqaafASTMGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPSEAPLVIEnNRPPPGWPSSGSIKFEDV 1243
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 864 NFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKMSIIPQEPV 942
Cdd:PLN03130 1244 VLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELErGRILIDGCDISKFGLMDLRKVLGIIPQAPV 1323
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 943 LFTGTMRKNLDPFNEHTDEELWNALQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATA 1022
Cdd:PLN03130 1324 LFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217293410 1023 NVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNKESLFYKMVQQLG 1094
Cdd:PLN03130 1404 AVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQSTG 1475
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
8-1094 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 814.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 8 TGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKLFSSLRSKTATFTD 87
Cdd:PLN03232 397 SGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTD 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 88 ARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVTFTTYVLLGSVITASR 167
Cdd:PLN03232 477 KRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFVLLGGDLTPAR 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 168 VFVAVTLYGAVRLTVTLFfPSAIERVSEAIVSIRRIQTFLLLDE-ISQRNRQLpSDGKKMVHVQDFTAFWDKASETPTLQ 246
Cdd:PLN03232 557 AFTSLSLFAVLRSPLNML-PNLLSQVVNANVSLQRIEELLLSEErILAQNPPL-QPGAPAISIKNGYFSWDSKTSKPTLS 634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 247 GLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSH-GLVSVHGRIAYVSQQPWVFSGTLRSNILFGKKYEKERYEKVI 325
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAI 714
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 326 KACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKITI 405
Cdd:PLN03232 715 DVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRV 794
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 406 LVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSGIDFGSLLKKDNEESEQPPV-PGTPTLRNRTFSESSVWSQQSSrp 484
Cdd:PLN03232 795 LVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKMDATQEVnTNDENILKLGPTVTIDVSERNL-- 872
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 485 slkdgALESQDTENVPVTLSEENRSEGKVGFQAYKNYFRA-GAHWIVFIfLILLNTAAQVAYVLQDWWLSYWANKQSMln 563
Cdd:PLN03232 873 -----GSTKQGKRGRSVLVKQEERETGIISWNVLMRYNKAvGGLWVVMI-LLVCYLTTEVLRVSSSTWLSIWTDQSTP-- 944
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 564 vtvngggnvtEKLDLNWYLGIYSGLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFS 643
Cdd:PLN03232 945 ----------KSYSPGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFS 1014
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 644 KDIGHLD----DLLPLtFLDFIQTLLQVVGVVSVAVAVIPWIAIPLVplgIIFIFLRRYFLETSRDVKRLESTTRSPVFS 719
Cdd:PLN03232 1015 KDIGDIDrnvaNLMNM-FMNQLWQLLSTFALIGTVSTISLWAIMPLL---ILFYAAYLYYQSTSREVRRLDSVTRSPIYA 1090
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 720 HLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAMFVIIVA-FGSLILAKTLD----AG 794
Cdd:PLN03232 1091 QFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTAtFAVLRNGNAENqagfAS 1170
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 795 QVGLALSYALTLMGMFQWCVRQSAEVENMMISVERVIEYTDLEKEAP-WEYQKRPPPAWPHEGVIIFDNVNFMYSPGGPL 873
Cdd:PLN03232 1171 TMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATaIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPP 1250
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 874 VLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNL 952
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEkGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI 1330
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 953 DPFNEHTDEELWNALQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELI 1032
Cdd:PLN03232 1331 DPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLI 1410
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217293410 1033 QKKIREKFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNKESLFYKMVQQLG 1094
Cdd:PLN03232 1411 QRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTG 1472
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-1086 |
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: 728.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 5 KTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKLFSSLRSKTAT 84
Cdd:TIGR01271 175 KISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAG 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 85 FTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVTFTTYVLLGSVIT 164
Cdd:TIGR01271 255 KISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVVFLSVVPYALIKGIIL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 165 aSRVFVAVTLYGAVRLTVTLFFPSAIERVSEAIVSIRRIQTFLLLDEISQRNRQLPSDGKKMVHVqdfTAFWD------- 237
Cdd:TIGR01271 335 -RRIFTTISYCIVLRMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEEYKTLEYNLTTTEVEMVNV---TASWDegigelf 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 238 -KASE-----------------------TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIA 293
Cdd:TIGR01271 411 eKIKQnnkarkqpngddglffsnfslyvTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRIS 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 294 YVSQQPWVFSGTLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIY 373
Cdd:TIGR01271 491 FSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLY 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 374 LLDDPLSAVDAEVSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSGIDFGSLL----K 449
Cdd:TIGR01271 571 LLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLlgleA 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 450 KDNEESE---------------------------------QPP------------------------------------- 459
Cdd:TIGR01271 651 FDNFSAErrnsiltetlrrvsidgdstvfsgpetikqsfkQPPpefaekrkqsiilnpiasarkfsfvqmgpqkaqatti 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 460 --------------VP----GTPTL------------------------------------RNRTFSESSVWSQQS---- 481
Cdd:TIGR01271 731 edavrepserkfslVPedeqGEESLprgnqyhhglqhqaqrrqsvlqlmthsnrgenrreqLQTSFRKKSSITQQNelas 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 482 -----SRPSLKDGALE--------------SQDTENVPVTLSeenrsegkvgFQAYKNYFRAGAHWIVFIFLILLNTAAQ 542
Cdd:TIGR01271 811 eldiySRRLSKDSVYEiseeineedlkecfADERENVFETTT----------WNTYLRYITTNRNLVFVLIFCLVIFLAE 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 543 VAYVLQDWWL----SYWANKQSMLNVTVNGGGNVTEKLDLN----WYLGIYSGLTVATVLFGIARSLLVFYVLVNSSQTL 614
Cdd:TIGR01271 881 VAASLLGLWLitdnPSAPNYVDQQHANASSPDVQKPVIITPtsayYIFYIYVGTADSVLALGFFRGLPLVHTLLTVSKRL 960
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 615 HNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQTLLQVVGVVSVAVAVIPWIAIPLVPLGIIFIF 694
Cdd:TIGR01271 961 HEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIM 1040
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 695 LRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICA 774
Cdd:TIGR01271 1041 LRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFV 1120
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 775 MFVIIVAFGSlILAKTLDAGQVGLALSYALTLMGMFQWCVRQSAEVENMMISVERVIEYTDLEKEAPwEYQKRPPPA--- 851
Cdd:TIGR01271 1121 FFFIAVTFIA-IGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEP-RPSGGGGKYqls 1198
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 852 -------------WPHEGVIIFDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPEGKIWID 918
Cdd:TIGR01271 1199 tvlvienphaqkcWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQID 1278
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 919 KILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLDPFNEHTDEELWNALQEVQLKETIEDLPGKMDTELAESGSNFSVGQ 998
Cdd:TIGR01271 1279 GVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGH 1358
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 999 RQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVL 1078
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKL 1438
|
....*...
gi 2217293410 1079 LqNKESLF 1086
Cdd:TIGR01271 1439 L-NETSLF 1445
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
8-1095 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 676.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 8 TGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKLFSSLRSKTATFTD 87
Cdd:PTZ00243 343 TGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAAD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 88 ARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISkilrssCLRGMNLA----SFFS--ASKIIVFVTFTTYVLLGS 161
Cdd:PTZ00243 423 ARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELR------YLRDVQLArvatSFVNnaTPTLMIAVVFTVYYLLGH 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 162 VITASRVFVAVTLYGAVRLTVTLFfPSAIERVSEAIVSIRRIQTFLLLDEIS-------------QRNR----------- 217
Cdd:PTZ00243 497 ELTPEVVFPTIALLGVLRMPFFMI-PWVFTTVLQFLVSIKRISTFLECDNATcstvqdmeeywreQREHstacqlaavle 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 218 ----------QLPSDGKKM--------------------------VHVQDF----------------TAFWDKASETPT- 244
Cdd:PTZ00243 576 nvdvtafvpvKLPRAPKVKtsllsralrmlcceqcrptkrhpspsVVVEDTdygspssasrhiveggTGGGHEATPTSEr 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 --------------------LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSQQPWVFSG 304
Cdd:PTZ00243 656 saktpkmktddffelepkvlLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNA 735
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 305 TLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 384
Cdd:PTZ00243 736 TVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 385 EVSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSGI--DFGSLLK---------KDNE 453
Cdd:PTZ00243 816 HVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTSLyaTLAAELKenkdskegdADAE 895
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 454 ESEQPPVPGTPTLRNRTFsessvwSQQSSRPSLKDGAleSQDTENVPVTLSEENRSeGKVGFQAYKNYFRA--GAHWIVF 531
Cdd:PTZ00243 896 VAEVDAAPGGAVDHEPPV------AKQEGNAEGGDGA--ALDAAAGRLMTREEKAS-GSVPWSTYVAYLRFcgGLHAAGF 966
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 532 IFLI-----LLNTAAQVayvlqdwWLSYWANKQsmlnvtvngggnvtEKLDLNWYLGIYSGLTVATVLFGIARSLLVFYV 606
Cdd:PTZ00243 967 VLATfavteLVTVSSGV-------WLSMWSTRS--------------FKLSAATYLYVYLGIVLLGTFSVPLRFFLSYEA 1025
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 607 LVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQTLLQVVGVVSVAVAVIPWIAIPLV 686
Cdd:PTZ00243 1026 MRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALV 1105
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 687 PLGIIFIFLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAY-KAEERCQELFdAHQDLHSEAWFLFLTTSRWF 765
Cdd:PTZ00243 1106 PCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYgKAHLVMQEAL-RRLDVVYSCSYLENVANRWL 1184
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 766 AVRLDAICAMFVIIVAF----GSLILAKTLDAGQVGLALSYALTLMGMFQWCVRQSAEVENMMISVERVIEYTD-LEKEA 840
Cdd:PTZ00243 1185 GVRVEFLSNIVVTVIALigviGTMLRATSQEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDeVPHED 1264
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 841 PWEY-------QKR-----------------PPPAWPH---EGVIIFDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGR 893
Cdd:PTZ00243 1265 MPELdeevdalERRtgmaadvtgtvviepasPTSAAPHpvqAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGR 1344
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 894 TGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLDPFNEHTDEELWNALQEVQL 972
Cdd:PTZ00243 1345 TGSGKSTLLLTFMRMVEVcGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGL 1424
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 973 KETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQILII-DEATANVDPRTDELIQKKIREKFAHCTVLTIAHR 1051
Cdd:PTZ00243 1425 RERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHR 1504
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....
gi 2217293410 1052 LNTIIDSDKIMVLDSGRLKEYDEPYVLLQNKESLFYKMVQQLGK 1095
Cdd:PTZ00243 1505 LHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVEALGR 1548
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
527-834 |
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: 566.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 527 HWIVFIFLILLNTAAQVAYVLQDWWLSYWANKQSMLNV------TVNGGGNVTEKLDLNWYLGIYSGLTVATVLFGIARS 600
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEEKLNDttdrvqGENSTNVDIEDLDRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 601 LLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQTLLQVVGVVSVAVAVIPW 680
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 681 IAIPLVPLGIIFIFLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLT 760
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217293410 761 TSRWFAVRLDAICAMFVIIVAFGSLILAKTLDAGQVGLALSYALTLMGMFQWCVRQSAEVENMMISVERVIEYT 834
Cdd:cd18601 241 TSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEYS 314
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
856-1075 |
1.29e-134 |
|
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: 407.26 E-value: 1.29e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 856 GVIIFDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKM 934
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELsSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 935 SIIPQEPVLFTGTMRKNLDPFNEHTDEELWNALQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQI 1014
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217293410 1015 LIIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEP 1075
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
531-834 |
1.23e-114 |
|
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: 357.58 E-value: 1.23e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 531 FIFLILLNTAAQVAYVLQDWWLSYWANKQSMlnvtvngggnvTEKLDLNWYLGIYSGLTV-ATVLFGIARSLLVFYVLVN 609
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSS-----------SPNSSSGYYLGVYAALLVlASVLLVLLRWLLFVLAGLR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 610 SSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQTLLQVVGVVSVAVAVIPWIAIPLVPLG 689
Cdd:cd18580 70 ASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 690 IIFIFLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRL 769
Cdd:cd18580 150 VVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217293410 770 DAICAMFVIIVAFGSLILAKTLDAGQVGLALSYALTLMGMFQWCVRQSAEVENMMISVERVIEYT 834
Cdd:cd18580 230 DLLGALLALVVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
227-427 |
2.06e-113 |
|
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: 350.62 E-value: 2.06e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 227 VHVQDFTAFWDKASET--PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSQQPWVFSG 304
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 305 TLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 384
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2217293410 385 EVSRHLFELCICQIL-HEKITILVTHQLQYLKAASQILILKDGK 427
Cdd:cd03250 161 HVGRHIFENCILGLLlNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
524-1091 |
5.60e-113 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 363.72 E-value: 5.60e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 524 AGAHWIVFIFLILLNTAAQVAYVLQDWWLSYWANkqsmlnvTVNGGGNVTEkldLNWYLGIYSGLTVATVLFGIARSLLV 603
Cdd:COG1132 16 LRPYRGLLILALLLLLLSALLELLLPLLLGRIID-------ALLAGGDLSA---LLLLLLLLLGLALLRALLSYLQRYLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 604 FYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQTLLQVVGVVSVAVAVIPWIAI 683
Cdd:COG1132 86 ARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 684 PLVPLGIIFIFLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSR 763
Cdd:COG1132 166 IVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 764 WFAVRLDAI--CAMFVIIVAFGSLILAKTLDAGQVGLALSYALTLMGMFQWCVRQSAEVENMMISVERVIEYTDLEKEAP 841
Cdd:COG1132 246 LFFPLMELLgnLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 842 WEYQKRPPPawPHEGVIIFDNVNFMYsPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKI 920
Cdd:COG1132 326 DPPGAVPLP--PVRGEIEFENVSFSY-PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPtSGRILIDGV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 921 LTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLDPFNEH-TDEELWNALQEVQLKETIEDLPGKMDTELAESGSNFSVGQR 999
Cdd:COG1132 403 DIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDaTDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQR 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1000 QLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLKE---YDEpy 1076
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEqgtHEE-- 560
|
570
....*....|....*
gi 2217293410 1077 vLLQNKEsLFYKMVQ 1091
Cdd:COG1132 561 -LLARGG-LYARLYR 573
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
1-203 |
7.24e-113 |
|
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: 352.68 E-value: 7.24e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1 MAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKLFSSLRS 80
Cdd:cd18593 89 AALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFGKLFSKLRR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 81 KTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVTFTTYVLLG 160
Cdd:cd18593 169 KTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTFLAYILLG 248
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2217293410 161 SVITASRVFVAVTLYGAVRLTVTLFFPSAIERVSEAIVSIRRI 203
Cdd:cd18593 249 NILTAERVFVTMALYNAVRLTMTLFFPFAIQFGSELSVSIRRI 291
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
528-834 |
2.82e-95 |
|
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: 305.55 E-value: 2.82e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 528 WIVFIFLILLntaAQVAYVLQDWWLSYWANKqsmlnvtvngggnvTEKLDLNWYLGIYSGLTVATVLFGIARSLLVFYVL 607
Cdd:cd18606 1 LPLLLLLLIL---SQFAQVFTNLWLSFWTED--------------FFGLSQGFYIGIYAGLGVLQAIFLFLFGLLLAYLG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 608 VNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQTLLQVVGVVSVAVAVIPWIAIPLVP 687
Cdd:cd18606 64 IRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 688 LGIIFIFLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAV 767
Cdd:cd18606 144 LLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAI 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 768 RLDAICAMFVIIVAFGSLILAKTLDAGQVGLALSYALTLMGMFQWCVRQSAEVENMMISVERVIEYT 834
Cdd:cd18606 224 RLDLLGSLLVLIVALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
2-204 |
2.35e-91 |
|
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: 294.93 E-value: 2.35e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 2 AMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKLFSSLRSK 81
Cdd:cd18594 89 ALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 82 TATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVTFTTYVLLGS 161
Cdd:cd18594 169 TAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVLTGN 248
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2217293410 162 VITASRVFVAVTLYGAVRLTVTLFFPSAIERVSEAIVSIRRIQ 204
Cdd:cd18594 249 TLTARKVFTVISLLNALRMTITRFFPESIQTLSESRVSLKRIQ 291
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
527-834 |
2.23e-90 |
|
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: 292.93 E-value: 2.23e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 527 HWIVFIFLILLNTAAQVAYVLQDWWLSYW-----ANKQSMLNVTVNGGGNVTEKLDLNWYLGIYSGLTVATVLFGIARSL 601
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWlkqgsGNTTNNVDNSTVDSGNISDNPDLNFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 602 LVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQTLLQVVGVVSVAVAVIPWI 681
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 682 AIPLVPLGIIFIFLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTT 761
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 762 SRWFAVRLDAICAMFVIIVAFGSLILAKTLDAGQVGLALSYALTLMGMFQWCVRQSAEVENMMISVERVIEYT 834
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
531-834 |
5.81e-90 |
|
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: 291.30 E-value: 5.81e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 531 FIFLILLNTAAQVAYVLQDWWLSYWANKQSMLNVTVNGggnvteklDLNWYLGIYSGLTVATVLFGIARSLLVFYVLVNS 610
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDTE--------QRDYRLGVYGALGLGQAIFVFLGSLALALGCVRA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 611 SQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQTLLQVVGVVSVAVAVIPWIAIPLVPLGI 690
Cdd:cd18603 73 SRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 691 IFIFLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLD 770
Cdd:cd18603 153 LYFFIQRFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLE 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 771 AICAmfvIIVAFGSL--ILAK-TLDAGQVGLALSYALTLMGMFQWCVRQSAEVENMMISVERVIEYT 834
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; ... |
528-834 |
1.02e-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: 290.52 E-value: 1.02e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 528 WIVFIFLILLntaAQVAYVLQDWWLSYWANKQSMLNVTVNGGGNVtekldlNWYLGIYSGLTVATVLFGIARSLLVFYVL 607
Cdd:cd18604 1 WALLLLLFVL---SQLLSVGQSWWLGIWASAYETSSALPPSEVSV------LYYLGIYALISLLSVLLGTLRYLLFFFGS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 608 VNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQTLLQVVGVVSVAVAVIPWIAIPLVP 687
Cdd:cd18604 72 LRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 688 LGIIFIFLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAV 767
Cdd:cd18604 152 LAALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSV 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 768 RLDAICAMFVIIVAFGsLILAKTLDAGQVGLALSYALTLMGMFQWCVRQSAEVENMMISVERVIEYT 834
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 ... |
852-1075 |
5.22e-89 |
|
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: 285.08 E-value: 5.22e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 852 WPHEGVIIFDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDL 930
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAeEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 931 RKKMSIIPQEPVLFTGTMRKNLDPFNEHTDEELWNALqevqlketiedlpgkmdtELAESGSNFSVGQRQLVCLARAILR 1010
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217293410 1011 KNQILIIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEP 1075
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
578-1092 |
7.24e-87 |
|
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: 296.75 E-value: 7.24e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 578 LNWYLGIYSGLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSkDIGHLDDLLPLTF 657
Cdd:COG2274 195 LWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 658 LDFIQTLLQVVGVVSVAVAVIPWIAIPLVPLGIIFIFLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAE 737
Cdd:COG2274 274 LTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 738 ERCQELFDAHQDLHSEA---WFLFLTTSRWFAVRLDAIcaMFVIIVAFGS-LILAKTLDAGQ-------VGLALSYALTL 806
Cdd:COG2274 354 SRFRRRWENLLAKYLNArfkLRRLSNLLSTLSGLLQQL--ATVALLWLGAyLVIDGQLTLGQliafnilSGRFLAPVAQL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 807 MGMFQwcvrqsaEVENMMISVERVIEYTDLEKEAPWEYQKRPPPawPHEGVIIFDNVNFMYSPGGPLVLKHLTALIKSQE 886
Cdd:COG2274 432 IGLLQ-------RFQDAKIALERLDDILDLPPEREEGRSKLSLP--RLKGDIELENVSFRYPGDSPPVLDNISLTIKPGE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 887 KVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLDPFNEH-TDEELW 964
Cdd:COG2274 503 RVAIVGRSGSGKSTLLKLLLGLYEPtSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDaTDEEII 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 965 NALQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIREKFAHCT 1044
Cdd:COG2274 583 EAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRT 662
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2217293410 1045 VLTIAHRLNTIIDSDKIMVLDSGRLKEyDEPYVLLQNKESLFYKMVQQ 1092
Cdd:COG2274 663 VIIIAHRLSTIRLADRIIVLDKGRIVE-DGTHEELLARKGLYAELVQQ 709
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
528-834 |
4.08e-81 |
|
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: 267.55 E-value: 4.08e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 528 WIVFIFLILLNTAAQVAyvlQDWWLSYWANKQSMLNVTVNGGGNVTEKLDLNW-YLGIYSGLTVATVLFGIARSLLVFYV 606
Cdd:cd18602 1 VALVLALALLKQGLRVA---TDFWLADWTEANHDVASVVFNITSSSLEDDEVSyYISVYAGLSLGAVILSLVTNLAGELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 607 LVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQTLLQVVGVVSVAVAVIPWIAIPLV 686
Cdd:cd18602 78 GLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 687 PLGIIFIFLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFA 766
Cdd:cd18602 158 PIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLG 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 767 VRLDAICAMFVIIVAFGSLI--LAKTLDAGQVGLALSYALTLMGMFQWCVRQSAEVENMMISVERVIEYT 834
Cdd:cd18602 238 IRLDYLGAVIVFLAALSSLTaaLAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
2-203 |
8.78e-80 |
|
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: 263.19 E-value: 8.78e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 2 AMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKLFSSLRSK 81
Cdd:cd18579 89 ARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKLISKLRKK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 82 TATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVTFTTYVLLGS 161
Cdd:cd18579 169 LMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFATYVLLGN 248
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2217293410 162 VITASRVFVAVTLYGAVRlTVTLFFPSAIERVSEAIVSIRRI 203
Cdd:cd18579 249 PLTAAKVFTALSLFNLLR-FPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
531-834 |
9.73e-76 |
|
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: 252.45 E-value: 9.73e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 531 FIFLILLNTAAQVAYVLQDWWLSYWANKQsmlnvtvNGGGNVTEKLDLNWYLGIYSGLTVATVLFGIARSLLVFYVLVNS 610
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWVSHS-------NNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 611 SQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQTLLQVVGVVSVAVAVIPWIAIPLVPLGI 690
Cdd:cd18605 74 ARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 691 IFIFLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLD 770
Cdd:cd18605 154 IYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQ 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 771 AICAMFVIIVAFGSLILA---KTLDAGQVGLALSYALTLMGMFQWCVRQSAEVENMMISVERVIEYT 834
Cdd:cd18605 234 LLGVLIVTFVALTAVVQHffgLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
856-1091 |
1.82e-71 |
|
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: 238.66 E-value: 1.82e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 856 GVIIFDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKM 934
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 935 SIIPQEPVLFTGTMRKNLDPFNEHTDEELWNALQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQI 1014
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 1015 LIIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNKESLFYKMVQ 1091
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVR 254
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
518-833 |
5.39e-71 |
|
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: 240.09 E-value: 5.39e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 518 YKNYFRAGAHWIVFIFLILLNTAAQVAYVLQDWWL---SYWANKQSMLNVTVNGGGNVTEKLDLNWYLGIYSGLTVATVL 594
Cdd:cd18600 6 YLRYITSHKSLIFVLILCLVIFAIEVAASLVGLWLlrsQADRVNTTRPESSSNTYAVIVTFTSSYYVFYIYVGVADSLLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 595 FGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQTLLQVVGVVSVA 674
Cdd:cd18600 86 MGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 675 VAVIPWIAIPLVPLGIIFIFLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEA 754
Cdd:cd18600 166 SILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTAN 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 755 WFLFLTTSRWFAVRLDAICAMFVIIVAFGSlILAKTLDAGQVGLALSYALTLMGMFQWCVRQSAEVENMMISVERVIEY 833
Cdd:cd18600 246 WFLYLSTLRWFQMRIEMIFVIFFTAVTFIS-IGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRIFKF 323
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
522-1082 |
1.00e-70 |
|
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: 246.98 E-value: 1.00e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 522 FRAGAHWIVFIFLILLNTAAQVAYVLQDWWLSywankqSMLNVTVNGGGNVTEkldLNWYLGIYSGLTVATVLFGIARSL 601
Cdd:COG4988 10 RLARGARRWLALAVLLGLLSGLLIIAQAWLLA------SLLAGLIIGGAPLSA---LLPLLGLLLAVLLLRALLAWLRER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 602 LVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDD-------------LLPLT------FLDFIQ 662
Cdd:COG4988 81 AAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGyfarylpqlflaaLVPLLilvavfPLDWLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 663 TLlqvvgvvsvavavIPWIAIPLVPLGIIFI------FLRRYFLETSRdvkrlesttrspVFSHLSSSLQGLWTIRAYKA 736
Cdd:COG4988 161 GL-------------ILLVTAPLIPLFMILVgkgaakASRRQWRALAR------------LSGHFLDRLRGLTTLKLFGR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 737 EER-CQELFDAHQDLHSE-------AwflFLTTsrwfAVrLDAICAMFVIIVAfgsLILAKTLDAGQVGLA-------LS 801
Cdd:COG4988 216 AKAeAERIAEASEDFRKRtmkvlrvA---FLSS----AV-LEFFASLSIALVA---VYIGFRLLGGSLTLFaalfvllLA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 802 ---YA-LTLMGMFqWCVRQSAevenmMISVERVIEYTDLEKEAPWEYQKRPPpaWPHEGVIIFDNVNFMYsPGGPLVLKH 877
Cdd:COG4988 285 pefFLpLRDLGSF-YHARANG-----IAAAEKIFALLDAPEPAAPAGTAPLP--AAGPPSIELEDVSFSY-PGGRPALDG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 878 LTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLDPFN 956
Cdd:COG4988 356 LSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPySGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGR 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 957 EH-TDEELWNALQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKK 1035
Cdd:COG4988 436 PDaSDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQA 515
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 2217293410 1036 IREKFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNK 1082
Cdd:COG4988 516 LRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
856-1082 |
1.72e-70 |
|
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: 234.81 E-value: 1.72e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 856 GVIIFDNVNFMYSPGGPlVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKM 934
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQkGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 935 SIIPQEPVLFTGTMRKNLDPFNEHTDEELWN-ALQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQ 1013
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIeAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 1014 ILIIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNK 1082
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
5-441 |
5.04e-65 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 231.21 E-value: 5.04e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 5 KTTTGQIVNLLSNDVNKFDQ-VTVFLHFLWAGPLQAIAVTALLWM---EIGISCLAGMAVLIILLPLqscFGKLFSSLRS 80
Cdd:COG1132 114 RRRTGDLLSRLTNDVDAVEQfLAHGLPQLVRSVVTLIGALVVLFVidwRLALIVLLVLPLLLLVLRL---FGRRLRKLFR 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 81 KTATFTDARIRTMNEVITGIRIIKMYAWEKS----FSNLITNLRKKEISKILRSSCLrgMNLASFFSASKIIVFVTFTTY 156
Cdd:COG1132 191 RVQEALAELNGRLQESLSGIRVVKAFGREERelerFREANEELRRANLRAARLSALF--FPLMELLGNLGLALVLLVGGL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 157 VLLGSVITASrVFVAVTLYgavrlTVTLFFP-----SAIERVSEAIVSIRRIQTFLLL-DEISQRNRQLP-SDGKKMVHV 229
Cdd:COG1132 269 LVLSGSLTVG-DLVAFILY-----LLRLFGPlrqlaNVLNQLQRALASAERIFELLDEpPEIPDPPGAVPlPPVRGEIEF 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 230 QDFTAFWDKasETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHG-------------LVSVHGRIAYVS 296
Cdd:COG1132 343 ENVSFSYPG--DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGrilidgvdirdltLESLRRQIGVVP 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 297 QQPWVFSGTLRSNILFGKK-YEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLL 375
Cdd:COG1132 421 QDTFLFSGTIRENIRYGRPdATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILIL 500
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 376 DDPLSAVDAEVSRHLFElCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 441
Cdd:COG1132 501 DEATSALDTETEALIQE-ALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARG 565
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
242-448 |
3.52e-64 |
|
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: 219.34 E-value: 3.52e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 242 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSQQPWVFSGTLRSNILFGKKYEKERY 321
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 322 EKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHE 401
Cdd:cd03291 130 KSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMAN 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2217293410 402 KITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSGIDFGSLL 448
Cdd:cd03291 210 KTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
858-1068 |
9.04e-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: 199.53 E-value: 9.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSI 936
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPtSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 937 IPQEPVLFTGTMRKNLdpfnehtdeelwnalqevqlketiedlpgkmdtelaesgsnFSVGQRQLVCLARAILRKNQILI 1016
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2217293410 1017 IDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIIDSDKIMVLDSGR 1068
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
856-1085 |
1.68e-58 |
|
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: 202.78 E-value: 1.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 856 GVIIFDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPEGKIWIDKILTTEIGLHDLRKKMS 935
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 936 IIPQEPVLFTGTMRKNLDPFNEHTDEELWNALQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQIL 1015
Cdd:cd03289 81 VIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1016 IIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNKESL 1085
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
858-1092 |
3.32e-58 |
|
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: 200.53 E-value: 3.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYSPGGPlVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSI 936
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVsSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 937 IPQEPVLFTGTMRKNLDPFNEH-TDEELWNALQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQIL 1015
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 1016 IIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLqNKESLFYKMVQQ 1092
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL-AKGGLYAEMWKA 235
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
858-1071 |
5.40e-57 |
|
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: 197.07 E-value: 5.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSI 936
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVdSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 937 IPQEPVLFTGTMRKNL---DPfnEHTDEELWNALQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQ 1013
Cdd:cd03251 81 VSQDVFLFNDTVAENIaygRP--GATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217293410 1014 ILIIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLKE 1071
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVE 216
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
5-203 |
2.22e-56 |
|
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: 197.31 E-value: 2.22e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 5 KTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKLFSSLRSKTAT 84
Cdd:cd18595 91 KSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIKKLQVKQMK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 85 FTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVTFTTYVLLGS--V 162
Cdd:cd18595 171 LKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFATYVLSDPdnV 250
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2217293410 163 ITASRVFVAVTLYGAVRLTVTlFFPSAIERVSEAIVSIRRI 203
Cdd:cd18595 251 LDAEKAFVSLSLFNILRFPLS-MLPMVISNLVQASVSLKRL 290
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
7-203 |
7.10e-56 |
|
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: 195.75 E-value: 7.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 7 TTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKLFSSLRSKTATFT 86
Cdd:cd18597 98 PNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGFLMKKLFKLRKKANKIT 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 87 DARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVTFTTYVLLGSVITAS 166
Cdd:cd18597 178 DKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASMLSFITYYATGHTLDPA 257
|
170 180 190
....*....|....*....|....*....|....*..
gi 2217293410 167 RVFVAVTLYGAVRLTVTlFFPSAIERVSEAIVSIRRI 203
Cdd:cd18597 258 NIFSSLALFNVLRMPLM-FLPLALSSLADALVALKRI 293
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
195-441 |
7.22e-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: 204.22 E-value: 7.22e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 195 EAIVSIRRIQTFLLLDE--ISQRNRQLPSDGKKMVHVQDFTAFWDkaSETPTLQGLSFTVRPGELLAVVGPVGAGKSSLL 272
Cdd:COG4988 303 NGIAAAEKIFALLDAPEpaAPAGTAPLPAAGPPSIELEDVSFSYP--GGRPALDGLSLTIPPGERVALVGPSGAGKSTLL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 273 SAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSGTLRSNILFGK-KYEKERYEKVIKACALKKDLQLLE 338
Cdd:COG4988 381 NLLLGFLPPYSGSILINGvdlsdldpaswrrQIAWVPQNPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDEFVAALP 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 339 DGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQILHEKITILVTHQLQYLKAAS 418
Cdd:COG4988 461 DGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQA-LRRLAKGRTVILITHRLALLAQAD 539
|
250 260
....*....|....*....|...
gi 2217293410 419 QILILKDGKMVQKGTYTEFLKSG 441
Cdd:COG4988 540 RILVLDDGRIVEQGTHEELLAKN 562
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-439 |
2.06e-54 |
|
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: 199.99 E-value: 2.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 2 AMGKTTTGQIVNLLSNDVNKFDqvTVFLHFL------WAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLqscfgkLF 75
Cdd:COG4987 105 GLARLRSGDLLNRLVADVDALD--NLYLRVLlpllvaLLVILAAVAFLAFFSPALALVLALGLLLAGLLLPL------LA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 76 SSL-----RSKTATFTDARIRTMnEVITGIRIIKMY----AWEKSFSNLITNLRKKEiskilrssclRGMNLASFFSASK 146
Cdd:COG4987 177 ARLgrragRRLAAARAALRARLT-DLLQGAAELAAYgaldRALARLDAAEARLAAAQ----------RRLARLSALAQAL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 147 IIVFVTFTTYVLLGSVITASR------VFVAVtlygAVRLTVTLF-----FPSAIERVSEAIVSIRRIqtFLLLDE---I 212
Cdd:COG4987 246 LQLAAGLAVVAVLWLAAPLVAagalsgPLLAL----LVLAALALFealapLPAAAQHLGRVRAAARRL--NELLDAppaV 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 213 SQRNRQLPSDGKKMVHVQDFTAFWDKASEtPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLV------ 286
Cdd:COG4987 320 TEPAEPAPAPGGPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSItlggvd 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 287 -------SVHGRIAYVSQQPWVFSGTLRSNILFGKKYEKEryEKVIKACA---LKKDLQLLEDGDLTVIGDRGTTLSGGQ 356
Cdd:COG4987 399 lrdldedDLRRRIAVVPQRPHLFDTTLRENLRLARPDATD--EELWAALErvgLGDWLAALPDGLDTWLGEGGRRLSGGE 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 357 KARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTE 436
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEE 555
|
...
gi 2217293410 437 FLK 439
Cdd:COG4987 556 LLA 558
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
59-449 |
1.54e-53 |
|
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: 200.45 E-value: 1.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 59 AVLIILLPLQSCFGKLFSSLRSKTA--TFTDARIR--TMNEVITGIRIIKMYA--------WEKSFSNLI-TNLRKKEIS 125
Cdd:COG2274 299 LVVLLLIPLYVLLGLLFQPRLRRLSreESEASAKRqsLLVETLRGIETIKALGaesrfrrrWENLLAKYLnARFKLRRLS 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 126 KILrssclrgMNLASFFSASKIIVFVTFTTYVLLGSVITASrVFVAVTLYgAVRLT---VTLFfpSAIERVSEAIVSIRR 202
Cdd:COG2274 379 NLL-------STLSGLLQQLATVALLWLGAYLVIDGQLTLG-QLIAFNIL-SGRFLapvAQLI--GLLQRFQDAKIALER 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 203 IQTFLLL--DEISQRNRQLPSDGKKMVHVQDFTaFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELA 280
Cdd:COG2274 448 LDDILDLppEREEGRSKLSLPRLKGDIELENVS-FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYE 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 281 PSHGLVSVHG-------------RIAYVSQQPWVFSGTLRSNILFGKKY-EKERYEKVIKACALKKDLQLLEDGDLTVIG 346
Cdd:COG2274 527 PTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGTIRENITLGDPDaTDEEIIEAARLAGLHDFIEALPMGYDTVVG 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 347 DRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQILHEKITILVTHQLQYLKAASQILILKDG 426
Cdd:COG2274 607 EGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILEN-LRRLLKGRTVIIIAHRLSTIRLADRIIVLDKG 685
|
410 420
....*....|....*....|...
gi 2217293410 427 KMVQKGTYTEFLKSGIDFGSLLK 449
Cdd:COG2274 686 RIVEDGTHEELLARKGLYAELVQ 708
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
593-1071 |
1.12e-52 |
|
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: 194.94 E-value: 1.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 593 VLFGIAR---SLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLpltfLDFIQTLLQVVG 669
Cdd:TIGR02203 65 VLRGICSfvsTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAA----TDAFIVLVRETL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 670 VVSVAVAVIPW----IAIPLVPLGIIFIFLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFD 745
Cdd:TIGR02203 141 TVIGLFIVLLYyswqLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 746 A-HQDLHSEAWFLFLTTSRWFA-VRLDAICAMFVIIVAFGSLILAKTLDAGQVGLALSYALTLMGMFQWCVRQSAEVENM 823
Cdd:TIGR02203 221 AvSNRNRRLAMKMTSAGSISSPiTQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 824 MISVERVIEYTDLEKEApwEYQKRPPPAwpHEGVIIFDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLIS 903
Cdd:TIGR02203 301 LAAAESLFTLLDSPPEK--DTGTRAIER--ARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVN 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 904 ALFRLSEPE-GKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNL---DPfNEHTDEELWNALQEVQLKETIEDL 979
Cdd:TIGR02203 377 LIPRFYEPDsGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT-EQADRAEIERALAAAYAQDFVDKL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 980 PGKMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIIDSD 1059
Cdd:TIGR02203 456 PLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKAD 535
|
490
....*....|..
gi 2217293410 1060 KIMVLDSGRLKE 1071
Cdd:TIGR02203 536 RIVVMDDGRIVE 547
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
582-1091 |
1.31e-51 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 192.24 E-value: 1.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 582 LGIYSGLTVATVLFGI-------ARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLlp 654
Cdd:PRK10790 61 LGLVAGLAAAYVGLQLlaaglhyAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDL-- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 655 ltFLDFIQTLLQVVGVVSVAVAV-------IPWIAIPLVPLGIIFIFLRRYFleTSRDVKRLESTTrSPVFSHLSSSLQG 727
Cdd:PRK10790 139 --YVTVVATVLRSAALIGAMLVAmfsldwrMALVAIMIFPAVLVVMVIYQRY--STPIVRRVRAYL-ADINDGFNEVING 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 728 LWTIRAYKAEERCQELFDAHQDLHSEAwflflttsRWFAVRLDA-----ICAMFVIIVAFGSLILAKTLDAGQVGLALSY 802
Cdd:PRK10790 214 MSVIQQFRQQARFGERMGEASRSHYMA--------RMQTLRLDGfllrpLLSLFSALILCGLLMLFGFSASGTIEVGVLY 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 803 A-LTLMG-----MFQWCVRQSAeVENMMISVERVIEYTDLEKEaPWEYQKRPPPAwpheGVIIFDNVNFMYSPGGPlVLK 876
Cdd:PRK10790 286 AfISYLGrlnepLIELTTQQSM-LQQAVVAGERVFELMDGPRQ-QYGNDDRPLQS----GRIDIDNVSFAYRDDNL-VLQ 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 877 HLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLDPF 955
Cdd:PRK10790 359 NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLtEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 956 NEHTDEELWNALQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKK 1035
Cdd:PRK10790 439 RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQA 518
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 1036 IREKFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQnKESLFYKMVQ 1091
Cdd:PRK10790 519 LAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLA-AQGRYWQMYQ 573
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
858-1092 |
3.48e-51 |
|
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: 180.43 E-value: 3.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYsPGGP--LVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKM 934
Cdd:cd03249 1 IEFKNVSFRY-PSRPdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPtSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 935 SIIPQEPVLFTGTMRKNL---DpfNEHTDEELWNALQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRK 1011
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIrygK--PDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1012 NQILIIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLKE---YDEpyvLLQNKEsLFYK 1088
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEqgtHDE---LMAQKG-VYAK 233
|
....
gi 2217293410 1089 MVQQ 1092
Cdd:cd03249 234 LVKA 237
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
229-426 |
4.90e-51 |
|
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: 179.45 E-value: 4.90e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 229 VQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLV-----------------SVHGR 291
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 292 IAYVSQQPWVFSGTLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDAD 371
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 372 IYLLDDPLSAVDAEVSRHLFELCICQILHE--KITILVTHQLQYLKAASQILILKDG 426
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
580-1090 |
1.08e-49 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 188.78 E-value: 1.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 580 WYLGIYSgltVATVLFGIAR--SLLVFYVLVNSSqtLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTF 657
Cdd:TIGR00958 205 FFMCLLS---IASSVSAGLRggSFNYTMARINLR--IREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNV 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 658 LDFIQTLLQVVGVVSVAVAVIPWIAI-PLVPLGIIFIFLRRY---FLETSRDVKrlESTTRSPVFSHlsSSLQGLWTIRA 733
Cdd:TIGR00958 280 NVLLRNLVMLLGLLGFMLWLSPRLTMvTLINLPLVFLAEKVFgkrYQLLSEELQ--EAVAKANQVAE--EALSGMRTVRS 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 734 YKAEE-RCQELFDAHQDLHSEAW------FLFLTTSRWFAVrldaicAMFVIIVAFGS-LILAKTLDAGQVglaLSYALT 805
Cdd:TIGR00958 356 FAAEEgEASRFKEALEETLQLNKrkalayAGYLWTTSVLGM------LIQVLVLYYGGqLVLTGKVSSGNL---VSFLLY 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 806 LMGMFQWcVRQSAEVEN-MMISV---ERVIEYTDLEKEAPWEYQKRPPPAwphEGVIIFDNVNFMYsPGGP--LVLKHLT 879
Cdd:TIGR00958 427 QEQLGEA-VRVLSYVYSgMMQAVgasEKVFEYLDRKPNIPLTGTLAPLNL---EGLIEFQDVSFSY-PNRPdvPVLKGLT 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 880 ALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLD-PFNE 957
Cdd:TIGR00958 502 FTLHPGEVVALVGPSGSGKSTVAALLQNLYQPtGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTD 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 958 HTDEELWNALQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKir 1037
Cdd:TIGR00958 582 TPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES-- 659
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 1038 EKFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEpYVLLQNKESLFYKMV 1090
Cdd:TIGR00958 660 RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGT-HKQLMEDQGCYKHLV 711
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
4-203 |
9.45e-49 |
|
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: 175.06 E-value: 9.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 4 GKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKLFSSLRSKTA 83
Cdd:cd18592 89 GDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAI 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 84 TFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVTFTTYVLLGSVI 163
Cdd:cd18592 169 VITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFLAHVALGNDL 248
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2217293410 164 TASRVFVAVTLYGAVRLTVTlFFPSAIERVSEAIVSIRRI 203
Cdd:cd18592 249 TAAQAFTVIAVFNSMRFSLR-MLPYAVKALAEAKVALQRI 287
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
4-203 |
1.93e-48 |
|
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: 174.99 E-value: 1.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 4 GKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKLFSSLRSKTA 83
Cdd:cd18596 110 SSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALVGLAVMVLLLPLNGYLAKRYSRAQKELM 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 84 TFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVTFTTYVLL-GSV 162
Cdd:cd18596 190 KARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLLLSLLWFLIPILVTVVTFATYTLVmGQE 269
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2217293410 163 ITASRVFVAVTLYGAVRLTVTlFFPSAIERVSEAIVSIRRI 203
Cdd:cd18596 270 LTASVAFTSLALFNMLRGPLN-VLPELITQLLQAKVSLDRI 309
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
822-1071 |
2.34e-47 |
|
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: 180.02 E-value: 2.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 822 NMMISVERVIEY--TDLEK-----EAPWEYQKRP--PPAWPHEGVIIFDNVNFMYSPGGPlVLKHLTALIKSQEKVGIVG 892
Cdd:COG5265 313 NFLGFVYREIRQalADMERmfdllDQPPEVADAPdaPPLVVGGGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVG 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 893 RTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNL---DPfnEHTDEELWNALQ 968
Cdd:COG5265 392 PSGAGKSTLARLLFRFYDVtSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIaygRP--DASEEEVEAAAR 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 969 EVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIREKFAHCTVLTI 1048
Cdd:COG5265 470 AAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVI 549
|
250 260
....*....|....*....|...
gi 2217293410 1049 AHRLNTIIDSDKIMVLDSGRLKE 1071
Cdd:COG5265 550 AHRLSTIVDADEILVLEAGRIVE 572
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
78-1066 |
3.44e-46 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 181.77 E-value: 3.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 78 LRSKTAT-FTDARIRTMNEVITGIRIIKMYAWEKSFSNLItNLRKKEISK-ILRSS--------CLRGMNLAS----FFS 143
Cdd:PTZ00265 223 INKKTSLlYNNNTMSIIEEALVGIRTVVSYCGEKTILKKF-NLSEKLYSKyILKANfmeslhigMINGFILASyafgFWY 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 144 ASKIIVFVTFTTY----VLLGSVITasrVFVAVtLYGAVRLTVTLffPSAIERVS--EAIVSIRRIQTFLLLDEISQRNR 217
Cdd:PTZ00265 302 GTRIIISDLSNQQpnndFHGGSVIS---ILLGV-LISMFMLTIIL--PNITEYMKslEATNSLYEIINRKPLVENNDDGK 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 218 QLPsDGKKmVHVQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVH-------- 289
Cdd:PTZ00265 376 KLK-DIKK-IQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdshnlkdi 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 290 ------GRIAYVSQQPWVFSGTLRSNI---LFGKK---YEKERYEK--------------VIKACA-------------- 329
Cdd:PTZ00265 454 nlkwwrSKIGVVSQDPLLFSNSIKNNIkysLYSLKdleALSNYYNEdgndsqenknkrnsCRAKCAgdlndmsnttdsne 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 330 ---LKKDLQLLEDGDL---------------------TVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE 385
Cdd:PTZ00265 534 lieMRKNYQTIKDSEVvdvskkvlihdfvsalpdkyeTLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 386 vSRHLFELCICQIL--HEKITILVTHQLQYLKAASQILILKDGkmvQKGTYTEFLKSGIDFGSLLKKDNEESEQPPVPGT 463
Cdd:PTZ00265 614 -SEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSNR---ERGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNN 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 464 PTLRNRTFS-ESSVWSQQSSRPSL---------------------------------KDGALESQDTENVPVTL------ 503
Cdd:PTZ00265 690 NNNNNNKINnAGSYIIEQGTHDALmknkngiyytminnqkvsskkssnndndkdsdmKSSAYKDSERGYDPDEMngnskh 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 504 -----------------SEENRSEGKVGFqaYKNYFRAGAHW-----------------IVFIFLILLnTAAQVAYVLQD 549
Cdd:PTZ00265 770 enesasnkksckmsdenASENNAGGKLPF--LRNLFKRKPKApnnlrivyreifsykkdVTIIALSIL-VAGGLYPVFAL 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 550 WWLSYWANKQSMLNVTVNGggnvtekldlNWYlGIYSgLTVATVLFgIARSLLVFYVLV---NSSQTLHNKMFESILKAP 626
Cdd:PTZ00265 847 LYAKYVSTLFDFANLEANS----------NKY-SLYI-LVIAIAMF-ISETLKNYYNNVigeKVEKTMKRRLFENILYQE 913
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 627 VLFFDR--NPIGRILNRFSKDIGHLDDLLPLTFLDFIQTLLQVVGVVSVAVAVIPWIAIPLVplGIIFIFLR----RYFL 700
Cdd:PTZ00265 914 ISFFDQdkHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVAAVLT--GTYFIFMRvfaiRARL 991
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 701 ETSRDVKRLESTTRSPVFSH-------------LSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAW--FLFLTTSRWf 765
Cdd:PTZ00265 992 TANKDVEKKEINQPGTVFAYnsddeifkdpsflIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQkrKTLVNSMLW- 1070
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 766 avRLDAICAMFVIIVA--FGSLILAK-TLDAGQVGLAL-------SYALTLMGMfqwcvrqSAEVENMMISVERVieYTD 835
Cdd:PTZ00265 1071 --GFSQSAQLFINSFAywFGSFLIRRgTILVDDFMKSLftflftgSYAGKLMSL-------KGDSENAKLSFEKY--YPL 1139
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 836 LEKEAPWEYQK----RPPPAWPHEGVIIFDNVNFMY--SPGGPlVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFR-- 907
Cdd:PTZ00265 1140 IIRKSNIDVRDnggiRIKNKNDIKGKIEIMDVNFRYisRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfy 1218
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 908 -----------------------------------------------------LSEPEGKIWIDKILTTEIGLHDLRKKM 934
Cdd:PTZ00265 1219 dlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstVFKNSGKILLDGVDICDYNLKDLRNLF 1298
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 935 SIIPQEPVLFTGTMRKNLDPFNEH-TDEELWNALQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQ 1013
Cdd:PTZ00265 1299 SIVSQEPMLFNMSIYENIKFGKEDaTREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPK 1378
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 1014 ILIIDEATANVDPRTDELIQKK---IREKfAHCTVLTIAHRLNTIIDSDKIMVLDS 1066
Cdd:PTZ00265 1379 ILLLDEATSSLDSNSEKLIEKTivdIKDK-ADKTIITIAHRIASIKRSDKIVVFNN 1433
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
856-1069 |
1.05e-45 |
|
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: 163.91 E-value: 1.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 856 GVIIFDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKM 934
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPtSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 935 SIIPQEPVLFTGTMRKNLDPFN-EHTDEELWNALQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQ 1013
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGApLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 1014 ILIIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIIDSDKIMVLDSGRL 1069
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
858-1091 |
9.31e-44 |
|
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: 159.19 E-value: 9.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKMSI 936
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPEnGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 937 IPQEPVLFTGTMRKNLDPFNEHTD-EELWNALQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQIL 1015
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSmERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 1016 IIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLKE---YDEpyvlLQNKESLFYKMVQ 1091
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEqgsHDE----LLAENGLYAYLYQ 235
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
681-1064 |
1.27e-43 |
|
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: 167.08 E-value: 1.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 681 IAIPLVPlgiIFIFLRRYFLEtSRDVKRLESTTRspVFSHLSSSLQGLWTIRAYKAEERCQE-LFDAHQDLHSE------ 753
Cdd:TIGR02857 152 LTAPLIP---IFMILIGWAAQ-AAARKQWAALSR--LSGHFLDRLRGLPTLKLFGRAKAQAAaIRRSSEEYRERtmrvlr 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 754 -AwflFLTTsrwFAVRLDAICAMFVIIVAFGSLILAKTLDAgQVGLalsYALTLMGMFQWCVRQ-------SAEVENMMI 825
Cdd:TIGR02857 226 iA---FLSS---AVLELFATLSVALVAVYIGFRLLAGDLDL-ATGL---FVLLLAPEFYLPLRQlgaqyhaRADGVAAAE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 826 SVERVIEytdlEKEAPwEYQKRPPPaWPHEGVIIFDNVNFMYsPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISAL 905
Cdd:TIGR02857 296 ALFAVLD----AAPRP-LAGKAPVT-AAPASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLL 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 906 FRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNL---DPfnEHTDEELWNALQEVQLKETIEDLPG 981
Cdd:TIGR02857 369 LGFVDPtEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRP--DASDAEIREALERAGLDEFVAALPQ 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 982 KMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIIDSDKI 1061
Cdd:TIGR02857 447 GLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRI 526
|
...
gi 2217293410 1062 MVL 1064
Cdd:TIGR02857 527 VVL 529
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
587-1093 |
7.72e-43 |
|
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: 167.44 E-value: 7.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 587 GLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFS--KDIGH-LDDLLPLTFLDFIQT 663
Cdd:TIGR03797 184 AAAVGAAAFQLAQSLAVLRLETRMDASLQAAVWDRLLRLPVSFFRQYSTGDLASRAMgiSQIRRiLSGSTLTTLLSGIFA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 664 LLQVVGVVSVAVAVIPW-IAIPLVPLGIIFI---FLRRYfletSRDVKRLESTtrspVFSHLSSSLQGLWTIRAYKAEER 739
Cdd:TIGR03797 264 LLNLGLMFYYSWKLALVaVALALVAIAVTLVlglLQVRK----ERRLLELSGK----ISGLTVQLINGISKLRVAGAENR 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 740 CqelFDAHQDLHSEAWFLFLTTSRW------FAVRLDAICaMFVIIVAFGSLILAKTLDAGQVgLALSYALtlmGMFQWC 813
Cdd:TIGR03797 336 A---FARWAKLFSRQRKLELSAQRIenlltvFNAVLPVLT-SAALFAAAISLLGGAGLSLGSF-LAFNTAF---GSFSGA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 814 VRQSAeveNMMISVERVI---EYTDLEKEAPWEYQKRPPPAWPHEGVIIFDNVNFMYSPGGPLVLKHLTALIKSQEKVGI 890
Cdd:TIGR03797 408 VTQLS---NTLISILAVIplwERAKPILEALPEVDEAKTDPGKLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAI 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 891 VGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLDPFNEHTDEELWNALQE 969
Cdd:TIGR03797 485 VGPSGSGKSTLLRLLLGFETPEsGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARM 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 970 VQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIrEKFAhCTVLTIA 1049
Cdd:TIGR03797 565 AGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESL-ERLK-VTRIVIA 642
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2217293410 1050 HRLNTIIDSDKIMVLDSGRLKE---YDEpyvlLQNKESLFYKMVQ-QL 1093
Cdd:TIGR03797 643 HRLSTIRNADRIYVLDAGRVVQqgtYDE----LMAREGLFAQLARrQL 686
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
1-203 |
8.08e-43 |
|
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: 158.10 E-value: 8.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1 MAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKLFSSLRS 80
Cdd:cd18598 87 SSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRIGALSE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 81 KTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEIS-----KILRSSClrgmnlaSFFSASK--IIVFVTF 153
Cdd:cd18598 167 KMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKalkgrKYLDALC-------VYFWATTpvLISILTF 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2217293410 154 TTYVLLGSVITASRVFVAVTLYGavRLTVTL-FFPSAIERVSEAIVSIRRI 203
Cdd:cd18598 240 ATYVLMGNTLTAAKVFTSLALFN--MLIGPLnAFPWVLNGLVEAWVSLKRL 288
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
240-427 |
2.90e-42 |
|
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: 152.15 E-value: 2.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 240 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLV-------------SVHGRIAYVSQQPWVFSGTL 306
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlidgvdlrdldleSLRKNIAYVPQDPFLFSGTI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 307 RSNIlfgkkyekeryekvikacalkkdlqlledgdltvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 386
Cdd:cd03228 93 RENI-----------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2217293410 387 SRHLFELcICQILHEKITILVTHQLQYLKAASQILILKDGK 427
Cdd:cd03228 132 EALILEA-LRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
681-1074 |
4.61e-42 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 163.59 E-value: 4.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 681 IAIPLVPLGIIFIFLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAY-KAEERCQELFDAHQDLHSeAWFLFL 759
Cdd:PRK13657 158 LSLVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYnRIEAETQALRDIADNLLA-AQMPVL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 760 TtsrWFAV-----RLDAICAMFVIIVAFGSLILAKTLDAGQVGLALSYALTLMGMFQwcvRQSAEVENMMISVERVIEYT 834
Cdd:PRK13657 237 S---WWALasvlnRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLD---QVVAFINQVFMAAPKLEEFF 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 835 DLEKEAPweyQKRPPPAWPH----EGVIIFDNVNFMYsPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSE 910
Cdd:PRK13657 311 EVEDAVP---DVRDPPGAIDlgrvKGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFD 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 911 PE-GKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLDPFNEH-TDEELWNALQEVQLKETIEDLPGKMDTELA 988
Cdd:PRK13657 387 PQsGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDaTDEEMRAAAERAQAHDFIERKPDGYDTVVG 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 989 ESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIIDSDKIMVLDSGR 1068
Cdd:PRK13657 467 ERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGR 546
|
....*....
gi 2217293410 1069 LKE---YDE 1074
Cdd:PRK13657 547 VVEsgsFDE 555
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
240-441 |
1.86e-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: 1.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 240 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHG-------------LVSVHGRIAYVSQQPWVFSGTL 306
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGqilidgidirdisRKSLRSMIGVVLQDTFLFSGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 307 RSNILFGKKYEKEryEKVIKACALKKDLQL---LEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 383
Cdd:cd03254 94 MENIRLGRPNATD--EEVIEAAKEAGAHDFimkLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217293410 384 AEvSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 441
Cdd:cd03254 172 TE-TEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
1-203 |
5.98e-41 |
|
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: 153.54 E-value: 5.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1 MAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKLFSSLRS 80
Cdd:cd18591 107 LSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALIGAALILVMTPLQYLIARKLSKNQK 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 81 KTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEIsKILRSSCLRGMNLASFFSASKIIV-FVTFTTYVLL 159
Cdd:cd18591 187 STLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKEL-KLLLKDAVYWSLMTFLTQASPILVtLVTFGLYPYL 265
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2217293410 160 -GSVITASRVFVAVTLYGavRLTVTLF-FPSAIERVSEAIVSIRRI 203
Cdd:cd18591 266 eGEPLTAAKAFSSLALFN--QLTVPLFiFPVVIPILINAVVSTRRL 309
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
238-432 |
6.41e-40 |
|
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: 147.35 E-value: 6.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 238 KASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSG 304
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVPQDVTLFYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 305 TLRSNILFGKKY-EKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 383
Cdd:cd03245 93 TLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2217293410 384 AEVSRHLFElCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKG 432
Cdd:cd03245 173 MNSEERLKE-RLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
203-454 |
8.13e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 156.93 E-value: 8.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 203 IQTFLLLDEISQRN--RQLPSDGKKMVHVQDFTAFwdKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELa 280
Cdd:PRK11174 324 LVTFLETPLAHPQQgeKELASNDPVTIEAEDLEIL--SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 281 PSHGLVSVHG-------------RIAYVSQQPWVFSGTLRSNILFGKK-YEKERYEKVIKACALKKDLQLLEDGDLTVIG 346
Cdd:PRK11174 401 PYQGSLKINGielreldpeswrkHLSWVGQNPQLPHGTLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 347 DRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEvSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDG 426
Cdd:PRK11174 481 DQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH-SEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDG 559
|
250 260
....*....|....*....|....*...
gi 2217293410 427 KMVQKGTYTEFLKSGIDFGSLLKKDNEE 454
Cdd:PRK11174 560 QIVQQGDYAELSQAGGLFATLLAHRQEE 587
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
531-808 |
9.15e-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: 148.95 E-value: 9.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 531 FIFLILLNTAAQVAYVLQDWWLSYWANkqsmlnvtVNGGGNVTEKLDLNWYLGIYSGLTVATVLFGIARSLLVFYVLVNS 610
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILD--------VLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 611 SQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQTLLQVVGVVSVAVAVIPWIAIPLVPLGI 690
Cdd:pfam00664 73 SRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 691 IFIFLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLD 770
Cdd:pfam00664 153 LYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQ 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2217293410 771 AIcAMFVIIVAF---GSLILAKTLDAGQVGLALSYALTLMG 808
Cdd:pfam00664 233 FI-GYLSYALALwfgAYLVISGELSVGDLVAFLSLFAQLFG 272
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
241-441 |
2.39e-39 |
|
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: 146.22 E-value: 2.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------------IAYVSQQPWVFSGTLR 307
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqIGLVSQDVFLFNDTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 308 SNILFGKKYE-KERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEv 386
Cdd:cd03251 94 ENIAYGRPGAtREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTE- 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2217293410 387 SRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 441
Cdd:cd03251 173 SERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
867-1092 |
3.24e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 155.00 E-value: 3.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 867 YSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPEGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTG 946
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 947 TMRKNLDPFNEH-TDEELWNALQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVD 1025
Cdd:PRK11174 438 TLRDNVLLGNPDaSDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1026 PRTDELIQKKIREKFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLKE---YDEpyvlLQNKESLFYKMVQQ 1092
Cdd:PRK11174 518 AHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQqgdYAE----LSQAGGLFATLLAH 583
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
855-1069 |
4.07e-39 |
|
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: 145.31 E-value: 4.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 855 EGVIIFDNVNFMYsPGGP--LVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLR 931
Cdd:cd03248 9 KGIVKFQNVTFAY-PTRPdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQgGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 932 KKMSIIPQEPVLFTGTMRKNLD-PFNEHTDEELWNALQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILR 1010
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 1011 KNQILIIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIIDSDKIMVLDSGRL 1069
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
241-423 |
5.05e-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: 153.60 E-value: 5.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSGTLR 307
Cdd:TIGR02857 334 RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 308 SNILFGKKYEKE-RYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 386
Cdd:TIGR02857 414 ENIRLARPDASDaEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET 493
|
170 180 190
....*....|....*....|....*....|....*....
gi 2217293410 387 SRHLFE--LCICQilhEKITILVTHQLQYLKAASQILIL 423
Cdd:TIGR02857 494 EAEVLEalRALAQ---GRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
241-441 |
7.92e-39 |
|
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: 144.99 E-value: 7.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSGTLR 307
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvdirdlnlrwlrsQIGLVSQEPVLFDGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 308 SNILFGKKYEK-ERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEv 386
Cdd:cd03249 95 ENIRYGKPDATdEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE- 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2217293410 387 SRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 441
Cdd:cd03249 174 SEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK 228
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
826-1093 |
1.76e-38 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 152.67 E-value: 1.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 826 SVERVIEYTDLEKEAPWEYQKRPPPAwphEGVIIFDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISAL 905
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTAAAD---QVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 906 FRLSEPE-GKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNL---DPfnEHTDEELWNALQEVQLKETIEDLPG 981
Cdd:PRK11160 387 TRAWDPQqGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKLLEDDKG 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 982 kMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIIDSDKI 1061
Cdd:PRK11160 465 -LNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRI 543
|
250 260 270
....*....|....*....|....*....|..
gi 2217293410 1062 MVLDSGRLKEYDEPYVLLQnKESLFYKMVQQL 1093
Cdd:PRK11160 544 CVMDNGQIIEQGTHQELLA-QQGRYYQLKQRL 574
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
590-1052 |
1.82e-38 |
|
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: 151.74 E-value: 1.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 590 VATVLFGIARSL------LVFYVLVNSSQT-LHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQ 662
Cdd:TIGR02868 57 VAVRAFGIGRAVfrylerLVGHDAALRSLGaLRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 663 TLLQVVGVVSVAVAVIPWIAIPL-VPLGIIFIFLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQ 741
Cdd:TIGR02868 137 ALVVGAAAVAAIAVLSVPAALILaAGLLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAAL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 742 -ELFDAHQDLH----SEAWFLFLTTSrwfAVRLDAICAMFVIIVAFGSLILAKTLD----AGQVGLALSyALTLMGMFQW 812
Cdd:TIGR02868 217 aQVEEADRELTraerRAAAATALGAA---LTLLAAGLAVLGALWAGGPAVADGRLApvtlAVLVLLPLA-AFEAFAALPA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 813 CVRQSAEVEnmmISVERVIEYTDLEKEAPWEYQKRPPPAWPHEGVIIFDNVNFMYsPGGPLVLKHLTALIKSQEKVGIVG 892
Cdd:TIGR02868 293 AAQQLTRVR---AAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILG 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 893 RTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNL---DPfnEHTDEELWNALQ 968
Cdd:TIGR02868 369 PSGSGKSTLLATLAGLLDPlQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLrlaRP--DATDEELWAALE 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 969 EVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIREKFAHCTVLTI 1048
Cdd:TIGR02868 447 RVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLI 526
|
....
gi 2217293410 1049 AHRL 1052
Cdd:TIGR02868 527 THHL 530
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
241-441 |
4.20e-38 |
|
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: 151.39 E-value: 4.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSGTLR 307
Cdd:TIGR02204 352 DQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGvdlrqldpaelraRMALVPQDPVLFAASVM 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 308 SNILFGKKYEKEryEKVIKACALKKD---LQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 384
Cdd:TIGR02204 432 ENIRYGRPDATD--EEVEAAARAAHAhefISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDA 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 385 EvSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 441
Cdd:TIGR02204 510 E-SEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKG 565
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
225-426 |
9.43e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 142.15 E-value: 9.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 225 KMVHVQDFTAFWDkasETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--------RIAYVS 296
Cdd:COG1121 5 PAIELENLTVSYG---GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 297 QQ---PWVF---------SGTLRSNILFgKKYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDR--GtTLSGGQKARVNL 362
Cdd:COG1121 82 QRaevDWDFpitvrdvvlMGRYGRRGLF-RRPSRADREAVDEA---------LERVGLEDLADRpiG-ELSGGQQQRVLL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 363 ARAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQILHEKITIL-VTHQLQYL-KAASQILILKDG 426
Cdd:COG1121 151 ARALAQDPDLLLLDEPFAGVDAATEEALYEL-LRELRREGKTILvVTHDLGAVrEYFDRVLLLNRG 215
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
220-428 |
5.91e-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: 5.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 220 PSDGKKMVHVQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSV----------- 288
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLdgkpisqyehk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 289 --HGRIAYVSQQPWVFSGTLRSNILFG---KKYEKeryekvIKACALKKD----LQLLEDGDLTVIGDRGTTLSGGQKAR 359
Cdd:cd03248 85 ylHSKVSLVGQEPVLFARSLQDNIAYGlqsCSFEC------VKEAAQKAHahsfISELASGYDTEVGEKGSQLSGGQKQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 360 VNLARAVYQDADIYLLDDPLSAVDAEvSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKM 428
Cdd:cd03248 159 VAIARALIRNPQVLILDEATSALDAE-SEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
240-440 |
8.71e-36 |
|
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: 144.12 E-value: 8.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 240 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------------IAYVSQQPWVFSGTL 306
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAdlsqwdreelgrhIGYLPQDVELFDGTI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 307 RSNI-LFGKkyekERYEKVIKACALK--KDLQL-LEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAV 382
Cdd:COG4618 423 AENIaRFGD----ADPEKVVAAAKLAgvHEMILrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217293410 383 DAEVSRHLFELcicqILHEK----ITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKS 440
Cdd:COG4618 499 DDEGEAALAAA----IRALKargaTVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
186-411 |
1.16e-35 |
|
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: 143.27 E-value: 1.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 186 FPSAIERVSEAIVSIRRIqTFLLLDEISQRNRQLPSDG-----KKMVHVQDFTAFWDKASetPTLQGLSFTVRPGELLAV 260
Cdd:TIGR02868 290 LPAAAQQLTRVRAAAERI-VEVLDAAGPVAEGSAPAAGavglgKPTLELRDLSAGYPGAP--PVLDGVSLDLPPGERVAI 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 261 VGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSGTLRSNILFGKK-YEKERYEKVIK 326
Cdd:TIGR02868 367 LGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssldqdevrrRVSVCAQDAHLFDTTVRENLRLARPdATDEELWAALE 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 327 ACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQILHEKITIL 406
Cdd:TIGR02868 447 RVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLED-LLAALSGRTVVL 525
|
....*
gi 2217293410 407 VTHQL 411
Cdd:TIGR02868 526 ITHHL 530
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
5-448 |
1.47e-35 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 145.25 E-value: 1.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 5 KTTTGQIVNLLSNDVNKF-----DQVTVFLHFLwagplqaIAVTALLWMEIGISCLAGMaVLIILLPL----QSCFGKLF 75
Cdd:TIGR00958 254 ENKTGELTSRLSSDTQTMsrslsLNVNVLLRNL-------VMLLGLLGFMLWLSPRLTM-VTLINLPLvflaEKVFGKRY 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 76 SSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKS----FSNLITNL----RKKEISKIL----RSSCLRGMNLASFFS 143
Cdd:TIGR00958 326 QLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGeasrFKEALEETlqlnKRKALAYAGylwtTSVLGMLIQVLVLYY 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 144 ASKIIV--------FVTFTTYVLLgsviTASRVFVAVTLYGAVRLTVtlffpSAIERVseaivsirriqtFLLLDeisqR 215
Cdd:TIGR00958 406 GGQLVLtgkvssgnLVSFLLYQEQ----LGEAVRVLSYVYSGMMQAV-----GASEKV------------FEYLD----R 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 216 NRQLPSDGKKM-------VHVQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLV-- 286
Cdd:TIGR00958 461 KPNIPLTGTLAplnleglIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVll 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 287 -----------SVHGRIAYVSQQPWVFSGTLRSNILFG-KKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSG 354
Cdd:TIGR00958 541 dgvplvqydhhYLHRQVALVGQEPVLFSGSVRENIAYGlTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSG 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 355 GQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcicQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTY 434
Cdd:TIGR00958 621 GQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES---RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTH 697
|
490
....*....|....
gi 2217293410 435 TEFLKSGIDFGSLL 448
Cdd:TIGR00958 698 KQLMEDQGCYKHLV 711
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
190-434 |
1.71e-35 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 143.31 E-value: 1.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 190 IERVSEAIVSIRRiqtflLLDE---ISQRNRQLPsDGKKMVHVqDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGA 266
Cdd:PRK10789 280 VERGSAAYSRIRA-----MLAEapvVKDGSEPVP-EGRGELDV-NIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 267 GKSSLLSAVLGELAPSHGLVSVH-------------GRIAYVSQQPWVFSGTLRSNILFGK-KYEKERYEKVIKACALKK 332
Cdd:PRK10789 353 GKSTLLSLIQRHFDVSEGDIRFHdipltklqldswrSRLAVVSQTPFLFSDTVANNIALGRpDATQQEIEHVARLASVHD 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 333 DLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRhlfelcicQILH-------EKITI 405
Cdd:PRK10789 433 DILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEH--------QILHnlrqwgeGRTVI 504
|
250 260
....*....|....*....|....*....
gi 2217293410 406 LVTHQLQYLKAASQILILKDGKMVQKGTY 434
Cdd:PRK10789 505 ISAHRLSALTEASEILVMQHGHIAQRGNH 533
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
243-441 |
1.75e-35 |
|
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: 135.05 E-value: 1.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 243 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------------IAYVSQQPWVFSGTLRSN 309
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirevtldslrraIGVVPQDTVLFNDTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 310 ILFGK-KYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 388
Cdd:cd03253 95 IRYGRpDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTER 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 389 HLFElCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 441
Cdd:cd03253 175 EIQA-ALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKG 226
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
240-424 |
1.16e-34 |
|
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: 131.89 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 240 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--------RIAYVSQQ---PWVFSGT--- 305
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRrsiDRDFPISvrd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 306 -----LRSNILFGKKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRG-TTLSGGQKARVNLARAVYQDADIYLLDDPL 379
Cdd:cd03235 90 vvlmgLYGHKGLFRRLSKADKAKV---------DEALERVGLSELADRQiGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2217293410 380 SAVDAEVSRHLFELcICQILHEKITIL-VTHQL-QYLKAASQILILK 424
Cdd:cd03235 161 AGVDPKTQEDIYEL-LRELRREGMTILvVTHDLgLVLEYFDRVLLLN 206
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
245-453 |
3.68e-34 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 131.34 E-value: 3.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQQPWVFSG-TLRSNIL 311
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALYPDlTVRENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 312 F-------GKKYEKERYEKVIKACALKKdlqlledgdltVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 384
Cdd:COG1131 96 FfarlyglPRKEARERIDELLELFGLTD-----------AADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 385 EVSRHLFELcICQILHEKITILV-THQLQYL-KAASQILILKDGKMVQKGTYTEFLKSGID--FGSLLKKDNE 453
Cdd:COG1131 165 EARRELWEL-LRELAAEGKTVLLsTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARLLEdvFLELTGEEAR 236
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
856-1082 |
4.98e-34 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 139.00 E-value: 4.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 856 GVIIFDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSE-PEGKIWIDKILTTEIGLHDLRKKM 934
Cdd:PRK11176 340 GDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDiDEGEILLDGHDLRDYTLASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 935 SIIPQEPVLFTGTMRKNLD-PFNEH-TDEELWNALQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKN 1012
Cdd:PRK11176 420 ALVSQNVHLFNDTIANNIAyARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1013 QILIIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNK 1082
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQN 569
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
240-432 |
2.87e-32 |
|
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: 123.96 E-value: 2.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 240 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQQPWVFSGTLR 307
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvsdlekalssLISVLNQRPYLFDTTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 308 SNIlfgkkyekeryekvikacalkkdlqlledgdltvigdrGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVS 387
Cdd:cd03247 93 NNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2217293410 388 RHLFELcICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKG 432
Cdd:cd03247 135 RQLLSL-IFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
227-432 |
3.61e-31 |
|
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: 121.86 E-value: 3.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 227 VHVQDFTAFWDkasETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYV 295
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvpperrnIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 296 SQQPWVFSG-TLRSNILFG----KKYEKERYEKVIKAcalkkdLQLLEDGDLtvIGDRGTTLSGGQKARVNLARAVYQDA 370
Cdd:cd03259 78 FQDYALFPHlTVAENIAFGlklrGVPKAEIRARVREL------LELVGLEGL--LNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217293410 371 DIYLLDDPLSAVDAEVSRHLFELcICQILHE--KITILVTH-QLQYLKAASQILILKDGKMVQKG 432
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREE-LKELQRElgITTIYVTHdQEEALALADRIAVMNEGRIVQVG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
221-426 |
4.63e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 123.28 E-value: 4.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 221 SDGKKMVHVQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--------R 291
Cdd:COG1116 2 SAAAPALELRGVSkRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 292 IAYVSQQ----PWVfsgTLRSNILFG----KKYEKERYEKVikacalkkdLQLLEDGDLTvigDRGT----TLSGGQKAR 359
Cdd:COG1116 82 RGVVFQEpallPWL---TVLDNVALGlelrGVPKAERRERA---------RELLELVGLA---GFEDayphQLSGGMRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217293410 360 VNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQILHE-KITIL-VTHQLQ---YLkaASQILILKDG 426
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALDALTRERLQDE-LLRLWQEtGKTVLfVTHDVDeavFL--ADRVVVLSAR 215
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
226-433 |
4.84e-31 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 122.84 E-value: 4.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 226 MVHVQDFTAfwdKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RI 292
Cdd:COG1120 1 MLEAENLSV---GYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 293 AYVSQQPWV-FSGTLRSNILFG--------KKYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDRG-TTLSGGQKARVNL 362
Cdd:COG1120 78 AYVPQEPPApFGLTVRELVALGryphlglfGRPSAEDREAVEEA---------LERTGLEHLADRPvDELSGGERQRVLI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 363 ARAVYQDADIYLLDDPLSAVD----AEVSRHLFELCICQilhEKITILVTHQL-QYLKAASQILILKDGKMVQKGT 433
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDlahqLEVLELLRRLARER---GRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
241-428 |
7.67e-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: 119.63 E-value: 7.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSGTLR 307
Cdd:cd03246 14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGadisqwdpnelgdHVGYLPQDDELFSGSIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 308 SNIlfgkkyekeryekvikacalkkdlqlledgdltvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVS 387
Cdd:cd03246 94 ENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2217293410 388 RHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKM 428
Cdd:cd03246 133 RALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
227-433 |
8.78e-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: 121.06 E-value: 8.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 227 VHVQDFTAFWDKASEtPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIA 293
Cdd:cd03244 3 IEFKNVSLRYRPNLP-PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 294 YVSQQPWVFSGTLRSNI-LFGKKYEKERYEkVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADI 372
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLdPFGEYSDEELWQ-ALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217293410 373 YLLDDPLSAVDAEVSRHLFELcICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGT 433
Cdd:cd03244 161 LVLDEATASVDPETDALIQKT-IREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
245-432 |
9.29e-31 |
|
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: 119.46 E-value: 9.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------------IAYVSQqpwvfsgtlrsnil 311
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaslspkelarkIAYVPQ-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 312 fgkkyekeryekvikacalkkdlqLLEDGDLTVIGDRG-TTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHL 390
Cdd:cd03214 81 ------------------------ALELLGLAHLADRPfNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2217293410 391 FELcICQILHE--KITILVTHQL-QYLKAASQILILKDGKMVQKG 432
Cdd:cd03214 137 LEL-LRRLARErgKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
875-1022 |
1.48e-30 |
|
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: 118.13 E-value: 1.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 875 LKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTG-TMRKNL 952
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPtEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 953 -------DPFNEHTDEELWNALQEVqlketieDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATA 1022
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKL-------GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
234-423 |
2.00e-30 |
|
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: 119.88 E-value: 2.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 234 AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------IAYVSQQ----PWV 301
Cdd:cd03293 9 TYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgpdRGYVFQQdallPWL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 302 fsgTLRSNILFG----KKYEKERYEKVikacalkkdLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLD 376
Cdd:cd03293 89 ---TVLDNVALGlelqGVPKAEARERA---------EELLELVGLSGFENAyPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2217293410 377 DPLSAVDAEVSRHLFELcICQILHE--KITILVTHQLQ---YLkaASQILIL 423
Cdd:cd03293 157 EPFSALDALTREQLQEE-LLDIWREtgKTVLLVTHDIDeavFL--ADRVVVL 205
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
858-1071 |
2.38e-30 |
|
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: 118.57 E-value: 2.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFR-LSEPEGKIWIDKILTTEIGlHDLRKKMSI 936
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 937 IPQEPVLFTGTMRKNLdpfnehtdeelwnalqevqlketiedlpgkmdtelaesGSNFSVGQRQLVCLARAILRKNQILI 1016
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 1017 IDEATANVDPRTD----ELIQKKIREKfahcTVLTIAHRLNTIIDSDKIMVLDSGRLKE 1071
Cdd:cd03247 122 LDEPTVGLDPITErqllSLIFEVLKDK----TLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
245-380 |
2.54e-30 |
|
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: 117.36 E-value: 2.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSG-TLRSNI 310
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217293410 311 LFGKkyEKERYEKVIKACALKKDLQLLEDGDL--TVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLS 380
Cdd:pfam00005 81 RLGL--LLKGLSKREKDARAEEALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
243-439 |
5.03e-30 |
|
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: 119.58 E-value: 5.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 243 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQQPWVFSG-TLRSN 309
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPDERGLYDRlTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 310 I-LFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVigdrgTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAeVSR 388
Cdd:COG4555 95 IrYFAELYGLFDEELKKRIEELIELLGLEEFLDRRV-----GELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV-MAR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 389 HLFELCICQILHEKITILV-THQLQYLKA-ASQILILKDGKMVQKGTYTEFLK 439
Cdd:COG4555 169 RLLREILRALKKEGKTVLFsSHIMQEVEAlCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
858-1068 |
9.27e-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: 117.57 E-value: 9.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYSPG---GPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALfrLSE---PEGKIWIdkiltteiglhdlR 931
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGElekLSGSVSV-------------P 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 932 KKMSIIPQEPVLFTGTMRKNL---DPFNEhtdEELWNALQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAI 1008
Cdd:cd03250 66 GSIAYVSQEPWIQNGTIRENIlfgKPFDE---ERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217293410 1009 LRKNQILIIDEATANVDPRT-DELIQKKIREKFAHC-TVLTIAHRLNTIIDSDKIMVLDSGR 1068
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
235-441 |
1.20e-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: 118.36 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 235 FWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWV 301
Cdd:cd03252 8 FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 302 FSGTLRSNILFGKkyEKERYEKVIKACALKKD---LQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDP 378
Cdd:cd03252 88 FNRSIRDNIALAD--PGMSMERVIEAAKLAGAhdfISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 379 LSAVDAEvSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 441
Cdd:cd03252 166 TSALDYE-SEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
243-464 |
1.25e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 125.84 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 243 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSGTLRSN 309
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtvtraslrrNIAVVFQDAGLFNRSIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 310 ILFGKK--YEKERYEKVIKACALkkDLQLL-EDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 386
Cdd:PRK13657 429 IRVGRPdaTDEEMRAAAERAQAH--DFIERkPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVET 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 387 SRHLfELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSGIDFGSLLK-----KDNEESEQPPVP 461
Cdd:PRK13657 507 EAKV-KAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRaqgmlQEDERRKQPAAE 585
|
...
gi 2217293410 462 GTP 464
Cdd:PRK13657 586 GAN 588
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
240-438 |
2.46e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 124.55 E-value: 2.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 240 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------------IAYVSQQPWVFSGTL 306
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiadyseaalrqaISVVSQRVHLFSATL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 307 RSNILFGK-KYEKERYEKVIKACALKKdlqLLEDGD-L-TVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 383
Cdd:PRK11160 431 RDNLLLAApNASDEALIEVLQQVGLEK---LLEDDKgLnAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLD 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2217293410 384 AEVSRHLFELcICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFL 438
Cdd:PRK11160 508 AETERQILEL-LAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
245-433 |
2.90e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 120.25 E-value: 2.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSQQP------WVFSG-------TLRSNIL 311
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPrerrvgFVFQHyalfphmTVAENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 312 FG----KKYEKERYEKVikacalkkdLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA-- 384
Cdd:COG1118 98 FGlrvrPPSKAEIRARV---------EELLELVQLEGLADRyPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAkv 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2217293410 385 --EVSRHLFElcicqiLHEKI---TILVTH-QLQYLKAASQILILKDGKMVQKGT 433
Cdd:COG1118 169 rkELRRWLRR------LHDELggtTVFVTHdQEEALELADRVVVMNQGRIEQVGT 217
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
861-1069 |
3.63e-29 |
|
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: 114.62 E-value: 3.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 861 DNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQ 939
Cdd:cd03246 4 ENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPtSGRVRLDGADISQWDPNELGDHVGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 940 EPVLFTGTMRKNLdpfnehtdeelwnalqevqlketiedlpgkmdtelaesgsnFSVGQRQLVCLARAILRKNQILIIDE 1019
Cdd:cd03246 84 DDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2217293410 1020 ATANVDPRTDELIQKKIRE-KFAHCTVLTIAHRLNTIIDSDKIMVLDSGRL 1069
Cdd:cd03246 123 PNSHLDVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
229-427 |
4.85e-29 |
|
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: 115.64 E-value: 4.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 229 VQDFTAFWDKaSETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYV 295
Cdd:cd03225 2 LKNLSFSYPD-GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 296 SQQP--WVFSGTLRSNILFGKKYEKERYEKVIkacalKKDLQLLEDGDLTVIGDRGT-TLSGGQKARVNLARAVYQDADI 372
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLENLGLPEEEIE-----ERVEEALELVGLEGLRDRSPfTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 373 YLLDDPLSAVDAEVSRHLFELcICQILHEKITIL-VTHQLQYLKA-ASQILILKDGK 427
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLEL-LKKLKAEGKTIIiVTHDLDLLLElADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
858-1085 |
5.33e-29 |
|
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: 116.28 E-value: 5.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYsPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSI 936
Cdd:COG1122 1 IELENLSFSY-PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPtSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 937 IPQEP------------VLFtGTMRKNLDPfnEHTDEELWNALQEVQLketiedlpgkmdTELAE------SGsnfsvGQ 998
Cdd:COG1122 80 VFQNPddqlfaptveedVAF-GPENLGLPR--EEIRERVEEALELVGL------------EHLADrpphelSG-----GQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 999 RQLVCLARAILRKNQILIIDEATANVDPR-TDELIQ--KKIREKfaHCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDE 1074
Cdd:COG1122 140 KQRVAIAGVLAMEPEVLVLDEPTAGLDPRgRRELLEllKRLNKE--GKTVIIVTHDLDLVAElADRVIVLDDGRIVADGT 217
|
250
....*....|.
gi 2217293410 1075 PYVLLQNKESL 1085
Cdd:COG1122 218 PREVFSDYELL 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
860-1068 |
7.35e-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: 113.49 E-value: 7.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 860 FDNVNFMYspGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIP 938
Cdd:cd00267 2 IENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPtSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 939 QepvlftgtmrknldpfnehtdeelwnalqevqlketiedlpgkmdtelaesgsnFSVGQRQLVCLARAILRKNQILIID 1018
Cdd:cd00267 80 Q------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2217293410 1019 EATANVDPRTDELIQKKIREKFAH-CTVLTIAHRLNTIID-SDKIMVLDSGR 1068
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
238-428 |
1.46e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 114.14 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 238 KASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSG 304
Cdd:COG4619 9 RVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYVPQEPALWGG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 305 TLRSNILFGKKYEKERYEKViKACALKKDLQLledgDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 384
Cdd:COG4619 89 TVRDNLPFPFQLRERKFDRE-RALELLERLGL----PPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2217293410 385 EVSRHLFELcICQILHEK-ITIL-VTH-QLQYLKAASQILILKDGKM 428
Cdd:COG4619 164 ENTRRVEEL-LREYLAEEgRAVLwVSHdPEQIERVADRVLTLEAGRL 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
241-436 |
5.58e-28 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 116.71 E-value: 5.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYVSQQPWVF-SGTLRS 308
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRdvtdlppkdrnIAMVFQSYALYpHMTVYE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 309 NILFG----KKYEKERYEKVIKACALkkdLQLLEdgdltvIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 383
Cdd:COG3839 95 NIAFPlklrKVPKAEIDRRVREAAEL---LGLED------LLDRkPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 384 AEvSRHLFELCICQiLHEKI---TILVTH-QLQYLKAASQILILKDGKMVQKGTYTE 436
Cdd:COG3839 166 AK-LRVEMRAEIKR-LHRRLgttTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEE 220
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
243-423 |
9.75e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 111.17 E-value: 9.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 243 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--RIAYVSQQ---PWVFSGTLRSNI---LFGK 314
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRsevPDSLPLTVRDLVamgRWAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 315 KYEKERY----EKVIKACALKKDLQLLEDGDLTvigdrgtTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHL 390
Cdd:NF040873 86 RGLWRRLtrddRAAVDDALERVGLADLAGRQLG-------ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI 158
|
170 180 190
....*....|....*....|....*....|....
gi 2217293410 391 FELcICQILHEKITIL-VTHQLQYLKAASQILIL 423
Cdd:NF040873 159 IAL-LAEEHARGATVVvVTHDLELVRRADPCVLL 191
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
860-1068 |
1.03e-27 |
|
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: 111.79 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 860 FDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIP 938
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPtSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 939 QEP--VLFTGTMRKNL--DPFNEHTDEE-----LWNALQEVQLKETIEDLPgkmdtelaesgSNFSVGQRQLVCLARAIL 1009
Cdd:cd03225 82 QNPddQFFGPTVEEEVafGLENLGLPEEeieerVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 1010 RKNQILIIDEATANVDPR-TDELIQ--KKIREKFAhcTVLTIAHRLNTIID-SDKIMVLDSGR 1068
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAgRRELLEllKKLKAEGK--TIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
241-439 |
1.40e-27 |
|
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: 112.04 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPW--VFSGT 305
Cdd:COG1122 13 GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknlrelrrKVGLVFQNPDdqLFAPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 306 LRSNILFGKKY----EKERYEKVIKAcalkkdlqlLEDGDLTVIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPLS 380
Cdd:COG1122 93 VEEDVAFGPENlglpREEIRERVEEA---------LELVGLEHLADRPPhELSGGQKQRVAIAGVLAMEPEVLVLDEPTA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217293410 381 AVDAEVSRHLFELcICQILHEKIT-ILVTHQLQYL-KAASQILILKDGKMVQKGTYTEFLK 439
Cdd:COG1122 164 GLDPRGRRELLEL-LKRLNKEGKTvIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
240-437 |
8.71e-27 |
|
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: 110.35 E-value: 8.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 240 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG----------------RIAYVSQQPW--- 300
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinklkgkalrqlrrQIGMIFQQFNlie 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 301 -------VFSG------TLRSniLFGKKYEKERYekviKACALKKDLQLLEDgdltvIGDRGTTLSGGQKARVNLARAVY 367
Cdd:cd03256 92 rlsvlenVLSGrlgrrsTWRS--LFGLFPKEEKQ----RALAALERVGLLDK-----AYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217293410 368 QDADIYLLDDPLSAVDAEVSRHLFELC--ICQilHEKITILVT-HQLQYLKA-ASQILILKDGKMVQKGTYTEF 437
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLkrINR--EEGITVIVSlHQVDLAREyADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
226-436 |
1.83e-26 |
|
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: 109.21 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 226 MVHVQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------- 290
Cdd:cd03258 1 MIELKNVSkVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltllsgkelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 291 --RIAYVSQQPWVFSG-TLRSNILF----GKKYEKERYEKVikacalkkdLQLLEDGDLTVIGDR-GTTLSGGQKARVNL 362
Cdd:cd03258 81 rrRIGMIFQHFNLLSSrTVFENVALpleiAGVPKAEIEERV---------LELLELVGLEDKADAyPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 363 ARAVYQDADIYLLDDPLSAVDAEVSRHLFELcicqiLHE-----KITI-LVTHQLQYLKA-ASQILILKDGKMVQKGTYT 435
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILAL-----LRDinrelGLTIvLITHEMEVVKRiCDRVAVMEKGEVVEEGTVE 226
|
.
gi 2217293410 436 E 436
Cdd:cd03258 227 E 227
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
834-1072 |
2.69e-26 |
|
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: 115.23 E-value: 2.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 834 TDLEKEAPWEYQKRPPPAwPhEGVIIFDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-E 912
Cdd:COG4618 309 NELLAAVPAEPERMPLPR-P-KGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPtA 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 913 GKIWIDKIlttEIGLHDLRKKMSII---PQEPVLFTGTMRKNLDPFNEHTDEELWNALQEVQLKETIEDLPGKMDTELAE 989
Cdd:COG4618 387 GSVRLDGA---DLSQWDREELGRHIgylPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 990 SGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIRE-KFAHCTVLTIAHRLNTIIDSDKIMVLDSGR 1068
Cdd:COG4618 464 GGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAlKARGATVVVITHRPSLLAAVDKLLVLRDGR 543
|
....
gi 2217293410 1069 LKEY 1072
Cdd:COG4618 544 VQAF 547
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
241-433 |
4.17e-26 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 111.34 E-value: 4.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYVSQqpwvfSGTL--- 306
Cdd:COG3842 17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppekrnVGMVFQ-----DYALfph 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 307 ---RSNILFG----KKYEKERYEKVIKACALkkdLQLledGDLtviGDRG-TTLSGGQKARVNLARAVYQDADIYLLDDP 378
Cdd:COG3842 92 ltvAENVAFGlrmrGVPKAEIRARVAELLEL---VGL---EGL---ADRYpHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 379 LSAVDAEVSRHL-FELciCQILHE-KIT-ILVTH-QLQYLKAASQILILKDGKMVQKGT 433
Cdd:COG3842 163 LSALDAKLREEMrEEL--RRLQRElGITfIYVTHdQEEALALADRIAVMNDGRIEQVGT 219
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
227-438 |
8.92e-26 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 113.58 E-value: 8.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 227 VHVQDFTaFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVL-------GE-LAPSHG-----LVSVHGRIA 293
Cdd:PRK11176 342 IEFRNVT-FTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTrfydideGEiLLDGHDlrdytLASLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 294 YVSQQPWVFSGTLRSNILF--GKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDAD 371
Cdd:PRK11176 421 LVSQNVHLFNDTIANNIAYarTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSP 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 372 IYLLDDPLSAVDAEvSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFL 438
Cdd:PRK11176 501 ILILDEATSALDTE-SERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELL 566
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
243-447 |
1.27e-25 |
|
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: 114.07 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 243 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------------IAYVSQQPWVFSGTLRSN 309
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFslkdidrhtlrqfINYLPQEPYIFSGSILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 310 ILFGKKyEKERYEKVIKACAL---KKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 386
Cdd:TIGR01193 568 LLLGAK-ENVSQDEIWAACEIaeiKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTIT 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217293410 387 SRHLFELCIcqILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSGIDFGSL 447
Cdd:TIGR01193 647 EKKIVNNLL--NLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
852-1069 |
1.80e-25 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 112.50 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 852 WPHEGVIIFDNVNFMYSPGGPLvlkhltaliksqekvGIVGRTGAGKSSLISALFRLSE-PEGKIWIDKILTTEIGLHDL 930
Cdd:PRK10789 323 YPQTDHPALENVNFTLKPGQML---------------GICGPTGSGKSTLLSLIQRHFDvSEGDIRFHDIPLTKLQLDSW 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 931 RKKMSIIPQEPVLFTGTMRKNL---DPfnEHTDEELWNALQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARA 1007
Cdd:PRK10789 388 RSRLAVVSQTPFLFSDTVANNIalgRP--DATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217293410 1008 ILRKNQILIIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIIDSDKIMVLDSGRL 1069
Cdd:PRK10789 466 LLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHI 527
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
226-427 |
1.92e-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: 105.25 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 226 MVHVQDFTAFWDkasETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIA 293
Cdd:COG4133 2 MLEAENLSCRRG---ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 294 YVSQQPWVFSG-TLRSNILFgkkyekeryekvikACALKKD-------LQLLEDGDLTVIGDR-GTTLSGGQKARVNLAR 364
Cdd:COG4133 79 YLGHADGLKPElTVRENLRF--------------WAALYGLradreaiDEALEAVGLAGLADLpVRQLSAGQKRRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217293410 365 AVYQDADIYLLDDPLSAVDAEvSRHLFElcicQILHE-----KITILVTHQLQYLKAAsQILILKDGK 427
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAA-GVALLA----ELIAAhlargGAVLLTTHQPLELAAA-RVLDLGDFK 206
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
243-436 |
2.77e-25 |
|
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: 105.88 E-value: 2.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 243 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYVSQQPWVFSG-TLRSNI 310
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvpvqernVGFVFQHYALFRHmTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 311 LFGKKyEKERYEKVIKACALKKDLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRH 389
Cdd:cd03296 96 AFGLR-VKPRSERPPEAEIRAKVHELLKLVQLDWLADRyPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2217293410 390 LFELciCQILHEKI---TILVTH-QLQYLKAASQILILKDGKMVQKGTYTE 436
Cdd:cd03296 175 LRRW--LRRLHDELhvtTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDE 223
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
226-423 |
4.11e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 104.49 E-value: 4.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 226 MVHVQDFTAFWDKaseTPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAP---SHGLVSVHG-----------R 291
Cdd:COG4136 1 MLSLENLTITLGG---RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGrrltalpaeqrR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 292 IAYVSQQPWVFSG-TLRSNILFG-----KKyeKERYEKVIKAcalkkdlqlLEDGDLTVIGDRG-TTLSGGQKARVNLAR 364
Cdd:COG4136 78 IGILFQDDLLFPHlSVGENLAFAlpptiGR--AQRRARVEQA---------LEEAGLAGFADRDpATLSGGQRARVALLR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 365 AVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKI-TILVTHQLQYLKAASQILIL 423
Cdd:COG4136 147 ALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIpALLVTHDEEDAPAAGRVLDL 206
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
242-440 |
4.19e-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: 105.46 E-value: 4.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 242 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSG-TLR 307
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFPHmTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 308 SNI-LFGK--KYEKERYEKVIKacalkkdlQLLEDGDLTVIGDRG---TTLSGGQKARVNLARAVYQDADIYLLDDPLSA 381
Cdd:cd03295 94 ENIaLVPKllKWPKEKIRERAD--------ELLALVGLDPAEFADrypHELSGGQQQRVGVARALAADPPLLLMDEPFGA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217293410 382 VDAEVSRHLFE--LCICQILHEKItILVTHQLQ-YLKAASQILILKDGKMVQKGTYTEFLKS 440
Cdd:cd03295 166 LDPITRDQLQEefKRLQQELGKTI-VFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
5-203 |
4.98e-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: 106.53 E-value: 4.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 5 KTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKLFSSLRSKTAT 84
Cdd:cd18559 91 RTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 85 FTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVTFTTYVLLGS--V 162
Cdd:cd18559 171 SKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHSlaG 250
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2217293410 163 ITASRVFVAVTLYGAVRLTVTLfFPSAIERVSEAIVSIRRI 203
Cdd:cd18559 251 LVALKVFYSLALTTYLNWPLNM-SPEVITNIVAAEVSLERS 290
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
241-440 |
7.63e-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: 104.51 E-value: 7.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG----------------RIAYVSQQPWVFSG 304
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglseaelyrlrrRMGMLFQSGALFDS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 305 -TLRSNILFGKKYEKERYEKVIKACALKKdlqlledgdLTVIGDRGTT------LSGGQKARVNLARAVYQDADIYLLDD 377
Cdd:cd03261 92 lTVFENVAFPLREHTRLSEEEIREIVLEK---------LEAVGLRGAEdlypaeLSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 378 PLSAVDAEVSRHLFELcicqI--LHEKI---TILVTHQLQ-YLKAASQILILKDGKMVQKGTYTEFLKS 440
Cdd:cd03261 163 PTAGLDPIASGVIDDL----IrsLKKELgltSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEELRAS 227
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
581-833 |
7.69e-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: 106.14 E-value: 7.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 581 YLGIYSGLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPlTFLDF 660
Cdd:cd18559 40 YLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAP-QVIKM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 661 IQTLLQVVGVVSVAVAVIPWIAIPLVPLGIIFIFLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERC 740
Cdd:cd18559 119 WMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAF 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 741 QELFDAHQDlHSEAWFLFLTTSRWFAVRLDAICAMFVIIVAFGSLILAKTLdAGQVGLALSYALTLMGMFQWCVRQSAEV 820
Cdd:cd18559 199 IRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHSL-AGLVALKVFYSLALTTYLNWPLNMSPEV 276
|
250
....*....|...
gi 2217293410 821 ENMMISVERVIEY 833
Cdd:cd18559 277 ITNIVAAEVSLER 289
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
241-427 |
8.03e-25 |
|
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: 103.72 E-value: 8.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------------IAYVSQQPWVFS 303
Cdd:cd03255 16 KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelaafrrrhIGFVFQSFNLLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 304 G-TLRSNILFGKkyekeRYEKVIKACALKKDLQLLEDGDLtviGDRGT----TLSGGQKARVNLARAVYQDADIYLLDDP 378
Cdd:cd03255 96 DlTALENVELPL-----LLAGVPKKERRERAEELLERVGL---GDRLNhypsELSGGQQQRVAIARALANDPKIILADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2217293410 379 LSAVDAEVSRHLFELcICQILHEKIT--ILVTHQLQYLKAASQILILKDGK 427
Cdd:cd03255 168 TGNLDSETGKEVMEL-LRELNKEAGTtiVVVTHDPELAEYADRIIELRDGK 217
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
857-1085 |
9.00e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 105.07 E-value: 9.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 857 VIIFDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMS 935
Cdd:PRK13632 7 MIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPqSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 936 IIPQEP------------VLFtGTMRKNLDPfnehtdEELWNALQEVQLKETIEDLpgkmdteLAESGSNFSVGQRQLVC 1003
Cdd:PRK13632 87 IIFQNPdnqfigatveddIAF-GLENKKVPP------KKMKDIIDDLAKKVGMEDY-------LDKEPQNLSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1004 LARAILRKNQILIIDEATANVDPRTDELIQKKIRE--KFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQN 1081
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
....
gi 2217293410 1082 KESL 1085
Cdd:PRK13632 233 KEIL 236
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
245-428 |
1.08e-24 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 102.09 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQQPWVFSG-TLRSNIl 311
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGkdikkepeevkrRIGYLPEEPSLYENlTVRENL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 312 fgkkyekeryekvikacalkkdlqlledgdltvigdrgtTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLF 391
Cdd:cd03230 95 ---------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFW 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 2217293410 392 ELcICQILHEKITILV-THQLQYLKA-ASQILILKDGKM 428
Cdd:cd03230 136 EL-LRELKKEGKTILLsSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
860-1075 |
1.26e-24 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 103.41 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 860 FDNVNFMYspGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSE------PEGKIWID--KILTTEIGLHDLR 931
Cdd:cd03260 3 LRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgapDEGEVLLDgkDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 932 KKMSIIPQEPVLFTGTMRKNLD--------PFNEHTDEELWNALQEVqlketieDLPGKMDTELAESGsnFSVGQRQLVC 1003
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAyglrlhgiKLKEELDERVEEALRKA-------ALWDEVKDRLHALG--LSGGQQQRLC 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 1004 LARAILRKNQILIIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEP 1075
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPT 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
241-427 |
1.42e-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: 101.17 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQqpwvfsgtlr 307
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGkdiaklpleelrrRIGYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 308 snilfgkkyekeryekvikacalkkdlqlledgdltvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEvS 387
Cdd:cd00267 81 --------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA-S 115
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2217293410 388 RHLFELCICQILHEKITIL-VTHQLQYL-KAASQILILKDGK 427
Cdd:cd00267 116 RERLLELLRELAEEGRTVIiVTHDPELAeLAADRVIVLKDGK 157
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
244-429 |
2.15e-24 |
|
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: 102.34 E-value: 2.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 244 TLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR----------IAYVSQQP--WVFSGTLRSNIL 311
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpikakerrksIGYVMQDVdyQLFTDSVREELL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 312 FGKKYEKERYEKVikACALKK-DLQLLEDgdltvigDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHL 390
Cdd:cd03226 95 LGLKELDAGNEQA--ETVLKDlDLYALKE-------RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2217293410 391 FELcicqILH----EKITILVTHQLQYL-KAASQILILKDGKMV 429
Cdd:cd03226 166 GEL----IRElaaqGKAVIVITHDYEFLaKVCDRVLLLANGAIV 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
226-467 |
4.39e-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: 4.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 226 MVHVQDFTaFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPS---HGLVSVHG------------ 290
Cdd:COG1123 4 LLEVRDLS-VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGrdllelsealrg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 291 -RIAYVSQQPWV--FSGTLRSNILFGKkyekeRYEKVIKACALKKDLQLLEDGDLTVIGDRGT-TLSGGQKARVNLARAV 366
Cdd:COG1123 83 rRIGMVFQDPMTqlNPVTVGDQIAEAL-----ENLGLSRAEARARVLELLEAVGLERRLDRYPhQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 367 YQDADIYLLDDPLSAVDAEVSRHLFELcICQILHEKIT--ILVTHQLQY-LKAASQILILKDGKMVQKGTYTEFLKSGID 443
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDL-LRELQRERGTtvLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
250 260
....*....|....*....|....*.
gi 2217293410 444 FGSL--LKKDNEESEQPPVPGTPTLR 467
Cdd:COG1123 237 LAAVprLGAARGRAAPAAAAAEPLLE 262
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
226-440 |
4.80e-24 |
|
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: 102.57 E-value: 4.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 226 MVHVQDFTA-FWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------R 291
Cdd:COG1124 1 MLEVRNLSVsYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGrpvtrrrrkafrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 292 IAYVSQQP-----------WVFSGTLRsniLFGKKYEKERYEKVIKACALKKDLQlledgdltvigDR-GTTLSGGQKAR 359
Cdd:COG1124 81 VQMVFQDPyaslhprhtvdRILAEPLR---IHGLPDREERIAELLEQVGLPPSFL-----------DRyPHQLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 360 VNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQILHE-KIT-ILVTHQLQYLKA-ASQILILKDGKMVQKGTYTE 436
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNL-LKDLREErGLTyLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVAD 225
|
....
gi 2217293410 437 FLKS 440
Cdd:COG1124 226 LLAG 229
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
757-1051 |
6.50e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 107.59 E-value: 6.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 757 LFLTTSRWFAVRLdaicAMFVIIVAFgsliLAKTLDAGQVGLALSYALTLMGMFQWCVRQSAEVENMMISVERVIEYTDL 836
Cdd:COG4178 270 FFTTGYGQLAVIF----PILVAAPRY----FAGEITLGGLMQAASAFGQVQGALSWFVDNYQSLAEWRATVDRLAGFEEA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 837 EKEAPWEYQKRPPPAWPHEGVIIFDNVNFmYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSePEGkiw 916
Cdd:COG4178 342 LEAADALPEAASRIETSEDGALALEDLTL-RTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLW-PYG--- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 917 idkilTTEIGLHDLRKKMsIIPQEPVLFTGTMRKNL---DPFNEHTDEELWNALQEVQLketiEDLPGKMDTElAESGSN 993
Cdd:COG4178 417 -----SGRIARPAGARVL-FLPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGL----GHLAERLDEE-ADWDQV 485
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217293410 994 FSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHR 1051
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
861-1069 |
7.16e-24 |
|
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: 99.82 E-value: 7.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 861 DNVNFMYspGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKMSIIPQ 939
Cdd:cd03214 3 ENLSVGY--GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSsGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 940 epvlftgtmrknldpfnehtdeelwnALQEVQlketIEDLPGKMDTELaeSGsnfsvGQRQLVCLARAILRKNQILIIDE 1019
Cdd:cd03214 81 --------------------------ALELLG----LAHLADRPFNEL--SG-----GERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2217293410 1020 ATANVDP----RTDELIQKKIREKfaHCTVLTIAHRLNTIID-SDKIMVLDSGRL 1069
Cdd:cd03214 124 PTSHLDIahqiELLELLRRLARER--GKTVVMVLHDLNLAARyADRVILLKDGRI 176
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
224-429 |
7.95e-24 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 101.27 E-value: 7.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 224 KKMVHVQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------ 290
Cdd:COG1136 2 SPLLELRNLTkSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdisslserela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 291 -----RIAYVSQQPWVFSG-TLRSNI----LFGKKYEKERYEKVikacalkkdLQLLED-GdltvIGDRG----TTLSGG 355
Cdd:COG1136 82 rlrrrHIGFVFQFFNLLPElTALENValplLLAGVSRKERRERA---------RELLERvG----LGDRLdhrpSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 356 QKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQILHEK-ITIL-VTHQLQYLKAASQILILKDGKMV 429
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLEL-LRELNRELgTTIVmVTHDPELAARADRVIRLRDGRIV 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
245-440 |
1.23e-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: 100.87 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------RIAYVSQQPWVFSG-TLRSNILF 312
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnlppekrDISYVPQNYALFPHmTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 313 GKKyeKERYEKVIKAcalKKDLQLLEDGDLTVIGDRG-TTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLF 391
Cdd:cd03299 95 GLK--KRKVDKKEIE---RKVLEIAEMLGIDHLLNRKpETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2217293410 392 ELcICQILHE-KITIL-VTHQLQYLKA-ASQILILKDGKMVQKGTYTEFLKS 440
Cdd:cd03299 170 EE-LKKIRKEfGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
857-1085 |
1.48e-23 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 106.14 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 857 VIIFDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRL----SEPEGKIWIDKILTTEIGLHDLRK 932
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphgGRISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 933 KMSIIPQEP------------VLFtGTMRKNLDPfnEHTDEELWNALQEVQLKETIEDLPgkmdtelaesgSNFSVGQRQ 1000
Cdd:COG1123 84 RIGMVFQDPmtqlnpvtvgdqIAE-ALENLGLSR--AEARARVLELLEAVGLERRLDRYP-----------HQLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1001 LVCLARAILRKNQILIIDEATANVDPRTDELIQKKIRE--KFAHCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYV 1077
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEE 229
|
....*...
gi 2217293410 1078 LLQNKESL 1085
Cdd:COG1123 230 ILAAPQAL 237
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
227-432 |
1.75e-23 |
|
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: 99.64 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 227 VHVQDFTAFWDKaseTPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYV 295
Cdd:cd03301 1 VELENVTKRFGN---VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlppkdrdIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 296 SQQPWVFSG-TLRSNILFGKKYEKERY----EKVIKACALKKDLQLLEDgdltvigdRGTTLSGGQKARVNLARAVYQDA 370
Cdd:cd03301 78 FQNYALYPHmTVYDNIAFGLKLRKVPKdeidERVREVAELLQIEHLLDR--------KPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217293410 371 DIYLLDDPLSAVDAEVSRHL-FELCICQILHEKITILVTH-QLQYLKAASQILILKDGKMVQKG 432
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMrAELKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
245-437 |
2.66e-23 |
|
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: 99.56 E-value: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAV-----LGELAPSHGLVSVHG---------------RIAYVSQQPWVFSG 304
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGkdiydldvdvlelrrRVGMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 305 TLRSNILFGKKYEKERYEKVIKAcalkKDLQLLEDGDLT-VIGDR--GTTLSGGQKARVNLARAVYQDADIYLLDDPLSA 381
Cdd:cd03260 96 SIYDNVAYGLRLHGIKLKEELDE----RVEEALRKAALWdEVKDRlhALGLSGGQQQRLCLARALANEPEVLLLDEPTSA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217293410 382 VDAeVSRHLFELCICQiLHEKITIL-VTHQL-QYLKAASQILILKDGKMVQKGTYTEF 437
Cdd:cd03260 172 LDP-ISTAKIEELIAE-LKKEYTIViVTHNMqQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
874-1072 |
4.01e-23 |
|
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: 99.12 E-value: 4.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 874 VLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID-KILTT--EIGLHDLRKKMSIIPQEPVL-FTGTM 948
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPtSGSIIFDgKDLLKlsRRLRKIRRKEIQMVFQDPMSsLNPRM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 949 R--KNL-DPFNEHTDEELWNALQEV--QLKETIEDLPGKMD---TELaeSGsnfsvGQRQLVCLARAILRKNQILIIDEA 1020
Cdd:cd03257 100 TigEQIaEPLRIHGKLSKKEARKEAvlLLLVGVGLPEEVLNrypHEL--SG-----GQRQRVAIARALALNPKLLIADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 1021 TANVDPRT-DELIQ--KKIREKFAhCTVLTIAHRLNTI-IDSDKIMVLDSGRLKEY 1072
Cdd:cd03257 173 TSALDVSVqAQILDllKKLQEELG-LTLLFITHDLGVVaKIADRVAVMYAGKIVEE 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
238-438 |
4.74e-23 |
|
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: 100.03 E-value: 4.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 238 KASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------------RIAYVSQQPW 300
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrelrrkKISMVFQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 301 VFSG-TLRSNILFG-------KKYEKERYEKVIKACALKKDLQLLEDgdltvigdrgtTLSGGQKARVNLARAVYQDADI 372
Cdd:cd03294 113 LLPHrTVLENVAFGlevqgvpRAEREERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDI 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217293410 373 YLLDDPLSAVD----AEVSRHLFELcicQILHEKITILVTHQL-QYLKAASQILILKDGKMVQKGTYTEFL 438
Cdd:cd03294 182 LLMDEAFSALDplirREMQDELLRL---QAELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
245-440 |
5.13e-23 |
|
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: 99.28 E-value: 5.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG----------------RIAYVSQQPWVFSG-TLR 307
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqditglsekelyelrrRIGMLFQGGALFDSlTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 308 SNILF-----GKKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRGTT-LSGGQKARVNLARAVYQDADIYLLDDPLSA 381
Cdd:COG1127 101 ENVAFplrehTDLSEAEIRELV---------LEKLELVGLPGAADKMPSeLSGGMRKRVALARALALDPEILLYDEPTAG 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217293410 382 VDAEVSRHLFELcICQILHE-KIT-ILVTHQLQYLKA-ASQILILKDGKMVQKGTYTEFLKS 440
Cdd:COG1127 172 LDPITSAVIDEL-IRELRDElGLTsVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLAS 232
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
226-432 |
8.79e-23 |
|
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: 98.35 E-value: 8.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 226 MVHVQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------- 290
Cdd:cd03257 1 LLEVKNLSvSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 291 --RIAYVSQQP-----------WVFSGTLRSNilfGKKYEKERYEKVIkacalkkdLQLLEDGDL--TVIGDRGTTLSGG 355
Cdd:cd03257 81 rkEIQMVFQDPmsslnprmtigEQIAEPLRIH---GKLSKKEARKEAV--------LLLLVGVGLpeEVLNRYPHELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 356 QKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFEL--CICQILheKITIL-VTHQLQYLKA-ASQILILKDGKMVQK 431
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLlkKLQEEL--GLTLLfITHDLGVVAKiADRVAVMYAGKIVEE 227
|
.
gi 2217293410 432 G 432
Cdd:cd03257 228 G 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
249-438 |
8.97e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 98.29 E-value: 8.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 249 SFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYVSQQPWVFSG-TLRSNILFGK-- 314
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltalppaerpVSMLFQENNLFPHlTVAQNIGLGLrp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 315 --KYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLF 391
Cdd:COG3840 99 glKLTAEQRAQVEQA---------LERVGLAGLLDRlPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEML 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2217293410 392 ELcICQILHE-KITIL-VTHQLQ-YLKAASQILILKDGKMVQKGTYTEFL 438
Cdd:COG3840 170 DL-VDELCRErGLTVLmVTHDPEdAARIADRVLLVADGRIAADGPTAALL 218
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
858-1068 |
1.40e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 99.35 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYSPGGPL---VLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTE--IGLHDLR 931
Cdd:PRK13637 3 IKIENLTHIYMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPtSGKIIIDGVDITDkkVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 932 KKMSIIPQEP--VLFTGTMRKNLD--PFNEH-TDEELWNalqevQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLAR 1006
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAfgPINLGlSEEEIEN-----RVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217293410 1007 AILRKNQILIIDEATANVDPRTDELIQKKIRE--KFAHCTVLTIAHRLNTIID-SDKIMVLDSGR 1068
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKElhKEYNMTIILVSHSMEDVAKlADRIIVMNKGK 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
245-427 |
2.14e-22 |
|
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: 95.33 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG---------------RIAYVSQQPWVFSG-TLRS 308
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelpplrrRIGMVFQDFALFPHlTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 309 NILFGkkyekeryekvikacalkkdlqlledgdltvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 388
Cdd:cd03229 96 NIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2217293410 389 HLFELciCQILHEK--IT-ILVTHQLQYL-KAASQILILKDGK 427
Cdd:cd03229 138 EVRAL--LKSLQAQlgITvVLVTHDLDEAaRLADRVVVLRDGK 178
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
248-432 |
5.71e-22 |
|
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: 95.44 E-value: 5.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 248 LSFTVrPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------------RIAYVSQQPWVFSG-TLRSN 309
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrkkinlppqqrKIGLVFQQYALFPHlNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 310 ILFGKKYeKERYEKVIKACALkkdLQLLedgDLTVIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 388
Cdd:cd03297 96 LAFGLKR-KRNREDRISVDEL---LDLL---GLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2217293410 389 hlfelcICQILHEKI-------TILVTH---QLQYLkaASQILILKDGKMVQKG 432
Cdd:cd03297 169 ------QLLPELKQIkknlnipVIFVTHdlsEAEYL--ADRIVVMEDGRLQYIG 214
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
9-438 |
1.21e-21 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 100.95 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 9 GQIVNLLSND--VNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGM---AVLIILLPLQSCFGKLFSSLRSKTA 83
Cdd:PRK10790 122 GQLISRVTNDteVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMifpAVLVVMVIYQRYSTPIVRRVRAYLA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 84 TFTDArirtMNEVITGIRIIKMYAWEKSFSnlitnlrkKEISKILRSSCLRGMN-----------LASFFSAskiivfvt 152
Cdd:PRK10790 202 DINDG----FNEVINGMSVIQQFRQQARFG--------ERMGEASRSHYMARMQtlrldgfllrpLLSLFSA-------- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 153 fttYVLLGSVITASrvFVAVtlyGAVRLTVTLFFPSAIERVSE--------------AIVSIRRIqtFLLLDEISQR--- 215
Cdd:PRK10790 262 ---LILCGLLMLFG--FSAS---GTIEVGVLYAFISYLGRLNEplielttqqsmlqqAVVAGERV--FELMDGPRQQygn 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 216 -NRQLPSdGKkmVHVQDFTAFWDKasETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--- 291
Cdd:PRK10790 332 dDRPLQS-GR--IDIDNVSFAYRD--DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRpls 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 292 ----------IAYVSQQPWVFSGTLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVN 361
Cdd:PRK10790 407 slshsvlrqgVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLA 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 362 LARAVYQDADIYLLDDPLSAVDA----EVSRHLfelcicQILHEKITILV-THQLQYLKAASQILILKDGKMVQKGTYTE 436
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSgteqAIQQAL------AAVREHTTLVViAHRLSTIVEADTILVLHRGQAVEQGTHQQ 560
|
..
gi 2217293410 437 FL 438
Cdd:PRK10790 561 LL 562
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
245-433 |
1.22e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 95.57 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRiAYVSQQPWV---------------FSGTLRSN 309
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGR-PLAAWSPWElarrravlpqhsslaFPFTVEEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 310 ILFGK---KYEKERYEKVIKACalkkdlqlLEDGDLTVIGDRG-TTLSGGQKARVNLARA---VYQDAD----IYLLDDP 378
Cdd:COG4559 96 VALGRaphGSSAAQDRQIVREA--------LALVGLAHLAGRSyQTLSGGEQQRVQLARVlaqLWEPVDggprWLFLDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217293410 379 LSAVDAevsRHlfELCICQIL----HEKITIL-VTHQL----QYlkaASQILILKDGKMVQKGT 433
Cdd:COG4559 168 TSALDL---AH--QHAVLRLArqlaRRGGGVVaVLHDLnlaaQY---ADRILLLHQGRLVAQGT 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
858-1085 |
1.45e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 96.44 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYSPGGPLVLKHLTAL---IKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWI-DKILTTEIG---LHD 929
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGLDNIsfeLEEGSFVALVGHTGSGKSTLMQHFNALLKPsSGTITIaGYHITPETGnknLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 930 LRKKMSIIPQ--EPVLFTGTMRKNLD--PFN-EHTDEELWNA----LQEVQLKetiEDLPGKMDTELaesgsnfSVGQRQ 1000
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEfgPKNfGFSEDEAKEKalkwLKKVGLS---EDLISKSPFEL-------SGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1001 LVCLARAILRKNQILIIDEATANVDPRT-DELIQKKIREKFAHCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVL 1078
Cdd:PRK13641 153 RVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEI 232
|
....*..
gi 2217293410 1079 LQNKESL 1085
Cdd:PRK13641 233 FSDKEWL 239
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
858-1077 |
1.53e-21 |
|
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: 94.88 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYspGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKI---LTTEIGLHDLRKK 933
Cdd:cd03261 1 IELRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDsGEVLIDGEdisGLSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 934 MSIIPQEPVLFTG-TMRKNLD-PFNEHT--DEELWNA-----LQEVQLKETIEDLPGkmdtELaeSGsnfsvGQRQLVCL 1004
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAfPLREHTrlSEEEIREivlekLEAVGLRGAEDLYPA----EL--SG-----GMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1005 ARAILRKNQILIIDEATANVDP----RTDELIQkKIREKFaHCTVLTIAHRLNTIID-SDKIMVLDSGR---------LK 1070
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPiasgVIDDLIR-SLKKEL-GLTSIMVTHDLDTAFAiADRIAVLYDGKivaegtpeeLR 225
|
....*..
gi 2217293410 1071 EYDEPYV 1077
Cdd:cd03261 226 ASDDPLV 232
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
226-432 |
1.88e-21 |
|
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: 93.97 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 226 MVHVQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGriAYVSQQPW---- 300
Cdd:cd03266 1 MITADALTkRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAearr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 301 ---VFSG--------TLRSNIL-FGKKYEKERYEkvIKAcALKKDLQLLEDGDLtvIGDRGTTLSGGQKARVNLARAVYQ 368
Cdd:cd03266 79 rlgFVSDstglydrlTARENLEyFAGLYGLKGDE--LTA-RLEELADRLGMEEL--LDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 369 DADIYLLDDPLSAVDAEVSRHLFELcICQILHEKITILV-THQLQYLKA-ASQILILKDGKMVQKG 432
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREF-IRQLRALGKCILFsTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
854-1071 |
1.97e-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: 94.87 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 854 HEGVIIFDNVNFMYSPGgplvlkhltaliksqEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRK 932
Cdd:COG1124 15 GRRVPVLKDVSLEVAPG---------------ESFGLVGESGSGKSTLLRALAGLERPwSGEVTFDGRPVTRRRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 933 KMSIIPQEPvlfTGTM--RKNLD-----PFNEH----TDEELWNALQEVQLKETIED-LPGkmdtELaeSGsnfsvGQRQ 1000
Cdd:COG1124 80 RVQMVFQDP---YASLhpRHTVDrilaePLRIHglpdREERIAELLEQVGLPPSFLDrYPH----QL--SG-----GQRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 1001 LVCLARAILRKNQILIIDEATANVDPRT-DELIQ--KKIREKFaHCTVLTIAHRLNtIID--SDKIMVLDSGRLKE 1071
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALDVSVqAEILNllKDLREER-GLTYLFVSHDLA-VVAhlCDRVAVMQNGRIVE 219
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
243-441 |
2.06e-21 |
|
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: 100.28 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 243 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLV-------------SVHGRIAYVSQQPWVFSGTLRSN 309
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlidgqdirdvtqaSLRAAIGIVPQDTVLFNDTIAYN 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 310 ILFGK-KYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD----- 383
Cdd:COG5265 452 IAYGRpDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDsrter 531
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217293410 384 ------AEVSRHlfelcicqilheKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 441
Cdd:COG5265 532 aiqaalREVARG------------RTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQG 583
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
241-438 |
3.75e-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: 93.27 E-value: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWVFSG-T 305
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEGRRIFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 306 LRSNILFG-----KKYEKERYEKVikacalkkdLQL---LEDgdltVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDD 377
Cdd:cd03224 92 VEENLLLGayarrRAKRKARLERV---------YELfprLKE----RRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217293410 378 P---LSAVdaeVSRHLFElCICQILHEKITILVTHqlQYLKAASQI----LILKDGKMVQKGTYTEFL 438
Cdd:cd03224 159 PsegLAPK---IVEEIFE-AIRELRDEGVTILLVE--QNARFALEIadraYVLERGRVVLEGTAAELL 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
858-1069 |
4.29e-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: 91.69 E-value: 4.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYspGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGlHDLRKKMSI 936
Cdd:cd03230 1 IEVRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPdSGEIKVLGKDIKKEP-EEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 937 IPQEPVLFTG-TMRKNLDpfnehtdeelwnalqevqlketiedlpgkmdtelaesgsnFSVGQRQLVCLARAILRKNQIL 1015
Cdd:cd03230 78 LPEEPSLYENlTVRENLK----------------------------------------LSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 1016 IIDEATANVDPRTDELIQKKIRE-KFAHCTVLTIAHRLNTIID-SDKIMVLDSGRL 1069
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
858-1068 |
4.82e-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: 91.48 E-value: 4.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYspGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID--KILTTEIGLHDLRKKM 934
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPdSGSILIDgeDLTDLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 935 SIIPQEPVLFTG-TMRKNLdpfnehtdeelwnalqevqlketiedlpgkmdtELAESGsnfsvGQRQLVCLARAILRKNQ 1013
Cdd:cd03229 79 GMVFQDFALFPHlTVLENI---------------------------------ALGLSG-----GQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217293410 1014 ILIIDEATANVDPRTDELIQKKIREKFAH--CTVLTIAHRLNTIID-SDKIMVLDSGR 1068
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
857-1074 |
4.94e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 92.81 E-value: 4.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 857 VIIFDNVNFMYsPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEI---GLHDLRK 932
Cdd:COG2884 1 MIRFENVSKRY-PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPtSGQVLVNGQDLSRLkrrEIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 933 KMSIIPQ-----------EPVLF----TGTMRKNLdpfNEHTDEelwnALQEVQLKETIEDLPGkmdtELaeSGsnfsvG 997
Cdd:COG2884 80 RIGVVFQdfrllpdrtvyENVALplrvTGKSRKEI---RRRVRE----VLDLVGLSDKAKALPH----EL--SG-----G 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 998 QRQLVCLARAILRKNQILIIDEATANVDPRT-DELIQ--KKIREkfAHCTVLtIA-HRLNtIIDS--DKIMVLDSGRLKE 1071
Cdd:COG2884 142 EQQRVAIARALVNRPELLLADEPTGNLDPETsWEIMEllEEINR--RGTTVL-IAtHDLE-LVDRmpKRVLELEDGRLVR 217
|
...
gi 2217293410 1072 YDE 1074
Cdd:COG2884 218 DEA 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
857-1081 |
7.21e-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: 92.64 E-value: 7.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 857 VIIFDNVNFMYSPGGPLV--LKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID-KILTT--EIGLHDL 930
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPtSGSVLVDgTDLTLlsGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 931 RKKMSIIPQEPVLFTG-TMRKNLD-PFnehtdeELWN---ALQEVQLKETIE--DLPGKMDTelaeSGSNFSVGQRQLVC 1003
Cdd:cd03258 81 RRRIGMIFQHFNLLSSrTVFENVAlPL------EIAGvpkAEIEERVLELLElvGLEDKADA----YPAQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1004 LARAILRKNQILIIDEATANVDPRTDELI---QKKIREKFAhCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVLL 1079
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSIlalLRDINRELG-LTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
..
gi 2217293410 1080 QN 1081
Cdd:cd03258 230 AN 231
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
245-432 |
1.09e-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: 91.83 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAyvsqqpWV------FSGTL--RSNILFG--- 313
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS------SLlglgggFNPELtgRENIYLNgrl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 314 ----KKYEKERYEKVIKACALKKDLqlledgDLTVigdrgTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE---- 385
Cdd:cd03220 112 lglsRKEIDEKIDEIIEFSELGDFI------DLPV-----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfqek 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2217293410 386 VSRHLFELcicqILHEKITILVTHQLQYLKA-ASQILILKDGKMVQKG 432
Cdd:cd03220 181 CQRRLREL----LKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
242-433 |
1.27e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.77 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 242 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------RIAYVSQQPWVFSG-TLRSN 309
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvsrlhardrKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 310 ILFGKKYeKERYEKVIKACALKKDLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 388
Cdd:PRK10851 95 IAFGLTV-LPRRERPNAAAIKAKVTQLLEMVQLAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2217293410 389 HLFELciCQILHE--KIT-ILVTH-QLQYLKAASQILILKDGKMVQKGT 433
Cdd:PRK10851 174 ELRRW--LRQLHEelKFTsVFVTHdQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
245-427 |
1.34e-20 |
|
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: 91.44 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG---------------RIAYVSQQPWVFSG-TLRS 308
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkltddkkninelrqKVGMVFQQFNLFPHlTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 309 NILFGKKYEKeryeKVIKACALKKDLQLLED-GDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVS 387
Cdd:cd03262 96 NITLAPIKVK----GMSKAEAEERALELLEKvGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2217293410 388 RHLFELcICQILHEKIT-ILVTHQLQY-LKAASQILILKDGK 427
Cdd:cd03262 172 GEVLDV-MKDLAEEGMTmVVVTHEMGFaREVADRVIFMDDGR 212
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
245-438 |
2.01e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.14 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWV-FSGTLRSNI 310
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHSSLsFPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 311 LFGkkyekeRYekvIKACALKKDLQL----LEDGDLTVIGDRG-TTLSGGQKARVNLARAVYQDAD------IYLLDDPL 379
Cdd:PRK13548 98 AMG------RA---PHGLSRAEDDALvaaaLAQVDLAHLAGRDyPQLSGGEQQRVQLARVLAQLWEpdgpprWLLLDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 380 SAVD----AEVSRHLFELCICQILHekiTILVTHQL----QYlkaASQILILKDGKMVQKGTYTEFL 438
Cdd:PRK13548 169 SALDlahqHHVLRLARQLAHERGLA---VIVVLHDLnlaaRY---ADRIVLLHQGRLVADGTPAEVL 229
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
245-436 |
2.19e-20 |
|
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: 91.34 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWVFSG-TLRSN 309
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglppheiarlgIGRTFQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 310 ILFG--------------KKYEKERYEKVikacalkkdLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYL 374
Cdd:cd03219 96 VMVAaqartgsglllaraRREEREARERA---------EELLERVGLADLADRpAGELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217293410 375 LDDPLSAVDAEVSRHLFELcICQILHEKITILVT-HQLQYLKA-ASQILILKDGKMVQKGTYTE 436
Cdd:cd03219 167 LDEPAAGLNPEETEELAEL-IRELRERGITVLLVeHDMDVVMSlADRVTVLDQGRVIAEGTPDE 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
193-433 |
2.98e-20 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 95.74 E-value: 2.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 193 VSEAIVSIRRIQTFLLLDEISQRNRQLPSDGKKMVHVQDFTA--FWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSS 270
Cdd:COG1123 227 PEEILAAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKryPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKST 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 271 LLSAVLGELAPSHGLVSVHG----------------RIAYVSQQPwvFSG-----TLRSNI-----LFGKKYEKERYEKV 324
Cdd:COG1123 307 LARLLLGLLRPTSGSILFDGkdltklsrrslrelrrRVQMVFQDP--YSSlnprmTVGDIIaeplrLHGLLSRAERRERV 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 325 ikacalkkdLQLLEDGDL--TVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcicqiLHE- 401
Cdd:COG1123 385 ---------AELLERVGLppDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNL-----LRDl 450
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2217293410 402 ----KITIL-VTHQL---QYLkaASQILILKDGKMVQKGT 433
Cdd:COG1123 451 qrelGLTYLfISHDLavvRYI--ADRVAVMYDGRIVEDGP 488
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
861-1075 |
3.74e-20 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 91.26 E-value: 3.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 861 DNVNFMYspGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQ 939
Cdd:COG1120 5 ENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPsSGEVLLDGRDLASLSRRELARRIAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 940 EPVL---FT-------GTM--RKNLDPFNEHTDEELWNALQEVQlketIEDLPGKMDTELaeSGsnfsvGQRQLVCLARA 1007
Cdd:COG1120 83 EPPApfgLTvrelvalGRYphLGLFGRPSAEDREAVEEALERTG----LEHLADRPVDEL--SG-----GERQRVLIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 1008 ILRKNQILIIDEATANVDPR----TDELIQKKIREKfaHCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEP 1075
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAhqleVLELLRRLARER--GRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPP 222
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-430 |
4.95e-20 |
|
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: 96.90 E-value: 4.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 2 AMGKTTTGQIVNLLSNDVNKFDQ---VTVF-LHFLWAGPLQAIAVTALLWMEIgisCLAGMAVLIILLPLQSCFGKLFSS 77
Cdd:TIGR01271 975 VLNTMKAGRILNRFTKDMAIIDDmlpLTLFdFIQLTLIVLGAIFVVSVLQPYI---FIAAIPVAVIFIMLRAYFLRTSQQ 1051
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 78 LRSKTAtftDARIRTMNEVITGIR---IIKMYAWEKSFSNLITN-LRKKEISKILRSSCLRgmnlasFFSASKIIVFVTF 153
Cdd:TIGR01271 1052 LKQLES---EARSPIFSHLITSLKglwTIRAFGRQSYFETLFHKaLNLHTANWFLYLSTLR------WFQMRIDIIFVFF 1122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 154 TTYVLLGSVIT----ASRVFVAVTLYGAVRLTVTLFFPSAIErVSEAIVSIRRIQTFL---------------------L 208
Cdd:TIGR01271 1123 FIAVTFIAIGTnqdgEGEVGIILTLAMNILSTLQWAVNSSID-VDGLMRSVSRVFKFIdlpqeeprpsggggkyqlstvL 1201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 209 LDEISQRNRQLPSDGKKMVhvQDFTAFWDKASETpTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLgELAPSHGLVSV 288
Cdd:TIGR01271 1202 VIENPHAQKCWPSGGQMDV--QGLTAKYTEAGRA-VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQI 1277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 289 HG-----------RIAY--VSQQPWVFSGTLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGG 355
Cdd:TIGR01271 1278 DGvswnsvtlqtwRKAFgvIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNG 1357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217293410 356 QKARVNLARAVYQDADIYLLDDPLSAVDAeVSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQ 430
Cdd:TIGR01271 1358 HKQLMCLARSILSKAKILLLDEPSAHLDP-VTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQ 1431
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
226-384 |
5.03e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 91.08 E-value: 5.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 226 MVHVQDFTAFWD-KASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRI--------AYVS 296
Cdd:COG4525 3 MLTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 297 QQ----PWVfsgTLRSNILFGKKY----EKERYEKvikACALkkdLQL--LEDgdltVIGDRGTTLSGGQKARVNLARAV 366
Cdd:COG4525 83 QKdallPWL---NVLDNVAFGLRLrgvpKAERRAR---AEEL---LALvgLAD----FARRRIWQLSGGMRQRVGIARAL 149
|
170
....*....|....*...
gi 2217293410 367 YQDADIYLLDDPLSAVDA 384
Cdd:COG4525 150 AADPRFLLMDEPFGALDA 167
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
238-439 |
8.53e-20 |
|
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: 89.49 E-value: 8.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 238 KASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQQPWVFSG- 304
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYCPQFDALFDEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 305 TLRSNILF-------GKKYEKERYEKVIKACALKKdlqlledgdltVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDD 377
Cdd:cd03263 91 TVREHLRFyarlkglPKSEIKEEVELLLRVLGLTD-----------KANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 378 PLSAVDAEVSRHLFELcICQILHEKITILVTHQLQYLKA-ASQILILKDGKMVQKGTYTEfLK 439
Cdd:cd03263 160 PTSGLDPASRRAIWDL-ILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQE-LK 220
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
220-433 |
9.25e-20 |
|
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: 89.01 E-value: 9.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 220 PSDGKkmVHVQDFTAFWdkASETP-TLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------- 290
Cdd:cd03369 2 PEHGE--IEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 291 -----RIAYVSQQPWVFSGTLRSNI-LFGKKYEKERYEkvikacALKkdlqlledgdltvIGDRGTTLSGGQKARVNLAR 364
Cdd:cd03369 78 edlrsSLTIIPQDPTLFSGTIRSNLdPFDEYSDEEIYG------ALR-------------VSEGGLNLSQGQRQLLCLAR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 365 AVYQDADIYLLDDPLSAVDAEvSRHLfelcICQILHE---KITIL-VTHQLQYLKAASQILILKDGKMVQKGT 433
Cdd:cd03369 139 ALLKRPRVLVLDEATASIDYA-TDAL----IQKTIREeftNSTILtIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
860-1065 |
9.59e-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: 89.13 E-value: 9.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 860 FDNVNFMYspGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKIltteiGLHDLRKKMSIIP 938
Cdd:cd03235 2 VEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPtSGSIRVFGK-----PLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 939 Q-------------EPVLFTGTMRKNLDPFNEHTD-EELWNALQEVQLKETIEDLPGKMdtelaeSGsnfsvGQRQLVCL 1004
Cdd:cd03235 75 QrrsidrdfpisvrDVVLMGLYGHKGLFRRLSKADkAKVDEALERVGLSELADRQIGEL------SG-----GQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 1005 ARAILRKNQILIIDEATANVDPRTDELIQKKIRE-KFAHCTVLTIAHRLNTIIDS-DKIMVLD 1065
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYfDRVLLLN 206
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
241-441 |
1.32e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.60 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWV-FSGTL 306
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASVPQDTSLsFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 307 RSNILFGKKYEKERYEKVIKACALKKDlQLLEDGDLTVIGDRG-TTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDae 385
Cdd:PRK09536 95 RQVVEMGRTPHRSRFDTWTETDRAAVE-RAMERTGVAQFADRPvTSLSGGERQRVLLARALAQATPVLLLDEPTASLD-- 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 386 VSRHLFELCICQILHE--KITILVTHQLQyLKA--ASQILILKDGKMVQKGTYTEFLKSG 441
Cdd:PRK09536 172 INHQVRTLELVRRLVDdgKTAVAAIHDLD-LAAryCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
245-440 |
1.82e-19 |
|
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: 88.75 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLV----------SVHGR----IAYVSQQPWVFSG-TLRSN 309
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqditklPMHKRarlgIGYLPQEASIFRKlTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 310 IL----FGKKYEKERYEKVIkacalkkdlQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD- 383
Cdd:cd03218 96 ILavleIRGLSKKEREEKLE---------ELLEEFHITHLRKSkASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDp 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 384 ---AEVSRhlfelcICQILHEK-ITILVT-HQL-QYLKAASQILILKDGKMVQKGTYTEFLKS 440
Cdd:cd03218 167 iavQDIQK------IIKILKDRgIGVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
854-1094 |
2.42e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 89.43 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 854 HEGVIIFDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRK 932
Cdd:PRK13648 4 KNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVkSGEIFYNNQAITDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 933 KMSIIPQEPV-LFTGTMRK---------NLDPFNEhTDEELWNALQEVQLKETIEDLPgkmdtelaesgSNFSVGQRQLV 1002
Cdd:PRK13648 84 HIGIVFQNPDnQFVGSIVKydvafglenHAVPYDE-MHRRVSEALKQVDMLERADYEP-----------NALSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1003 CLARAILRKNQILIIDEATANVDPRTDE----LIQKKIREKfaHCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVL 1078
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQnlldLVRKVKSEH--NITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
250 260
....*....|....*....|....*
gi 2217293410 1079 LQNKESLF---------YKMVQQLG 1094
Cdd:PRK13648 230 FDHAEELTrigldlpfpIKINQMLG 254
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
159-410 |
2.43e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 93.33 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 159 LGSVITASRVFVAVTlyGAVRltvtlFFPSAIERVSEAIVSIRRIQTFL----LLDEISQRNRQLPSDGKKMVHVQDFTA 234
Cdd:COG4178 298 LGGLMQAASAFGQVQ--GALS-----WFVDNYQSLAEWRATVDRLAGFEealeAADALPEAASRIETSEDGALALEDLTL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 235 FwdKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGeLAPS-HGLVSV--HGRIAYVSQQPWVFSGTLRSNIL 311
Cdd:COG4178 371 R--TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYgSGRIARpaGARVLFLPQRPYLPLGTLREALL 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 312 F---GKKYEKERYEKVIKACALKKDLQLLEDGDltvigDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 388
Cdd:COG4178 448 YpatAEAFSDAELREALEAVGLGHLAERLDEEA-----DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEA 522
|
250 260
....*....|....*....|..
gi 2217293410 389 HLFELcICQILHEKITILVTHQ 410
Cdd:COG4178 523 ALYQL-LREELPGTTVISVGHR 543
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
826-1081 |
2.70e-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: 92.66 E-value: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 826 SVERVIEYTDLEKEAPWEYQKRPPPAWPHEG---VIIFDNVNFMY---SPGGPLVLKHLTALIKSQEKVGIVGRTGAGKS 899
Cdd:COG1123 226 PPEEILAAPQALAAVPRLGAARGRAAPAAAAaepLLEVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKS 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 900 SLISALFRLSEP-EGKIWIDKILTTEIG---LHDLRKKMSIIPQ-----------------EPVLFTGTMRKnldpfnEH 958
Cdd:COG1123 306 TLARLLLGLLRPtSGSILFDGKDLTKLSrrsLRELRRRVQMVFQdpysslnprmtvgdiiaEPLRLHGLLSR------AE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 959 TDEELWNALQEVQLKETIED-LPGkmdtELaeSGsnfsvGQRQLVCLARAILRKNQILIIDEATANVDPRTD----ELIq 1033
Cdd:COG1123 380 RRERVAELLERVGLPPDLADrYPH----EL--SG-----GQRQRVAIARALALEPKLLILDEPTSALDVSVQaqilNLL- 447
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2217293410 1034 KKIREKFaHCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVLLQN 1081
Cdd:COG1123 448 RDLQREL-GLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
857-1069 |
3.05e-19 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 88.22 E-value: 3.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 857 VIIFDNVNFMYspGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIwidKILTTEIGLHdlRKKMS 935
Cdd:COG1121 6 AIELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPtSGTV---RLFGKPPRRA--RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 936 IIPQEP------------VLFTGTMRKN--LDPFNEHTDEELWNALQEVQLketiEDLPGKMDTELaeSGsnfsvGQRQL 1001
Cdd:COG1121 79 YVPQRAevdwdfpitvrdVVLMGRYGRRglFRRPSRADREAVDEALERVGL----EDLADRPIGEL--SG-----GQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1002 VCLARAILRKNQILIIDEATANVDPRTDELIQKKIRE-KFAHCTVLTIAHRLNTIID-SDKIMVLDSGRL 1069
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
245-433 |
3.93e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 88.21 E-value: 3.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAyvsqqpWVF---SG-----TLRSNILFG--- 313
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVS------ALLelgAGfhpelTGRENIYLNgrl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 314 ----KKYEKERYEKVIkacalkkdlqlledgDLTVIGD------RgtTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 383
Cdd:COG1134 116 lglsRKEIDEKFDEIV---------------EFAELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVGD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2217293410 384 AE----VSRHLFELcicqILHEKITILVTHQLQYLKA-ASQILILKDGKMVQKGT 433
Cdd:COG1134 179 AAfqkkCLARIREL----RESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
226-464 |
5.17e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.15 E-value: 5.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 226 MVHVQDFTAFWDKaseTPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RI 292
Cdd:PRK11231 2 TLRTENLTVGYGT---KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 293 AYVSQQPWVFSG-TLRS---------NILFGKKYEKERyEKVIKAcalkkdlqlLEDGDLTVIGDRG-TTLSGGQKARVN 361
Cdd:PRK11231 79 ALLPQHHLTPEGiTVRElvaygrspwLSLWGRLSAEDN-ARVNQA---------MEQTRINHLADRRlTDLSGGQRQRAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 362 LARAVYQDADIYLLDDPLSAVDAEvsrHLFELC-ICQILHE--KITILVTHQL-QYLKAASQILILKDGKMVQKGTYTEF 437
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDIN---HQVELMrLMRELNTqgKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEV 225
|
250 260 270
....*....|....*....|....*....|
gi 2217293410 438 LKSGidfgsLLKKD---NEESEQPPVPGTP 464
Cdd:PRK11231 226 MTPG-----LLRTVfdvEAEIHPEPVSGTP 250
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
245-433 |
7.66e-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: 7.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRI-----AYVSQQPWVFSG-------TLRSNILF 312
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnlpPHKRPVNTVFQNyalfphlTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 313 G----KKYEKERYEKVIKACALkkdLQLLEDGDltvigDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 388
Cdd:cd03300 96 GlrlkKLPKAEIKERVAEALDL---VQLEGYAN-----RKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2217293410 389 HL-FELcicQILHEK--IT-ILVTH-QLQYLKAASQILILKDGKMVQKGT 433
Cdd:cd03300 168 DMqLEL---KRLQKElgITfVFVTHdQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
242-429 |
1.02e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 86.26 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 242 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG----------------RIAYVSQQPWVFSGt 305
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlkrreipylrrRIGVVFQDFRLLPD- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 306 lRS---NILF-----GKKyEKERYEKVIKacALKKdLQLLEDGDLTVIgdrgtTLSGGQKARVNLARAVYQDADIYLLDD 377
Cdd:COG2884 94 -RTvyeNVALplrvtGKS-RKEIRRRVRE--VLDL-VGLSDKAKALPH-----ELSGGEQQRVAIARALVNRPELLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2217293410 378 PLSAVDAEVSRHLFELcICQILHEKITILV-THQLQYL-KAASQILILKDGKMV 429
Cdd:COG2884 164 PTGNLDPETSWEIMEL-LEEINRRGTTVLIaTHDLELVdRMPKRVLELEDGRLV 216
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
248-432 |
1.18e-18 |
|
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: 85.62 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 248 LSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYVSQQPWVFSG-TLRSNILFGK- 314
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdvtaappadrpVSMLFQENNLFAHlTVEQNVGLGLs 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 315 ---KYEKERYEKVIKACAlKKDLQLLEDgdltvigDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLF 391
Cdd:cd03298 97 pglKLTAEDRQAIEVALA-RVGLAGLEK-------RLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2217293410 392 ELC--ICQilHEKITIL-VTHQLQYLKAASQILI-LKDGKMVQKG 432
Cdd:cd03298 169 DLVldLHA--ETKMTVLmVTHQPEDAKRLAQRVVfLDNGRIAAQG 211
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
245-440 |
1.21e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.89 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--RIAYVSQQPWVFSG-TLRSNILFG-------- 313
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDDDlTVLDTVLDGdaelrale 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 314 KKYEK------------ERYEKVI-------------KACALKKDLQL-LEDGDLTVigdrgTTLSGGQKARVNLARAVY 367
Cdd:COG0488 94 AELEEleaklaepdedlERLAELQeefealggweaeaRAEEILSGLGFpEEDLDRPV-----SELSGGWRRRVALARALL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 368 QDADIYLLDDP---LsavDAEvSRHLFElcicQILHE-KIT-ILVTHQLQYL-KAASQILILKDGKMVQ-KGTYTEFLKS 440
Cdd:COG0488 169 SEPDLLLLDEPtnhL---DLE-SIEWLE----EFLKNyPGTvLVVSHDRYFLdRVATRILELDRGKLTLyPGNYSAYLEQ 240
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
245-432 |
1.39e-18 |
|
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: 85.71 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGeLLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQQPwvfsgTLRSNIlf 312
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQEF-----GVYPNF-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 313 gKKYEKERYEKVIKACALKKD----LQLLEDGDLT-VIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEvS 387
Cdd:cd03264 88 -TVREFLDYIAWLKGIPSKEVkarvDEVLELVNLGdRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE-E 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2217293410 388 RHLFELCICQILHEKITILVTHQLQYLKA-ASQILILKDGKMVQKG 432
Cdd:cd03264 166 RIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
858-1081 |
2.02e-18 |
|
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: 85.82 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYsPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSI 936
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPtSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 937 IPQEPVLFTG-TMRKN--LDPFNEHTDEElwnalqevQLKETIEDLPGKMDTELAESG----SNFSVGQRQLVCLARAIL 1009
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPKLLKWPKE--------KIRERADELLALVGLDPAEFAdrypHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217293410 1010 RKNQILIIDEATANVDPRTDELIQKKIR--EKFAHCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVLLQN 1081
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKrlQQELGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
855-1075 |
2.28e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 86.61 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 855 EGVIIFDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKK 933
Cdd:PRK13635 3 EEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEaGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 934 MSIIPQEP-VLFTGTMRKNLDPFN------EHTD--EELWNALQEVQLKETIEDLPgkmdtelaesgSNFSVGQRQLVCL 1004
Cdd:PRK13635 83 VGMVFQNPdNQFVGATVQDDVAFGlenigvPREEmvERVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 1005 ARAILRKNQILIIDEATANVDPRTDELIQKKIRE--KFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEP 1075
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTP 224
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
243-412 |
2.50e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.91 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 243 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRI--------AYVSQQ----PWVfsgTLRSNI 310
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPvegpgaerGVVFQNegllPWR---NVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 311 LFGKkyekeRYEKVIKACALKKDLQLLEDGDLTVIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRH 389
Cdd:PRK11248 92 AFGL-----QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|....*
gi 2217293410 390 LFELcICQILHE--KITILVTHQLQ 412
Cdd:PRK11248 167 MQTL-LLKLWQEtgKQVLLITHDIE 190
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
249-438 |
3.20e-18 |
|
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: 87.85 E-value: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 249 SFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------------RIAYVSQQPWVFSG-TLRSNI 310
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargiflpphrrRIGYVFQEARLFPHlSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 311 LFGKKYE-----KERYEKVIkacalkkdlQLLEDGDLTvigDRG-TTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 384
Cdd:COG4148 99 LYGRKRApraerRISFDEVV---------ELLGIGHLL---DRRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 385 EvSRHlfelcicQIL------HEKITI---LVTHQL---QYLkaASQILILKDGKMVQKGTYTEFL 438
Cdd:COG4148 167 A-RKA-------EILpylerlRDELDIpilYVSHSLdevARL--ADHVVLLEQGRVVASGPLAEVL 222
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
222-441 |
3.42e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 86.22 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 222 DGKKMVHVQDFTaFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG----------- 290
Cdd:PRK13635 1 MKEEIIRVEHIS-FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseetvwdv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 291 --RIAYVSQQP-WVFSG-TLRSNILFGKKYE----KERYEKVIKACALKKDLQLLEdgdltvigDRGTTLSGGQKARVNL 362
Cdd:PRK13635 80 rrQVGMVFQNPdNQFVGaTVQDDVAFGLENIgvprEEMVERVDQALRQVGMEDFLN--------REPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 363 ARAVYQDADIYLLDDPLSAVD----AEVsrhlfeLCICQILHEK--ITIL-VTHQLQYLKAASQILILKDGKMVQKGTYT 435
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDprgrREV------LETVRQLKEQkgITVLsITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
....*.
gi 2217293410 436 EFLKSG 441
Cdd:PRK13635 226 EIFKSG 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
245-429 |
3.92e-18 |
|
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: 82.86 E-value: 3.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQqpwvfsgtlrsni 310
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevsfasprdarragIAMVYQ------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 311 lfgkkyekeryekvikacalkkdlqlledgdltvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHL 390
Cdd:cd03216 83 -----------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2217293410 391 FELcICQILHEKITIL-VTHQLQYLKA-ASQILILKDGKMV 429
Cdd:cd03216 122 FKV-IRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
857-1081 |
3.98e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.81 E-value: 3.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 857 VIIFDNVNFMYSPGGPlVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIG-LHDLRKKM 934
Cdd:PRK13644 1 MIRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQkGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 935 SIIPQEP-VLFTGTMrknldpfnehTDEELWNALQEVQLKETieDLPGKMDTELAESG---------SNFSVGQRQLVCL 1004
Cdd:PRK13644 80 GIVFQNPeTQFVGRT----------VEEDLAFGPENLCLPPI--EIRKRVDRALAEIGlekyrhrspKTLSGGQGQCVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1005 ARAILRKNQILIIDEATANVDPRTDELIQ---KKIREKFAhcTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQN 1081
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLeriKKLHEKGK--TIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
529-830 |
4.29e-18 |
|
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: 86.07 E-value: 4.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 529 IVFIFLILLNTAAQVAYvlqdwwlsYWANKQSMLNVTVNGGGNVtekldLNWYLGIYSGLTVATVLFGIARSLLVFYVLV 608
Cdd:cd07346 2 LLALLLLLLATALGLAL--------PLLTKLLIDDVIPAGDLSL-----LLWIALLLLLLALLRALLSYLRRYLAARLGQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 609 NSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQTLLQvVGVVSVAVAVIPW----IAIP 684
Cdd:cd07346 69 RVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLT-LIGALVILFYLNWkltlVALL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 685 LVPL-GIIFIFLRRYFLETSRDVKRLESTtrspVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSR 763
Cdd:cd07346 148 LLPLyVLILRYFRRRIRKASREVRESLAE----LSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSA 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 764 WFAVRLDAICAMFVIIVAF--GSLILAKTLDAGQVGLALSYaltlMGMFQWCVRQSAEVENM----MISVERV 830
Cdd:cd07346 224 LFSPLIGLLTALGTALVLLygGYLVLQGSLTIGELVAFLAY----LGMLFGPIQRLANLYNQlqqaLASLERI 292
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
865-1067 |
5.69e-18 |
|
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: 83.92 E-value: 5.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 865 FMYSPGGPlVLKHLTALIKSQEKVGIVGRTGAGKSSLISALF-RLSEPEGKIWIDKILTTEIGLHDLRKK----MSIIPQ 939
Cdd:cd03290 8 FSWGSGLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILgEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 940 EPVLFTGTMRKNL---DPFNEHTDEELWNAlqeVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQILI 1016
Cdd:cd03290 87 KPWLLNATVEENItfgSPFNKQRYKAVTDA---CSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2217293410 1017 IDEATANVDPR-TDELIQKKIREKFA--HCTVLTIAHRLNTIIDSDKIMVLDSG 1067
Cdd:cd03290 164 LDDPFSALDIHlSDHLMQEGILKFLQddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
858-1069 |
7.11e-18 |
|
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: 83.69 E-value: 7.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYSPGGP--LVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDL---- 930
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPtSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 931 RKKMSIIPQE---------------PVLFTGTmrknldpFNEHTDEELWNALQEVQLKETIEDLPGKMdtelaesgsnfS 995
Cdd:cd03255 81 RRHIGFVFQSfnllpdltalenvelPLLLAGV-------PKKERRERAEELLERVGLGDRLNHYPSEL-----------S 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 996 VGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIRE--KFAHCTVLTIAHRLNTIIDSDKIMVLDSGRL 1069
Cdd:cd03255 143 GGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
249-448 |
8.04e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 83.86 E-value: 8.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 249 SFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG---RIAYVSQQPW--------VFSG-TLRSNILFG--- 313
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhTTTPPSRRPVsmlfqennLFSHlTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 314 ----KKYEKERYEKVIKACALKKDLQLLEdgdltvigdrgTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRH 389
Cdd:PRK10771 99 glklNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217293410 390 LFELcICQILHEK-ITIL-VTHQLQ-YLKAASQILILKDGKMVQKGTYTEFLKSGIDFGSLL 448
Cdd:PRK10771 168 MLTL-VSQVCQERqLTLLmVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGKASASALL 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
857-1094 |
8.62e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 84.78 E-value: 8.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 857 VIIFDNVNFMYSPGGP-LVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKM 934
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAEsGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 935 SIIPQEP-VLFTGTMRKNLDPFNehtdeeLWNalQEVQLKETIE------DLPGKMDTELAESgSNFSVGQRQLVCLARA 1007
Cdd:PRK13650 84 GMVFQNPdNQFVGATVEDDVAFG------LEN--KGIPHEEMKErvnealELVGMQDFKEREP-ARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1008 ILRKNQILIIDEATANVDPRTD-ELIQ--KKIREKFaHCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNKES 1084
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRlELIKtiKGIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGND 233
|
250
....*....|
gi 2217293410 1085 LfykmvQQLG 1094
Cdd:PRK13650 234 L-----LQLG 238
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
241-440 |
9.78e-18 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 83.98 E-value: 9.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGL-VSVHG-------------RIAYVS---QQPWVFS 303
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGerrggedvwelrkRIGLVSpalQLRFPRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 304 GTLRSNIL---FG-----KKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRG-TTLSGGQKARVNLARAVYQDADIYL 374
Cdd:COG1119 95 ETVLDVVLsgfFDsiglyREPTDEQRERA---------RELLELLGLAHLADRPfGTLSQGEQRRVLIARALVKDPELLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 375 LDDPLSAVDAEvSRHLFELCICQILHEKIT--ILVTHQLQYLKAA-SQILILKDGKMVQKGTYTEFLKS 440
Cdd:COG1119 166 LDEPTAGLDLG-ARELLLALLDKLAAEGAPtlVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVLTS 233
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
227-427 |
1.44e-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: 80.57 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 227 VHVQDFTAFWDKaseTPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--RIAYVSQqpwvfsg 304
Cdd:cd03221 1 IELENLSKTYGG---KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGStvKIGYFEQ------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 305 tlrsnilfgkkyekeryekvikacalkkdlqlledgdltvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 384
Cdd:cd03221 71 -----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2217293410 385 EvSRHLFElcicQIL--HEKITILVTHQLQYLKA-ASQILILKDGK 427
Cdd:cd03221 104 E-SIEALE----EALkeYPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
207-439 |
2.56e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.66 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 207 LLLDEISQRNR----QLPSD---GKKMVHVQDFTAFWDkasETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGEL 279
Cdd:COG0488 289 LEREEPPRRDKtveiRFPPPerlGKKVLELEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGEL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 280 APSHGLVsVHG---RIAYVSQQPWVFSG--TLRSNIlfgKKYEKERYEKVIKacalkkdlQLLED----GD--LTVIGDr 348
Cdd:COG0488 366 EPDSGTV-KLGetvKIGYFDQHQEELDPdkTVLDEL---RDGAPGGTEQEVR--------GYLGRflfsGDdaFKPVGV- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 349 gttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEvSRHL-------FELCIcqilhekitILVTHQLQYLKA-ASQI 420
Cdd:COG0488 433 ---LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIE-TLEAleealddFPGTV---------LLVSHDRYFLDRvATRI 499
|
250 260
....*....|....*....|
gi 2217293410 421 LILKDGKMVQK-GTYTEFLK 439
Cdd:COG0488 500 LEFEDGGVREYpGGYDDYLE 519
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
858-1085 |
2.60e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.92 E-value: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYSPGGP---LVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWI-DKILTTEI---GLHD 929
Cdd:PRK13634 3 ITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPtSGTVTIgERVITAGKknkKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 930 LRKKMSIIPQ--EPVLFTGTMRKNL--DPFNEHTDEElwNALQEVqlKETIEdLPGKMDTELAESGSNFSVGQRQLVCLA 1005
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDIcfGPMNFGVSEE--DAKQKA--REMIE-LVGLPEELLARSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1006 RAILRKNQILIIDEATANVDPRTdeliQKKIREKFA--H----CTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVL 1078
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKG----RKEMMEMFYklHkekgLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
....*..
gi 2217293410 1079 LQNKESL 1085
Cdd:PRK13634 234 FADPDEL 240
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
245-439 |
3.24e-17 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 81.65 E-value: 3.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQQPWVFSG-TLRSNI- 310
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGWENLy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 311 LFGKKY------EKERYEKVIKAcalkkdLQLLEDGDLTVigdrgTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 384
Cdd:cd03265 96 IHARLYgvpgaeRRERIDELLDF------VGLLEAADRLV-----KTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 385 EVSRHLFELcICQILHEK-ITILVThqLQYLKAASQ----ILILKDGKMVQKGTYTEfLK 439
Cdd:cd03265 165 QTRAHVWEY-IEKLKEEFgMTILLT--THYMEEAEQlcdrVAIIDHGRIIAEGTPEE-LK 220
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
245-425 |
3.74e-17 |
|
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: 79.89 E-value: 3.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLsAVLGELAPSH-GLVSVHGR--IAYVSQQPWVFSGTLRSNILfgkkYEKERy 321
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLF-RALAGLWPWGsGRIGMPEGedLLFLPQRPYLPLGTLREQLI----YPWDD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 322 ekvikacalkkdlqlledgdltvigdrgtTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCicqiLHE 401
Cdd:cd03223 91 -----------------------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL----KEL 137
|
170 180
....*....|....*....|....*
gi 2217293410 402 KITIL-VTHQLQYLKAASQILILKD 425
Cdd:cd03223 138 GITVIsVGHRPSLWKFHDRVLDLDG 162
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
870-1069 |
5.60e-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: 81.03 E-value: 5.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 870 GGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHdlRKKMSIIPQEPVLFTG-T 947
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPdSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPHlT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 948 MRKNL--------DPFNEHTDEELWnALQEVQLKETIEDLPgkmdTELaeSGsnfsvGQRQLVCLARAILRKNQILIIDE 1019
Cdd:cd03259 89 VAENIafglklrgVPKAEIRARVRE-LLELVGLEGLLNRYP----HEL--SG-----GQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 1020 ATANVDPRTDELIQKKIRE--KFAHCTVLTIAHRLNTIID-SDKIMVLDSGRL 1069
Cdd:cd03259 157 PLSALDAKLREELREELKElqRELGITTIYVTHDQEEALAlADRIAVMNEGRI 209
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
245-432 |
5.63e-17 |
|
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: 80.72 E-value: 5.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------RIAYVSQQPWVFSG-TLRSNILF 312
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGksyqkniealrRIGALIEAPGFYPNlTARENLRL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 313 GKKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLF 391
Cdd:cd03268 96 LARLLGIRKKRI---------DEVLDVVGLKDSAKKKVkGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2217293410 392 ELcICQILHEKITILV-THQLQYL-KAASQILILKDGKMVQKG 432
Cdd:cd03268 167 EL-ILSLRDQGITVLIsSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
237-433 |
5.65e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.81 E-value: 5.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 237 DKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGeLAPSHGLVSVHGRI-------------AYVSQQpwvfs 303
Cdd:COG4138 4 NDVAVAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPlsdwsaaelarhrAYLSQQ----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 304 gTLRSNILFGKKY------EKERYEKVIKACAlkkdlQLLEDGDLTVIGDRG-TTLSGGQKARVNLARAVYQ-------D 369
Cdd:COG4138 78 -QSPPFAMPVFQYlalhqpAGASSEAVEQLLA-----QLAEALGLEDKLSRPlTQLSGGEWQRVRLAAVLLQvwptinpE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 370 ADIYLLDDPLSAVD----AEVSRHLFELCICQilhekITILV-THQLQY-LKAASQILILKDGKMVQKGT 433
Cdd:COG4138 152 GQLLLLDEPMNSLDvaqqAALDRLLRELCQQG-----ITVVMsSHDLNHtLRHADRVWLLKQGKLVASGE 216
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
853-1095 |
6.67e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 82.54 E-value: 6.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 853 PHEGVIIFDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSS---LISALFRLSE-PEGKIWIDKILTTEIGLH 928
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDnPNSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 929 DLRKKMSIIPQEP-VLFTGTMRKNLDPFNEHTDEELWNALQEVqLKETIEDLpGKMDTELAESgSNFSVGQRQLVCLARA 1007
Cdd:PRK13640 81 DIREKVGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKI-VRDVLADV-GMLDYIDSEP-ANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1008 ILRKNQILIIDEATANVDPRTDELIQKKIRE--KFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNKESL 1085
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKlkKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVEML 237
|
250
....*....|....*....
gi 2217293410 1086 ---------FYKMVQQLGK 1095
Cdd:PRK13640 238 keigldipfVYKLKNKLKE 256
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
858-1051 |
1.05e-16 |
|
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: 78.73 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMySPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALfrlsepeGKIWidKILTTEIGLHDlRKKMSII 937
Cdd:cd03223 1 IELENLSLA-TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-------AGLW--PWGSGRIGMPE-GEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 938 PQEPVLFTGTMRknldpfnehtdEEL---WnalqevqlketiedlpgkmDTELaesgsnfSVGQRQLVCLARAILRKNQI 1014
Cdd:cd03223 70 PQRPYLPLGTLR-----------EQLiypW-------------------DDVL-------SGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*..
gi 2217293410 1015 LIIDEATANVDPRTDELIQKKIREKFAhcTVLTIAHR 1051
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
227-432 |
1.10e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 81.71 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 227 VHVQDFTAFWDKAseTPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSQQPW------ 300
Cdd:PRK13647 5 IEVEDLHFRYKDG--TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrskvg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 301 ---------VFSGTLRSNILFG-------KKYEKERYEKVIKACALKKdlqlledgdltvIGDRGTT-LSGGQKARVNLA 363
Cdd:PRK13647 83 lvfqdpddqVFSSTVWDDVAFGpvnmgldKDEVERRVEEALKAVRMWD------------FRDKPPYhLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217293410 364 RAVYQDADIYLLDDPLSAVDAEVSRHLFElcICQILHE--KITILVTHQLQY-LKAASQILILKDGKMVQKG 432
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLME--ILDRLHNqgKTVIVATHDVDLaAEWADQVIVLKEGRVLAEG 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
858-1068 |
1.11e-16 |
|
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: 80.69 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYsPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIG---LHDLRKK 933
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPtSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 934 MSIIPQEP-----------VL-----FTGTMRKNLDPFNEHTDEELWNALQEVQLketiEDLPGKMDTELaeSGsnfsvG 997
Cdd:cd03256 80 IGMIFQQFnlierlsvlenVLsgrlgRRSTWRSLFGLFPKEEKQRALAALERVGL----LDKAYQRADQL--SG-----G 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217293410 998 QRQLVCLARAILRKNQILIIDEATANVDPRTDELIQ---KKIREKFAHCTVLTIaHRLNTIID-SDKIMVLDSGR 1068
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMdllKRINREEGITVIVSL-HQVDLAREyADRIVGLKDGR 222
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
248-437 |
1.83e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 80.06 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 248 LSFTVRPGELLAVVGPVGAGKSSLLSaVLGEL-APSHGLVSVHGRIAYVSQQPWVFSG-TLRSNIlfGKKYEK------- 318
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLeMPRSGTLNIAGNHFDFSKTPSDKAIrELRRNV--GMVFQQynlwphl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 319 -------ERYEKVI---KACALKKDLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVS 387
Cdd:PRK11124 98 tvqqnliEAPCRVLglsKDQALARAEKLLERLRLKPYADRfPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEIT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 388 RHlfelcICQILHE----KIT-ILVTHQLQYL-KAASQILILKDGKMVQKGTYTEF 437
Cdd:PRK11124 178 AQ-----IVSIIRElaetGITqVIVTHEVEVArKTASRVVYMENGHIVEQGDASCF 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
245-410 |
2.12e-16 |
|
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: 79.62 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGeLAPSHGLVS----VHG----------RIAYVSQ-----------QP 299
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISG-RVEGGGTTSgqilFNGqprkpdqfqkCVAYVRQddillpgltvrET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 300 WVFSGTLRSNILFGKKYEKERYEkvikacalkkDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPL 379
Cdd:cd03234 102 LTYTAILRLPRKSSDAIRKKRVE----------DVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190
....*....|....*....|....*....|..
gi 2217293410 380 SAVDAEVSRHLFELcICQILHEKITILVT-HQ 410
Cdd:cd03234 172 SGLDSFTALNLVST-LSQLARRNRIVILTiHQ 202
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
236-432 |
2.15e-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: 78.75 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 236 WDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHglvsvhgriayvsqqpwvFSGTLRSNilfGKK 315
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLG------------------VSGEVLIN---GRP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 316 YEKERYEKVIkaCALKKDLQLLedGDLTV-------IGDRGttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 388
Cdd:cd03213 75 LDKRSFRKII--GYVPQDDILH--PTLTVretlmfaAKLRG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2217293410 389 HLFELcICQILHEKITILVT-HQLQYL--KAASQILILKDGKMVQKG 432
Cdd:cd03213 149 QVMSL-LRRLADTGRTIICSiHQPSSEifELFDKLLLLSQGRVIYFG 194
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
870-1043 |
2.32e-16 |
|
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: 79.06 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 870 GGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGlHDLRKKMSIIPQEPVLFTG-T 947
Cdd:COG4133 13 GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPsAGEVLWNGEPIRDAR-EDYRRRLAYLGHADGLKPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 948 MRKNLDpF------NEHTDEELWNALQEVQLkETIEDLPGKMdtelaesgsnFSVGQRQLVCLARAILRKNQILIIDEAT 1021
Cdd:COG4133 92 VRENLR-FwaalygLRADREAIDEALEAVGL-AGLADLPVRQ----------LSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180
....*....|....*....|..
gi 2217293410 1022 ANVDPRTDELIQKKIRekfAHC 1043
Cdd:COG4133 160 TALDAAGVALLAELIA---AHL 178
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
229-473 |
2.51e-16 |
|
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: 80.67 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 229 VQDFTAFWDKASETpTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLgELAPSHGLVSVHG-----------RIAY--V 295
Cdd:cd03289 5 VKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwRKAFgvI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 296 SQQPWVFSGTLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLL 375
Cdd:cd03289 83 PQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 376 DDPLSAVDA-------EVSRHLFELCicqilhekITILVTHQLQYLKAASQILILKDGKMVQKGTY------TEFLKSGI 442
Cdd:cd03289 163 DEPSAHLDPityqvirKTLKQAFADC--------TVILSEHRIEAMLECQRFLVIEENKVRQYDSIqkllneKSHFKQAI 234
|
250 260 270
....*....|....*....|....*....|....*
gi 2217293410 443 DFGSLLK----KDNEESEQPPVPGTPTLRNRTFSE 473
Cdd:cd03289 235 SPSDRLKlfprRNSSKSKRKPRPQIQALQEETEEE 269
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
245-394 |
2.87e-16 |
|
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: 84.03 E-value: 2.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSaVLGELAPSHG---LVSVHGRIAYVSQQPWVFSGTLRSNILFGKKYEkERY 321
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDSSE-DMK 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 322 EKVIKACALKKDLQLL-------EDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELC 394
Cdd:TIGR00954 546 RRGLSDKDLEQILDNVqlthileREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC 625
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
858-1083 |
5.16e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 78.64 E-value: 5.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYspggPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISAL--FrLSEPEGKIWID--KILTTEIGlhdlRKK 933
Cdd:COG3840 2 LRLDDLTYRY----GDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIagF-LPPDSGRILWNgqDLTALPPA----ERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 934 MSIIPQEPVLFTG-TMRKN----LDP---FNEHTDEELWNALQEVQLKETIEDLPGKMdtelaeSGsnfsvGQRQLVCLA 1005
Cdd:COG3840 73 VSMLFQENNLFPHlTVAQNiglgLRPglkLTAEQRAQVEQALERVGLAGLLDRLPGQL------SG-----GQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1006 RAILRKNQILIIDEATANVDP--RTD--ELIQKKIREKFAhcTVLTIAHRLNTIID-SDKIMVLDSGRLkEYDEPYVLLQ 1080
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDPalRQEmlDLVDELCRERGL--TVLMVTHDPEDAARiADRVLLVADGRI-AADGPTAALL 218
|
...
gi 2217293410 1081 NKE 1083
Cdd:COG3840 219 DGE 221
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
238-423 |
6.49e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.22 E-value: 6.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 238 KASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSG 304
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGedistlkpeiyrqQVSYCAQTPTLFGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 305 TLRSNILFGKKYEKERYEKVikacALKKDLQLLEDgDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 384
Cdd:PRK10247 96 TVYDNLIFPWQIRNQQPDPA----IFLDDLERFAL-PDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2217293410 385 EVSRHLFELcICQILHEK-ITIL-VTHQLQYLKAASQILIL 423
Cdd:PRK10247 171 SNKHNVNEI-IHRYVREQnIAVLwVTHDKDEINHADKVITL 210
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
243-408 |
9.66e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 79.87 E-value: 9.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 243 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQqpwvFSG-----T 305
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpararlaraRIGVVPQ----FDNldlefT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 306 LRSNIL-FGKKY--EKERYEKVIKAcalkkdlqLLEDGDLTVIGD-RGTTLSGGQKARVNLARAVYQDADIYLLDDPLSA 381
Cdd:PRK13536 131 VRENLLvFGRYFgmSTREIEAVIPS--------LLEFARLESKADaRVSDLSGGMKRRLTLARALINDPQLLILDEPTTG 202
|
170 180
....*....|....*....|....*..
gi 2217293410 382 VDAEvSRHLFELCICQILHEKITILVT 408
Cdd:PRK13536 203 LDPH-ARHLIWERLRSLLARGKTILLT 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
224-420 |
1.17e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.89 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 224 KKMVHVQDFTAFWDKASetpTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAV--LGELAPShglVSVHGRIAY------- 294
Cdd:PRK14239 3 EPILQVSDLSVYYNKKK---ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPE---VTITGSIVYnghniys 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 295 --------------VSQQPWVFSGTLRSNILFGKKYEKERYEKVIKAcALKKDLQ--LLEDGDLTVIGDRGTTLSGGQKA 358
Cdd:PRK14239 77 prtdtvdlrkeigmVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDE-AVEKSLKgaSIWDEVKDRLHDSALGLSGGQQQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217293410 359 RVNLARAVYQDADIYLLDDPLSAVDAeVSRHLFELCICQILHEKITILVTHQLQylkAASQI 420
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDP-ISAGKIEETLLGLKDDYTMLLVTRSMQ---QASRI 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
245-407 |
1.36e-15 |
|
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: 77.77 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWVFSG-TLRSN 309
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRditglpphriarlgIARTFQNPRLFPElTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 310 ILFG-------------------KKYEKERYEKVikacalkkdLQLLEDGDLT-VIGDRGTTLSGGQKARVNLARAVYQD 369
Cdd:COG0411 100 VLVAaharlgrgllaallrlpraRREEREARERA---------EELLERVGLAdRADEPAGNLSYGQQRRLEIARALATE 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 2217293410 370 ADIYLLDDPLSAVDAEVSRHLFELcICQILHE-KITILV 407
Cdd:COG0411 171 PKLLLLDEPAAGLNPEETEELAEL-IRRLRDErGITILL 208
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
245-390 |
1.61e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.45 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG----------RIAYVSQQ----PwvfSGTLRSNI 310
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpdvaeACHYLGHRnamkP---ALTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 311 LFGKKYeKERYEKVIKACALKKDLQLLEDgdltvigDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE----- 385
Cdd:PRK13539 95 EFWAAF-LGGEELDIAAALEAVGLAPLAH-------LPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAavalf 166
|
....*...
gi 2217293410 386 ---VSRHL 390
Cdd:PRK13539 167 aelIRAHL 174
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
226-433 |
2.11e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 78.97 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 226 MVHVQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------- 290
Cdd:COG1135 1 MIELENLSkTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGvdltalserelraa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 291 --RIAYVSQQpwvF----SGTLRSNILF-----GKKyEKERYEKVikacalkkdLQLLEdgdLTVIGDRGTT----LSGG 355
Cdd:COG1135 81 rrKIGMIFQH---FnllsSRTVAENVALpleiaGVP-KAEIRKRV---------AELLE---LVGLSDKADAypsqLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 356 QKARVNLARAVYQDADIYLLDDPLSAVDAEVSRhlfelcicQIL------HEK--ITI-LVTHQLQYLKA-ASQILILKD 425
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETTR--------SILdllkdiNRElgLTIvLITHEMDVVRRiCDRVAVLEN 216
|
....*...
gi 2217293410 426 GKMVQKGT 433
Cdd:COG1135 217 GRIVEQGP 224
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
855-1070 |
2.15e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 77.82 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 855 EGVIIFDNVNFMYSPGG----PLVLKHLTALIKSQEKVGIVGRTGAGKSSL---ISALFRLSEpeGKIWIDKILTTEIG- 926
Cdd:PRK13633 2 NEMIKCKNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALLIPSE--GKVYVDGLDTSDEEn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 927 LHDLRKKMSIIPQEP------------VLFTgtmRKNLDPFNEHTDEELWNALQEVQLKETIEDLPGKMdtelaeSGsnf 994
Cdd:PRK13633 80 LWDIRNKAGMVFQNPdnqivativeedVAFG---PENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLL------SG--- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217293410 995 svGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIRE--KFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLK 1070
Cdd:PRK13633 148 --GQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
858-1028 |
2.54e-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: 76.29 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYsPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTeiGLHD-----LR 931
Cdd:cd03292 1 IEFINVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPtSGTIRVNGQDVS--DLRGraipyLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 932 KKMSIIPQE-PVLFTGTMRKNLDPFNEHTDE--ELWN-----ALQEVQLKETIEDLPgkmdtelaesgSNFSVGQRQLVC 1003
Cdd:cd03292 78 RKIGVVFQDfRLLPDRNVYENVAFALEVTGVppREIRkrvpaALELVGLSHKHRALP-----------AELSGGEQQRVA 146
|
170 180
....*....|....*....|....*
gi 2217293410 1004 LARAILRKNQILIIDEATANVDPRT 1028
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDT 171
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
849-1074 |
2.88e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 77.00 E-value: 2.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 849 PPAWPHEGVIIFDNVNFMYspGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSE--P----EGKIWIDK--I 920
Cdd:COG1117 3 APASTLEPKIEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarvEGEILLDGedI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 921 LTTEIGLHDLRKKMSIIPQEPVLFTGTMRKN----------LDPfnEHTDEELWNALQEVQLKETIEDlpgkmdtELAES 990
Cdd:COG1117 81 YDPDVDVVELRRRVGMVFQKPNPFPKSIYDNvayglrlhgiKSK--SELDEIVEESLRKAALWDEVKD-------RLKKS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 991 GSNFSVGQRQLVCLARAILRKNQILIIDEATANVDP----RTDELIQkKIREKFahcTVLTIAH------RLntiidSDK 1060
Cdd:COG1117 152 ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPistaKIEELIL-ELKKDY---TIVIVTHnmqqaaRV-----SDY 222
|
250
....*....|....
gi 2217293410 1061 IMVLDSGRLKEYDE 1074
Cdd:COG1117 223 TAFFYLGELVEFGP 236
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
245-383 |
3.06e-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: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWVFSG-TLRSN 309
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIGYLPQEASIFRKlTVEDN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 310 IL----FGKKYEKERYEKVIkacalkkdlQLLEDGDLTVIGD-RGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 383
Cdd:COG1137 99 ILavleLRKLSKKEREERLE---------ELLEEFGITHLRKsKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
241-410 |
3.41e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 75.47 E-value: 3.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR------------IAYVSQQPWVfSGTLRS 308
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeqrdephenILYLGHLPGL-KPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 309 nilfgkkYEKERYEKVIKACALKKDLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVS 387
Cdd:TIGR01189 91 -------LENLHFWAAIHGGAQRTIEDALAAVGLTGFEDLpAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV 163
|
170 180
....*....|....*....|...
gi 2217293410 388 RHLFELCICQILHEKITILVTHQ 410
Cdd:TIGR01189 164 ALLAGLLRAHLARGGIVLLTTHQ 186
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
241-439 |
3.50e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 77.40 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG---------------RIAYVSQQP--WVFS 303
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkKVGLVFQYPeyQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 304 GTLRSNILFGKK----YEKERYEKVIKACALKKDlqlledgDLTVIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDP 378
Cdd:PRK13637 99 ETIEKDIAFGPInlglSEEEIENRVKRAMNIVGL-------DYEDYKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217293410 379 LSAVDAEVSRHLFELciCQILHEK---ITILVTHQLQYL-KAASQILILKDGKMVQKGTYTEFLK 439
Cdd:PRK13637 172 TAGLDPKGRDEILNK--IKELHKEynmTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
245-437 |
4.00e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.59 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLL----SAVLGELAP-SH-----GLVSVHGRIA-----------YVSQQ-PWVF 302
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAgSHiellgRTVQREGRLArdirksrantgYIFQQfNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 303 SGTLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDgdLTVIG------DRGTTLSGGQKARVNLARAVYQDADIYLLD 376
Cdd:PRK09984 100 RLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQA--LTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 377 DPLSAVDAEVSRHLFELCICQILHEKITILVT-HQLQY-LKAASQILILKDGKMVQKGTYTEF 437
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDINQNDGITVVVTlHQVDYaLRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
220-412 |
4.91e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 76.23 E-value: 4.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 220 PSDGKKMVHVQDFTAFWDkasETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAV--LGELAPS---HGLVSVHG---- 290
Cdd:COG1117 5 ASTLEPKIEVRNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPGarvEGEILLDGediy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 291 -----------RIAYVSQQPWVFSGTLRSNILFG--------KKYEKERYEKVIKACAL----KKDLQlledgdltvigD 347
Cdd:COG1117 82 dpdvdvvelrrRVGMVFQKPNPFPKSIYDNVAYGlrlhgiksKSELDEIVEESLRKAALwdevKDRLK-----------K 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 348 RGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQiLHEKITI-LVTHQLQ 412
Cdd:COG1117 151 SALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEEL-ILE-LKKDYTIvIVTHNMQ 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
227-432 |
5.01e-15 |
|
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: 75.01 E-value: 5.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 227 VHVQDFT-AFWDKASetptLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG---------RIAYVS 296
Cdd:cd03269 1 LEVENVTkRFGRVTA----LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaarnRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 297 QQPWVfsgtlrsnilfgkkYEKERYEKVI----------KACALKKDLQLLEDGDLTVIGD-RGTTLSGGQKARVNLARA 365
Cdd:cd03269 77 EERGL--------------YPKMKVIDQLvylaqlkglkKEEARRRIDEWLERLELSEYANkRVEELSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 366 VYQDADIYLLDDPLSAVDAeVSRHLFELCICQILHEKIT-ILVTHQLQYLKA-ASQILILKDGKMVQKG 432
Cdd:cd03269 143 VIHDPELLILDEPFSGLDP-VNVELLKDVIRELARAGKTvILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
242-433 |
5.23e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 78.07 E-value: 5.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 242 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIayVSQQP-------WVFSG-------TLR 307
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQD--ITHVPaenrhvnTVFQSyalfphmTVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 308 SNILFGKKYEK----ERYEKVIKACALkkdLQLLEDGDltvigDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 383
Cdd:PRK09452 105 ENVAFGLRMQKtpaaEITPRVMEALRM---VQLEEFAQ-----RKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2217293410 384 AEVSRHL-FELcicQILHEK--IT-ILVTH-QLQYLKAASQILILKDGKMVQKGT 433
Cdd:PRK09452 177 YKLRKQMqNEL---KALQRKlgITfVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
240-442 |
5.58e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 75.89 E-value: 5.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 240 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSG-T 305
Cdd:COG4604 12 GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvattpsrelakRLAILRQENHINSRlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 306 LRSNILFGK------KYEKERYEKVIKAcalkkdLQLLedgDLTVIGDRG-TTLSGGQKARVNLARAVYQDADIYLLDDP 378
Cdd:COG4604 92 VRELVAFGRfpyskgRLTAEDREIIDEA------IAYL---DLEDLADRYlDELSGGQRQRAFIAMVLAQDTDYVLLDEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217293410 379 LSAVD----AEVSRHLFELCicqilHE--KITILVTHQLQYLKA-ASQILILKDGKMVQKGTYTEFLKSGI 442
Cdd:COG4604 163 LNNLDmkhsVQMMKLLRRLA-----DElgKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPEEIITPEV 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
870-1069 |
5.89e-15 |
|
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: 73.62 E-value: 5.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 870 GGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDkiltteiglhdlrkkmsiipQEPVLFTGTM 948
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPdSGEILVD--------------------GKEVSFASPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 949 RknldpfnehtdeelwnALQE-----VQLketiedlpgkmdtelaesgsnfSVGQRQLVCLARAILRKNQILIIDEATAN 1023
Cdd:cd03216 71 D----------------ARRAgiamvYQL----------------------SVGERQMVEIARALARNARLLILDEPTAA 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1024 VDPR-TDELIQ--KKIREKfaHCTVLTIAHRLNTIID-SDKIMVLDSGRL 1069
Cdd:cd03216 113 LTPAeVERLFKviRRLRAQ--GVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
248-455 |
7.30e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 77.95 E-value: 7.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 248 LSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-IAYVS--QQP--WVFSG-------TLRSNILFGKK 315
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdLSHVPpyQRPinMMFQSyalfphmTVEQNIAFGLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 316 yeKERYEKVIKACALKKDLQLLEDGDLTviGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVsRHLFELCI 395
Cdd:PRK11607 118 --QDKLPKAEIASRVNEMLGLVHMQEFA--KRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL-RDRMQLEV 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 396 CQILhEKI---TILVTH-QLQYLKAASQILILKDGKMVQKGT------------YTEFLKSGIDFGSLLKKDNEES 455
Cdd:PRK11607 193 VDIL-ERVgvtCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEpeeiyehpttrySAEFIGSVNVFEGVLKERQEDG 267
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
242-436 |
7.54e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 76.27 E-value: 7.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 242 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-IAY--------------VSQQP--WVFSG 304
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpIKYdkksllevrktvgiVFQNPddQLFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 305 TLRSNILFGK---KYEKERYEKVIKAcALKKdlqlledgdltvIGDRGTT------LSGGQKARVNLARAVYQDADIYLL 375
Cdd:PRK13639 95 TVEEDVAFGPlnlGLSKEEVEKRVKE-ALKA------------VGMEGFEnkpphhLSGGQKKRVAIAGILAMKPEIIVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 376 DDPLSAVD----AEVSRHLFELCicqilHEKITILV-THQLQYL-KAASQILILKDGKMVQKGTYTE 436
Cdd:PRK13639 162 DEPTSGLDpmgaSQIMKLLYDLN-----KEGITIIIsTHDVDLVpVYADKVYVMSDGKIIKEGTPKE 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
227-411 |
7.60e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.07 E-value: 7.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 227 VHVQDFTAFWDKASETptLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR----------IAYVS 296
Cdd:PRK15056 7 IVVNDVTVTWRNGHTA--LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 297 QQP---WVFSGTLRSNILFGK-------KYEKERYEKVIKACALKKDLQLLEDGDltvIGDrgttLSGGQKARVNLARAV 366
Cdd:PRK15056 85 QSEevdWSFPVLVEDVVMMGRyghmgwlRRAKKRDRQIVTAALARVDMVEFRHRQ---IGE----LSGGQKKRVFLARAI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2217293410 367 YQDADIYLLDDPLSAVDAEVSRHLFELcICQILHEKITILV-THQL 411
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISL-LRELRDEGKTMLVsTHNL 202
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
882-1085 |
1.07e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.90 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 882 IKSQEKVGIVGRTGAGKSS---LISALFRlsEPEGKIWIDKILTTEIGLHDLRKKMSIIPQEP-VLFTGTMRKNLDPFNE 957
Cdd:PRK13642 30 ITKGEWVSIIGQNGSGKSTtarLIDGLFE--EFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdNQFVGATVEDDVAFGM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 958 HTD----EELWNALQEVQLKETIEDLPGKMDTELaesgsnfSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQ 1033
Cdd:PRK13642 108 ENQgiprEEMIKRVDEALLAVNMLDFKTREPARL-------SGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIM 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2217293410 1034 K---KIREKFaHCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNKESL 1085
Cdd:PRK13642 181 RvihEIKEKY-QLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDM 234
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
248-440 |
1.24e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 75.26 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 248 LSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPwvfSGTL--RSNI-- 310
Cdd:COG4167 32 VSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhkleygdykyrckHIRMIFQDP---NTSLnpRLNIgq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 311 -------LFGKKYEKERYEKVIKAcaLKKdLQLLEDGDLTVIgdrgTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 383
Cdd:COG4167 109 ileeplrLNTDLTAEEREERIFAT--LRL-VGLLPEHANFYP----HMLSSGQKQRVALARALILQPKIIIADEALAALD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217293410 384 AEVSRHLFELCIcqILHEKIT---ILVTHQLQYLKAAS-QILILKDGKMVQKGTYTEFLKS 440
Cdd:COG4167 182 MSVRSQIINLML--ELQEKLGisyIYVSQHLGIVKHISdKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
226-430 |
1.29e-14 |
|
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: 74.39 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 226 MVHVQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------- 290
Cdd:COG4181 8 IIELRGLTkTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGqdlfaldedararl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 291 RIAYVSqqpWVF-------SGTLRSNI-----LFGKKYEKERYEKVIKACALkkdlqlledgdltviGDRGT----TLSG 354
Cdd:COG4181 88 RARHVG---FVFqsfqllpTLTALENVmlpleLAGRRDARARARALLERVGL---------------GHRLDhypaQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 355 GQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRH----LFELCicqilHEKIT--ILVTHQLQYLKAASQILILKDGKM 428
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQiidlLFELN-----RERGTtlVLVTHDPALAARCDRVLRLRAGRL 224
|
..
gi 2217293410 429 VQ 430
Cdd:COG4181 225 VE 226
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
245-438 |
1.32e-14 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 74.65 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG---------------RIAYVSQQPWVFSG-TLRS 308
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGedltdskkdinklrrKVGMVFQQFNLFPHlTVLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 309 NILFGKKYEKeryeKVIKACALKKDLQLLEdgdlTV-IGDRG----TTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 383
Cdd:COG1126 97 NVTLAPIKVK----KMSKAEAEERAMELLE----RVgLADKAdaypAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217293410 384 ----AEVsrhlfeL-CICQILHEKIT-ILVTHQLQY-LKAASQILILKDGKMVQKGTYTEFL 438
Cdd:COG1126 169 pelvGEV------LdVMRDLAKEGMTmVVVTHEMGFaREVADRVVFMDGGRIVEEGPPEEFF 224
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
241-442 |
1.48e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 76.00 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQqpwvFSG---- 304
Cdd:PRK13537 19 DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpsrarharqRVGVVPQ----FDNldpd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 305 -TLRSNIL-FGkkyekeRYEKVIKACALKKDLQLLEDGDLTVIGD-RGTTLSGGQKARVNLARAVYQDADIYLLDDPLSA 381
Cdd:PRK13537 95 fTVRENLLvFG------RYFGLSAAAARALVPPLLEFAKLENKADaKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217293410 382 VDAEvSRHLFELCICQILHEKITILVThqLQYLKAASQ----ILILKDGKMVQKGTYTEFLKSGI 442
Cdd:PRK13537 169 LDPQ-ARHLMWERLRSLLARGKTILLT--THFMEEAERlcdrLCVIEEGRKIAEGAPHALIESEI 230
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
225-451 |
2.05e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.13 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 225 KMVHVQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------R 291
Cdd:PRK13642 3 KILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGelltaenvwnlrrK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 292 IAYVSQQP--WVFSGTLRSNILFGKKYEKERYEKVIKacalKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQD 369
Cdd:PRK13642 83 IGMVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIK----RVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 370 ADIYLLDDPLSAVDAEVSRHlfelcICQILHE-----KITIL-VTHQLQYLKAASQILILKDGKMVQKGTYTEFLKS--- 440
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQE-----IMRVIHEikekyQLTVLsITHDLDEAASSDRILVMKAGEIIKEAAPSELFATsed 233
|
250
....*....|....*..
gi 2217293410 441 ----GID--FGSLLKKD 451
Cdd:PRK13642 234 mveiGLDvpFSSNLMKD 250
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
219-437 |
2.14e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.40 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 219 LPSDGKKMVHVQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR------- 291
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 292 -------IAYVSQQPWVFSG-TLRSNILFGKKYEKERYEKVIK-----ACALKKDLQ--LLEdgdltvIGDRGTtlsggq 356
Cdd:PRK15439 81 akahqlgIYLVPQEPLLFPNlSVKENILFGLPKRQASMQKMKQllaalGCQLDLDSSagSLE------VADRQI------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 357 karVNLARAVYQDADIYLLDDPLSAVD-AEVSRhLFELcICQILHEKITIL-VTHQLQYLKA-ASQILILKDGKMVQKGT 433
Cdd:PRK15439 149 ---VEILRGLMRDSRILILDEPTASLTpAETER-LFSR-IRELLAQGVGIVfISHKLPEIRQlADRISVMRDGTIALSGK 223
|
....
gi 2217293410 434 YTEF 437
Cdd:PRK15439 224 TADL 227
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
295-438 |
2.65e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 78.15 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 295 VSQQPWVFSGTLRSNILFGKkyEKERYEKVIKAC---ALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDAD 371
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGK--EDATREDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPK 1378
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217293410 372 IYLLDDPLSAVDAEvSRHLFELCICQILH--EKITILVTHQLQYLKAASQILIL----KDGKMVQ-KGTYTEFL 438
Cdd:PTZ00265 1379 ILLLDEATSSLDSN-SEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELL 1451
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
858-1070 |
2.85e-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: 73.31 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKI-LTTEIglHDLRKKMS 935
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPtSGTAYINGYsIRTDR--KAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 936 IIPQEPVLFTG-TMRKNLDPF-------NEHTDEELWNALQEVQLKEtiedlpgKMDTELaesgSNFSVGQRQLVCLARA 1007
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFYarlkglpKSEIKEEVELLLRVLGLTD-------KANKRA----RTLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217293410 1008 ILRKNQILIIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTI-IDSDKIMVLDSGRLK 1070
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKLR 211
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
532-830 |
3.07e-14 |
|
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: 74.73 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 532 IFLILLNTAAQVA--YVLqdwwlsywanKQSMLNVTVNGGGNVTEkldLNWYLGIYSGLTVATVLFGIARSLLVFYVLVN 609
Cdd:cd18544 5 LLLLLLATALELLgpLLI----------KRAIDDYIVPGQGDLQG---LLLLALLYLGLLLLSFLLQYLQTYLLQKLGQR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 610 SSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQTLLQVVGVVSVAVAVIPWIA----IPL 685
Cdd:cd18544 72 IIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLAlislLVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 686 VPLGIIFIFLRRYfletSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWF 765
Cdd:cd18544 152 PLLLLATYLFRKK----SRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALF 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217293410 766 --AVRLDAICAMFVIIVAFGSLILAKTLDAGQVglalsYA-LTLMGMFQWCVRQSAEVENM----MISVERV 830
Cdd:cd18544 228 rpLVELLSSLALALVLWYGGGQVLSGAVTLGVL-----YAfIQYIQRFFRPIRDLAEKFNIlqsaMASAERI 294
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
5-182 |
3.71e-14 |
|
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: 74.22 E-value: 3.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 5 KTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGIS-CLAGMAVLIILLPLQSCFGKLFSSLRSKTA 83
Cdd:pfam00664 94 TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPLYILVSAVFAKILRKLSRKEQ 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 84 TFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVT--FTTYVLLGS 161
Cdd:pfam00664 174 KAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALAlwFGAYLVISG 253
|
170 180
....*....|....*....|.
gi 2217293410 162 VITASRVFVAVTLYGAVRLTV 182
Cdd:pfam00664 254 ELSVGDLVAFLSLFAQLFGPL 274
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
857-1071 |
4.81e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 72.77 E-value: 4.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 857 VIIFDNVNFMYSPGGPLV--LKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDL--- 930
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPtSGEVLIDGQDISSLSERELarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 931 -RKKMSIIPQE---------------PVLFTGTMRKNldpfnehTDEELWNALQEVQLKETIEDLPGKMdtelaesgsnf 994
Cdd:COG1136 84 rRRHIGFVFQFfnllpeltalenvalPLLLAGVSRKE-------RRERARELLERVGLGDRLDHRPSQL----------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 995 SVGQRQLVCLARAILRKNQILIIDEATANVDPRT-DELIQ--KKIREKFaHCTVLTIAHRLNTIIDSDKIMVLDSGRLKE 1071
Cdd:COG1136 146 SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgEEVLEllRELNREL-GTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
245-410 |
4.88e-14 |
|
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: 72.14 E-value: 4.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR------------IAYVSQQPWVfSGTL--RSNI 310
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldfqrdsiargLLYLGHAPGI-KTTLsvLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 311 LFGKKYekeryekvikaCALKKDLQLLEDGDLTVIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRH 389
Cdd:cd03231 95 RFWHAD-----------HSDEQVEEALARVGLNGFEDRPVaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180
....*....|....*....|.
gi 2217293410 390 LFELCICQILHEKITILVTHQ 410
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTHQ 184
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
860-1067 |
5.36e-14 |
|
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: 73.74 E-value: 5.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 860 FDNVNFMYSPggplVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIwidkiltteigLHDLRkkMSIIP 938
Cdd:cd03291 42 FSNLCLVGAP----VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPsEGKI-----------KHSGR--ISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 939 QEPVLFTGTMRKNLdPFNEHTDEELWNA-LQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQILII 1017
Cdd:cd03291 105 QFSWIMPGTIKENI-IFGVSYDEYRYKSvVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2217293410 1018 DEATANVDPRTD-ELIQKKIREKFAHCTVLTIAHRLNTIIDSDKIMVLDSG 1067
Cdd:cd03291 184 DSPFGYLDVFTEkEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
241-432 |
6.65e-14 |
|
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: 72.37 E-value: 6.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIayvsqqPWVFSGTLRSNI--LFGKK--- 315
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV------PWKRRKKFLRRIgvVFGQKtql 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 316 ----------------Y--EKERYEKVIKACAlkkdlQLLEDGDLTVIGDRgtTLSGGQKARVNLARAVYQDADIYLLDD 377
Cdd:cd03267 107 wwdlpvidsfyllaaiYdlPPARFKKRLDELS-----ELLDLEELLDTPVR--QLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 378 PLSAVDAEVSRHLFE-LCICQILHEKITILVTHQLQYLKA-ASQILILKDGKMVQKG 432
Cdd:cd03267 180 PTIGLDVVAQENIRNfLKEYNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
889-1070 |
1.03e-13 |
|
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: 71.46 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 889 GIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGlHDLRKKMSIIPQEPVLFTG-TMRKNLDPF-------NEHT 959
Cdd:cd03264 29 GLLGPNGAGKTTLMRILATLTPPsSGTIRIDGQDVLKQP-QKLRRRIGYLPQEFGVYPNfTVREFLDYIawlkgipSKEV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 960 DEELWNALQEVQLKETIEDLPGKmdtelaesgsnFSVGQRQLVCLARAILRKNQILIIDEATANVDP----RTDELIQKK 1035
Cdd:cd03264 108 KARVDEVLELVNLGDRAKKKIGS-----------LSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPeeriRFRNLLSEL 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 2217293410 1036 IREKfahcTVLTIAHRLNTIIDS-DKIMVLDSGRLK 1070
Cdd:cd03264 177 GEDR----IVILSTHIVEDVESLcNQVAVLNKGKLV 208
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
864-1055 |
1.07e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 72.38 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 864 NFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPEGKIWID--------KILTTEIGLHDLRKKMS 935
Cdd:PRK14258 12 NLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEgrveffnqNIYERRVNLNRLRRQVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 936 IIPQEPVLFTGTMRKNL----DPFNEHTDEELwNALQEVQLKETieDLPGKMDTELAESGSNFSVGQRQLVCLARAILRK 1011
Cdd:PRK14258 92 MVHPKPNLFPMSVYDNVaygvKIVGWRPKLEI-DDIVESALKDA--DLWDEIKHKIHKSALDLSGGQQQRLCIARALAVK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2217293410 1012 NQILIIDEATANVDP----RTDELIQK-KIREKFahcTVLTIAHRLNTI 1055
Cdd:PRK14258 169 PKVLLMDEPCFGLDPiasmKVESLIQSlRLRSEL---TMVIVSHNLHQV 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
245-432 |
1.20e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 72.09 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSV--------------HGRIAYVSQQ-PWVFSG----- 304
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarslsqqKGLIRQLRQHvGFVFQNfnlfp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 305 --TLRSNILFGKKYEKeryeKVIKACALKKDLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSA 381
Cdd:PRK11264 99 hrTVLENIIEGPVIVK----GEPKEEATARARELLAKVGLAGKETSyPRRLSGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 382 VDAEVSRHLFElCICQILHEKIT-ILVTHQLQYLK-AASQILILKDGKMVQKG 432
Cdd:PRK11264 175 LDPELVGEVLN-TIRQLAQEKRTmVIVTHEMSFARdVADRAIFMDQGRIVEQG 226
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
246-410 |
1.34e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.99 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 246 QGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIayVSQQPWVFsgtlRSNILF-----GKKYEKER 320
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP--IRRQRDEY----HQDLLYlghqpGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 321 YEKVIKACALKkdlQLLEDGD----LTVIGDRGT------TLSGGQKARVNLARAVYQDADIYLLDDPLSAVD----AEV 386
Cdd:PRK13538 92 LENLRFYQRLH---GPGDDEAlweaLAQVGLAGFedvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDkqgvARL 168
|
170 180
....*....|....*....|....*.
gi 2217293410 387 SRHLFELCicqilhEK--ITILVTHQ 410
Cdd:PRK13538 169 EALLAQHA------EQggMVILTTHQ 188
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
858-1069 |
1.52e-13 |
|
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: 71.02 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYspGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID--KILTTEIGLHDLRKKM 934
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPdSGTIIIDglKLTDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 935 SIIPQEPVLF---------TGTMRKNLDPFNEHTDEELWNALQEVQLKETIEDLPGKMdtelaeSGsnfsvGQRQLVCLA 1005
Cdd:cd03262 79 GMVFQQFNLFphltvleniTLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQL------SG-----GQQQRVAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 1006 RAILRKNQILIIDEATANVDPrtdELIQK--KIREKFAH--CTVLTIAHRLNTIID-SDKIMVLDSGRL 1069
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDP---ELVGEvlDVMKDLAEegMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
245-454 |
1.61e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.12 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAV--LGELAPS---HGLVSVHG---------------RIAYVSQQPWVFSG 304
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVTFHGknlyapdvdpvevrrRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 305 TLRSNILFGKK---YE---KERYEKVIKACAL----KKDLQlledgdltvigDRGTTLSGGQKARVNLARAVYQDADIYL 374
Cdd:PRK14243 106 SIYDNIAYGARingYKgdmDELVERSLRQAALwdevKDKLK-----------QSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 375 LDDPLSAVDAEVSRHLFELciCQILHEKITI-LVTHQLQYLKAASQILILKDGKMVQKGTYT----EFLKSGIDFGSLLK 449
Cdd:PRK14243 175 MDEPCSALDPISTLRIEEL--MHELKEQYTIiIVTHNMQQAARVSDMTAFFNVELTEGGGRYgylvEFDRTEKIFNSPQQ 252
|
....*
gi 2217293410 450 KDNEE 454
Cdd:PRK14243 253 QATRD 257
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
229-450 |
1.79e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 72.43 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 229 VQDFTAFWDK--ASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLV-------------------- 286
Cdd:PRK13651 5 VKNIVKIFNKklPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekvl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 287 -----------------SVHGRIAYVSQ--QPWVFSGTLRSNILFG-------KKYEKERYEKVIKACALkkDLQLLEDG 340
Cdd:PRK13651 85 eklviqktrfkkikkikEIRRRVGVVFQfaEYQLFEQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGL--DESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 341 DLTvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFElcICQILHE--KITILVTHQLQY-LKAA 417
Cdd:PRK13651 163 PFE--------LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKqgKTIILVTHDLDNvLEWT 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2217293410 418 SQILILKDGKMVQKG-TY-----TEFLKSG-------IDFGSLLKK 450
Cdd:PRK13651 233 KRTIFFKDGKIIKDGdTYdilsdNKFLIENnmeppklLNFVNKLEK 278
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
248-433 |
1.91e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 73.22 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 248 LSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYVSQQPWVFSG-TLRSNILFGKK 315
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvthrsiqqrdICMVFQSYALFPHmSLGENVGYGLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 316 YEK----ERYEKVIKACALKkdlqlledgDLTVIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHL 390
Cdd:PRK11432 105 MLGvpkeERKQRVKEALELV---------DLAGFEDRYVdQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2217293410 391 FElcicQI--LHEK--ITIL-VTH-QLQYLKAASQILILKDGKMVQKGT 433
Cdd:PRK11432 176 RE----KIreLQQQfnITSLyVTHdQSEAFAVSDTVIVMNKGKIMQIGS 220
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
243-451 |
2.93e-13 |
|
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: 71.09 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 243 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSGTLRSN 309
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 310 ILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAeVSRH 389
Cdd:cd03288 115 LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDM-ATEN 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217293410 390 LFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFL--KSGIdFGSLLKKD 451
Cdd:cd03288 194 ILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaqEDGV-FASLVRTD 256
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
858-1084 |
3.17e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 70.38 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYspggplvlKHL----TALIKSQEKVGIVGRTGAGKSSLIS--ALFrLSEPEGKIWIDKILTTEIGlhDLR 931
Cdd:PRK10771 2 LKLTDITWLY--------HHLpmrfDLTVERGERVAILGPSGAGKSTLLNliAGF-LTPASGSLTLNGQDHTTTP--PSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 932 KKMSIIPQEPVLFTG-TMRKN----LDP---FNEHTDEELWNALQEVQLKETIEDLPGKMdtelaeSGsnfsvGQRQLVC 1003
Cdd:PRK10771 71 RPVSMLFQENNLFSHlTVAQNiglgLNPglkLNAAQREKLHAIARQMGIEDLLARLPGQL------SG-----GQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1004 LARAILRKNQILIIDEATANVDP--RTD--ELIQKKIREKfaHCTVLTIAHRLNtiiDSDKI----MVLDSGRLkEYDEP 1075
Cdd:PRK10771 140 LARCLVREQPILLLDEPFSALDPalRQEmlTLVSQVCQER--QLTLLMVSHSLE---DAARIaprsLVVADGRI-AWDGP 213
|
....*....
gi 2217293410 1076 YVLLQNKES 1084
Cdd:PRK10771 214 TDELLSGKA 222
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
873-1069 |
3.18e-13 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 70.09 E-value: 3.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 873 LVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLhDLRKKMSIIPQEPVLFTG-TMRK 950
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDaGFATVDGFDVVKEPA-EARRRLGFVSDSTGLYDRlTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 951 NLDPFNEhtdeelWNALQEVQLKETIEDLPGKMDTE--LAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRT 1028
Cdd:cd03266 98 NLEYFAG------LYGLKGDELTARLEELADRLGMEelLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2217293410 1029 DELIQKKIRE-KFAHCTVLTIAHRLNTIID-SDKIMVLDSGRL 1069
Cdd:cd03266 172 TRALREFIRQlRALGKCILFSTHIMQEVERlCDRVVVLHRGRV 214
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
200-440 |
3.22e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 73.77 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 200 IRRIQtfllLDEISQRNRQLPS----DGKKM----VHVQDFTAFWDkasETPTLQGLSFTVRPGELLAVVGPVGAGKSSL 271
Cdd:PRK15064 289 IDKIK----LEEVKPSSRQNPFirfeQDKKLhrnaLEVENLTKGFD---NGPLFKNLNLLLEAGERLAIIGENGVGKTTL 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 272 LSAVLGELAPSHGLV--SVHGRIAYVSQQPwvfsgtlrsnilfgkkyekeryekvikACALKKDLQLLE---------DG 340
Cdd:PRK15064 362 LRTLVGELEPDSGTVkwSENANIGYYAQDH---------------------------AYDFENDLTLFDwmsqwrqegDD 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 341 DLTVigdRGT----------------TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLfelcicQILHEKIT 404
Cdd:PRK15064 415 EQAV---RGTlgrllfsqddikksvkVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESL------NMALEKYE 485
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2217293410 405 ---ILVTHQLQYLKA-ASQILILKDGKMVQ-KGTYTEFLKS 440
Cdd:PRK15064 486 gtlIFVSHDREFVSSlATRIIEITPDGVVDfSGTYEEYLRS 526
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
241-430 |
3.43e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 71.40 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------------RIAYVSQQP--WV 301
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkKVSLVFQFPeaQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 302 FSGTLRSNILFGKK----YEKERYEKVIKacALKKdLQLLEDgdltVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDD 377
Cdd:PRK13641 99 FENTVLKDVEFGPKnfgfSEDEAKEKALK--WLKK-VGLSED----LISKSPFELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2217293410 378 PLSAVDAEVSRHLFELCICQILHEKITILVTHQLQYL-KAASQILILKDGKMVQ 430
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIK 225
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
856-1085 |
3.48e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 71.58 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 856 GVIIFDNVNFMYSPGGPLVLKHL--TALIKSQEKVG-IVGRTGAGKSSLISAL--FRLSEPEGKIWIDKILTTEIG---- 926
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFEFKALnnTSLTFKKNKVTcVIGTTGSGKSTMIQLTngLIISETGQTIVGDYAIPANLKkike 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 927 LHDLRKKMSIIPQEP--VLFTGTMRKNL--DPFNEHTD-EELWNALQEV-QLKETIEDLPGKMDTELaesgsnfSVGQRQ 1000
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIafGPVNLGENkQEAYKKVPELlKLVQLPEDYVKRSPFEL-------SGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1001 LVCLARAILRKNQILIIDEATANVDPRTDE----LIQKKIREKFAHctVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEP 1075
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfinLFERLNKEYKKR--IIMVTHNMDQVLRiADEVIVMHEGKVISIGSP 235
|
250
....*....|
gi 2217293410 1076 YVLLQNKESL 1085
Cdd:PRK13645 236 FEIFSNQELL 245
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
224-447 |
3.52e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 71.30 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 224 KKMVHVQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------- 290
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteenvwdirh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 291 RIAYVSQQP-WVFSG-TLRSNILFGKKYE----KERYEKVIKAcalkkdLQLLedgDLTVIGDRGTT-LSGGQKARVNLA 363
Cdd:PRK13650 82 KIGMVFQNPdNQFVGaTVEDDVAFGLENKgiphEEMKERVNEA------LELV---GMQDFKEREPArLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 364 RAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQILHE-KITIL-VTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 441
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKT-IKGIRDDyQMTVIsITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRG 231
|
....*.
gi 2217293410 442 IDFGSL 447
Cdd:PRK13650 232 NDLLQL 237
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
870-1075 |
4.45e-13 |
|
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: 70.06 E-value: 4.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 870 GGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEigLHDLRKKMSIIPQEPVLFTG-T 947
Cdd:cd03299 10 WKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDsGKILLNGKDITN--LPPEKRDISYVPQNYALFPHmT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 948 MRKNLDPFNEHTDEELWNALQEVqlKETIEDLpgKMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPR 1027
Cdd:cd03299 88 VYKNIAYGLKKRKVDKKEIERKV--LEIAEML--GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2217293410 1028 TDELIQ---KKIREKFAhCTVLTIAHRLNTI-IDSDKIMVLDSGRLKEYDEP 1075
Cdd:cd03299 164 TKEKLReelKKIRKEFG-VTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKP 214
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
220-433 |
4.60e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 71.42 E-value: 4.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 220 PSDGKKMVHVQDFTAFWDKASETP--TLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------- 290
Cdd:PRK13631 15 PLSDDIILRVKNLYCVFDEKQENElvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkk 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 291 ----------------------RIAYVSQQP--WVFSGTLRSNILFG------KKYE-KERYEKVIKACALKKDLqlLED 339
Cdd:PRK13631 95 nnhelitnpyskkiknfkelrrRVSMVFQFPeyQLFKDTIEKDIMFGpvalgvKKSEaKKLAKFYLNKMGLDDSY--LER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 340 GDLTvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKITILVTHQL-QYLKAAS 418
Cdd:PRK13631 173 SPFG--------LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMeHVLEVAD 244
|
250
....*....|....*
gi 2217293410 419 QILILKDGKMVQKGT 433
Cdd:PRK13631 245 EVIVMDKGKILKTGT 259
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
243-385 |
6.81e-13 |
|
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: 69.39 E-value: 6.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 243 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVH---------------------GRIAYVSQ---- 297
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggwvdlaqaspreilalrrRTIGYVSQflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 298 -----------QPWVFSGTlrsnilfgkkyekERYEKVIKACALKKDLQLLEdgdltvigdR-----GTTLSGGQKARVN 361
Cdd:COG4778 105 iprvsaldvvaEPLLERGV-------------DREEARARARELLARLNLPE---------RlwdlpPATFSGGEQQRVN 162
|
170 180
....*....|....*....|....
gi 2217293410 362 LARAVYQDADIYLLDDPLSAVDAE 385
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAA 186
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
242-428 |
7.62e-13 |
|
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: 68.97 E-value: 7.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 242 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG---------RIAYVSQQPWVfsgTLRSNILF 312
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgrAIPYLRRKIGV---VFQDFRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 313 gkkYEKERYEKVikACAL-----------KKDLQLLEDGDLT-VIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLS 380
Cdd:cd03292 91 ---PDRNVYENV--AFALevtgvppreirKRVPAALELVGLShKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2217293410 381 AVDAEVSRHLFELcICQILHEKITILV-THQLQYLKAAS-QILILKDGKM 428
Cdd:cd03292 166 NLDPDTTWEIMNL-LKKINKAGTTVVVaTHAKELVDTTRhRVIALERGKL 214
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
874-1069 |
9.16e-13 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 68.35 E-value: 9.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 874 VLKHLTALIKSQEKVGIVGRTGAGKSSLISALF-RLSEP--EGKIWIDKIlttEIGLHDLRKKMSIIPQEPVLF-TGTMR 949
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgRRTGLgvSGEVLINGR---PLDKRSFRKIIGYVPQDDILHpTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 950 KNLDpFNehtdeelwnalqeVQLKetiedlpgkmdtelaesgsNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTD 1029
Cdd:cd03213 101 ETLM-FA-------------AKLR-------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2217293410 1030 ELIQKKIReKFA--HCTVLTIAHRLNTIIDS--DKIMVLDSGRL 1069
Cdd:cd03213 148 LQVMSLLR-RLAdtGRTIICSIHQPSSEIFElfDKLLLLSQGRV 190
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
860-1076 |
9.35e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.02 E-value: 9.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 860 FDNVNFMYspGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKiltteiglhdlRKKMSIIP 938
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPdSGEVSIPK-----------GLRIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 939 QEPVLFTG-TMRKNLdpfnEHTDEELWNALQEvqlKETIEDLPGKMDTELAESG-------------------------- 991
Cdd:COG0488 68 QEPPLDDDlTVLDTV----LDGDAELRALEAE---LEELEAKLAEPDEDLERLAelqeefealggweaearaeeilsglg 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 992 ----------SNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRT-----DELIQKKirekfahCTVLTIAH-R--LN 1053
Cdd:COG0488 141 fpeedldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKNYP-------GTVLVVSHdRyfLD 213
|
250 260
....*....|....*....|...
gi 2217293410 1054 TIidSDKIMVLDSGRLKEYDEPY 1076
Cdd:COG0488 214 RV--ATRILELDRGKLTLYPGNY 234
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
242-435 |
9.60e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.07 E-value: 9.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 242 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRiaYVSQQPWVFSGTLRSN------------ 309
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ--PMSKLSSAAKAELRNQklgfiyqfhhll 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 310 ------------ILFGKKYEKERYEK---VIKACALKKDLQlledgdltvigDRGTTLSGGQKARVNLARAVYQDADIYL 374
Cdd:PRK11629 100 pdftalenvampLLIGKKKPAEINSRaleMLAAVGLEHRAN-----------HRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217293410 375 LDDPLSAVDAEVSRHLFELC-ICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYT 435
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLgELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSLM 230
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
259-436 |
9.69e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.06 E-value: 9.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 259 AVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------------IAYVSQQPWVFSG-TLRSNILFG-KKYEKE 319
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekgiclppekrrIGYVFQDARLFPHyKVRGNLRYGmAKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 320 RYEKVIKACALKKdlqLLedgdltvigDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLfeLCICQI 398
Cdd:PRK11144 108 QFDKIVALLGIEP---LL---------DRyPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKREL--LPYLER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2217293410 399 LHE--KITIL-VTHQLQ-YLKAASQILILKDGKMVQKGTYTE 436
Cdd:PRK11144 174 LAReiNIPILyVSHSLDeILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
241-438 |
1.27e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 68.97 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAV--LGELAPSHGLV---SVHGRIA----------YVSQQPWVFSG- 304
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITSGDLIVdglKVNDPKVderlirqeagMVFQQFYLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 305 TLRSNILFGKKyekeRYEKVIKACALKKDLQLLEDGDLtviGDRG----TTLSGGQKARVNLARAVYQDADIYLLDDPLS 380
Cdd:PRK09493 93 TALENVMFGPL----RVRGASKEEAEKQARELLAKVGL---AERAhhypSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217293410 381 AVDAEVsRHlfE-LCICQILHEK--ITILVTHQLQYL-KAASQILILKDGKMVQKGTYTEFL 438
Cdd:PRK09493 166 ALDPEL-RH--EvLKVMQDLAEEgmTMVIVTHEIGFAeKVASRLIFIDKGRIAEDGDPQVLI 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
886-1072 |
1.49e-12 |
|
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: 70.08 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 886 EKVGIVGRTGAGKSSLISALFRLSEP----EGKIWIDKILTTEIGLHDLR----KKMSIIPQE------PVLftgTMRKN 951
Cdd:COG0444 32 ETLGLVGESGSGKSTLARAILGLLPPpgitSGEILFDGEDLLKLSEKELRkirgREIQMIFQDpmtslnPVM---TVGDQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 952 L-DPFNEHTD---EELWN----ALQEVQL---KETIEDLPGkmdtELaeSGsnfsvGQRQLVCLARAILRKNQILIIDEA 1020
Cdd:COG0444 109 IaEPLRIHGGlskAEAREraieLLERVGLpdpERRLDRYPH----EL--SG-----GMRQRVMIARALALEPKLLIADEP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217293410 1021 TANVDPrtdeLIQ-------KKIREKFaHCTVLTIAHRLNTI--IdSDKIMVLDSGRLKEY 1072
Cdd:COG0444 178 TTALDV----TIQaqilnllKDLQREL-GLAILFITHDLGVVaeI-ADRVAVMYAGRIVEE 232
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
246-438 |
1.55e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 69.24 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 246 QGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQ----------QPWVF 302
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqhyaskevarRIGLLAQnattpgditvQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 303 SGTLRSNILFgKKYEKERYEKVIKAcalkkdlqLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAV 382
Cdd:PRK10253 104 RGRYPHQPLF-TRWRKEDEEAVTKA--------MQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 383 DAEVSRHLFELcICQILHEKITIL--VTHQL-QYLKAASQILILKDGKMVQKGTYTEFL 438
Cdd:PRK10253 175 DISHQIDLLEL-LSELNREKGYTLaaVLHDLnQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
232-439 |
1.64e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 71.62 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 232 FTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPS---HGLVSVHG----------RIAYVsQQ 298
Cdd:TIGR00955 28 RGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGmpidakemraISAYV-QQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 299 PWVFSGTL--RSNILF----------GKKYEKERYEKVIKACALKKDLQlledgdlTVIGDRGTT--LSGGQKARVNLAR 364
Cdd:TIGR00955 107 DDLFIPTLtvREHLMFqahlrmprrvTKKEKRERVDEVLQALGLRKCAN-------TRIGVPGRVkgLSGGERKRLAFAS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 365 AVYQDADIYLLDDPLSAVDA----EVSRHLFELCicqiLHEKITILVTHQLQY--LKAASQILILKDGKMVQKGTYTEFL 438
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSfmaySVVQVLKGLA----QKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
|
.
gi 2217293410 439 K 439
Cdd:TIGR00955 256 P 256
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
241-441 |
1.80e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 69.42 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------------RIAYVSQQP--WV 301
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrkRIGMVFQFPesQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 302 FSGTLRSNILFGKKYEKERYEKViKACALKKDLQLLEDGDltVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSA 381
Cdd:PRK13646 99 FEDTVEREIIFGPKNFKMNLDEV-KNYAHRLLMDLGFSRD--VMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217293410 382 VDAEVSRHLFELCI-CQILHEKITILVTHQLQYL-KAASQILILKDGKMVQKGTYTEFLKSG 441
Cdd:PRK13646 176 LDPQSKRQVMRLLKsLQTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
245-416 |
1.93e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.60 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--RIAYVSQQ-------PWVFS-------GTLRS 308
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGklRIGYVPQKlyldttlPLTVNrflrlrpGTKKE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 309 NILfgkkyekERYEKVIKACALKKDLQlledgdltvigdrgtTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 388
Cdd:PRK09544 100 DIL-------PALKRVQAGHLIDAPMQ---------------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV 157
|
170 180 190
....*....|....*....|....*....|
gi 2217293410 389 HLFELcICQILHEK--ITILVTHQLQYLKA 416
Cdd:PRK09544 158 ALYDL-IDQLRRELdcAVLMVSHDLHLVMA 186
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
224-440 |
2.62e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 68.48 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 224 KKMVHVQDFTaFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------- 290
Cdd:PRK13632 5 SVMIKVENVS-FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskenlkeirk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 291 RIAYVSQQP-WVFSG-TLRSNILFG---KKYEKERYEKVIKACALKKDLQLLEDGDltvigdrGTTLSGGQKARVNLARA 365
Cdd:PRK13632 84 KIGIIFQNPdNQFIGaTVEDDIAFGlenKKVPPKKMKDIIDDLAKKVGMEDYLDKE-------PQNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 366 VYQDADIYLLDDPLSAVDAEVSRHlfelcICQILHE------KITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLK 439
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKRE-----IKKIMVDlrktrkKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231
|
.
gi 2217293410 440 S 440
Cdd:PRK13632 232 N 232
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
241-432 |
2.64e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 68.46 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--------------------------RIAY 294
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlkvadknqlrllrtRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 295 VSQQPWVFSG-TLRSNIL--------FGKKYEKERYEKVIKACALKKDLQlledgdltviGDRGTTLSGGQKARVNLARA 365
Cdd:PRK10619 97 VFQHFNLWSHmTVLENVMeapiqvlgLSKQEARERAVKYLAKVGIDERAQ----------GKYPVHLSGGQQQRVSIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 366 VYQDADIYLLDDPLSAVDAEVSRHLfeLCICQILHE--KITILVTHQLQYLK-AASQILILKDGKMVQKG 432
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDPELVGEV--LRIMQQLAEegKTMVVVTHEMGFARhVSSHVIFLHQGKIEEEG 234
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
241-429 |
2.70e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 68.19 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLV----------SVHGRIAYVSQqpwVF-------- 302
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIlidgkdvtklPEYKRAKYIGR---VFqdpmmgta 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 303 -SGTLRSNILF----GKKY---------EKERY-EKVikacalkKDLQL-LEDGDLTVIGdrgtTLSGGQKARVNLARAV 366
Cdd:COG1101 95 pSMTIEENLALayrrGKRRglrrgltkkRRELFrELL-------ATLGLgLENRLDTKVG----LLSGGQRQALSLLMAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 367 YQDADIYLLDDPLSAVDAEVSRHLFELcICQILHEK--ITILVTHQLQY-LKAASQILILKDGKMV 429
Cdd:COG1101 164 LTKPKLLLLDEHTAALDPKTAALVLEL-TEKIVEENnlTTLMVTHNMEQaLDYGNRLIMMHEGRII 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
245-467 |
2.87e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.43 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWVFSG-TLRSN 309
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvrfrsprdaqaagIAIIHQELNLVPNlSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 310 ILFG----------KKYEKERYEKVIKACALKKDLQlledgdlTVIGDrgttLSGGQKARVNLARAVYQDADIYLLDDPL 379
Cdd:COG1129 100 IFLGreprrgglidWRAMRRRARELLARLGLDIDPD-------TPVGD----LSVAQQQLVEIARALSRDARVLILDEPT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 380 SAVDAEVSRHLFELcICQILHEKITIL-VTHQLQYLKA-ASQILILKDGKMVqkgtyTEFLKSGIDFGSLLKK------D 451
Cdd:COG1129 169 ASLTEREVERLFRI-IRRLKAQGVAIIyISHRLDEVFEiADRVTVLRDGRLV-----GTGPVAELTEDELVRLmvgrelE 242
|
250
....*....|....*.
gi 2217293410 452 NEESEQPPVPGTPTLR 467
Cdd:COG1129 243 DLFPKRAAAPGEVVLE 258
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
858-1071 |
3.04e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 69.34 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYSPGGPLVlkhlTAL------IKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID-KILTT--EIGL 927
Cdd:COG1135 2 IELENLSKTFPTKGGPV----TALddvsltIEKGEIFGIIGYSGAGKSTLIRCINLLERPtSGSVLVDgVDLTAlsEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 928 HDLRKKMSIIPQEPVLFTG-TMRKN----LdpfnehtdeELWN---ALQEVQLKETIE--DLPGKMDTELAE-SGsnfsv 996
Cdd:COG1135 78 RAARRKIGMIFQHFNLLSSrTVAENvalpL---------EIAGvpkAEIRKRVAELLElvGLSDKADAYPSQlSG----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 997 GQRQLVCLARAILRKNQILIIDEATANVDPRTD----ELIqKKIREKFaHCTVLTIAHRLNTI--IdSDKIMVLDSGRLK 1070
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTrsilDLL-KDINREL-GLTIVLITHEMDVVrrI-CDRVAVLENGRIV 220
|
.
gi 2217293410 1071 E 1071
Cdd:COG1135 221 E 221
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
862-1050 |
3.04e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 67.94 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 862 NVNFMYspGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSE------PEGKIWI--DKILTTEIGLHDLRKK 933
Cdd:PRK14267 9 NLRVYY--GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneearVEGEVRLfgRNIYSPDVDPIEVRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 934 MSIIPQEPVLF----------TGTMRKNLDPFNEHTDEELWNALQEVQLKETIEDlpgkmdtELAESGSNFSVGQRQLVC 1003
Cdd:PRK14267 87 VGMVFQYPNPFphltiydnvaIGVKLNGLVKSKKELDERVEWALKKAALWDEVKD-------RLNDYPSNLSGGQRQRLV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2217293410 1004 LARAILRKNQILIIDEATANVDPRTDELIQKKIREKFAHCTVLTIAH 1050
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
242-433 |
3.24e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 68.48 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 242 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWV-FSG-T 305
Cdd:PRK13644 15 TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgdfsklqgirklVGIVFQNPETqFVGrT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 306 LRSNILFGKKyekeryekviKACALKKDLQLLEDGDLTVIG------DRGTTLSGGQKARVNLARAVYQDADIYLLDDPL 379
Cdd:PRK13644 95 VEEDLAFGPE----------NLCLPPIEIRKRVDRALAEIGlekyrhRSPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 380 SAVDAEVSRHLFELCicQILHEK--ITILVTHQLQYLKAASQILILKDGKMVQKGT 433
Cdd:PRK13644 165 SMLDPDSGIAVLERI--KKLHEKgkTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
563-830 |
4.82e-12 |
|
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: 67.92 E-value: 4.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 563 NVTVNGGGNVTEKLdLNWYLGIYSGLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRF 642
Cdd:cd18563 28 DVLIQLGPGGNTSL-LLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 643 SKDIGHLDDLLPLTFLDFIQTLLQVVGVVSVAVAVIPWIA----IPLVPLGIIFIFLRRYFletsRDVKRLESTTRSPVF 718
Cdd:cd18563 107 TSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLAllvlIPVPLVVWGSYFFWKKI----RRLFHRQWRRWSRLN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 719 SHLSSSLQGLWTIRAYKAEER--------CQELFDAHQDLHSeawflflTTSRWFAVrLDAICAMFVIIVAF--GSLILA 788
Cdd:cd18563 183 SVLNDTLPGIRVVKAFGQEKReikrfdeaNQELLDANIRAEK-------LWATFFPL-LTFLTSLGTLIVWYfgGRQVLS 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2217293410 789 KTLDAGQVGLALSYaltlMGMF----QWCVRQSAEVENMMISVERV 830
Cdd:cd18563 255 GTMTLGTLVAFLSY----LGMFygplQWLSRLNNWITRALTSAERI 296
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
240-439 |
4.84e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.27 E-value: 4.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 240 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGeLAPSHGLVSVHGRI-------------AYVSQQpwvfsgtl 306
Cdd:PRK03695 7 AVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPleawsaaelarhrAYLSQQ-------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 307 rSNILF------------GKKYEKERYEKVIKACAlkkdlQLLEDGDLtvIGDRGTTLSGGQKARVNLARAVYQ------ 368
Cdd:PRK03695 78 -QTPPFampvfqyltlhqPDKTRTEAVASALNEVA-----EALGLDDK--LGRSVNQLSGGEWQRVRLAAVVLQvwpdin 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217293410 369 -DADIYLLDDPLSAVD----AEVSRHLFELCicqilHEKITILVT-HQLQY-LKAASQILILKDGKMVQKGTYTEFLK 439
Cdd:PRK03695 150 pAGQLLLLDEPMNSLDvaqqAALDRLLSELC-----QQGIAVVMSsHDLNHtLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
245-442 |
5.00e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 67.26 E-value: 5.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR----------------------IAYVSQQPwvf 302
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrdlyalseaerrrllrteWGFVHQHP--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 303 SGTLRSNILFGKKY-EK-----ERYEKVIKACALKKdLQLLEDgDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLD 376
Cdd:PRK11701 99 RDGLRMQVSAGGNIgERlmavgARHYGDIRATAGDW-LERVEI-DAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 377 DPLSAVDAEVSRHLFELcICQILHEK--ITILVTHQLQYLKA-ASQILILKDGKMVQKG-----------TYTEFLKSGI 442
Cdd:PRK11701 177 EPTGGLDVSVQARLLDL-LRGLVRELglAVVIVTHDLAVARLlAHRLLVMKQGRVVESGltdqvlddpqhPYTQLLVSSV 255
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
244-441 |
6.17e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 67.47 E-value: 6.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 244 TLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHG-------------LVSVHGRIAYVSQQP---WVFSgTLR 307
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGeifynnqaitddnFEKLRKHIGIVFQNPdnqFVGS-IVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 308 SNILFGKKYEKERYEKVIKACAlkkdlQLLEDGDLTVIGD-RGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 386
Cdd:PRK13648 103 YDVAFGLENHAVPYDEMHRRVS-----EALKQVDMLERADyEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 387 SRHLFELcICQILHEK-ITIL-VTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 441
Cdd:PRK13648 178 RQNLLDL-VRKVKSEHnITIIsITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
234-439 |
6.42e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 67.52 E-value: 6.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 234 AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAP---SHGLVSVHG-------------RIAYVSQ 297
Cdd:PRK13640 12 SFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGitltaktvwdireKVGIVFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 298 QP-WVFSG-TLRSNILFGKKYEKERYEKVIKACAlkkdlQLLED-GDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYL 374
Cdd:PRK13640 92 NPdNQFVGaTVGDDVAFGLENRAVPRPEMIKIVR-----DVLADvGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIII 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 375 LDDPLSAVDAEVSRHLFELcICQILHEK-ITIL-VTHQLQYLKAASQILILKDGKMVQKGTYTEFLK 439
Cdd:PRK13640 167 LDESTSMLDPAGKEQILKL-IRKLKKKNnLTVIsITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
858-1071 |
6.76e-12 |
|
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: 66.34 E-value: 6.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYSPGGP--LVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDkiltteiG--LHDLRK 932
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPtSGEVLVD-------GepVTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 933 KMSIIPQEPVLF---------------TGTMRKNLDpfnEHTDEelwnALQEVQLKETIEDLPGkmdtELaeSGsnfsvG 997
Cdd:cd03293 74 DRGYVFQQDALLpwltvldnvalglelQGVPKAEAR---ERAEE----LLELVGLSGFENAYPH----QL--SG-----G 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 998 QRQLVCLARAILRKNQILIIDEATANVDPRTDELIQ---KKIREKfAHCTVLTIAHRlntiID-----SDKIMVLDS--G 1067
Cdd:cd03293 136 MRQRVALARALAVDPDVLLLDEPFSALDALTREQLQeelLDIWRE-TGKTVLLVTHD----IDeavflADRVVVLSArpG 210
|
....
gi 2217293410 1068 RLKE 1071
Cdd:cd03293 211 RIVA 214
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
244-427 |
7.89e-12 |
|
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: 66.66 E-value: 7.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 244 TLQGLSFTVRPG-----ELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-RIAYVSQQPWV-FSGTLRSnILFGK-- 314
Cdd:cd03237 9 TLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKAdYEGTVRD-LLSSItk 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 315 -KYEKERYEKVIKacalkKDLQLlEDgdltVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE-------V 386
Cdd:cd03237 88 dFYTHPYFKTEIA-----KPLQI-EQ----ILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlmaskV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2217293410 387 SRHLfelcicqILHEKITILVT-HQLQYLKAASQILILKDGK 427
Cdd:cd03237 158 IRRF-------AENNEKTAFVVeHDIIMIDYLADRLIVFEGE 192
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
242-436 |
8.39e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 67.95 E-value: 8.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 242 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYVSQQ----PWVfsgTL 306
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnelepadrdIAMVFQNyalyPHM---SV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 307 RSNILFG---KKYEKERYEKVIKACAlkkdlQLLEDGDLTvigDRG-TTLSGGQKARVNLARAVYQDADIYLLDDPLSAV 382
Cdd:PRK11650 94 RENMAYGlkiRGMPKAEIEERVAEAA-----RILELEPLL---DRKpRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 383 DAEVSRHL-FELcicQILHEKI---TILVTH-QLQYLKAASQILILKDGKMVQKGTYTE 436
Cdd:PRK11650 166 DAKLRVQMrLEI---QRLHRRLkttSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVE 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
857-1071 |
9.02e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 67.90 E-value: 9.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 857 VIIFDNVNFMYSPGGPLV--LKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKI-LTT--EIGLHDL 930
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPtSGRVLVDGQdLTAlsEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 931 RKKMSIIPQE---------------PVLFTGTMRKNLDPfnehTDEELwnaLQEVQLKETIEDLPgkmdtelaesgSNFS 995
Cdd:PRK11153 81 RRQIGMIFQHfnllssrtvfdnvalPLELAGTPKAEIKA----RVTEL---LELVGLSDKADRYP-----------AQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 996 VGQRQLVCLARAILRKNQILIIDEATANVDPRTD----ELIqKKIREKFaHCTVLTIAHRLNTI--IdSDKIMVLDSGRL 1069
Cdd:PRK11153 143 GGQKQRVAIARALASNPKVLLCDEATSALDPATTrsilELL-KDINREL-GLTIVLITHEMDVVkrI-CDRVAVIDAGRL 219
|
..
gi 2217293410 1070 KE 1071
Cdd:PRK11153 220 VE 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
857-1085 |
1.15e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.07 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 857 VIIFDNVNFMYSPGGPLVLKHLTAL---IKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIG----LH 928
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRALFDIdleVKKGSYTALIGHTGSGKSTLLQHLNGLLQPtEGKVTVGDIVVSSTSkqkeIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 929 DLRKKMSIIPQEP--VLFTGTMRKNL--DPFNEHTDEELWNALQEVQLketieDLPGKMDTELAESGSNFSVGQRQLVCL 1004
Cdd:PRK13643 81 PVRKKVGVVFQFPesQLFEETVLKDVafGPQNFGIPKEKAEKIAAEKL-----EMVGLADEFWEKSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1005 ARAILRKNQILIIDEATANVDPRTdELIQKKIREKFAHC--TVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVLLQN 1081
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKA-RIEMMQLFESIHQSgqTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
|
....
gi 2217293410 1082 KESL 1085
Cdd:PRK13643 235 VDFL 238
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
245-436 |
1.48e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 67.13 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR----------------IAYVSQQpwvF----SG 304
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltalsekelrkarrqIGMIFQH---FnllsSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 305 TLRSNILFGKKYEKERYEKvIKacalKKDLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 383
Cdd:PRK11153 98 TVFDNVALPLELAGTPKAE-IK----ARVTELLELVGLSDKADRyPAQLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 384 AEVSRHLFELcICQILHE-KITI-LVTHQLQYLKA-ASQILILKDGKMVQKGTYTE 436
Cdd:PRK11153 173 PATTRSILEL-LKDINRElGLTIvLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSE 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
220-378 |
1.74e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.12 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 220 PSDGKKMVHVQDFTAfwdkaseTPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------- 291
Cdd:COG1129 250 AAPGEVVLEVEGLSV-------GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirspr 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 292 ------IAYVS----QQPWVFSGTLRSNI------------LFGKKYEKERYEKVIKACALKkdlqlLEDGDLTVigdrg 349
Cdd:COG1129 323 dairagIAYVPedrkGEGLVLDLSIRENItlasldrlsrggLLDRRRERALAEEYIKRLRIK-----TPSPEQPV----- 392
|
170 180 190
....*....|....*....|....*....|.
gi 2217293410 350 TTLSGG--QKarVNLARAVYQDADIYLLDDP 378
Cdd:COG1129 393 GNLSGGnqQK--VVLAKWLATDPKVLILDEP 421
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
245-433 |
1.76e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 66.29 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRiayvsqqPwvFSGTLRSNIlfGkkY--EkER-- 320
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE-------P--LDPEDRRRI--G--YlpE-ERgl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 321 Y--EKVI-------------KACALKKDLQLLEDGDltvIGDRGT----TLSGGQKARVNLARAVYQDADIYLLDDPLSA 381
Cdd:COG4152 83 YpkMKVGeqlvylarlkglsKAEAKRRADEWLERLG---LGDRANkkveELSKGNQQKVQLIAALLHDPELLILDEPFSG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217293410 382 VDAeVSRHLFElcicQILHE-----KITILVTHQLQYLKA-ASQILILKDGKMVQKGT 433
Cdd:COG4152 160 LDP-VNVELLK----DVIRElaakgTTVIFSSHQMELVEElCDRIVIINKGRKVLSGS 212
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
532-830 |
1.85e-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: 66.34 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 532 IFLILLNTAAQVA--YVLqdwwlsywanKQSMLNVTVNGggNVTeklDLNWYLGIYSGLTVATVLFGIARSLLVFYVlvn 609
Cdd:cd18545 6 LLLMLLSTAASLAgpYLI----------KIAIDEYIPNG--DLS---GLLIIALLFLALNLVNWVASRLRIYLMAKV--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 610 SSQTLHN---KMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQTLLQVVGVVSVAVAVIPW---IAI 683
Cdd:cd18545 68 GQRILYDlrqDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRlalVTL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 684 PLVPLGIIFIFlrrYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWflfLTTSR 763
Cdd:cd18545 148 AVLPLLVLVVF---LLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKAN---MRAVR 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 764 -----WFAVRLDAICAMFVIIVAFGSLILAKTLDAGQVGLALSYaltlMGMFQWCVRQSAEVENMMISV----ERV 830
Cdd:cd18545 222 lnalfWPLVELISALGTALVYWYGGKLVLGGAITVGVLVAFIGY----VGRFWQPIRNLSNFYNQLQSAmasaERI 293
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
245-433 |
2.16e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 65.62 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGEL---APSHGlVSVHGRI-------------------AYVSQ--QPw 300
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtggGAPRG-ARVTGDVtlngeplaaidaprlarlrAVLPQaaQP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 301 VFSGTLRSNILFGkkyekeRYEKVIKACALKKdlqllEDGDL-----------TVIGDRGTTLSGGQKARVNLARAVYQ- 368
Cdd:PRK13547 95 AFAFSAREIVLLG------RYPHARRAGALTH-----RDGEIawqalalagatALVGRDVTTLSGGELARVQFARVLAQl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 369 --------DADIYLLDDPLSAVDAEVSRHLFE----------LCICQILHEkITILVTHqlqylkaASQILILKDGKMVQ 430
Cdd:PRK13547 164 wpphdaaqPPRYLLLDEPTAALDLAHQHRLLDtvrrlardwnLGVLAIVHD-PNLAARH-------ADRIAMLADGAIVA 235
|
...
gi 2217293410 431 KGT 433
Cdd:PRK13547 236 HGA 238
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
237-440 |
2.25e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 67.37 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 237 DKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------------RIAYVSQQP 299
Cdd:PRK10070 36 EKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 300 WVFSG-TLRSNILFGKKYE----KERYEKVIKAcalkkdlqLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYL 374
Cdd:PRK10070 116 ALMPHmTVLDNTAFGMELAginaEERREKALDA--------LRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217293410 375 LDDPLSAVDAEVSRHLF-ELCICQILHEKITILVTHQL-QYLKAASQILILKDGKMVQKGTYTEFLKS 440
Cdd:PRK10070 188 MDEAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
857-1068 |
2.63e-11 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 65.11 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 857 VIIFDNVNFMYspGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGK-IwidKILTTEIG---LHDLR 931
Cdd:COG1119 3 LLELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNdV---RLFGERRGgedVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 932 KKMSII---------PQEPVL------FTGTmrknLDPFNEHTDEEL---WNALQEVQLKETIEDLPGKMdtelaesgsn 993
Cdd:COG1119 78 KRIGLVspalqlrfpRDETVLdvvlsgFFDS----IGLYREPTDEQReraRELLELLGLAHLADRPFGTL---------- 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 994 fSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIReKFAH---CTVLTIAHRLNTIIDS-DKIMVLDSGR 1068
Cdd:COG1119 144 -SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLD-KLAAegaPTLVLVTHHVEEIPPGiTHVLLLKDGR 220
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
248-438 |
3.10e-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: 67.27 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 248 LSFTvrPGELLAVVGPVGAGKSSLL-------SAVLGELAPSHGLvsvhgRIAYVSQQPWV-FSGTLRSNILFG------ 313
Cdd:TIGR03719 26 LSFF--PGAKIGVLGLNGAGKSTLLrimagvdKDFNGEARPQPGI-----KVGYLPQEPQLdPTKTVRENVEEGvaeikd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 314 --KKY-------------------EKERYEKVIKAC-ALKKDLQL--------LEDGDLTVigdrgTTLSGGQKARVNLA 363
Cdd:TIGR03719 99 alDRFneisakyaepdadfdklaaEQAELQEIIDAAdAWDLDSQLeiamdalrCPPWDADV-----TKLSGGERRRVALC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 364 RAVYQDADIYLLDDPLSAVDAE----VSRHLFElcicqilHEKITILVTHQLQYL-KAASQILILKDGKMVQ-KGTYTEF 437
Cdd:TIGR03719 174 RLLLSKPDMLLLDEPTNHLDAEsvawLERHLQE-------YPGTVVAVTHDRYFLdNVAGWILELDRGRGIPwEGNYSSW 246
|
.
gi 2217293410 438 L 438
Cdd:TIGR03719 247 L 247
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
874-1050 |
3.34e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 64.93 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 874 VLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSE--PE----GKIWIDKILTTEIGLHDLRKKMSIIPQEP------ 941
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvsGEVYLDGQDIFKMDVIELRRRVQMVFQIPnpipnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 942 VLFT----GTMRKNLDPFNEHTDEELWNALQEVQLKETIEDlpgkmdtELAESGSNFSVGQRQLVCLARAILRKNQILII 1017
Cdd:PRK14247 98 SIFEnvalGLKLNRLVKSKKELQERVRWALEKAQLWDEVKD-------RLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190
....*....|....*....|....*....|...
gi 2217293410 1018 DEATANVDPRTDELIQKKIREKFAHCTVLTIAH 1050
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
868-1071 |
3.47e-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: 64.38 E-value: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 868 SPGGPL-VLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID-KILTT--EIGLHDLR-KKMSIIPQ-E 940
Cdd:COG4181 20 TGAGELtILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPtSGTVRLAgQDLFAldEDARARLRaRHVGFVFQsF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 941 PVLFTGTMRKNL----------DPFNEHTDEelwnaLQEVQLKETIEDLPGKMdtelaeSGsnfsvGQRQLVCLARAILR 1010
Cdd:COG4181 100 QLLPTLTALENVmlplelagrrDARARARAL-----LERVGLGHRLDHYPAQL------SG-----GEQQRVALARAFAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 1011 KNQILIIDEATANVDPRTDELIQKKIRE--KFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLKE 1071
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFElnRERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
861-1081 |
4.50e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 64.80 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 861 DNVNFMYspGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSE------PEGKI-WIDK-ILTTEIGLHDLRK 932
Cdd:PRK14243 14 ENLNVYY--GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfrVEGKVtFHGKnLYAPDVDPVEVRR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 933 KMSIIPQEPVLFTGTMRKNL------DPFNEHTDEELWNALQEVQLKETIEDlpgkmdtELAESGSNFSVGQRQLVCLAR 1006
Cdd:PRK14243 92 RIGMVFQKPNPFPKSIYDNIaygariNGYKGDMDELVERSLRQAALWDEVKD-------KLKQSGLSLSGGQQQRLCIAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1007 AILRKNQILIIDEATANVDP----RTDELIqKKIREKFahcTVLTIAHRL-------------NTIIDSDKIMVldsGRL 1069
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPistlRIEELM-HELKEQY---TIIIVTHNMqqaarvsdmtaffNVELTEGGGRY---GYL 237
|
250
....*....|..
gi 2217293410 1070 KEYDEPYVLLQN 1081
Cdd:PRK14243 238 VEFDRTEKIFNS 249
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
227-443 |
4.53e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 64.67 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 227 VHVQDFTAFWDKASetpTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAvLGELAPSHGLVSVHGRIAYVSQ--------- 297
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQniyerrvnl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 298 ------------QPWVFSGTLRSNILFGKK----YEKERYEKVIKACALKKDLQlleDGDLTVIGDRGTTLSGGQKARVN 361
Cdd:PRK14258 84 nrlrrqvsmvhpKPNLFPMSVYDNVAYGVKivgwRPKLEIDDIVESALKDADLW---DEIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 362 LARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKITI-LVTHQLQYLKAASQILIL------KDGKMVQKGTY 434
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMvIVSHNLHQVSRLSDFTAFfkgnenRIGQLVEFGLT 240
|
....*....
gi 2217293410 435 TEFLKSGID 443
Cdd:PRK14258 241 KKIFNSPHD 249
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
858-1086 |
4.81e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 65.86 E-value: 4.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYspGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSL---ISALFRLSEpeGKIWIDKILTTEIGLHDlRKkM 934
Cdd:COG3839 4 LELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLlrmIAGLEDPTS--GEILIGGRDVTDLPPKD-RN-I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 935 SIIPQEPVLF-TGTMRKNL---------DPfnEHTDEELWNALQEVQLKETIEDLPGkmdtELaeSGsnfsvGQRQLVCL 1004
Cdd:COG3839 78 AMVFQSYALYpHMTVYENIafplklrkvPK--AEIDRRVREAAELLGLEDLLDRKPK----QL--SG-----GQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1005 ARAILRKNQILIIDEATANVDP------RTdELiqKKIREKFAHCTV---------LTIAhrlntiidsDKIMVLDSGRL 1069
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDAklrvemRA-EI--KRLHRRLGTTTIyvthdqveaMTLA---------DRIAVMNDGRI 212
|
250
....*....|....*..
gi 2217293410 1070 KEYDEPYVLLQNKESLF 1086
Cdd:COG3839 213 QQVGTPEELYDRPANLF 229
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
874-1071 |
5.92e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 64.32 E-value: 5.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 874 VLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKI-WIDKILTT-------------------EIGLHDLRK 932
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPsQGNVsWRGEPLAKlnraqrkafrrdiqmvfqdSISAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 933 KMSIIPQEPvlftgtMRK--NLDPFN-EHTDEELwnaLQEVQLKETIED-LPGKMdtelaeSGsnfsvGQRQLVCLARAI 1008
Cdd:PRK10419 107 TVREIIREP------LRHllSLDKAErLARASEM---LRAVDLDDSVLDkRPPQL------SG-----GQLQRVCLARAL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 1009 LRKNQILIIDEATANVDPRTD-ELIQ--KKIREKFAHCTVLtIAHRLNTIID-SDKIMVLDSGRLKE 1071
Cdd:PRK10419 167 AVEPKLLILDEAVSNLDLVLQaGVIRllKKLQQQFGTACLF-ITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
863-1071 |
6.78e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 64.35 E-value: 6.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 863 VNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLH------DLRKKMS 935
Cdd:PRK14271 25 VNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvSGYRYSGDVLLGGRSIFnyrdvlEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 936 IIPQEPVLFTGTMRKN-LDPFNEH--TDEELWNALQEVQLKETieDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKN 1012
Cdd:PRK14271 105 MLFQRPNPFPMSIMDNvLAGVRAHklVPRKEFRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1013 QILIIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIID-SDKIMVLDSGRLKE 1071
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVE 242
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
874-1072 |
7.93e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.91 E-value: 7.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 874 VLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID-KIL-----TTEIGLHDLRKKMSIIPQEPVLFTG 946
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSKIKVDgKVLyfgkdIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 947 -TMRKNLD-PFNEHTDEE-------LWNALQEVQLKETIEDlpgkmdtELAESGSNFSVGQRQLVCLARAILRKNQILII 1017
Cdd:PRK14246 105 lSIYDNIAyPLKSHGIKEkreikkiVEECLRKVGLWKEVYD-------RLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 1018 DEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIID-SDKIMVLDSGRLKEY 1072
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEW 233
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
239-433 |
9.39e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 64.26 E-value: 9.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 239 ASETP----TLQGLSFTVRPGELLAVVGPVGAGKSSLLS------------AVLGELAPSHGLVSV------HGRIAYVS 296
Cdd:PRK13645 17 AKKTPfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqTIVGDYAIPANLKKIkevkrlRKEIGLVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 297 QQP--WVFSGTLRSNILFGKKYEKERYEKVIKACA-LKKDLQLLEDgdltVIGDRGTTLSGGQKARVNLARAVYQDADIY 373
Cdd:PRK13645 97 QFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPeLLKLVQLPED----YVKRSPFELSGGQKRRVALAGIIAMDGNTL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217293410 374 LLDDPLSAVDAEVSRHLFELCI-CQILHEKITILVTHQL-QYLKAASQILILKDGKMVQKGT 433
Cdd:PRK13645 173 VLDEPTGGLDPKGEEDFINLFErLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
240-385 |
9.72e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.94 E-value: 9.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 240 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR----------IAYVSQQPwvfsgtlrsn 309
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsrfMAYLGHLP---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 310 ilfGKKYEKERYEKVIKACALK-KDLQLLEDGDLTVIGDRG------TTLSGGQKARVNLARAVYQDADIYLLDDPLSAV 382
Cdd:PRK13543 92 ---GLKADLSTLENLHFLCGLHgRRAKQMPGSALAIVGLAGyedtlvRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
...
gi 2217293410 383 DAE 385
Cdd:PRK13543 169 DLE 171
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
874-1036 |
9.97e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.88 E-value: 9.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 874 VLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPEGKIWIDkilttEIGLHDL--------RKKMSIIPQEP---- 941
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFD-----GQPLHNLnrrqllpvRHRIQVVFQDPnssl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 942 --------VLFTG--TMRKNLDPfnEHTDEELWNALQEVQLK-ETIEDLPgkmdtelaesgSNFSVGQRQLVCLARAILR 1010
Cdd:PRK15134 376 nprlnvlqIIEEGlrVHQPTLSA--AQREQQVIAVMEEVGLDpETRHRYP-----------AEFSGGQRQRIAIARALIL 442
|
170 180
....*....|....*....|....*.
gi 2217293410 1011 KNQILIIDEATANVDpRTdelIQKKI 1036
Cdd:PRK15134 443 KPSLIILDEPTSSLD-KT---VQAQI 464
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
245-433 |
1.08e-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: 65.48 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGeLAPSHGLVSVHGR-IAYVSQ---QPW------VFS---GTL--RSN 309
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQdLDGLSRralRPLrrrmqvVFQdpfGSLspRMT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 310 I----------LFGKKYEKERYEKVIkacalkkdlQLLEDGDLtvigDRGTT------LSGGQKARVNLARAVYQDADIY 373
Cdd:COG4172 381 VgqiiaeglrvHGPGLSAAERRARVA---------EALEEVGL----DPAARhrypheFSGGQRQRIAIARALILEPKLL 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 374 LLDDPLSAVDAEVSRhlfelcicQIL--------HEKIT-ILVTHQLQYLKA-ASQILILKDGKMVQKGT 433
Cdd:COG4172 448 VLDEPTSALDVSVQA--------QILdllrdlqrEHGLAyLFISHDLAVVRAlAHRVMVMKDGKVVEQGP 509
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
874-1068 |
1.15e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 62.30 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 874 VLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID-KILTTEIGLH--------DLRKKMSIIPQepVL 943
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPdSGEVLFDgKPLDIAARNRigylpeerGLYPKMKVIDQ--LV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 944 FTGTMrKNLDPFNEHTDEELWnaLQEVQL----KETIEDLpgkmdtelaesgsnfSVGQRQLVCLARAILRKNQILIIDE 1019
Cdd:cd03269 93 YLAQL-KGLKKEEARRRIDEW--LERLELseyaNKRVEEL---------------SKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2217293410 1020 ATANVDPRTDELIQKKIRE-KFAHCTVLTIAHRLNTIID-SDKIMVLDSGR 1068
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGR 205
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
890-1081 |
1.24e-10 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 63.43 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 890 IVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDL----RKKMSII-------PQEPVLFTGTMRKNLDPFNE 957
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPtSGKVLIDGQDIAAMSRKELrelrRKKISMVfqsfallPHRTVLENVAFGLEVQGVPR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 958 HTDEEL-WNALQEVQLKETIEDLPGkmdtELaeSGsnfsvGQRQLVCLARAILRKNQILIIDEATANVDP--RT---DEL 1031
Cdd:cd03294 135 AEREERaAEALELVGLEGWEHKYPD----EL--SG-----GMQQRVGLARALAVDPDILLMDEAFSALDPliRRemqDEL 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 1032 --IQKKIREkfahcTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVLLQN 1081
Cdd:cd03294 204 lrLQAELQK-----TIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
245-429 |
1.30e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.52 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSaVLGEL-APSHGLVSVHGR-----------------IAYVSQQPWVFSG-T 305
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLdKPTSGTYRVAGQdvatldadalaqlrrehFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 306 LRSNILFGKKYE-KERYEKVIKACALKKDLQLLEDgdltvIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 384
Cdd:PRK10535 103 AAQNVEVPAVYAgLERKQRLLRAQELLQRLGLEDR-----VEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2217293410 385 EVSRHLfeLCICQILHEK--ITILVTHQLQYLKAASQILILKDGKMV 429
Cdd:PRK10535 178 HSGEEV--MAILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
245-438 |
1.40e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.99 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHG----------LVSVHGR----IAYVSQQPWVFSgtlRSNI 310
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGniiiddedisLLPLHARarrgIGYLPQEASIFR---RLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 311 lfgkkyekerYEKVIKACALKKDL----------QLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPL 379
Cdd:PRK10895 96 ----------YDNLMAVLQIRDDLsaeqredranELMEEFHIEHLRDSmGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217293410 380 SAVDAeVSRHLFELCICQILHEKITILVT-HQL-QYLKAASQILILKDGKMVQKGTYTEFL 438
Cdd:PRK10895 166 AGVDP-ISVIDIKRIIEHLRDSGLGVLITdHNVrETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
245-429 |
1.47e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 62.58 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-IAYVSQQPWVFsgtLRSNI--LFGKKY---EK 318
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHdITRLKNREVPF---LRRQIgmIFQDHHllmDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 319 ERYEKV----IKACALKKDLQLLEDGDLTVIG--DRGTT----LSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 388
Cdd:PRK10908 95 TVYDNVaiplIIAGASGDDIRRRVSAALDKVGllDKAKNfpiqLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2217293410 389 ---HLFElcicQILHEKITILV-THQLQYLKAAS-QILILKDGKMV 429
Cdd:PRK10908 175 gilRLFE----EFNRVGVTVLMaTHDIGLISRRSyRMLTLSDGHLH 216
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
890-1083 |
1.48e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 64.10 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 890 IVGRTGAGKSSLISALFRLSEPE-GKIWIDKI---------------LTTEI-GLHDLRKKMSIIPQEP--VLFTGTMRK 950
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKyGTIQVGDIyigdkknnhelitnpYSKKIkNFKELRRRVSMVFQFPeyQLFKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 951 NL--DPFNEHTDEELWNALQEVQLKETiedlpGKMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRT 1028
Cdd:PRK13631 137 DImfGPVALGVKKSEAKKLAKFYLNKM-----GLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKG 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 1029 DELIQKKIRE-KFAHCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVLLQNKE 1083
Cdd:PRK13631 212 EHEMMQLILDaKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
889-1069 |
1.66e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.04 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 889 GIVGRTGAGKSSLISALFRLSEP-EGKIWID----KILTTeigLHDLRKKMSIIPQEPVL----------FTGTMRKNLD 953
Cdd:COG1129 34 ALLGENGAGKSTLMKILSGVYQPdSGEILLDgepvRFRSP---RDAQAAGIAIIHQELNLvpnlsvaeniFLGREPRRGG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 954 PFNehtdeelWNALQEvQLKETIEDLpgKMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPR-TDELI 1032
Cdd:COG1129 111 LID-------WRAMRR-RARELLARL--GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEReVERLF 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2217293410 1033 Q--KKIREKfaHCTVLTIAHRLNTIID-SDKIMVLDSGRL 1069
Cdd:COG1129 181 RiiRRLKAQ--GVAIIYISHRLDEVFEiADRVTVLRDGRL 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
877-1069 |
1.68e-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: 62.13 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 877 HLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTeiGLHDLRKKMSIIPQEPVLFTG-TMRKNLD- 953
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQsGRVLINGVDVT--AAPPADRPVSMLFQENNLFAHlTVEQNVGl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 954 ---P---FNEHTDEELWNALQEVQLKETIEDLPGKMdtelaeSGsnfsvGQRQLVCLARAILRKNQILIIDEATANVDP- 1026
Cdd:cd03298 94 glsPglkLTAEDRQAIEVALARVGLAGLEKRLPGEL------SG-----GERQRVALARVLVRDKPVLLLDEPFAALDPa 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2217293410 1027 -RTD--ELIQKKIREKfaHCTVLTIAHRLNTIID-SDKIMVLDSGRL 1069
Cdd:cd03298 163 lRAEmlDLVLDLHAET--KMTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
245-432 |
1.75e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.94 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAV-----LGELAPSHGLVSVHGRIAY---------------VSQQPWVFSG 304
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYspdvdpievrrevgmVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 305 -TLRSNILFGKKYEK---------ERYEKVIKACALKKDLQlledgdlTVIGDRGTTLSGGQKARVNLARAVYQDADIYL 374
Cdd:PRK14267 100 lTIYDNVAIGVKLNGlvkskkeldERVEWALKKAALWDEVK-------DRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 375 LDDPLSAVDAEVSRHLFELcICQILHEKITILVTHQ-LQYLKAASQILILKDGKMVQKG 432
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEEL-LFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
855-1071 |
1.79e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 62.04 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 855 EGVIIFDNVNFMYSPGgplvlkhltaliksQEKVgIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKK 933
Cdd:PRK10247 18 GDAKILNNISFSLRAG--------------EFKL-ITGPSGCGKSTLLKIVASLISPtSGTLLFEGEDISTLKPEIYRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 934 MSIIPQEPVLFTGTMRKNLD-PF---NEHTDEELWNA-LQEVQLKETIedlpgkmdteLAESGSNFSVGQRQLVCLARAI 1008
Cdd:PRK10247 83 VSYCAQTPTLFGDTVYDNLIfPWqirNQQPDPAIFLDdLERFALPDTI----------LTKNIAELSGGEKQRISLIRNL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 1009 LRKNQILIIDEATANVDP----RTDELIQKKIREKfaHCTVLTIAHRLNTIIDSDKIMVLDS--GRLKE 1071
Cdd:PRK10247 153 QFMPKVLLLDEITSALDEsnkhNVNEIIHRYVREQ--NIAVLWVTHDKDEINHADKVITLQPhaGEMQE 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
874-1038 |
1.86e-10 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 62.18 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 874 VLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHD-LRKKMSIIPQEPVLFTG-TMRK 950
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPdSGKILLDGQDITKLPMHKrARLGIGYLPQEASIFRKlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 951 NLDPFNEHTdeELWNALQEVQLKETIEDLpgKMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDE 1030
Cdd:cd03218 95 NILAVLEIR--GLSKKEREEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQ 170
|
....*...
gi 2217293410 1031 LIQKKIRE 1038
Cdd:cd03218 171 DIQKIIKI 178
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
122-429 |
1.86e-10 |
|
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: 64.82 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 122 KEISKILRSSCLRGMNlasFFSASKIIVFVTFttYVLLGSVITASRVFVAVTLYGAVRLTVTLFF---P-----SAIERV 193
Cdd:COG4615 215 QPTAERYRDLRIRADT---IFALANNWGNLLF--FALIGLILFLLPALGWADPAVLSGFVLVLLFlrgPlsqlvGALPTL 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 194 SEAIVSIRRIQTF-LLLDEISQRNRQLPSDgkkmVHVQDFT---------AFWDKASETP-TLQGLSFTVRPGELLAVVG 262
Cdd:COG4615 290 SRANVALRKIEELeLALAAAEPAAADAAAP----PAPADFQtlelrgvtyRYPGEDGDEGfTLGPIDLTIRRGELVFIVG 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 263 PVGAGKSSLLSAVLGELAPSHGLVSVHGRIayVSQQPWvfsGTLRSNI--------LFGKKYEKERYEKVIKACALKKDL 334
Cdd:COG4615 366 GNGSGKSTLAKLLTGLYRPESGEILLDGQP--VTADNR---EAYRQLFsavfsdfhLFDRLLGLDGEADPARARELLERL 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 335 QLleDGDLTVIGDRGTT--LSGGQKARVNLARAVYQDADIYLLD------DPlsavdaeVSRHLFelcICQILHE----- 401
Cdd:COG4615 441 EL--DHKVSVEDGRFSTtdLSQGQRKRLALLVALLEDRPILVFDewaadqDP-------EFRRVF---YTELLPElkarg 508
|
330 340
....*....|....*....|....*...
gi 2217293410 402 KITILVTHQLQYLKAASQILILKDGKMV 429
Cdd:COG4615 509 KTVIAISHDDRYFDLADRVLKMDYGKLV 536
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
886-1071 |
2.03e-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: 64.71 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 886 EKVGIVGRTGAGKSSLISALFRLSEPEGKIWID--KILT-TEIGLHDLRKKMSIIPQEP-------------------VL 943
Cdd:COG4172 313 ETLGLVGESGSGKSTLGLALLRLIPSEGEIRFDgqDLDGlSRRALRPLRRRMQVVFQDPfgslsprmtvgqiiaeglrVH 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 944 FTGtmrknLDPfnEHTDEELWNALQEVQLKetiedlPGKMD---TElaesgsnFSVGQRQLVCLARAILRKNQILIIDEA 1020
Cdd:COG4172 393 GPG-----LSA--AERRARVAEALEEVGLD------PAARHrypHE-------FSGGQRQRIAIARALILEPKLLVLDEP 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 1021 TANVDpRTdelIQKKIREKFA------HCTVLTIAHRLNTI--IdSDKIMVLDSGRLKE 1071
Cdd:COG4172 453 TSALD-VS---VQAQILDLLRdlqrehGLAYLFISHDLAVVraL-AHRVMVMKDGKVVE 506
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
245-472 |
2.06e-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: 64.82 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLG--ELAPSHGLVSVH----------GRIAYVSQQPWVFSGTL------ 306
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHvalcekcgyvERPSKVGEPCPVCGGTLepeevd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 307 --------------RSNILFGKK---YEKER-YEKVIKAC---------ALKKDLQLLEdgdLTVIGDRGT----TLSGG 355
Cdd:TIGR03269 96 fwnlsdklrrrirkRIAIMLQRTfalYGDDTvLDNVLEALeeigyegkeAVGRAVDLIE---MVQLSHRIThiarDLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 356 QKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKITILVT-HQLQYL-KAASQILILKDGKMVQKGT 433
Cdd:TIGR03269 173 EKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTsHWPEVIeDLSDKAIWLENGEIKEEGT 252
|
250 260 270
....*....|....*....|....*....|....*....
gi 2217293410 434 YTEFLKSGIDFGSLLKKDNEESEQPPVPGTPTLRNRTFS 472
Cdd:TIGR03269 253 PDEVVAVFMEGVSEVEKECEVEVGEPIIKVRNVSKRYIS 291
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
245-430 |
2.16e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.55 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQ-PWVFSGTLRSN 309
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttaalaagVAIIYQElHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 310 ILFGKKYEKeryEKVIKACALKKD--LQLLEDG-DLtvigDRGT---TLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 383
Cdd:PRK11288 100 LYLGQLPHK---GGIVNRRLLNYEarEQLEHLGvDI----DPDTplkYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2217293410 384 AEVSRHLFELcICQILHE-KITILVTHQLQYLKAAS-QILILKDGKMVQ 430
Cdd:PRK11288 173 AREIEQLFRV-IRELRAEgRVILYVSHRMEEIFALCdAITVFKDGRYVA 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
245-429 |
2.17e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 64.66 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWVFSG-TLRSN 309
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvrirsprdaialgIGMVHQHFMLVPNlTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 310 IL------FGKKYEKERYEKVIKACALKKDLQLledgDL-TVIGDrgttLSGGQKARVNLARAVYQDADIYLLDDPlSAV 382
Cdd:COG3845 101 IVlgleptKGGRLDRKAARARIRELSERYGLDV----DPdAKVED----LSVGEQQRVEILKALYRGARILILDEP-TAV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2217293410 383 --DAEVsRHLFElcicqILHE-----KITILVTHQLQYLKAAS-QILILKDGKMV 429
Cdd:COG3845 172 ltPQEA-DELFE-----ILRRlaaegKSIIFITHKLREVMAIAdRVTVLRRGKVV 220
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
245-427 |
2.25e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.39 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHG--------LVSVHGRIAYVSQQ----PWvfsgtlrsnilf 312
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGellagtapLAEAREDTRLMFQDarllPW------------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 313 gkkyekeryEKVIKACAL-------KKDLQLLEDGDLTvigDRGT----TLSGGQKARVNLARAVYQDADIYLLDDPLSA 381
Cdd:PRK11247 96 ---------KKVIDNVGLglkgqwrDAALQALAAVGLA---DRANewpaALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2217293410 382 VDAeVSR----HLFELCICQilHEKITILVTHQLQYLKA-ASQILILKDGK 427
Cdd:PRK11247 164 LDA-LTRiemqDLIESLWQQ--HGFTVLLVTHDVSEAVAmADRVLLIEEGK 211
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
248-440 |
2.59e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.50 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 248 LSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWV-------FSGTLR 307
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysyrsqRIRMIFQDPSTslnprqrISQILD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 308 SNILFGKKYEKERYEKVIKAcALKKdLQLLEDGdltvIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVS 387
Cdd:PRK15112 112 FPLRLNTDLEPEQREKQIIE-TLRQ-VGLLPDH----ASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2217293410 388 RHLFELCI-CQILHEKITILVTHQLQYLKAAS-QILILKDGKMVQKGTYTEFLKS 440
Cdd:PRK15112 186 SQLINLMLeLQEKQGISYIYVTQHLGMMKHISdQVLVMHQGEVVERGSTADVLAS 240
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
223-440 |
2.64e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 62.37 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 223 GKKMVHVQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAY-------- 294
Cdd:PRK14246 4 GKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 295 -----------VSQQPWVFSG-TLRSNILFGKKY----EKERYEKVIKACALKKDLqlledgdLTVIGDR----GTTLSG 354
Cdd:PRK14246 84 daiklrkevgmVFQQPNPFPHlSIYDNIAYPLKShgikEKREIKKIVEECLRKVGL-------WKEVYDRlnspASQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 355 GQKARVNLARAVYQDADIYLLDDPLSAVDAeVSRHLFELCICQILHEKITILVTHQLQYL-KAASQILILKDGKMVQKGT 433
Cdd:PRK14246 157 GQQQRLTIARALALKPKVLLMDEPTSMIDI-VNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGS 235
|
....*..
gi 2217293410 434 YTEFLKS 440
Cdd:PRK14246 236 SNEIFTS 242
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
870-1081 |
2.83e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 63.90 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 870 GGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLR----KKMSIIPQEPVLF 944
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPtRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 945 TGTMRKNLDPFN--------EHTDEELWNALQEVQLKETIEDLPGKMdtelaesgsnfSVGQRQLVCLARAILRKNQILI 1016
Cdd:PRK10070 119 PHMTVLDNTAFGmelaginaEERREKALDALRQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217293410 1017 IDEATANVDP--RT---DELIQKKIREKFahcTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVLLQN 1081
Cdd:PRK10070 188 MDEAFSALDPliRTemqDELVKLQAKHQR---TIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
826-1068 |
2.86e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 63.31 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 826 SVERVIEYTDLEKEAPWEYQKRPPPAWPHEGVIIfDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISAL 905
Cdd:PRK13536 9 EAPRRLELSPIERKHQGISEAKASIPGSMSTVAI-DLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 906 FRLSEP-EGKIwidkiltTEIGL------HDLRKKMSIIPQEPVL-FTGTMRKNLDPF------NEHTDEELWNALQEvq 971
Cdd:PRK13536 88 LGMTSPdAGKI-------TVLGVpvparaRLARARIGVVPQFDNLdLEFTVRENLLVFgryfgmSTREIEAVIPSLLE-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 972 lketIEDLPGKMDTELAEsgsnFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIREKFAHC-TVLTIAH 1050
Cdd:PRK13536 159 ----FARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGkTILLTTH 230
|
250 260
....*....|....*....|....
gi 2217293410 1051 ------RLntiidSDKIMVLDSGR 1068
Cdd:PRK13536 231 fmeeaeRL-----CDRLCVLEAGR 249
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
857-1076 |
2.86e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 64.32 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 857 VIIFDNVNFMYspGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKilTTEIGlhdlrkkms 935
Cdd:COG0488 315 VLELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPdSGTVKLGE--TVKIG--------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 936 IIPQEpvlftgtmRKNLDPfnehtDEELWNALQEVQlketiedlPGKMDTELAE-------SG-------SNFSVGQRQL 1001
Cdd:COG0488 382 YFDQH--------QEELDP-----DKTVLDELRDGA--------PGGTEQEVRGylgrflfSGddafkpvGVLSGGEKAR 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217293410 1002 VCLARAILRKNQILIIDEATANVDPRTDELIQKKIREkFAHcTVLTIAH-R--LNTIidSDKIMVLDSGRLKEYDEPY 1076
Cdd:COG0488 441 LALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD-FPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREYPGGY 514
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
886-1069 |
2.89e-10 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 61.68 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 886 EKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDlRKKMSIIP--QEPVLFTG-TMRKNLD----PFNE 957
Cdd:cd03219 27 EIHGLIGPNGAGKTTLFNLISGFLRPtSGSVLFDGEDITGLPPHE-IARLGIGRtfQIPRLFPElTVLENVMvaaqARTG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 958 HTDEELWNALQEVQLKETIED------LPGKMDtELAesgSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPR-TDE 1030
Cdd:cd03219 106 SGLLLARARREEREARERAEEllervgLADLAD-RPA---GELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEeTEE 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2217293410 1031 LIQ--KKIREKfaHCTVLTIAHRLNTIID-SDKIMVLDSGRL 1069
Cdd:cd03219 182 LAEliRELRER--GITVLLVEHDMDVVMSlADRVTVLDQGRV 221
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
238-429 |
3.24e-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: 61.12 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 238 KASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELapsHGLVSV------------------HGRIAYVSQQP 299
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRT---EGNVSVegdihyngipykefaekyPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 300 WVFSG-TLRSNILFgkkyekeryekvikACALKkdlqlledGDLTVigdRGttLSGGQKARVNLARAVYQDADIYLLDDP 378
Cdd:cd03233 93 VHFPTlTVRETLDF--------------ALRCK--------GNEFV---RG--ISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 379 LSAVDAEVSRHLFElCICQILHE-KITILVThqlqyLKAAS--------QILILKDGKMV 429
Cdd:cd03233 146 TRGLDSSTALEILK-CIRTMADVlKTTTFVS-----LYQASdeiydlfdKVLVLYEGRQI 199
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
245-447 |
3.34e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.11 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------------IAYVSQQ-PWVFSGTLRSNI 310
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafarkVAYLPQQlPAAEGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 311 LFGK-----------KYEKERYEKVIKACALKKDLQLLEDgdltvigdrgtTLSGGQKARVNLARAVYQDADIYLLDDPL 379
Cdd:PRK10575 107 AIGRypwhgalgrfgAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 380 SAVDaeVSRHLFELCICQILHEKITILVTHQLQYLKAASQ----ILILKDGKMVQKGTYTEFLKS-------GIDFGSL 447
Cdd:PRK10575 176 SALD--IAHQVDVLALVHRLSQERGLTVIAVLHDINMAARycdyLVALRGGEMIAQGTPAELMRGetleqiyGIPMGIL 252
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
855-1073 |
3.43e-10 |
|
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: 61.39 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 855 EGVIIFDNVNFMyspggplvlkhltalIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHdlrkk 933
Cdd:cd03220 33 GEFWALKDVSFE---------------VPRGERIGLIGRNGAGKSTLLRLLAGIYPPdSGTVTVRGRVSSLLGLG----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 934 MSIIPQ----EPVLFTGTMrKNLDPfnehtdEELWNALQEV----QLKETIeDLPGKmdtelaesgsNFSVGQRQLVCLA 1005
Cdd:cd03220 93 GGFNPEltgrENIYLNGRL-LGLSR------KEIDEKIDEIiefsELGDFI-DLPVK----------TYSSGMKARLAFA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1006 RAILRKNQILIIDEATANVDPRTDELIQKKIREKFAHC-TVLTIAHRLNTIID-SDKIMVLDSGRLKEYD 1073
Cdd:cd03220 155 IATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGkTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
245-432 |
4.21e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.57 E-value: 4.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVL------GEL----APSHG-----LVSVHGRIAYVSQQPwvfSGTL--R 307
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTGLALLrlinsqGEIwfdgQPLHNlnrrqLLPVRHRIQVVFQDP---NSSLnpR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 308 SNIL----------FGKKYEKERYEKVIKAcalkkdlqLLEDG-DLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLD 376
Cdd:PRK15134 379 LNVLqiieeglrvhQPTLSAAQREQQVIAV--------MEEVGlDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217293410 377 DPLSAVDAEVSRHLFELC-ICQILHEKITILVTHQLQYLKA-ASQILILKDGKMVQKG 432
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLkSLQQKHQLAYLFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
858-1068 |
4.27e-10 |
|
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: 59.00 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYspGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILtteiglhdlrkKMSI 936
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPdEGIVTWGSTV-----------KIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 937 IPQepvlftgtmrknldpfnehtdeelwnalqevqlketiedlpgkmdtelaesgsnFSVGQRQLVCLARAILRKNQILI 1016
Cdd:cd03221 68 FEQ------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2217293410 1017 IDEATANVDPRTDELIQKKIREKfaHCTVLTIAH-R--LNTIIdsDKIMVLDSGR 1068
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEY--PGTVILVSHdRyfLDQVA--TKIIELEDGK 144
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
870-1075 |
4.68e-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: 63.67 E-value: 4.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 870 GGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLS--EP-EGKI-----------WID--------------KIL 921
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPtSGRIiyhvalcekcgYVErpskvgepcpvcggTLE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 922 TTEIGL--------HDLRKKMSIIPQEPVLFTGTMR------KNLDPFNEHTDEELWNA---LQEVQLKETIedlpgkmd 984
Cdd:TIGR03269 91 PEEVDFwnlsdklrRRIRKRIAIMLQRTFALYGDDTvldnvlEALEEIGYEGKEAVGRAvdlIEMVQLSHRI-------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 985 TELAEsgsNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIRE--KFAHCTVLTIAHRLNTIID-SDKI 1061
Cdd:TIGR03269 163 THIAR---DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIEDlSDKA 239
|
250
....*....|....
gi 2217293410 1062 MVLDSGRLKEYDEP 1075
Cdd:TIGR03269 240 IWLENGEIKEEGTP 253
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
251-433 |
4.97e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.96 E-value: 4.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 251 TVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------------IAYVSQQP--WVFSGTLRSNIL 311
Cdd:PRK13634 29 SIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitagkknkklkplrkkVGIVFQFPehQLFEETVEKDIC 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 312 FG-------KKYEKERYEKVIKACALKKDLQlledgdltvigDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 383
Cdd:PRK13634 109 FGpmnfgvsEEDAKQKAREMIELVGLPEELL-----------ARSPfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 384 AEVSRHLFELcICQILHEK--ITILVTHQL----QYlkaASQILILKDGKMVQKGT 433
Cdd:PRK13634 178 PKGRKEMMEM-FYKLHKEKglTTVLVTHSMedaaRY---ADQIVVMHKGTVFLQGT 229
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
251-444 |
5.45e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.29 E-value: 5.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 251 TVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSQqpWV---FSGT----LRSNilfGKKYEKERYE- 322
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQ--YIkpdYDGTvedlLRSI---TDDLGSSYYKs 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 323 KVIKACALKKdlqLLEDgdltvigdRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE-------VSRHLFElci 395
Cdd:PRK13409 436 EIIKPLQLER---LLDK--------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlavakAIRRIAE--- 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 396 cqiLHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYT----------EFLKS-GIDF 444
Cdd:PRK13409 502 ---EREATALVVDHDIYMIDYISDRLMVFEGEPGKHGHASgpmdmregmnRFLKElGITF 558
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
856-1068 |
6.09e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.02 E-value: 6.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 856 GVIIFDNVNFMYSPGgplvlkhltaliksqEKVGIVGRTGAGKSSL---ISALFRLSEPEGKIWID-------KILTTEi 925
Cdd:PRK13549 17 GVKALDNVSLKVRAG---------------EIVSLCGENGAGKSTLmkvLSGVYPHGTYEGEIIFEgeelqasNIRDTE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 926 glhdlRKKMSIIPQEPVLFTG-TMRKNLDPFNEHTDEEL--WNALQEvQLKETIEDLpgKMDTELAESGSNFSVGQRQLV 1002
Cdd:PRK13549 81 -----RAGIAIIHQELALVKElSVLENIFLGNEITPGGImdYDAMYL-RAQKLLAQL--KLDINPATPVGNLGLGQQQLV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217293410 1003 CLARAILRKNQILIIDEATANVDPRTDELIQKKIREKFAH-CTVLTIAHRLNTIID-SDKIMVLDSGR 1068
Cdd:PRK13549 153 EIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHgIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
255-432 |
6.18e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 62.35 E-value: 6.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 255 GELLAVVGPVGAGKSSLLSAVLG-ELAPSHGLVSVHGRIAYVsqQP------WVFSG-------TLRSNILFGKKYEK-- 318
Cdd:PRK11000 29 GEFVVFVGPSGCGKSTLLRMIAGlEDITSGDLFIGEKRMNDV--PPaergvgMVFQSyalyphlSVAENMSFGLKLAGak 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 319 --ERYEKVIKACALKKDLQLLEDgdltvigdRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA--------EVSR 388
Cdd:PRK11000 107 keEINQRVNQVAEVLQLAHLLDR--------KPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalrvqmriEISR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2217293410 389 hlfelcicqiLHEKI---TILVTH-QLQYLKAASQILILKDGKMVQKG 432
Cdd:PRK11000 179 ----------LHKRLgrtMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
858-1085 |
6.22e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 61.72 E-value: 6.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYSPGGPL---VLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKIL----TTEIGLHD 929
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTtGTVTVDDITithkTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 930 LRKKMSIIPQ--EPVLFTGTMRKNLD--PFNEHTDEElwnalqevQLKETIEDLPGKMDTE---LAESGSNFSVGQRQLV 1002
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIfgPKNFKMNLD--------EVKNYAHRLLMDLGFSrdvMSQSPFQMSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1003 CLARAILRKNQILIIDEATANVDPRTDELIQ---KKIREKfAHCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVL 1078
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMrllKSLQTD-ENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKEL 233
|
....*..
gi 2217293410 1079 LQNKESL 1085
Cdd:PRK13646 234 FKDKKKL 240
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
251-414 |
6.26e-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: 61.23 E-value: 6.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 251 TVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGL------------------------------VSVHGRIAYVSQQPW 300
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeildefrgselqnyftkllegdVKVIVKPQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 301 VFSGTLRSniLFGKKYEKERYEKVIKACALKKDLqlledgdltvigDRG-TTLSGGQKARVNLARAVYQDADIYLLDDPL 379
Cdd:cd03236 102 AVKGKVGE--LLKKKDERGKLDELVDQLELRHVL------------DRNiDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2217293410 380 SAVD-------AEVSRHLFElcicqilHEKITILVTHQLQYL 414
Cdd:cd03236 168 SYLDikqrlnaARLIRELAE-------DDNYVLVVEHDLAVL 202
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
245-432 |
6.62e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.88 E-value: 6.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWVFSG-TLRSN 309
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhklaaqlgIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 310 ILFGK--------------KYEKERYEKVIKACALKKDLQlledgdlTVIGDrgttLSGGQKARVNLARAVYQDADIYLL 375
Cdd:PRK09700 101 LYIGRhltkkvcgvniidwREMRVRAAMMLLRVGLKVDLD-------EKVAN----LSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 376 DDPLSAVDAEVSRHLFeLCICQILHE-KITILVTHQLQYLKA-ASQILILKDGKMVQKG 432
Cdd:PRK09700 170 DEPTSSLTNKEVDYLF-LIMNQLRKEgTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
864-1069 |
7.83e-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: 60.08 E-value: 7.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 864 NFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKI-LTTEIGlhDLRKKMSIIPQEP 941
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTsGRATVAGHdVVREPR--EVRRRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 942 VLFTG-TMRKNLdpfnehtdeELWNALQEV---QLKETIEDLPGKMdtELAESG----SNFSVGQRQLVCLARAILRKNQ 1013
Cdd:cd03265 83 SVDDElTGWENL---------YIHARLYGVpgaERRERIDELLDFV--GLLEAAdrlvKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1014 ILIIDEATANVDPRTDELIQ---KKIREKFAhCTVLTIAHRLNTIID-SDKIMVLDSGRL 1069
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWeyiEKLKEEFG-MTILLTTHYMEEAEQlCDRVAIIDHGRI 210
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
242-436 |
8.60e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 61.02 E-value: 8.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 242 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR---------------IAYVSQQP--WVFSG 304
Cdd:PRK13636 19 THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkglmklresVGMVFQDPdnQLFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 305 TLRSNILFG----KKYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPL 379
Cdd:PRK13636 99 SVYQDVSFGavnlKLPEDEVRKRVDNA---------LKRTGIEHLKDKPThCLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 380 SAVDAEVSRHLFELCICQILHEKITILV-THQLQYLKA-ASQILILKDGKMVQKGTYTE 436
Cdd:PRK13636 170 AGLDPMGVSEIMKLLVEMQKELGLTIIIaTHDIDIVPLyCDNVFVMKEGRVILQGNPKE 228
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
241-444 |
9.22e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.97 E-value: 9.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSH--GLVSVHG---------RIAYVSQQPWVFSG-TLRS 308
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNrkptkqilkRTGFVTQDDILYPHlTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 309 NILF------GKKYEKEryEKVIKACALKKDLQLLEDGDlTVIGD---RGttLSGGQKARVNLARAVYQDADIYLLDDPL 379
Cdd:PLN03211 160 TLVFcsllrlPKSLTKQ--EKILVAESVISELGLTKCEN-TIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 380 SAVDAEVSRHLFeLCICQILHEKITILVT-HQ--LQYLKAASQILILKDGK--MVQKGTYTEFLKSGIDF 444
Cdd:PLN03211 235 SGLDATAAYRLV-LTLGSLAQKGKTIVTSmHQpsSRVYQMFDSVLVLSEGRclFFGKGSDAMAYFESVGF 303
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
243-402 |
9.43e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 62.96 E-value: 9.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 243 PTL-QGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLV--SVHGRIAYVSQQPwVFSGTLRSNILFgkkYEKE 319
Cdd:PLN03073 522 PLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrSAKVRMAVFSQHH-VDGLDLSSNPLL---YMMR 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 320 RYEKVIKAcALKKDLqlledGDLTVIGDRGT----TLSGGQKARVNLARAVYQDADIYLLDDP-----LSAVDAEVS-RH 389
Cdd:PLN03073 598 CFPGVPEQ-KLRAHL-----GSFGVTGNLALqpmyTLSGGQKSRVAFAKITFKKPHILLLDEPsnhldLDAVEALIQgLV 671
|
170
....*....|...
gi 2217293410 390 LFELCICQILHEK 402
Cdd:PLN03073 672 LFQGGVLMVSHDE 684
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
874-1068 |
9.74e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 60.48 E-value: 9.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 874 VLKHLTALIKSQEKVGIVGRTGAGKSSL---ISALFRLSEpeGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFT----- 945
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLlnaIAGSLPPDS--GSILIDGKDVTKLPEYKRAKYIGRVFQDPMMGTapsmt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 946 -------------------GTMRKNLDPFNEhtdeelwnalqevQLKETIEDLPGKMDTELaesgSNFSVGQRQLVCLAR 1006
Cdd:COG1101 99 ieenlalayrrgkrrglrrGLTKKRRELFRE-------------LLATLGLGLENRLDTKV----GLLSGGQRQALSLLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 1007 AILRKNQILIIDEATANVDPRTDELI----QKKIREKfaHCTVLTIAHRLNTIID-SDKIMVLDSGR 1068
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALDPKTAALVleltEKIVEEN--NLTTLMVTHNMEQALDyGNRLIMMHEGR 226
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
251-444 |
1.12e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.49 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 251 TVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAY----VSQQpwvFSGT----LRSNI---LFGKKYEKE 319
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYkpqyISPD---YDGTveefLRSANtddFGSSYYKTE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 320 ryekVIKACALKKdlqLLEDgdltvigdRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE-------VSRHLFE 392
Cdd:COG1245 439 ----IIKPLGLEK---LLDK--------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlavakAIRRFAE 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 393 lcicqiLHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYT----------EFLKS-GIDF 444
Cdd:COG1245 504 ------NRGKTAMVVDHDIYLIDYISDRLMVFEGEPGVHGHASgpmdmregmnRFLKElGITF 560
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
857-1068 |
1.14e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 60.63 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 857 VIIFDNVNFMYsPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDK--ILTTEIGLHDLRKK 933
Cdd:PRK13636 5 ILKVEELNYNY-SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPsSGRILFDGkpIDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 934 MSIIPQEP--VLFTGTMRKNLD--PFNEHTDE-ELWNALQEVQLKETIEDLPGKMDTELaesgsnfSVGQRQLVCLARAI 1008
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSfgAVNLKLPEdEVRKRVDNALKRTGIEHLKDKPTHCL-------SFGQKKRVAIAGVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 1009 LRKNQILIIDEATANVDPRTDELIQKKIRE--KFAHCTVLTIAHRLNTI-IDSDKIMVLDSGR 1068
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEmqKELGLTIIIATHDIDIVpLYCDNVFVMKEGR 219
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
884-1073 |
1.36e-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: 59.23 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 884 SQEKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKIL--TTEIGLH--DLRKKMSIIPQEPVLFTG-TMRKNLdpfnE 957
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDgGTIVLNGTVlfDSRKKINlpPQQRKIGLVFQQYALFPHlNVRENL----A 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 958 HTDEELWNALQEVQLKETIEDLpgKMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIR 1037
Cdd:cd03297 98 FGLKRKRNREDRISVDELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELK 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 2217293410 1038 E--KFAHCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYD 1073
Cdd:cd03297 176 QikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
863-1054 |
1.65e-09 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 58.91 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 863 VNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKiltTEIGlhdlrkKMSIIPQEP 941
Cdd:TIGR01189 4 RNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDsGEVRWNG---TPLA------EQRDEPHEN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 942 VLFTG---------TMRKNLD---PFNEHTDEELWNALQEVQLKEtIEDLPGkmdtelaesgSNFSVGQRQLVCLARAIL 1009
Cdd:TIGR01189 75 ILYLGhlpglkpelSALENLHfwaAIHGGAQRTIEDALAAVGLTG-FEDLPA----------AQLSAGQQRRLALARLWL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1010 RKNQILIIDEATANVDPRTDELIQKKIRekfAHC-----TVLTIAHRLNT 1054
Cdd:TIGR01189 144 SRRPLWILDEPTTALDKAGVALLAGLLR---AHLarggiVLLTTHQDLGL 190
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
202-413 |
1.70e-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: 61.87 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 202 RIQTF--LLLDEISQRNRQL-------PSDGKKMVHVQDFT-AFWDKasetPTLQGLSFTVRPGELLAVVGPVGAGKSSL 271
Cdd:TIGR03719 289 RLARYeeLLSQEFQKRNETAeiyippgPRLGDKVIEAENLTkAFGDK----LLIDDLSFKLPPGGIVGVIGPNGAGKSTL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 272 LSAVLGELAPSHGLVSVhG---RIAYVSQQpwvfsgtlRSNIlfgkKYEKERYEKVikacalkkdlqllEDG-DLTVIGD 347
Cdd:TIGR03719 365 FRMITGQEQPDSGTIEI-GetvKLAYVDQS--------RDAL----DPNKTVWEEI-------------SGGlDIIKLGK 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 348 R--------------GT-------TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHL------FELCICQILH 400
Cdd:TIGR03719 419 ReipsrayvgrfnfkGSdqqkkvgQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALeeallnFAGCAVVISH 498
|
250
....*....|....*
gi 2217293410 401 EK--ITILVTHQLQY 413
Cdd:TIGR03719 499 DRwfLDRIATHILAF 513
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
858-1085 |
1.89e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.49 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYSPGGPLVLKHL---TALIKSQEKVGIVGRTGAGKSSLISALFRLSEPE-GKI-WI------------DKI 920
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKALdnvSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDtGTIeWIfkdeknkkktkeKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 921 LTTEIGLH-----------DLRKKMSIIPQ--EPVLFTGTMRKNL--DPFNEHTDEElwNALQEVqlKETIEdLPGKMDT 985
Cdd:PRK13651 83 VLEKLVIQktrfkkikkikEIRRRVGVVFQfaEYQLFEQTIEKDIifGPVSMGVSKE--EAKKRA--AKYIE-LVGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 986 ELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPR-TDEL--IQKKIREKFAhcTVLTIAHRLNTIID-SDKI 1061
Cdd:PRK13651 158 YLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEIleIFDNLNKQGK--TIILVTHDLDNVLEwTKRT 235
|
250 260
....*....|....*....|....
gi 2217293410 1062 MVLDSGRLKEYDEPYVLLQNKESL 1085
Cdd:PRK13651 236 IFFKDGKIIKDGDTYDILSDNKFL 259
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
245-429 |
1.91e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.48 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSL---LSAVL------GE-------LAPSH-------GLVSVHGRIAYVSQQpwv 301
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLmkvLSGVYphgtyeGEiifegeeLQASNirdteraGIAIIHQELALVKEL--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 302 fsgTLRSNILFGKKYEKE---RYEKVIKAC-ALKKDLQLLEDGDLTViGDrgttLSGGQKARVNLARAVYQDADIYLLDD 377
Cdd:PRK13549 98 ---SVLENIFLGNEITPGgimDYDAMYLRAqKLLAQLKLDINPATPV-GN----LGLGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2217293410 378 PLSAVDAEVSRHLFELcICQILHEKIT-ILVTHQLQYLKAAS-QILILKDGKMV 429
Cdd:PRK13549 170 PTASLTESETAVLLDI-IRDLKAHGIAcIYISHKLNEVKAISdTICVIRDGRHI 222
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
245-436 |
1.99e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 59.82 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------------IAYVSQQP--WVFSGTLRSN 309
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfVGLVFQNPddQIFSPTVEQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 310 ILFG-------KKYEKERYEKVIKACALKKdlqlledgdltvIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPLSA 381
Cdd:PRK13652 100 IAFGpinlgldEETVAHRVSSALHMLGLEE------------LRDRVPhHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 382 VDAEVSRHLFELCICQILHEKIT-ILVTHQLQYL-KAASQILILKDGKMVQKGTYTE 436
Cdd:PRK13652 168 LDPQGVKELIDFLNDLPETYGMTvIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEE 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
245-433 |
2.10e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 59.12 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWVFSG-TLRSN 309
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKditdwqtakimreaVAIVPEGRRVFSRmTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 310 ILFGKKY-EKERYEKVIKACAlkkDL--QLLEDGdltviGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 386
Cdd:PRK11614 101 LAMGGFFaERDQFQERIKWVY---ELfpRLHERR-----IQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2217293410 387 SRHLFELcICQILHEKITILVTHQ--LQYLKAASQILILKDGKMVQKGT 433
Cdd:PRK11614 173 IQQIFDT-IEQLREQGMTIFLVEQnaNQALKLADRGYVLENGHVVLEDT 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
882-1075 |
2.16e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 61.36 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 882 IKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWI----DKILTTEIGLhDLR----KKMSIIPQEPVLFTgtMRKNL 952
Cdd:TIGR03269 307 VKEGEIFGIVGTSGAGKTTLSKIIAGVLEPtSGEVNVrvgdEWVDMTKPGP-DGRgrakRYIGILHQEYDLYP--HRTVL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 953 DPFNEHTDEELWNALqeVQLKETIEDLPGKMDTELAES-----GSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPR 1027
Cdd:TIGR03269 384 DNLTEAIGLELPDEL--ARMKAVITLKMVGFDEEKAEEildkyPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPI 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2217293410 1028 TDELIQKKI---REKFAHcTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEP 1075
Cdd:TIGR03269 462 TKVDVTHSIlkaREEMEQ-TFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDP 512
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
886-1068 |
2.20e-09 |
|
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: 58.98 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 886 EKVGIVGRTGAGKSSLISALFRLSEP-EGKIW-----IDKILTTEIglhdLRKKMSIIPQEPVLFTG-TMRKNLdpfneh 958
Cdd:cd03224 27 EIVALLGRNGAGKTTLLKTIMGLLPPrSGSIRfdgrdITGLPPHER----ARAGIGYVPEGRRIFPElTVEENL------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 959 tdeEL-WNALQEVQLKETIEDL----PgKMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQ 1033
Cdd:cd03224 97 ---LLgAYARRRAKRKARLERVyelfP-RLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIF 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 2217293410 1034 KKIRE-KFAHCTVLTIAHRLNTIID-SDKIMVLDSGR 1068
Cdd:cd03224 173 EAIRElRDEGVTILLVEQNARFALEiADRAYVLERGR 209
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
859-1085 |
3.17e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 59.32 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 859 IFDNVNFMYS-PGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID--KILTTEIGLHDLRKKM 934
Cdd:PRK13639 1 ILETRDLKYSyPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPtSGEVLIKgePIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 935 SIIPQEP--VLFTGTMRKNL--DPFN-----EHTDEELWNALQEVQLkETIEDLPGKmdtelaesgsNFSVGQRQLVCLA 1005
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEEDVafGPLNlglskEEVEKRVKEALKAVGM-EGFENKPPH----------HLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1006 RAILRKNQILIIDEATANVDPRTDELIQKKIRE-KFAHCTVLTIAHRLNTI-IDSDKIMVLDSGRLKEYDEPYVLLQNKE 1083
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDlNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
..
gi 2217293410 1084 SL 1085
Cdd:PRK13639 230 TI 231
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
858-1094 |
3.46e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 59.37 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYSPGGPL---VLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIG----LHD 929
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPtQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 930 LRKKMSIIPQ--EPVLFTGTMRKNL----DPFNEHTDEELWNALQEVQLKETIEDLPGKMDTELaesgsnfSVGQRQLVC 1003
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVafgpQNFGVSQEEAEALAREKLALVGISESLFEKNPFEL-------SGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1004 LARAILRKNQILIIDEATANVDPR-TDELIQ--KKIREkfAHCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVLL 1079
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKgRKELMTlfKKLHQ--SGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIF 233
|
250
....*....|....*
gi 2217293410 1080 QNKESLFYKmvqQLG 1094
Cdd:PRK13649 234 QDVDFLEEK---QLG 245
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
245-438 |
3.82e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 58.93 E-value: 3.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR----------------IAYVSQQP--------- 299
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplaklnraqrkafrrdIQMVFQDSisavnprkt 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 300 --WVFSGTLRSNILFGKKYEKERYEKVIKACALkkdlqlledgDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDD 377
Cdd:PRK10419 108 vrEIIREPLRHLLSLDKAERLARASEMLRAVDL----------DDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217293410 378 PLSAVDaevsRHLfELCICQIL----HEKIT--ILVTHQLQYL-KAASQILILKDGKMVQKGTYTEFL 438
Cdd:PRK10419 178 AVSNLD----LVL-QAGVIRLLkklqQQFGTacLFITHDLRLVeRFCQRVMVMDNGQIVETQPVGDKL 240
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
245-393 |
3.90e-09 |
|
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: 57.44 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPShglvsvhgriayvsqqpwvfSGTLRsniLFGKKYEKERYEKV 324
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPA--------------------SGEIT---LDGKPVTRRSPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 325 IKA-CALkkdlqLLED-------GDLTV-----IGDRgttLSGG--QKarVNLARAVYQDADIYLLDDPLSAVD----AE 385
Cdd:cd03215 73 IRAgIAY-----VPEDrkreglvLDLSVaeniaLSSL---LSGGnqQK--VVLARWLARDPRVLILDEPTRGVDvgakAE 142
|
....*...
gi 2217293410 386 VSRHLFEL 393
Cdd:cd03215 143 IYRLIREL 150
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
529-830 |
3.91e-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: 59.34 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 529 IVFIFLILLNTAAQVA--YVLQDWWLSYWANKQSMLNVTVNGggnvtekldLNWYLGIYSGLTVATVLFGIARSLLVFYV 606
Cdd:cd18547 2 ILVIILAIISTLLSVLgpYLLGKAIDLIIEGLGGGGGVDFSG---------LLRILLLLLGLYLLSALFSYLQNRLMARV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 607 LVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQTLLQVVGVVSVAVAVIPW---IAI 683
Cdd:cd18547 73 SQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLltlIVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 684 PLVPLGIIFIFL-----RRYFLETSRDVKRLEsttrspvfSHLSSSLQGLWTIRAYKAEERCQELFDAH-QDLHSEAWfl 757
Cdd:cd18547 153 VTVPLSLLVTKFiakrsQKYFRKQQKALGELN--------GYIEEMISGQKVVKAFNREEEAIEEFDEInEELYKASF-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 758 fltTSRWFA------VR-LDAIcaMFVIIVAFGS-LILAKTLDAGQVGLALSYALTLMGMFQwcvrQSAEVENMMIS--- 826
Cdd:cd18547 223 ---KAQFYSgllmpiMNfINNL--GYVLVAVVGGlLVINGALTVGVIQAFLQYSRQFSQPIN----QISQQINSLQSala 293
|
....*
gi 2217293410 827 -VERV 830
Cdd:cd18547 294 gAERV 298
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
889-1069 |
3.93e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.43 E-value: 3.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 889 GIVGRTGAGKSSLISALFRLSEP-EGKIWID----KILTTE------IGlhdlrkkMsiIPQEPVL---FT--------- 945
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGLYQPdSGEILIDgkpvRIRSPRdaialgIG-------M--VHQHFMLvpnLTvaenivlgl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 946 -GTMRKNLDPfnehtdEELWNALQE--------VQLKETIEDLpgkmdtelaesgsnfSVGQRQLVCLARAILRKNQILI 1016
Cdd:COG3845 106 ePTKGGRLDR------KAARARIRElserygldVDPDAKVEDL---------------SVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 1017 IDEATANVDPR-TDELIQ--KKIREkfAHCTVLTIAHRLNTIID-SDKIMVLDSGRL 1069
Cdd:COG3845 165 LDEPTAVLTPQeADELFEilRRLAA--EGKSIIFITHKLREVMAiADRVTVLRRGKV 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
874-1075 |
4.95e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 58.87 E-value: 4.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 874 VLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPE--GKIWIDKILT-TEIGLHDLRKKMSIIPQEPvlftgtmrk 950
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQkgAVLWQGKPLDySKRGLLALRQQVATVFQDP--------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 951 NLDPFNEHTDEELWNALQEVQLKEtiEDLPGKMDTELAESGSN---------FSVGQRQLVCLARAILRKNQILIIDEAT 1021
Cdd:PRK13638 87 EQQIFYTDIDSDIAFSLRNLGVPE--AEITRRVDEALTLVDAQhfrhqpiqcLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217293410 1022 ANVDP--RTDEL-IQKKIREKFAHctVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEP 1075
Cdd:PRK13638 165 AGLDPagRTQMIaIIRRIVAQGNH--VIISSHDIDLIYEiSDAVYVLRQGQILTHGAP 220
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
243-472 |
5.21e-09 |
|
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: 60.80 E-value: 5.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 243 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR------------IAYVSQQPWVFSG-TLRSN 309
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdietnldavrqsLGMCPQHNILFHHlTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 310 ILFGKKYEKERYEKVikacALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRH 389
Cdd:TIGR01257 1024 ILFYAQLKGRSWEEA----QLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 390 LFELcICQILHEKITILVTHQLQYLKA-ASQILILKDGKMVQKGTyTEFLKSGIDFGSLL----KKDNEESEQPPVPGTP 464
Cdd:TIGR01257 1100 IWDL-LLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT-PLFLKNCFGTGFYLtlvrKMKNIQSQRGGCEGTC 1177
|
....*...
gi 2217293410 465 TLRNRTFS 472
Cdd:TIGR01257 1178 SCTSKGFS 1185
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
235-436 |
8.40e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.56 E-value: 8.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 235 FWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-IAYVSQQPW---------VFSG 304
Cdd:PRK15079 27 FWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdLLGMKDDEWravrsdiqmIFQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 305 TL-----RSNI---------LFGKKYEKERYEKVIKACALKkdLQLLEDgdltVIGDRGTTLSGGQKARVNLARAVYQDA 370
Cdd:PRK15079 107 PLaslnpRMTIgeiiaeplrTYHPKLSRQEVKDRVKAMMLK--VGLLPN----LINRYPHEFSGGQCQRIGIARALILEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 371 DIYLLDDPLSAVDAEVSRHLFELciCQILHEKI---TILVTHQLQYLKAAS-QILILKDGKMVQKGTYTE 436
Cdd:PRK15079 181 KLIICDEPVSALDVSIQAQVVNL--LQQLQREMglsLIFIAHDLAVVKHISdRVLVMYLGHAVELGTYDE 248
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
824-1075 |
8.55e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 57.40 E-value: 8.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 824 MISVERV-IEY------TDLEKEAPWEYQKRPppawpHEGVIIFDNVNFMYSPGgplvlkhltaliksqEKVGIVGRTGA 896
Cdd:COG1134 4 MIEVENVsKSYrlyhepSRSLKELLLRRRRTR-----REEFWALKDVSFEVERG---------------ESVGIIGRNGA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 897 GKSSLISALFRLSEP-EGKIWIDKILTTEIGL-----HDL--RkkmsiipqEPVLFTGTM----RKNLDpfnEHTDE--- 961
Cdd:COG1134 64 GKSTLLKLIAGILEPtSGRVEVNGRVSALLELgagfhPELtgR--------ENIYLNGRLlglsRKEID---EKFDEive 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 962 --ELWNALqevqlketieDLPGK-----MDTELAesgsnFSVgqrqlvclarAILRKNQILIIDEATAnVdprTDELIQK 1034
Cdd:COG1134 133 faELGDFI----------DQPVKtyssgMRARLA-----FAV----------ATAVDPDILLVDEVLA-V---GDAAFQK 183
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2217293410 1035 K----IREKFAH-CTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEP 1075
Cdd:COG1134 184 KclarIRELRESgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDP 230
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
840-1071 |
8.96e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.60 E-value: 8.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 840 APWEYQKRPPPAWPHEGVIIFDNVNFMYSPGGpLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID 918
Cdd:PRK10522 305 APYKAEFPRPQAFPDWQTLELRNVTFAYQDNG-FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPqSGEILLD 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 919 KILTTEIGLHDLRKKMSIIPQEPVLFTgtmrKNLDPFNEHTDEEL---WNALQEVQLKETIEDlpGKMdtelaeSGSNFS 995
Cdd:PRK10522 384 GKPVTAEQPEDYRKLFSAVFTDFHLFD----QLLGPEGKPANPALvekWLERLKMAHKLELED--GRI------SNLKLS 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 996 VGQRQLVCLARAILRKNQILIIDEATANVDPR------TDELIQKKIREKfahcTVLTIAHRLNTIIDSDKIMVLDSGRL 1069
Cdd:PRK10522 452 KGQKKRLALLLALAEERDILLLDEWAADQDPHfrrefyQVLLPLLQEMGK----TIFAISHDDHYFIHADRLLEMRNGQL 527
|
..
gi 2217293410 1070 KE 1071
Cdd:PRK10522 528 SE 529
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
210-440 |
1.03e-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: 60.03 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 210 DEISQRNRQLPSDGKK--MVHVQDFTAFWDKASeTPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHG--- 284
Cdd:TIGR01257 1919 DDVAEERQRIISGGNKtdILRLNELTKVYSGTS-SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGdat 1997
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 285 ---------LVSVHGRIAYVSQqpwvFSGTlrSNILFGKK--YEKERYEKVIKACALKKDLQLLEDGDLTVIGDR-GTTL 352
Cdd:TIGR01257 1998 vagksiltnISDVHQNMGYCPQ----FDAI--DDLLTGREhlYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRlAGTY 2071
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 353 SGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKITILVTHQLQYLKA-ASQILILKDGKMVQK 431
Cdd:TIGR01257 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCL 2151
|
....*....
gi 2217293410 432 GTyTEFLKS 440
Cdd:TIGR01257 2152 GT-IQHLKS 2159
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
245-429 |
1.08e-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: 59.07 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLG----------------ELAPSH-------GLVSVHGRIAYVSQQpwv 301
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdgeiywsgsPLKASNirdteraGIVIIHQELTLVPEL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 302 fsgTLRSNILFGK----KYEKERYEKVIKAC-ALKKDLQLLEDGDLTVIGDRGttlsGGQKARVNLARAVYQDADIYLLD 376
Cdd:TIGR02633 94 ---SVAENIFLGNeitlPGGRMAYNAMYLRAkNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2217293410 377 DPLSAVDAEVSRHLFELCICQILHEKITILVTHQLQYLKAAS-QILILKDGKMV 429
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCdTICVIRDGQHV 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
245-432 |
1.09e-08 |
|
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: 56.38 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGElapsHGLVSVHGRIAYVSQqpwvfsgtlrsNILFGKKYEKER---- 320
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH----PKYEVTEGEILFKGE-----------DITDLPPEERARlgif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 321 ----YEKVIKACALKKDLQLLEDGdltvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcIC 396
Cdd:cd03217 81 lafqYPPEIPGVKNADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEV-IN 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2217293410 397 QILHEKIT-ILVTHQ---LQYLKaASQILILKDGKMVQKG 432
Cdd:cd03217 149 KLREEGKSvLIITHYqrlLDYIK-PDRVHVLYDGRIVKSG 187
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
867-1069 |
1.38e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 57.09 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 867 YSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALF-RLSEPEGKIWIDKILTTEIGLHDLRKKMSIIPQEPVL-- 943
Cdd:PRK13548 10 VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSgELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 944 -FT-------GTMRKNLDPfnEHTDEELWNALQEVQLketiEDLPGKMDTELaeSGsnfsvGQRQLVCLARAILR----- 1010
Cdd:PRK13548 90 pFTveevvamGRAPHGLSR--AEDDALVAAALAQVDL----AHLAGRDYPQL--SG-----GEQQRVQLARVLAQlwepd 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217293410 1011 -KNQILIIDEATANVDPRTDELIQKKIREkFAH---CTVLTIAHRLN-TIIDSDKIMVLDSGRL 1069
Cdd:PRK13548 157 gPPRWLLLDEPTSALDLAHQHHVLRLARQ-LAHergLAVIVVLHDLNlAARYADRIVLLHQGRL 219
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
855-1051 |
1.41e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 58.99 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 855 EGVIIFDNVNFMySPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLisalFRLSepeGKIW--IDKILTTeiglhDLRK 932
Cdd:TIGR00954 449 DNGIKFENIPLV-TPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSL----FRIL---GELWpvYGGRLTK-----PAKG 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 933 KMSIIPQEPVLFTGTMRKNL------DPFNEH--TDEELWNALQEVQLKETIEDlPGKMDTeLAESGSNFSVGQRQLVCL 1004
Cdd:TIGR00954 516 KLFYVPQRPYMTLGTLRDQIiypdssEDMKRRglSDKDLEQILDNVQLTHILER-EGGWSA-VQDWMDVLSGGEKQRIAM 593
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2217293410 1005 ARAILRKNQILIIDEATANVDPRTDELIQKKIREkfAHCTVLTIAHR 1051
Cdd:TIGR00954 594 ARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHR 638
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
890-1073 |
1.44e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 57.96 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 890 IVGRTGAGKSSLISALFRLSEP-EGKIWI-DKIltteigLHDLRKKMSIIP---------QEPVLFTG-TMRKNLDPFNE 957
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPqKGRIVLnGRV------LFDAEKGICLPPekrrigyvfQDARLFPHyKVRGNLRYGMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 958 HTDEELWNALqeVQLKeTIEDLpgkmdteLAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVD-PRTDELI---Q 1033
Cdd:PRK11144 103 KSMVAQFDKI--VALL-GIEPL-------LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRELLpylE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2217293410 1034 KKIREkfAHCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYD 1073
Cdd:PRK11144 173 RLARE--INIPILYVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
857-1069 |
1.57e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 56.42 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 857 VIIFDNVNFMYSpGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPE-GKIW-----IDKILTTEIGLhdL 930
Cdd:PRK10908 1 MIRFEHVSKAYL-GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSaGKIWfsghdITRLKNREVPF--L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 931 RKKMSIIPQEP-VLFTGTMRKNLD-PF------NEHTDEELWNALQEVQLKETIEDLPGKMdtelaesgsnfSVGQRQLV 1002
Cdd:PRK10908 78 RRQIGMIFQDHhLLMDRTVYDNVAiPLiiagasGDDIRRRVSAALDKVGLLDKAKNFPIQL-----------SGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1003 CLARAILRKNQILIIDEATANVDPRTDELIQkKIREKFAH--CTVLTIAHRLNTIIDSD-KIMVLDSGRL 1069
Cdd:PRK10908 147 GIARAVVNKPAVLLADEPTGNLDDALSEGIL-RLFEEFNRvgVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
580-795 |
1.61e-08 |
|
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: 57.19 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 580 WYLGIYSGLTVATVLFGIARSLLVFYVLVNssqtLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLD 659
Cdd:cd18557 41 ILLAIYLLQSVFTFVRYYLFNIAGERIVAR----LRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 660 FIQTLLQvVGVVSVAVAVIPW-----IAIPLVPLGIIFIFLRRYFLETSRDVkrLESTTRSPvfSHLSSSLQGLWTIRAY 734
Cdd:cd18557 117 LLRNILQ-VIGGLIILFILSWkltlvLLLVIPLLLIASKIYGRYIRKLSKEV--QDALAKAG--QVAEESLSNIRTVRSF 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 735 KAEERCQELFDAH-QDLHSEAWFLFLTTSRWFAV-RLDAICAMFVIIVAFGSLILAKTLDAGQ 795
Cdd:cd18557 192 SAEEKEIRRYSEAlDRSYRLARKKALANALFQGItSLLIYLSLLLVLWYGGYLVLSGQLTVGE 254
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
241-383 |
1.83e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.73 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------RIAYvsQQPWVFSG---------T 305
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikkdLCTY--QKQLCFVGhrsginpylT 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217293410 306 LRSNILFGKKYEKERYEkVIKACALKKdLQLLEDGDLTVigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 383
Cdd:PRK13540 91 LRENCLYDIHFSPGAVG-ITELCRLFS-LEHLIDYPCGL-------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
526-1075 |
1.89e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 58.27 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 526 AHWIVFIFLILLNTAAQVAYVlqdWWLSywankqsMLNVTVNGGGNVtekldLNWYLGIYSGLTVATVLFGIArSLLVFY 605
Cdd:COG4615 10 ESRWLLLLALLLGLLSGLANA---GLIA-------LINQALNATGAA-----LARLLLLFAGLLVLLLLSRLA-SQLLLT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 606 VLVNssQTLHN---KMFESILKAPVLFFDRnpIG--RILNRFSKDIGHLDDLLPLtfldfIQTLLQVVGVVSVAVAVIPW 680
Cdd:COG4615 74 RLGQ--HAVARlrlRLSRRILAAPLERLER--IGaaRLLAALTEDVRTISQAFVR-----LPELLQSVALVLGCLAYLAW 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 681 IAIPL-------VPLGIIFIFLRRY----FLETSRDvkrlestTRSPVFSHLSSSLQGLWTIRAYKAeeRCQELFDAH-- 747
Cdd:COG4615 145 LSPPLflltlvlLGLGVAGYRLLVRrarrHLRRARE-------AEDRLFKHFRALLEGFKELKLNRR--RRRAFFDEDlq 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 748 ------QDLHSEAWFLFLTTSRWfavrldAICAMFVIIVAFgsLILAKTLDAGQVGLALSYALTLMGMfqwcvrqSAEVE 821
Cdd:COG4615 216 ptaeryRDLRIRADTIFALANNW------GNLLFFALIGLI--LFLLPALGWADPAVLSGFVLVLLFL-------RGPLS 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 822 NMM----------ISVERV--IEyTDLEKEAPWEYQKRPPPAWPHEGVIIFDNVNFMYSPG--------GPLvlkHLTal 881
Cdd:COG4615 281 QLVgalptlsranVALRKIeeLE-LALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEdgdegftlGPI---DLT-- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 882 IKSQEKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFtgtmRKNLDPFNEHTD 960
Cdd:COG4615 355 IRRGELVFIVGGNGSGKSTLAKLLTGLYRPEsGEILLDGQPVTADNREAYRQLFSAVFSDFHLF----DRLLGLDGEADP 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 961 EELWNALQEVQLKE--TIEDlpGK-MDTELaesgsnfSVGQRQLVCLARAILRKNQILIIDEATANVDPR-----TDELI 1032
Cdd:COG4615 431 ARARELLERLELDHkvSVED--GRfSTTDL-------SQGQRKRLALLVALLEDRPILVFDEWAADQDPEfrrvfYTELL 501
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1033 QK-KIREKfahcTVLTIAHrlntiiD------SDKIMVLDSGRLKEYDEP 1075
Cdd:COG4615 502 PElKARGK----TVIAISH------DdryfdlADRVLKMDYGKLVELTGP 541
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
241-436 |
2.41e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 56.46 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAV--LGELAPS---HGLVSVHG-------------RIAYVSQQP-WV 301
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYPEarvSGEVYLDGqdifkmdvielrrRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 302 FSGTLRSNILFGKKY------EKERYEKVIKacALKKdLQLLEDgdltvIGDR----GTTLSGGQKARVNLARAVYQDAD 371
Cdd:PRK14247 95 PNLSIFENVALGLKLnrlvksKKELQERVRW--ALEK-AQLWDE-----VKDRldapAGKLSGGQQQRLCIARALAFQPE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 372 IYLLDDPLSAVDAEVSRHLFELCIcQILHEKITILVTH-QLQYLKAASQILILKDGKMVQKGTYTE 436
Cdd:PRK14247 167 VLLADEPTANLDPENTAKIESLFL-ELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
857-1079 |
2.85e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 56.28 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 857 VIIFDNVNFMYsPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKMS 935
Cdd:PRK13647 4 IIEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQrGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 936 IIPQEP--VLFTGTMRKNL--DPFN-----EHTDEELWNALQEVQLKETIEDLPgkmdtelaesgSNFSVGQRQLVCLAR 1006
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVafGPVNmgldkDEVERRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217293410 1007 AILRKNQILIIDEATANVDPRTDELIQKKIREKFAHCTVLTIA-HRLNTIID-SDKIMVLDSGRLKEYDEPYVLL 1079
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKSLLT 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
259-440 |
2.97e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 56.26 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 259 AVVGPVGAGKSSLL-----------------SAVLG--ELAPSHGLVSVHGRIAYVSQQPWVFSGTLRSNILFGKKYEKE 319
Cdd:PRK14271 51 SLMGPTGSGKTTFLrtlnrmndkvsgyrysgDVLLGgrSIFNYRDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 320 RYEKVIKACALKKdlqLLEDGDLTVIGDRGTT----LSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELci 395
Cdd:PRK14271 131 VPRKEFRGVAQAR---LTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEF-- 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2217293410 396 CQILHEKIT-ILVTHQL-QYLKAASQILILKDGKMVQKGTYTEFLKS 440
Cdd:PRK14271 206 IRSLADRLTvIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
248-444 |
3.25e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 56.28 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 248 LSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSV-----------------HGRIAYVSQQP--WVFSGTLRS 308
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstskqkeikpvRKKVGVVFQFPesQLFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 309 NILFGKK---YEKERYEKV----IKACALKKdlQLLEDGDLTvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSA 381
Cdd:PRK13643 105 DVAFGPQnfgIPKEKAEKIaaekLEMVGLAD--EFWEKSPFE--------LSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 382 VDAEVSRHLFELciCQILHE--KITILVTHQLQYL-KAASQILILKDGKMVQKGTYTEFLKSgIDF 444
Cdd:PRK13643 175 LDPKARIEMMQL--FESIHQsgQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVFQE-VDF 237
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
241-388 |
3.29e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.35 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGEL--APSHGLVSVhgriayvsqqPWVFSGTLRSNI-LFGKKYE 317
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDV----------PDNQFGREASLIdAIGRKGD 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217293410 318 KERYEKVIKACALkkdlqlledGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 388
Cdd:COG2401 112 FKDAVELLNAVGL---------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
860-1050 |
3.52e-08 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 55.52 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 860 FDNVNFMYSPGgplvlkhltaliksqEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKI-----LTT--EIGLHDLR 931
Cdd:COG4778 27 LDGVSFSVAAG---------------ECVALTGPSGAGKSTLLKCIYGNYLPdSGSILVRHDggwvdLAQasPREILALR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 932 KK--------MSIIPQ--------EPVLFTGTMRKN--------LDPFNehTDEELWNAlqevqlketiedlpgkmdtel 987
Cdd:COG4778 92 RRtigyvsqfLRVIPRvsaldvvaEPLLERGVDREEarararelLARLN--LPERLWDL--------------------- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217293410 988 aeSGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIRE-KFAHCTVLTIAH 1050
Cdd:COG4778 149 --PPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEaKARGTAIIGIFH 210
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
876-1074 |
3.64e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 55.94 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 876 KHLTALIksqekvgivGRTGAGKSSLISALFRLSE--PE----GKIWID--KILTTEIGLHDLRKKMSIIPQEPVLFTGT 947
Cdd:PRK14239 31 NEITALI---------GPSGSGKSTLLRSINRMNDlnPEvtitGSIVYNghNIYSPRTDTVDLRKEIGMVFQQPNPFPMS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 948 MRKNLD---PFNEHTDEELWNALQEVQLKE-TIEDlpgKMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATAN 1023
Cdd:PRK14239 102 IYENVVyglRLKGIKDKQVLDEAVEKSLKGaSIWD---EVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2217293410 1024 VDPRTDELIQK---KIREKFahcTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDE 1074
Cdd:PRK14239 179 LDPISAGKIEEtllGLKDDY---TMLLVTRSMQQASRiSDRTGFFLDGDLIEYND 230
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
870-1067 |
4.18e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.37 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 870 GGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPEGKiwidkilTTEIGLHDLRK-------KMSI--IPQE 940
Cdd:PRK15439 22 SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSG-------TLEIGGNPCARltpakahQLGIylVPQE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 941 PVLFTG-TMRKNLD---PFNEHTDEELWNALQE--VQLKetiedlpgkmdteLAESGSNFSVGQRQLVCLARAILRKNQI 1014
Cdd:PRK15439 95 PLLFPNlSVKENILfglPKRQASMQKMKQLLAAlgCQLD-------------LDSSAGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2217293410 1015 LIIDEATANVDPRTDELIQKKIREKFAH-CTVLTIAHRLNTIID-SDKIMVLDSG 1067
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIRELLAQgVGIVFISHKLPEIRQlADRISVMRDG 216
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
858-1038 |
4.48e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 55.41 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYspGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPE-GKIWI-----DkiLTTEIG---LH 928
Cdd:PRK11124 3 IQLNGINCFY--GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRsGTLNIagnhfD--FSKTPSdkaIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 929 DLRKKMSIIPQE----PVLftgTMRKNL--DPFN------EHTDEELWNALQEVQLKETIEDLPgkmdteLAESGsnfsv 996
Cdd:PRK11124 79 ELRRNVGMVFQQynlwPHL---TVQQNLieAPCRvlglskDQALARAEKLLERLRLKPYADRFP------LHLSG----- 144
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2217293410 997 GQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIRE 1038
Cdd:PRK11124 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRE 186
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
254-429 |
5.46e-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: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 254 PGELLAVVGPVGAGKSSLLSAVLGELAPSHGlvsvhgriayvsqqpwvfsgtlrsnilfgkkyekeryeKVIKACALKKD 333
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG--------------------------------------GVIYIDGEDIL 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 334 LQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQIL-----HEKITILVT 408
Cdd:smart00382 43 EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLlllksEKNLTVILT 122
|
170 180
....*....|....*....|.
gi 2217293410 409 HQLQYLKAASQILILKDGKMV 429
Cdd:smart00382 123 TNDEKDLGPALLRRRFDRRIV 143
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
858-1086 |
5.55e-08 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 54.94 E-value: 5.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYspGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHdlRKKMSI 936
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPtSGEILLDGKDITNLPPH--KRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 937 IPQEPVLFT----------GTMRKNLDPfnEHTDEELWNALQEVQLketiEDLPGKMDTELaeSGsnfsvGQRQLVCLAR 1006
Cdd:cd03300 77 VFQNYALFPhltvfeniafGLRLKKLPK--AEIKERVAEALDLVQL----EGYANRKPSQL--SG-----GQQQRVAIAR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1007 AILRKNQILIIDEATANVDP--RTD---EL--IQKKIREKFAHCT-----VLTIahrlntiidSDKIMVLDSGRLKEYDE 1074
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLklRKDmqlELkrLQKELGITFVFVThdqeeALTM---------SDRIAVMNKGKIQQIGT 214
|
250
....*....|..
gi 2217293410 1075 PYVLLQNKESLF 1086
Cdd:cd03300 215 PEEIYEEPANRF 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
874-1075 |
6.12e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 55.58 E-value: 6.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 874 VLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQEP--VLFTGTMRK 950
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPtSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 951 NL--DPFNEHTDEE-----LWNALQEVQLKETIEDLPgkmdtelaesgSNFSVGQRQLVCLARAILRKNQILIIDEATAN 1023
Cdd:PRK13652 99 DIafGPINLGLDEEtvahrVSSALHMLGLEELRDRVP-----------HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 1024 VDPR-TDELIQ--KKIREKFAHcTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEP 1075
Cdd:PRK13652 168 LDPQgVKELIDflNDLPETYGM-TVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTV 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
858-1069 |
6.71e-08 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 54.18 E-value: 6.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYspGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDlrKKMSI 936
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPtSGRIYIGGRDVTDLPPKD--RDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 937 IPQEPVLFTG-TMRKNLdPFN---EHTDEELWNAlqevQLKETIEDLpgKMDTELAESGSNFSVGQRQLVCLARAILRKN 1012
Cdd:cd03301 77 VFQNYALYPHmTVYDNI-AFGlklRKVPKDEIDE----RVREVAELL--QIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 1013 QILIIDEATANVDPRT-----DEL--IQKKIREKFAHCT-----VLTIAhrlntiidsDKIMVLDSGRL 1069
Cdd:cd03301 150 KVFLMDEPLSNLDAKLrvqmrAELkrLQQRLGTTTIYVThdqveAMTMA---------DRIAVMNDGQI 209
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
870-1067 |
9.01e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 53.65 E-value: 9.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 870 GGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPEGkiwiDKILTTEIGLHDLRKkmsiIPQEPVLFTG--- 946
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLA----GRVLLNGGPLDFQRD----SIARGLLYLGhap 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 947 ------TMRKNLDPFNE-HTDEELWNALQEVQLKeTIEDLPGkmdtelaesgSNFSVGQRQLVCLARAILRKNQILIIDE 1019
Cdd:cd03231 83 gikttlSVLENLRFWHAdHSDEQVEEALARVGLN-GFEDRPV----------AQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 1020 ATANVDPRTDELIQKKIRekfAHC-----TVLTIAHRLNtiIDSDKIMVLDSG 1067
Cdd:cd03231 152 PTTALDKAGVARFAEAMA---GHCarggmVVLTTHQDLG--LSEAGARELDLG 199
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
245-430 |
9.74e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.95 E-value: 9.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSL---LSAVL------------GELA--------PSHGLVSVHGRIAYVSQQpwv 301
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLmkvLSGVYphgsyegeilfdGEVCrfkdirdsEALGIVIIHQELALIPYL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 302 fsgTLRSNILFGKkyEKERY------EKVIKACALKKDLQLLEDGDlTVIGDRGTtlsgGQKARVNLARAVYQDADIYLL 375
Cdd:NF040905 94 ---SIAENIFLGN--ERAKRgvidwnETNRRARELLAKVGLDESPD-TLVTDIGV----GKQQLVEIAKALSKDVKLLIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 376 DDPLSAVDAEVSRHLFELcICQILHEKIT-ILVTHQL-QYLKAASQILILKDGKMVQ 430
Cdd:NF040905 164 DEPTAALNEEDSAALLDL-LLELKAQGITsIIISHKLnEIRRVADSITVLRDGRTIE 219
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
871-1083 |
1.30e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 54.13 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 871 GPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRL-SEPEGKIWIDKILTTEIGLHD-LRKKMSIIPQEPVLFtgtm 948
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIvPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIF---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 949 rKNLDPF-NEHTDEELWNALQEVQLKETIEDLPGKMD-TELAES-GSNFSVGQRQLVCLARAILRKNQILIIDEATANVD 1025
Cdd:PRK10895 91 -RRLSVYdNLMAVLQIRDDLSAEQREDRANELMEEFHiEHLRDSmGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1026 PRTDELIQKKIRE-KFAHCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVLLQNKE 1083
Cdd:PRK10895 170 PISVIDIKRIIEHlRDSGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
251-411 |
1.57e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 251 TVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHG-------------------------------LVSVHgRIAYVSQQP 299
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGdyeeepswdevlkrfrgtelqnyfkklyngeIKVVH-KPQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 300 WVFSGTLRSniLFGKKYEKERYEKVIKACALKKDLqlledgdltvigDRG-TTLSGGQKARVNLARAVYQDADIYLLDDP 378
Cdd:PRK13409 174 KVFKGKVRE--LLKKVDERGKLDEVVERLGLENIL------------DRDiSELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2217293410 379 LSAVD-------AEVSRHLFElcicqilhEKITILVTHQL 411
Cdd:PRK13409 240 TSYLDirqrlnvARLIRELAE--------GKYVLVVEHDL 271
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
241-433 |
1.59e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 54.37 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------------RIAYVSQQP--WV 301
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstsknkdikqirkKVGLVFQFPesQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 302 FSGTLRSNILFGKK---YEKERYEKVikacALKKdlqlledgdLTVIG------DRGT-TLSGGQKARVNLARAVYQDAD 371
Cdd:PRK13649 99 FEETVLKDVAFGPQnfgVSQEEAEAL----AREK---------LALVGiseslfEKNPfELSGGQMRRVAIAGILAMEPK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217293410 372 IYLLDDPLSAVDAEVSRHLFELciCQILHEK-ITI-LVTHQLQYL-KAASQILILKDGKMVQKGT 433
Cdd:PRK13649 166 ILVLDEPTAGLDPKGRKELMTL--FKKLHQSgMTIvLVTHLMDDVaNYADFVYVLEKGKLVLSGK 228
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
243-432 |
1.64e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 53.94 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 243 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPshGLVSVHGRIAY--VSQQPWVFSGTLRSNIL------FG- 313
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVLLdgKPVAPCALRGRKIATIMqnprsaFNp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 314 ----KKYEKERYEKVIKACALKKDLQLLEDGDLtviGDRGTTL-------SGGQKARVNLARAVYQDADIYLLDDPLSAV 382
Cdd:PRK10418 95 lhtmHTHARETCLALGKPADDATLTAALEAVGL---ENAARVLklypfemSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 383 DAEVSRHLFELcICQILHEKI--TILVTHQLQYL-KAASQILILKDGKMVQKG 432
Cdd:PRK10418 172 DVVAQARILDL-LESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQG 223
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
254-435 |
1.64e-07 |
|
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: 51.98 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 254 PGELLAVVGPVGAGKSSLLSAVLgelapshglvsvhgriayvsqqpWVFSGtlRSNILFGKKYEKERYekvIKACAlkkD 333
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIG-----------------------LALGG--AQSATRRRSGVKAGC---IVAAV---S 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 334 LQLLedgdLTVIGdrgttLSGGQKARVNLARAV----YQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKITILVTH 409
Cdd:cd03227 69 AELI----FTRLQ-----LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITH 139
|
170 180
....*....|....*....|....*.
gi 2217293410 410 QLQYLKAASQILILkdgKMVQKGTYT 435
Cdd:cd03227 140 LPELAELADKLIHI---KKVITGVYK 162
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
882-1070 |
1.75e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 55.22 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 882 IKSQEKVGIVGRTGAGKSSLISALFRLSEP--EGKIWID-KILTTEIGLHDLRKKMSIIPQE-------PVLFTGtmrKN 951
Cdd:TIGR02633 283 LRRGEILGVAGLVGAGRTELVQALFGAYPGkfEGNVFINgKPVDIRNPAQAIRAGIAMVPEDrkrhgivPILGVG---KN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 952 --LDPFNEHTDEELWNALQEVQ-LKETIEDLPGKMDTELAESGSnFSVGQRQLVCLARAILRKNQILIIDEATANVDPRT 1028
Cdd:TIGR02633 360 itLSVLKSFCFKMRIDAAAELQiIGSAIQRLKVKTASPFLPIGR-LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2217293410 1029 DELIQKKI----REKFAhctVLTIAHRLNTIID-SDKIMVLDSGRLK 1070
Cdd:TIGR02633 439 KYEIYKLInqlaQEGVA---IIVVSSELAEVLGlSDRVLVIGEGKLK 482
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
870-1068 |
2.43e-07 |
|
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: 54.83 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 870 GGPLVLKHLTALIKSQEKVGIVGRTGAGKSSL---ISALFRLSEPEGKIWIDKILTTEIGLHDL-RKKMSIIPQEPVLFT 945
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLmkiLSGVYPHGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 946 G-TMRKNLDPFNEHT-------DEELW----NALQEVQLKetiedlpgkmDTELAESGSNFSVGQRQLVCLARAILRKNQ 1013
Cdd:TIGR02633 92 ElSVAENIFLGNEITlpggrmaYNAMYlrakNLLRELQLD----------ADNVTRPVGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 1014 ILIIDEATANVDPRTDELIQKKIREKFAH-CTVLTIAHRLNTIID-SDKIMVLDSGR 1068
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAHgVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
245-439 |
2.60e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 53.94 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------RIAYVSQQPWVFsG-------------T 305
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfkrRKEFARRIGVVF-GqrsqlwwdlpaidS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 306 LRsniLFGKKYE--KERYEKVIKACAlkkdlQLLEDGDLTVIGDRgtTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 383
Cdd:COG4586 117 FR---LLKAIYRipDAEYKKRLDELV-----ELLDLGELLDTPVR--QLSLGQRMRCELAAALLHRPKILFLDEPTIGLD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 384 AEVSRHLFELcICQILHE-KITILVT-HQLQYLKA-ASQILILKDGKMVQKGTYTEFLK 439
Cdd:COG4586 187 VVSKEAIREF-LKEYNRErGTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
855-1068 |
3.01e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 53.66 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 855 EGVIIFDNVNFMYspGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPE-GKIWI-DKILTTEIglHDLRK 932
Cdd:PRK13537 5 VAPIDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDaGSISLcGEPVPSRA--RHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 933 KMSIIPQ----EPVLftgTMRKNLDPFNEHTDEELWNALQEVQLKETIEDLPGKMDTELAEsgsnFSVGQRQLVCLARAI 1008
Cdd:PRK13537 81 RVGVVPQfdnlDPDF---TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 1009 LRKNQILIIDEATANVDPRTDELIQKKIREKFAHC-TVLTIAH------RLntiidSDKIMVLDSGR 1068
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGkTILLTTHfmeeaeRL-----CDRLCVIEEGR 215
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
245-428 |
3.03e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.47 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG----------RIAYVSQ------QPWVFSGTLRS 308
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqmdeeaRAKLRAKhvgfvfQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 309 -------NILFGkkyEKERYEKViKACALKKDLQLledgdltviGDR----GTTLSGGQKARVNLARAVYQDADIYLLDD 377
Cdd:PRK10584 106 lenvelpALLRG---ESSRQSRN-GAKALLEQLGL---------GKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 378 PLSAVDAEVSRHLFELcICQILHEKIT--ILVTHQLQYLKAASQILILKDGKM 428
Cdd:PRK10584 173 PTGNLDRQTGDKIADL-LFSLNREHGTtlILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
251-393 |
3.72e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.41 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 251 TVRPGELLAVVGPVGAGKSSLLSAVLGELAP------------------------------SHGLVSVHGRIAYVSQQPW 300
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPnlgdydeepswdevlkrfrgtelqdyfkklANGEIKVAHKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 301 VFSGTLRSnILfgKKY-EKERYEKVIKACALKKDLqlleDGDLtvigdrgTTLSGGQKARVNLARAVYQDADIYLLDDPL 379
Cdd:COG1245 175 VFKGTVRE-LL--EKVdERGKLDELAEKLGLENIL----DRDI-------SELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170
....*....|....*...
gi 2217293410 380 SAVD----AEVSRHLFEL 393
Cdd:COG1245 241 SYLDiyqrLNVARLIREL 258
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
233-383 |
4.41e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 52.70 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 233 TAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSH---------------GLVSVHGRIAYVSQ 297
Cdd:PRK13638 5 SDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKgavlwqgkpldyskrGLLALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 298 QP--WVFSGTLRSNILFGKK----YEKERYEKVIKACALkKDLQLLEDGDLTVigdrgttLSGGQKARVNLARAVYQDAD 371
Cdd:PRK13638 85 DPeqQIFYTDIDSDIAFSLRnlgvPEAEITRRVDEALTL-VDAQHFRHQPIQC-------LSHGQKKRVAIAGALVLQAR 156
|
170
....*....|..
gi 2217293410 372 IYLLDDPLSAVD 383
Cdd:PRK13638 157 YLLLDEPTAGLD 168
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
243-412 |
4.56e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.87 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 243 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGE--LAPSHGLVsVHGR--------------IAYVSQQ---PWVFS 303
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhpQGYSNDLT-LFGRrrgsgetiwdikkhIGYVSSSlhlDYRVS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 304 GTLRSNILFGKKYEKERYEKVIKAcalkkdLQLLEDGDLTVIGDRGTT-------LSGGQKARVNLARAVYQDADIYLLD 376
Cdd:PRK10938 353 TSVRNVILSGFFDSIGIYQAVSDR------QQKLAQQWLDILGIDKRTadapfhsLSWGQQRLALIVRALVKHPTLLILD 426
|
170 180 190
....*....|....*....|....*....|....*...
gi 2217293410 377 DPLSAVDAeVSRHLFELCICQILHEKITIL--VTHQLQ 412
Cdd:PRK10938 427 EPLQGLDP-LNRQLVRRFVDVLISEGETQLlfVSHHAE 463
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
875-1075 |
5.59e-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: 51.96 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 875 LKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID-------KILTTEIGL----HDLRKKMSIIpqEPV 942
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPdSGTILFGgedatdvPVQERNVGFvfqhYALFRHMTVF--DNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 943 LFTGTMRKNLDPFNEHT-DEELWNALQEVQLKETIEDLPgkmdtelaesgSNFSVGQRQLVCLARAILRKNQILIIDEAT 1021
Cdd:cd03296 96 AFGLRVKPRSERPPEAEiRAKVHELLKLVQLDWLADRYP-----------AQLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217293410 1022 ANVDPRTDELIQKKIREKF--AHCTVLTIAHRLNTIID-SDKIMVLDSGRLKE-------YDEP 1075
Cdd:cd03296 165 GALDAKVRKELRRWLRRLHdeLHVTTVFVTHDQEEALEvADRVVVMNKGRIEQvgtpdevYDHP 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
859-1069 |
6.07e-07 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 51.94 E-value: 6.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 859 IFDNVNFMYSPGgplvlkHLTALIksqekvgivGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKMSII 937
Cdd:PRK11231 17 ILNDLSLSLPTG------KITALI---------GPNGCGKSTLLKCFARLLTPQsGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 938 PQEPVLFTGTMRKNL-----DPFNEH------TDEELWN-ALQEVQlketIEDLPGKMDTELaeSGsnfsvGQRQLVCLA 1005
Cdd:PRK11231 82 PQHHLTPEGITVRELvaygrSPWLSLwgrlsaEDNARVNqAMEQTR----INHLADRRLTDL--SG-----GQRQRAFLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 1006 RAILRKNQILIIDEATANVD-PRTDELIqKKIRE-KFAHCTVLTIAHRLNTIID-SDKIMVLDSGRL 1069
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDiNHQVELM-RLMRElNTQGKTVVTVLHDLNQASRyCDHLVVLANGHV 216
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
223-390 |
6.71e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 6.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 223 GKKMVHVQDFT-AFWDKasetpTL-QGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVhG---RIAYVSQ 297
Cdd:PRK11819 321 GDKVIEAENLSkSFGDR-----LLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GetvKLAYVDQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 298 QpwvfsgtlRSNIlfgkKYEKERYEKVikacalkkdlqllEDG-DLTVIGDR--------------GT-------TLSGG 355
Cdd:PRK11819 395 S--------RDAL----DPNKTVWEEI-------------SGGlDIIKVGNReipsrayvgrfnfkGGdqqkkvgVLSGG 449
|
170 180 190
....*....|....*....|....*....|....*
gi 2217293410 356 QKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHL 390
Cdd:PRK11819 450 ERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRAL 484
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
254-428 |
6.98e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.64 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 254 PGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--RIAYVSQQPWVFsgtLRSNilfgkkyekERYEKVIKACALK 331
Cdd:PRK10636 337 PGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKgiKLGYFAQHQLEF---LRAD---------ESPLQHLARLAPQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 332 KDLQLLED--GDLTVIGDRGTT----LSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICqilHEKITI 405
Cdd:PRK10636 405 ELEQKLRDylGGFGFQGDKVTEetrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALID---FEGALV 481
|
170 180
....*....|....*....|....
gi 2217293410 406 LVTHQLQYLKAASQILIL-KDGKM 428
Cdd:PRK10636 482 VVSHDRHLLRSTTDDLYLvHDGKV 505
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
578-830 |
9.29e-07 |
|
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: 52.05 E-value: 9.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 578 LNWYLGIYSGLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTF 657
Cdd:cd18542 38 LWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 658 LDFIQTLLqVVGVVSVAVAVIPW----IAIPLVPlgIIFIFLRRYFletsrdvKRLEsttrsPVFSH-------LSSSLQ 726
Cdd:cd18542 118 VELVRAVL-LFIGALIIMFSINWkltlISLAIIP--FIALFSYVFF-------KKVR-----PAFEEireqegeLNTVLQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 727 ----GLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAIC-AMFVIIVAFGS-LILAKTLDAGQVGLAL 800
Cdd:cd18542 183 enltGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSgLQIVLVLWVGGyLVINGEITLGELVAFI 262
|
250 260 270
....*....|....*....|....*....|....
gi 2217293410 801 SYaltlMGMFQWCVRQSAEVENMM----ISVERV 830
Cdd:cd18542 263 SY----LWMLIWPVRQLGRLINDMsrasASAERI 292
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
248-438 |
9.54e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 9.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 248 LSFTvrPGELLAVVGPVGAGKSSLLS--AVL-----GELAPSHGLvsvhgRIAYVSQQPWV-FSGTLRSNILFG---KKY 316
Cdd:PRK11819 28 LSFF--PGAKIGVLGLNGAGKSTLLRimAGVdkefeGEARPAPGI-----KVGYLPQEPQLdPEKTVRENVEEGvaeVKA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 317 EKERYEKV------------------------IKAC-ALKKDLQL--------LEDGDLTVigdrgTTLSGGQKARVNLA 363
Cdd:PRK11819 101 ALDRFNEIyaayaepdadfdalaaeqgelqeiIDAAdAWDLDSQLeiamdalrCPPWDAKV-----TKLSGGERRRVALC 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 364 RAVYQDADIYLLDDPLSAVDAE-VS---RHL--FELCIcqilhekitILVTHQLQYL-KAASQILILKDGKMVQ-KGTYT 435
Cdd:PRK11819 176 RLLLEKPDMLLLDEPTNHLDAEsVAwleQFLhdYPGTV---------VAVTHDRYFLdNVAGWILELDRGRGIPwEGNYS 246
|
...
gi 2217293410 436 EFL 438
Cdd:PRK11819 247 SWL 249
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
252-439 |
1.00e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 50.26 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 252 VRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-RIAYVSQQpwvfsgtlrsnilfgkkyekeryekvikacal 330
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQY-------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 331 kkdlqlledgdltvigdrgTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE-------VSRHLFElcicqiLHEKI 403
Cdd:cd03222 70 -------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnaarAIRRLSE------EGKKT 124
|
170 180 190
....*....|....*....|....*....|....*.
gi 2217293410 404 TILVTHQLQYLKAASQILILKDGkmvQKGTYTEFLK 439
Cdd:cd03222 125 ALVVEHDLAVLDYLSDRIHVFEG---EPGVYGIASQ 157
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
245-386 |
1.06e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.89 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG----------------RIAYVSQQPWvfsGTL-- 306
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqdllkadpeaqkllrqKIQIVFQNPY---GSLnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 307 RSNIlfGKKYE-----------KERYEKVikacalkkdLQLLEdgdltVIGDRGT-------TLSGGQKARVNLARAVYQ 368
Cdd:PRK11308 108 RKKV--GQILEepllintslsaAERREKA---------LAMMA-----KVGLRPEhydryphMFSGGQRQRIAIARALML 171
|
170
....*....|....*...
gi 2217293410 369 DADIYLLDDPLSAVDAEV 386
Cdd:PRK11308 172 DPDVVVADEPVSALDVSV 189
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
237-439 |
1.23e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 51.63 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 237 DKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--------------RIAYVSQQP--W 300
Cdd:PRK13633 18 EESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeenlwdirnKAGMVFQNPdnQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 301 VFSGTLRSNILFG-------KKYEKERYEKVIKACAL---KKDLQLLedgdltvigdrgttLSGGQKARVNLARAVYQDA 370
Cdd:PRK13633 98 IVATIVEEDVAFGpenlgipPEEIRERVDESLKKVGMyeyRRHAPHL--------------LSGGQKQRVAIAGILAMRP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217293410 371 DIYLLDDPLSAVDA----EVSRHLFELCicqiLHEKIT-ILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLK 439
Cdd:PRK13633 164 ECIIFDEPTAMLDPsgrrEVVNTIKELN----KKYGITiILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
889-1069 |
1.33e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.22 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 889 GIVGRTGAGKSSLISALFRLSEP-EGKIWID----KILTTEIGLHdlrKKMSIIPQE----PVLftgTMRKNLdpFNEH- 958
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGNYQPdAGSILIDgqemRFASTTAALA---AGVAIIYQElhlvPEM---TVAENL--YLGQl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 959 ------TDEELWNALQEVQLKETIEDL-PgkmDTELAEsgsnFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDEL 1031
Cdd:PRK11288 106 phkggiVNRRLLNYEAREQLEHLGVDIdP---DTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2217293410 1032 IQKKIREKFAHCTV-LTIAHRLNTIID-SDKIMVLDSGRL 1069
Cdd:PRK11288 179 LFRVIRELRAEGRViLYVSHRMEEIFAlCDAITVFKDGRY 218
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
5-203 |
1.52e-06 |
|
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: 51.40 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 5 KTTTGQIVNLLSNDVNKFDQ-VTVFLHFLWAGPLQAIAVTA-LLWMEIGIScLAGMAVLIILLPLQSCFGK----LFSSL 78
Cdd:cd07346 92 RNRTGDLMSRLTSDVDAVQNlVSSGLLQLLSDVLTLIGALViLFYLNWKLT-LVALLLLPLYVLILRYFRRrirkASREV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 79 RSKTATFTdariRTMNEVITGIRIIKMYAWEKS----FSNLITNLRKKEISKILRSSCLRGMnLASFFSASKIIVFVtFT 154
Cdd:cd07346 171 RESLAELS----AFLQESLSGIRVVKAFAAEEReierFREANRDLRDANLRAARLSALFSPL-IGLLTALGTALVLL-YG 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 155 TYVLLGSVITASrVFVAVTLYgavrlTVTLFFPsaIERVSE-------AIVSIRRI 203
Cdd:cd07346 245 GYLVLQGSLTIG-ELVAFLAY-----LGMLFGP--IQRLANlynqlqqALASLERI 292
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
870-1086 |
1.64e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 51.64 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 870 GGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHdlRKKMSIIPQEPVLF---- 944
Cdd:PRK11432 17 GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPtEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFphms 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 945 ----TGTMRKNLDPFNEHTDEELWNALQEVqlketieDLPGKMDTELAEsgsnFSVGQRQLVCLARAILRKNQILIIDEA 1020
Cdd:PRK11432 95 lgenVGYGLKMLGVPKEERKQRVKEALELV-------DLAGFEDRYVDQ----ISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 1021 TANVDPRTDELIQKKIRE--KFAHCTVLTIAH-RLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNKESLF 1086
Cdd:PRK11432 164 LSNLDANLRRSMREKIRElqQQFNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
582-830 |
2.05e-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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 51.03 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 582 LGIYSGLTVATVLFGIARSLLVFYVLVNSSQ-TLHN---KMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTF 657
Cdd:cd18565 53 LWLLGGLTVAAFLLESLFQYLSGVLWRRFAQrVQHDlrtDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 658 LDFIQTLLQVVGVVSVAVAVIPWIA-IPLVPLGIIFIFLRRYfletSRDVKRLESTTRSPV---FSHLSSSLQGLWTIRA 733
Cdd:cd18565 133 NSIIRVVVTVLGIGAILFYLNWQLAlVALLPVPLIIAGTYWF----QRRIEPRYRAVREAVgdlNARLENNLSGIAVIKA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 734 YKAE--ERcQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAMFVIIVAFGSL-------ILAKTLDAGqvglALSYAL 804
Cdd:cd18565 209 FTAEdfER-ERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYwvldgppLFTGTLTVG----TLVTFL 283
|
250 260 270
....*....|....*....|....*....|
gi 2217293410 805 TLMGMFQWCVRQSAEV----ENMMISVERV 830
Cdd:cd18565 284 FYTQRLLWPLTRLGDLidqyQRAMASAKRV 313
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
614-784 |
2.53e-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: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 614 LHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTF----LDFIqTLLQVVGVVSVAVAVIPWIAIPLVPlg 689
Cdd:cd18554 81 IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLmniwLDMI-TIIIAICIMLVLNPKLTFVSLVIFP-- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 690 iIFIFLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFD-AHQDLHSEAwflfLTTSRWFAVR 768
Cdd:cd18554 158 -FYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDkRNGHFLTRA----LKHTRWNAKT 232
|
170 180
....*....|....*....|
gi 2217293410 769 LDAICAMF----VIIVAFGS 784
Cdd:cd18554 233 FSAVNTITdlapLLVIGFAA 252
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
859-1038 |
2.86e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 50.15 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 859 IFDNVNfMYSPGGplvlkHLTAliksqekvgIVGRTGAGKSSLISALFRLSEPE-GKIWID--KILT-TEIGLHDLRKKM 934
Cdd:PRK11831 22 IFDNIS-LTVPRG-----KITA---------IMGPSGIGKTTLLRLIGGQIAPDhGEILFDgeNIPAmSRSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 935 SIIPQEPVLFTG-TMRKNLD-PFNEHTD--EELWNA-----LQEVQLKETIEDLPgkmdtelaesgSNFSVGQRQLVCLA 1005
Cdd:PRK11831 87 SMLFQSGALFTDmNVFDNVAyPLREHTQlpAPLLHStvmmkLEAVGLRGAAKLMP-----------SELSGGMARRAALA 155
|
170 180 190
....*....|....*....|....*....|...
gi 2217293410 1006 RAILRKNQILIIDEATANVDPRTDELIQKKIRE 1038
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISE 188
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
247-438 |
2.92e-06 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 51.34 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 247 GLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSV----------------HGR----IAYVSQQPWVFS-GT 305
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgpdgRGRakryIGILHQEYDLYPhRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 306 LRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE 385
Cdd:TIGR03269 382 VLDNLTEAIGLELPDELARMKAVITLKMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPI 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 386 VSRHLFElcicQILH-----EKITILVTHQLQY-LKAASQILILKDGKMVQKGTYTEFL 438
Cdd:TIGR03269 462 TKVDVTH----SILKareemEQTFIIVSHDMDFvLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
831-1069 |
3.32e-06 |
|
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: 49.64 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 831 IEYTDLEKEapweYQKRPPPAWPHEGVIIFDNVNFMYSPggplVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSE 910
Cdd:cd03267 1 IEVSNLSKS----YRVYSKEPGLIGSLKSLFKRKYREVE----ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 911 P-EGKI-------WIDKIltteiglhDLRKKMSIIPQE--------PVLftgtmrknlDPFNEHTDeeLWNaLQEVQLKE 974
Cdd:cd03267 73 PtSGEVrvaglvpWKRRK--------KFLRRIGVVFGQktqlwwdlPVI---------DSFYLLAA--IYD-LPPARFKK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 975 TIEDLPGKMDTE--LAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIRE--KFAHCTVLTIAH 1050
Cdd:cd03267 133 RLDELSELLDLEelLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEynRERGTTVLLTSH 212
|
250 260
....*....|....*....|
gi 2217293410 1051 RLNTIID-SDKIMVLDSGRL 1069
Cdd:cd03267 213 YMKDIEAlARRVLVIDKGRL 232
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
577-795 |
3.45e-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: 50.10 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 577 DLNWYLGIYSGLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLT 656
Cdd:cd18541 38 QLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 657 FLDFIQTLLQVVGVVSVAVAVIPWIA----IPLVPLGIIFIFLRRYFLETSRDVKrlESttrspvFSHLSSSLQ----GL 728
Cdd:cd18541 118 ILYLVDALFLGVLVLVMMFTISPKLTlialLPLPLLALLVYRLGKKIHKRFRKVQ--EA------FSDLSDRVQesfsGI 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 729 WTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAM-FVIIVAFGS-LILAKTLDAGQ 795
Cdd:cd18541 190 RVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLsFLIVLWYGGrLVIRGTITLGD 258
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
828-1069 |
3.73e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.55 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 828 ERVIEYTD---LEKEAPwEYQK--------RPPPAWPhEGVIIfDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGA 896
Cdd:TIGR01257 891 ERALEKTEpltEEMEDP-EHPEgindsffeRELPGLV-PGVCV-KNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGA 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 897 GKSSLISALFRLSEPEGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLDPFNEHTDEELWNALQeVQLKETI 976
Cdd:TIGR01257 968 GKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQ-LEMEAML 1046
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 977 EDLpgKMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTI- 1055
Cdd:TIGR01257 1047 EDT--GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEAd 1124
|
250
....*....|....
gi 2217293410 1056 IDSDKIMVLDSGRL 1069
Cdd:TIGR01257 1125 LLGDRIAIISQGRL 1138
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
874-1065 |
3.95e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 49.73 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 874 VLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILttEIGLhdLRKKMSIIPQEPVLFTGTMRknL 952
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPdEGVIKRNGKL--RIGY--VPQKLYLDTTLPLTVNRFLR--L 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 953 DPFNEHTDeeLWNALQEVQLKETIEDLPGKMdtelaesgsnfSVGQRQLVCLARAILRKNQILIIDEATANVDPRTD--- 1029
Cdd:PRK09544 93 RPGTKKED--ILPALKRVQAGHLIDAPMQKL-----------SGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQval 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 2217293410 1030 -ELIQKKIREkfAHCTVLTIAHRLNTII-DSDKIMVLD 1065
Cdd:PRK09544 160 yDLIDQLRRE--LDCAVLMVSHDLHLVMaKTDEVLCLN 195
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
584-666 |
4.31e-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: 49.85 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 584 IYSGLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQT 663
Cdd:cd18572 41 LLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRN 120
|
...
gi 2217293410 664 LLQ 666
Cdd:cd18572 121 LVQ 123
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
214-372 |
4.48e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.80 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 214 QRNRQLPSDGKKMVHVQDFTAfwDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-- 291
Cdd:COG3845 245 RVEKAPAEPGEVVLEVENLSV--RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEdi 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 292 ------------IAYVSQQPW----VFSGTLRSNILFGkKYEKERYEK--VIKACALKKD-LQLLEDGDL--TVIGDRGT 350
Cdd:COG3845 323 tglsprerrrlgVAYIPEDRLgrglVPDMSVAENLILG-RYRRPPFSRggFLDRKAIRAFaEELIEEFDVrtPGPDTPAR 401
|
170 180
....*....|....*....|....
gi 2217293410 351 TLSGG--QKarVNLARAVYQDADI 372
Cdd:COG3845 402 SLSGGnqQK--VILARELSRDPKL 423
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
858-1086 |
5.69e-06 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 49.71 E-value: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYspGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSL---ISALFRLSEpeGKIWID-KILTteiglhDL--- 930
Cdd:COG3842 6 LELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLlrmIAGFETPDS--GRILLDgRDVT------GLppe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 931 RKKMSIIPQEPVLF---T-------GTMRKNLDPfnEHTDEELWNALQEVQLketiEDLPGKMDTELaeSGsnfsvGQRQ 1000
Cdd:COG3842 76 KRNVGMVFQDYALFphlTvaenvafGLRMRGVPK--AEIRARVAELLELVGL----EGLADRYPHQL--SG-----GQQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 1001 LVCLARAILRKNQILIIDEATANVDPRT-----DEL--IQKKIRekfahCTVLTIAHrlntiiD-------SDKIMVLDS 1066
Cdd:COG3842 143 RVALARALAPEPRVLLLDEPLSALDAKLreemrEELrrLQRELG-----ITFIYVTH------DqeealalADRIAVMND 211
|
250 260
....*....|....*....|
gi 2217293410 1067 GRLKEYDEPYVLLQNKESLF 1086
Cdd:COG3842 212 GRIEQVGTPEEIYERPATRF 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
861-1070 |
5.70e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.31 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 861 DNVNFMyspggplvlkhltalIKSQEKVGIVGRTGAGKSSLISALFRlSEP---EGKIWID-KILTTEIGLHDL------ 930
Cdd:PRK13549 279 DDVSFS---------------LRRGEILGIAGLVGAGRTELVQCLFG-AYPgrwEGEIFIDgKPVKIRNPQQAIaqgiam 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 931 ----RKKMSIIPQEPVLFTGTMrKNLDPFNEHTdeELWNALQEVQLKETIEDLPGKMDTELAESGsNFSVGQRQLVCLAR 1006
Cdd:PRK13549 343 vpedRKRDGIVPVMGVGKNITL-AALDRFTGGS--RIDDAAELKTILESIQRLKVKTASPELAIA-RLSGGNQQKAVLAK 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 1007 AILRKNQILIIDEATANVDPRTDELIQKKIREKFA-HCTVLTIAHRLNTIID-SDKIMVLDSGRLK 1070
Cdd:PRK13549 419 CLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQqGVAIIVISSELPEVLGlSDRVLVMHEGKLK 484
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
860-1082 |
5.76e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 49.11 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 860 FDNVNFMYspGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALfrLSEP---EGKIWID-KILTTEIGLHDLRKKMS 935
Cdd:PRK11614 8 FDKVSAHY--GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTL--CGDPratSGRIVFDgKDITDWQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 936 IIPQEPVLFTG-TMRKNLDPFNEHTDEElwnalQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQI 1014
Cdd:PRK11614 84 IVPEGRRVFSRmTVEENLAMGGFFAERD-----QFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 1015 LIIDEATANVDP----RTDELIQkKIREKfaHCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVLLQNK 1082
Cdd:PRK11614 159 LLLDEPSLGLAPiiiqQIFDTIE-QLREQ--GMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALLANE 228
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
245-410 |
8.85e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.11 E-value: 8.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAP---SHGLVSVHGR---------IAYVSQQ-----------PWV 301
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRpldssfqrsIGYVQQQdlhlptstvreSLR 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 302 FSGTLR-SNILfgKKYEKERY-EKVIKacalkkdlqLLEDGDL--TVIGDRGTTLSGGQKARVNLA-RAVYQDADIYLLD 376
Cdd:TIGR00956 859 FSAYLRqPKSV--SKSEKMEYvEEVIK---------LLEMESYadAVVGVPGEGLNVEQRKRLTIGvELVAKPKLLLFLD 927
|
170 180 190
....*....|....*....|....*....|....*....
gi 2217293410 377 DPLSAVDAEVSrhlfeLCICQILHEKI----TILVT-HQ 410
Cdd:TIGR00956 928 EPTSGLDSQTA-----WSICKLMRKLAdhgqAILCTiHQ 961
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
587-830 |
9.68e-06 |
|
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: 48.96 E-value: 9.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 587 GLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQTLLQ 666
Cdd:cd18552 47 GLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 667 vVGVVSVAVAVIPW----IAIPLVPL-GIIFIFLRRYFLETSRDVkrLESTTRspVFSHLSSSLQGLWTIRAYKAEERCQ 741
Cdd:cd18552 127 -VIGLLGVLFYLDWkltlIALVVLPLaALPIRRIGKRLRKISRRS--QESMGD--LTSVLQETLSGIRVVKAFGAEDYEI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 742 ELFDAhqdlhsEAWFLFLTTSRWFAVR---------LDAICAMFVIIVAfGSLILAKTLDAGQVglaLSYaLTLMGMFQW 812
Cdd:cd18552 202 KRFRK------ANERLRRLSMKIARARalssplmelLGAIAIALVLWYG-GYQVISGELTPGEF---ISF-ITALLLLYQ 270
|
250 260
....*....|....*....|..
gi 2217293410 813 CVRQ----SAEVENMMISVERV 830
Cdd:cd18552 271 PIKRlsnvNANLQRGLAAAERI 292
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
245-433 |
1.04e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 48.38 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVL-----------GELAPSHGLVSVH---GRIAYVSQQPwvFSGTLRSN- 309
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLypalarrlhlkKEQPGNHDRIEGLehiDKVIVIDQSP--IGRTPRSNp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 310 -----------ILF-----GKKYEKE----RYE-KVI----------------KACALKKDLQLLEDGDLTVI--GDRGT 350
Cdd:cd03271 89 atytgvfdeirELFcevckGKRYNREtlevRYKgKSIadvldmtveealeffeNIPKIARKLQTLCDVGLGYIklGQPAT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 351 TLSGGQKARVNLARAVYQDAD---IYLLDDPLSAVDAEVSRHLFElcicqILHEKI----TILVT-HQLQYLKAASQILI 422
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLE-----VLQRLVdkgnTVVVIeHNLDVIKCADWIID 243
|
250
....*....|....*..
gi 2217293410 423 L------KDGKMVQKGT 433
Cdd:cd03271 244 LgpeggdGGGQVVASGT 260
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
886-1072 |
1.29e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.57 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 886 EKVGIVGRTGAGKSSLISALFRLSEPEGKIW------IDKILT-TEIGLHDLR-KKMSIIPQEPVlftgtmrKNLDPFNE 957
Cdd:PRK09473 43 ETLGIVGESGSGKSQTAFALMGLLAANGRIGgsatfnGREILNlPEKELNKLRaEQISMIFQDPM-------TSLNPYMR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 958 HTDEelwnaLQEVQL-------KETIEDLPGKMDT-ELAESGS-------NFSVGQRQLVCLARAILRKNQILIIDEATA 1022
Cdd:PRK09473 116 VGEQ-----LMEVLMlhkgmskAEAFEESVRMLDAvKMPEARKrmkmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTT 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2217293410 1023 NVDPRTDELIQKKIRE---KFaHCTVLTIAHRLNTIIDS-DKIMVLDSGRLKEY 1072
Cdd:PRK09473 191 ALDVTVQAQIMTLLNElkrEF-NTAIIMITHDLGVVAGIcDKVLVMYAGRTMEY 243
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
247-433 |
1.46e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 48.06 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 247 GLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-IAYVSQQPWVFSGTLR------------------ 307
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQhIEGLPGHQIARMGVVRtfqhvrlfremtvienll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 308 --------SNILFG-------KKYEKEryekvikacALKKDLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDAD 371
Cdd:PRK11300 103 vaqhqqlkTGLFSGllktpafRRAESE---------ALDRAATWLERVGLLEHANRqAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217293410 372 IYLLDDPLSAVDAEVSRHLFELcICQILHE-KITI-LVTHQLQYLKAAS-QILILKDGKMVQKGT 433
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDEL-IAELRNEhNVTVlLIEHDMKLVMGISdRIYVVNQGTPLANGT 237
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
245-421 |
1.55e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.55 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVlgeLAPSHGLVSVHGRIAYvSQQPWVFSGTLRSNILFGKKYekeryekv 324
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG---LYASGKARLISFLPKF-SRNKLIFIDQLQFLIDVGLGY-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 325 ikacalkkdlqlledgdLTvIGDRGTTLSGGQKARVNLARAVYQDAD--IYLLDDPLSAVDAEVSRHLFElCICQILHEK 402
Cdd:cd03238 79 -----------------LT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLE-VIKGLIDLG 139
|
170 180
....*....|....*....|
gi 2217293410 403 IT-ILVTHQLQYLKAASQIL 421
Cdd:cd03238 140 NTvILIEHNLDVLSSADWII 159
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
874-1069 |
1.57e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 48.95 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 874 VLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPEGKIWidKILTTEIG------LHDLRKK-MSIIPQE------ 940
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTY--RVAGQDVAtldadaLAQLRREhFGFIFQRyhllsh 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 941 ---------PVLFTGTMRKNldpfNEHTDEELwnaLQEVQLKETIEDLPGKMdtelaesgsnfSVGQRQLVCLARAILRK 1011
Cdd:PRK10535 101 ltaaqnvevPAVYAGLERKQ----RLLRAQEL---LQRLGLEDRVEYQPSQL-----------SGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217293410 1012 NQILIIDEATANVDPRTDE---LIQKKIREKfAHcTVLTIAHRLNTIIDSDKIMVLDSGRL 1069
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEevmAILHQLRDR-GH-TVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
882-1065 |
1.93e-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: 47.40 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 882 IKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDkiltteiglhdlRKKMSIIPQE-PVLFTGTMRKNL----DPF 955
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPdEGDIEIE------------LDTVSYKPQYiKADYEGTVRDLLssitKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 956 NEHT--DEELWNALQevqlketIEDLpgkMDTELAEsgsnFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQ 1033
Cdd:cd03237 90 YTHPyfKTEIAKPLQ-------IEQI---LDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMAS 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 2217293410 1034 KKIReKFA---HCTVLTIAHRLnTIID--SDKIMVLD 1065
Cdd:cd03237 156 KVIR-RFAennEKTAFVVEHDI-IMIDylADRLIVFE 190
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
245-429 |
2.46e-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: 46.47 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSaVL---GELAPSHGLVSVHGR---------IAYVSQQPwVFSG--TLRSNI 310
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLD-VLagrKTAGVITGEILINGRpldknfqrsTGYVEQQD-VHSPnlTVREAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 311 LFgkkyekeryekvikACALkkdlqlledgdltvigdRGttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSrhl 390
Cdd:cd03232 101 RF--------------SALL-----------------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA--- 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2217293410 391 feLCICQILhEKI-----TILVT-HQ--LQYLKAASQILILK-DGKMV 429
Cdd:cd03232 145 --YNIVRFL-KKLadsgqAILCTiHQpsASIFEKFDRLLLLKrGGKTV 189
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
222-469 |
2.92e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.31 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 222 DGKKMVHVQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVS------------- 287
Cdd:PRK10261 8 DARDVLAVENLNiAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrrrsrqv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 288 -------------VHGR-IAYVSQQPWVfsgTLRSNILFGKKY-EKER-YEKVIKACALKKDLQLLEDGDL----TVIGD 347
Cdd:PRK10261 88 ielseqsaaqmrhVRGAdMAMIFQEPMT---SLNPVFTVGEQIaESIRlHQGASREEAMVEAKRMLDQVRIpeaqTILSR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 348 RGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELciCQILHEKIT---ILVTHQLQYL-KAASQILIL 423
Cdd:PRK10261 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQL--IKVLQKEMSmgvIFITHDMGVVaEIADRVLVM 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217293410 424 KDGKMVQKGT-----------YTEFL---------KSGIDFG---SLLKKDNEESEQPP------VPGTPTLRNR 469
Cdd:PRK10261 243 YQGEAVETGSveqifhapqhpYTRALlaavpqlgaMKGLDYPrrfPLISLEHPAKQEPPieqdtvVDGEPILQVR 317
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
249-393 |
3.31e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.98 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 249 SFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-RIAYVSQQPWVFSG-----------------TLRSNI 310
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkPIDIRSPRDAIRAGimlcpedrkaegiipvhSVADNI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 311 -------------LFGKKYEKERYEKVIKACALKKdlqllEDGDlTVIGdrgtTLSGGQKARVNLARAVYQDADIYLLDD 377
Cdd:PRK11288 353 nisarrhhlragcLINNRWEAENADRFIRSLNIKT-----PSRE-QLIM----NLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180
....*....|....*....|
gi 2217293410 378 PLSAVD----AEVSRHLFEL 393
Cdd:PRK11288 423 PTRGIDvgakHEIYNVIYEL 442
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
245-429 |
3.40e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.80 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQ-PWVFSGTLRSN 309
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfksskealengISMVHQElNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 310 ILFGkkyekeRYEK----VIKACALKKDLQLLEDGDLTV-IGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 384
Cdd:PRK10982 94 MWLG------RYPTkgmfVDQDKMYRDTKAIFDELDIDIdPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2217293410 385 EVSRHLFElcICQILHEK--ITILVTHQL-QYLKAASQILILKDGKMV 429
Cdd:PRK10982 168 KEVNHLFT--IIRKLKERgcGIVYISHKMeEIFQLCDEITILRDGQWI 213
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
245-383 |
4.08e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.58 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSqqpwVFSG-----TLRSNI-----LFG- 313
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIA----ISSGlngqlTGIENIelkglMMGl 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217293410 314 -KKYEKERYEKVIKACALKKdlqlledgdltVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 383
Cdd:PRK13545 116 tKEKIKEIIPEIIEFADIGK-----------FIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD 175
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
578-830 |
4.38e-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: 349984 [Multi-domain] Cd Length: 295 Bit Score: 46.70 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 578 LNWYLGIYSGLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTF 657
Cdd:cd18540 41 LTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 658 LDFIQTLLqVVGVVSVAVAVIPW----IAIPLVP-LGIIFIFLRRYFLETSRDVKRLESTtrspVFSHLSSSLQGLWTIR 732
Cdd:cd18540 121 VDLVWGIT-YMIGILIVMLILNWklalIVLAVVPvLAVVSIYFQKKILKAYRKVRKINSR----ITGAFNEGITGAKTTK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 733 AYKAEERCQELFDAH-QDLHSEawflflttsrwfAVRLDAICAMFVIIVAF-------------GSLILAKTLDAGQVGL 798
Cdd:cd18540 196 TLVREEKNLREFKELtEEMRRA------------SVRAARLSALFLPIVLFlgsiatalvlwygGILVLAGAITIGTLVA 263
|
250 260 270
....*....|....*....|....*....|..
gi 2217293410 799 ALSYALTLMGMFQWCVRQSAEVENMMISVERV 830
Cdd:cd18540 264 FISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
870-1067 |
4.60e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.47 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 870 GGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKI--------LTTEIGLHDLRKKMSIIPQE 940
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPtKGTITINNInynkldhkLAAQLGIGIIYQELSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 941 PV---LFTGtmrknldpfnEHTDEELW--NALQEVQLKETIEDLPGKMD--TELAESGSNFSVGQRQLVCLARAILRKNQ 1013
Cdd:PRK09700 96 TVlenLYIG----------RHLTKKVCgvNIIDWREMRVRAAMMLLRVGlkVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217293410 1014 ILIIDEATANV-DPRTDEL--IQKKIREKFAhcTVLTIAHRLNTIID-SDKIMVLDSG 1067
Cdd:PRK09700 166 VIIMDEPTSSLtNKEVDYLflIMNQLRKEGT--AIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
229-294 |
4.84e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 47.37 E-value: 4.84e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217293410 229 VQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKS-SLLSaVLGeLAPsHGLVSVHGRIAY 294
Cdd:COG4172 9 VEDLSvAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALS-ILR-LLP-DPAAHPSGSILF 73
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
5-168 |
5.24e-05 |
|
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: 46.40 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 5 KTTTGQIVNLLSNDVNKF-DQVTVFLHFLWAGPLQAIAVTALLWMeigISC-LAGmaVLIILLPLQSCFGKLFSS-LRSK 81
Cdd:cd18557 89 KHKTGELTSRLSSDTSVLqSAVTDNLSQLLRNILQVIGGLIILFI---LSWkLTL--VLLLVIPLLLIASKIYGRyIRKL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 82 TATFTDARIRTM---NEVITGIRIIkmyaweKSFSNLITNLRK--KEISKILRSSCLRGMNLASFFSASKIIVFV-TFTT 155
Cdd:cd18557 164 SKEVQDALAKAGqvaEESLSNIRTV------RSFSAEEKEIRRysEALDRSYRLARKKALANALFQGITSLLIYLsLLLV 237
|
170
....*....|...
gi 2217293410 156 YVLLGSVITASRV 168
Cdd:cd18557 238 LWYGGYLVLSGQL 250
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
243-428 |
5.80e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 5.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 243 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQ---QPWVFS-- 303
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKkinnhnaneainhgFALVTEerrSTGIYAyl 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 304 ----GTLRSNIlfgKKYeKERYeKVIKACALKKDLQLLED-------GDLTVIGdrgtTLSGGQKARVNLARAVYQDADI 372
Cdd:PRK10982 342 digfNSLISNI---RNY-KNKV-GLLDNSRMKSDTQWVIDsmrvktpGHRTQIG----SLSGGNQQKVIIGRWLLTQPEI 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 373 YLLDDPLSAVDAEVSRHLFELCICQILHEKITILVTHQL-QYLKAASQILILKDGKM 428
Cdd:PRK10982 413 LMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMpELLGITDRILVMSNGLV 469
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
572-785 |
6.32e-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: 46.42 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 572 VTEKLDLNWYLGIysGLTVATV---LFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFsKDIGH 648
Cdd:cd18566 34 PNESIPTLQVLVI--GVVIAILlesLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 649 LDDLLP----LTFLD--FIQTLLQVVGVVSVAVAVIPWIAIPLVPLGIIFI--FLRRYFLETSR-DVKRlesttrspvFS 719
Cdd:cd18566 111 IREFLTgqalLALLDlpFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLgpILRRALKERSRaDERR---------QN 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 720 HLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWF-------LFLTTSRWFAVrldaicAMFVIIVAFGSL 785
Cdd:cd18566 182 FLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFkvakinaVAQTLGQLFSQ------VSMVAVVAFGAL 248
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
578-810 |
6.50e-05 |
|
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: 46.33 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 578 LNWYLGIYSGLTVATVLFGIARSLLVFYVlvnsSQ----TLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLL 653
Cdd:cd18546 38 LLLAAAAYLAVVLAGWVAQRAQTRLTGRT----GErllyDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 654 PLTFLDFIQTLLQVVGVVSVAVAVIPWIAI----PLVPLGIIFIFLRRYfletSRDVKRLESTTRSPVFSHLSSSLQGLW 729
Cdd:cd18546 114 QTGLVQLVVSLLTLVGIAVVLLVLDPRLALvalaALPPLALATRWFRRR----SSRAYRRARERIAAVNADLQETLAGIR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 730 TIRAYKAEERCQELFDAHQDLHSEAwflFLTTSRWFA-----VRLDAICAMFVIIVAFGSLILAKTLDAGqvglALSYAL 804
Cdd:cd18546 190 VVQAFRRERRNAERFAELSDDYRDA---RLRAQRLVAiyfpgVELLGNLATAAVLLVGAWRVAAGTLTVG----VLVAFL 262
|
....*.
gi 2217293410 805 TLMGMF 810
Cdd:cd18546 263 LYLRRF 268
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
874-1069 |
7.90e-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: 44.83 E-value: 7.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 874 VLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPE---GKIWIDKILTTEIGLHDlRKKMSII--PQEPVLFTGtm 948
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvteGEILFKGEDITDLPPEE-RARLGIFlaFQYPPEIPG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 949 rknldpfnehtdeelwnalqeVQLKETIEDLpgkmdtelaesGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRT 1028
Cdd:cd03217 92 ---------------------VKNADFLRYV-----------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2217293410 1029 DELIQKKIRE-KFAHCTVLTIAH--RLNTIIDSDKIMVLDSGRL 1069
Cdd:cd03217 140 LRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRI 183
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
874-1084 |
8.40e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 45.73 E-value: 8.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 874 VLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLftgtmRKNL 952
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPsEGSIVVNGQTINLVRDKDGQLKVADKNQLRLL-----RTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 953 DPFNEHTDeeLWN----------------ALQEVQLKETIEDLPGKMDTELAESG---SNFSVGQRQLVCLARAILRKNQ 1013
Cdd:PRK10619 95 TMVFQHFN--LWShmtvlenvmeapiqvlGLSKQEARERAVKYLAKVGIDERAQGkypVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217293410 1014 ILIIDEATANVDPrtdELIQK--KIREKFAH--CTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVLLQNKES 1084
Cdd:PRK10619 173 VLLFDEPTSALDP---ELVGEvlRIMQQLAEegKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
246-430 |
1.06e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.32 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 246 QGLSFTVRPGELLAVVGPVGAGKSSLLSAVLG--------------ELAPSHGLVSVHGRIAYVSQ---QPWVFSG-TLR 307
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGvdkraggeirlngkDISPRSPLDAVKKGMAYITEsrrDNGFFPNfSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 308 SNILFGKKYEKERYEKVIKACALKKDLQLLED--GDLTV----IGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSA 381
Cdd:PRK09700 360 QNMAISRSLKDGGYKGAMGLFHEVDEQRTAENqrELLALkchsVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRG 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2217293410 382 VDAEVSRHLFELcICQILHEKITIL-VTHQL-QYLKAASQILILKDGKMVQ 430
Cdd:PRK09700 440 IDVGAKAEIYKV-MRQLADDGKVILmVSSELpEIITVCDRIAVFCEGRLTQ 489
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
252-479 |
1.24e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 252 VRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSvhGRIAY-----------------------------VSQQPWVF 302
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVE--GVITYdgitpeeikkhyrgdvvynaetdvhfphlTVGETLDF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 303 SGTLRSNILFGKKYEKERYEKVIKACALKK-DLQLLEDgdlTVIGD---RGttLSGGQKARVNLARAVYQDADIYLLDDP 378
Cdd:TIGR00956 162 AARCKTPQNRPDGVSREEYAKHIADVYMATyGLSHTRN---TKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 379 LSAVDAEVSrhlfeLCICQILHEKITILVTHQLQYLKAASQ--------ILILKDGKMVQKGTYTE----FLKSGI---- 442
Cdd:TIGR00956 237 TRGLDSATA-----LEFIRALKTSANILDTTPLVAIYQCSQdayelfdkVIVLYEGYQIYFGPADKakqyFEKMGFkcpd 311
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2217293410 443 -----DFGSLLKKDNEESEQP----PVPGTPTLRNRTFSESSVWSQ 479
Cdd:TIGR00956 312 rqttaDFLTSLTSPAERQIKPgyekKVPRTPQEFETYWRNSPEYAQ 357
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
884-1057 |
1.36e-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: 43.52 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 884 SQEKVGIVGRTGAGKSSLISALFRLSEPEGKiwidkiltteiglhdlrkkmsiipqepvlftGTMRKNLDPFNEHTDEEL 963
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG-------------------------------GVIYIDGEDILEEVLDQL 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 964 WNALQEvqlketiedlpgkmdtelaESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQ-------KKI 1036
Cdd:smart00382 50 LLIIVG-------------------GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrlLLL 110
|
170 180
....*....|....*....|.
gi 2217293410 1037 REKFAHCTVLTIAHRLNTIID 1057
Cdd:smart00382 111 LKSEKNLTVILTTNDEKDLGP 131
|
|
| YfjP |
cd11383 |
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
889-909 |
1.63e-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: 43.10 E-value: 1.63e-04
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
249-413 |
1.83e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.71 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 249 SFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--IAYVSQ-----QPwvfSGTLRSNILFGKKyekery 321
Cdd:PRK11147 339 SAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKleVAYFDQhraelDP---EKTVMDNLAEGKQ------ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 322 ekvikacalkkdlqlledgDLTVIG----------------DRGTT----LSGGQKARVNLARAVYQDADIYLLDDPLSA 381
Cdd:PRK11147 410 -------------------EVMVNGrprhvlgylqdflfhpKRAMTpvkaLSGGERNRLLLARLFLKPSNLLILDEPTND 470
|
170 180 190
....*....|....*....|....*....|....*...
gi 2217293410 382 VDAEVsrhlFELcicqiLHEKIT------ILVTHQLQY 413
Cdd:PRK11147 471 LDVET----LEL-----LEELLDsyqgtvLLVSHDRQF 499
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
245-383 |
1.87e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.89 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--------------RIAYVSQqpwvfsG------ 304
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGgdmadarhrravcpRIAYMPQ------Glgknly 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 305 -TL--RSNI-----LFGKKyEKERYEKVikacalkkdLQLLEDGDLTVIGDR--GtTLSGGQKARVNLARAVYQDADIYL 374
Cdd:NF033858 91 pTLsvFENLdffgrLFGQD-AAERRRRI---------DELLRATGLAPFADRpaG-KLSGGMKQKLGLCCALIHDPDLLI 159
|
....*....
gi 2217293410 375 LDDPLSAVD 383
Cdd:NF033858 160 LDEPTTGVD 168
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
882-1086 |
1.98e-04 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 45.14 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 882 IKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID-KILTTEIGLHDlrKKMSIIPQEPVLF-TGTMRKN------- 951
Cdd:COG1118 25 IASGELVALLGPSGSGKTTLLRIIAGLETPdSGRIVLNgRDLFTNLPPRE--RRVGFVFQHYALFpHMTVAENiafglrv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 952 LDPFNEHTD---EELwnaLQEVQLkETIED-LPgkmdTELaeSGsnfsvGQRQLVCLARAILRKNQILIIDEATANVDPR 1027
Cdd:COG1118 103 RPPSKAEIRarvEEL---LELVQL-EGLADrYP----SQL--SG-----GQRQRVALARALAVEPEVLLLDEPFGALDAK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 1028 TDELIQKKIRE--KFAHCTVLTIAH------RLntiidSDKIMVLDSGRLKEYDEPYVLLQNKESLF 1086
Cdd:COG1118 168 VRKELRRWLRRlhDELGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEVYDRPATPF 229
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
245-454 |
2.21e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.42 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSQQPWVfSGTLR--SNILFgKKYEKERYE 322
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGL-SGQLTgiENIEF-KMLCMGFKR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 323 KVIKACaLKKDLQLLEDGDLtvIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHlfelCICQILH-- 400
Cdd:PRK13546 118 KEIKAM-TPKIIEFSELGEF--IYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK----CLDKIYEfk 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217293410 401 --EKITILVTHQL-QYLKAASQILILKDGKMVQKG-------TYTEFLKsgiDFGSLLKKDNEE 454
Cdd:PRK13546 191 eqNKTIFFVSHNLgQVRQFCTKIAWIEGGKLKDYGelddvlpKYEAFLN---DFKKKSKAEQKE 251
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
888-907 |
2.36e-04 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 44.76 E-value: 2.36e-04
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
248-428 |
2.39e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.96 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 248 LSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHG-------LVSVHGRIAYVSQQPWVFSGTLrsniLF-------G 313
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGeilldgkPVTAEQPEDYRKLFSAVFTDFH----LFdqllgpeG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 314 KKYEKERYEKVIKACALKKDLQLlEDGDLTvigdrGTTLSGGQKARVNLARAVYQDADIYLLD------DPlsavdaeVS 387
Cdd:PRK10522 418 KPANPALVEKWLERLKMAHKLEL-EDGRIS-----NLKLSKGQKKRLALLLALAEERDILLLDewaadqDP-------HF 484
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2217293410 388 RHLFELCICQILHEK-ITIL-VTHQLQYLKAASQILILKDGKM 428
Cdd:PRK10522 485 RREFYQVLLPLLQEMgKTIFaISHDDHYFIHADRLLEMRNGQL 527
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
882-1038 |
2.41e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 44.23 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 882 IKSQEKVGIVGRTGAGKSSLISALfrlsepEGKIWIDKILTTEIGL------------HDLRKKMSiipqepvlFTGTMR 949
Cdd:PRK09984 27 IHHGEMVALLGPSGSGKSTLLRHL------SGLITGDKSAGSHIELlgrtvqregrlaRDIRKSRA--------NTGYIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 950 KNLDPFNEHTDEE-----------LWNA----LQEVQLKETIEDLPGKMDTELA-ESGSNFSVGQRQLVCLARAILRKNQ 1013
Cdd:PRK09984 93 QQFNLVNRLSVLEnvligalgstpFWRTcfswFTREQKQRALQALTRVGMVHFAhQRVSTLSGGQQQRVAIARALMQQAK 172
|
170 180
....*....|....*....|....*
gi 2217293410 1014 ILIIDEATANVDPRTDELIQKKIRE 1038
Cdd:PRK09984 173 VILADEPIASLDPESARIVMDTLRD 197
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
240-438 |
2.63e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 240 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHG-LVSVHGRIAYVS---QQPWVFSGTLRSN--IL-- 311
Cdd:PRK10938 14 SDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGeRQSQFSHITRLSfeqLQKLVSDEWQRNNtdMLsp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 312 ----FGKKYEKERYEKVIKACALKKDLQLLEDGDLtvIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVS 387
Cdd:PRK10938 94 geddTGRTTAEIIQDEVKDPARCEQLAQQFGITAL--LDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2217293410 388 RHLFELcICQILHEKITI-LVTHQLQYLKA-ASQILILKDGKMVQKGTYTEFL 438
Cdd:PRK10938 172 QQLAEL-LASLHQSGITLvLVLNRFDEIPDfVQFAGVLADCTLAETGEREEIL 223
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
869-1050 |
2.63e-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: 44.93 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 869 PGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRL-SEPEGKIWIDKILTteIGlhdlrkkmsIIPQEPVL-FTG 946
Cdd:TIGR03719 15 PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdKDFNGEARPQPGIK--VG---------YLPQEPQLdPTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 947 TMRKN-----------LDPFNEHT------DEELwNALQEVQ--LKETIE-----DLPGKMdtELAESG----------S 992
Cdd:TIGR03719 84 TVRENveegvaeikdaLDRFNEISakyaepDADF-DKLAAEQaeLQEIIDaadawDLDSQL--EIAMDAlrcppwdadvT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217293410 993 NFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIREkFAHcTVLTIAH 1050
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE-YPG-TVVAVTH 216
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
995-1090 |
2.72e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.99 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 995 SVGQRQLVCLARAILRKNQILIIDEAT-ANVDPRTDELIqKKIRE-KFAHCTVLTIAHRLNTIID-SDKIMVLDSGRLke 1071
Cdd:PRK10762 143 SIGEQQMVEIAKVLSFESKVIIMDEPTdALTDTETESLF-RVIRElKSQGRGIVYISHRLKEIFEiCDDVTVFRDGQF-- 219
|
90
....*....|....*....
gi 2217293410 1072 YDEPYVLLQNKESLFYKMV 1090
Cdd:PRK10762 220 IAEREVADLTEDSLIEMMV 238
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
862-1071 |
3.27e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.85 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 862 NVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPEG------KIWIDKILTTEIGLHDLRKK-- 933
Cdd:PRK10261 19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGglvqcdKMLLRRRSRQVIELSEQSAAqm 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 934 -------MSIIPQEPV-----LFT------GTMRKNLDPFNEHTDEELWNALQEVQLKETiedlpgkmDTELAESGSNFS 995
Cdd:PRK10261 99 rhvrgadMAMIFQEPMtslnpVFTvgeqiaESIRLHQGASREEAMVEAKRMLDQVRIPEA--------QTILSRYPHQLS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217293410 996 VGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIR--EKFAHCTVLTIAHRLNTIID-SDKIMVLDSGRLKE 1071
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlQKEMSMGVIFITHDMGVVAEiADRVLVMYQGEAVE 249
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
578-810 |
3.85e-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: 43.97 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 578 LNWYLGIYSGLTVATVLFGIARSLLVFYVlvnsSQTLHNKM----FESILKAPVLFFDRNPIGRILNRFSkDIGHLDDLL 653
Cdd:cd18570 41 LNIISIGLILLYLFQSLLSYIRSYLLLKL----SQKLDIRLilgyFKHLLKLPLSFFETRKTGEIISRFN-DANKIREAI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 654 PLT----FLDFIqTLLQVVGVVSVAVAVIPWIAIPLVPLGIIFIFL-RRYFLETSRDVKRLESTTRspvfSHLSSSLQGL 728
Cdd:cd18570 116 SSTtislFLDLL-MVIISGIILFFYNWKLFLITLLIIPLYILIILLfNKPFKKKNREVMESNAELN----SYLIESLKGI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 729 WTIRAYKAEERCQELFDAHqdlhseawFLFLTTSRWFAVRLDAICAMF---------VIIVAFGS-LILAKTLDAGQVgl 798
Cdd:cd18570 191 ETIKSLNAEEQFLKKIEKK--------FSKLLKKSFKLGKLSNLQSSIkglisligsLLILWIGSyLVIKGQLSLGQL-- 260
|
250
....*....|..
gi 2217293410 799 aLSYaLTLMGMF 810
Cdd:cd18570 261 -IAF-NALLGYF 270
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
882-1065 |
3.96e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.41 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 882 IKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIwidkiltteiglhDLRKKMSIIPQE-PVLFTGTMRKNLDPFNEHT 959
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPdEGEV-------------DPELKISYKPQYiKPDYDGTVEDLLRSITDDL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 960 DEELWNalQEVQLKETIEDLpgkMDTELAE-SGsnfsvGQRQLVCLARAILRKNQILIIDEATANVDP----RTDELIQK 1034
Cdd:PRK13409 429 GSSYYK--SEIIKPLQLERL---LDKNVKDlSG-----GELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAIRR 498
|
170 180 190
....*....|....*....|....*....|...
gi 2217293410 1035 KIREKFAhcTVLTIAHRLnTIID--SDKIMVLD 1065
Cdd:PRK13409 499 IAEEREA--TALVVDHDI-YMIDyiSDRLMVFE 528
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
985-1068 |
4.04e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 43.44 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 985 TELA-ESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPR-TDELIQ--KKIREKFAhCTVLTIAHRLNTIID-SD 1059
Cdd:PRK11300 144 LEHAnRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKeTKELDEliAELRNEHN-VTVLLIEHDMKLVMGiSD 222
|
....*....
gi 2217293410 1060 KIMVLDSGR 1068
Cdd:PRK11300 223 RIYVVNQGT 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
243-428 |
4.15e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.22 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 243 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQpwvfsgTLRS 308
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHevvtrspqdglangIVYISED------RKRD 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 309 NILFGKKYeKERyekvIKACAL----KKDLQLLEDGDLTVIGD-----------RGTT---LSGGQKARVNLARAVYQDA 370
Cdd:PRK10762 340 GLVLGMSV-KEN----MSLTALryfsRAGGSLKHADEQQAVSDfirlfniktpsMEQAiglLSGGNQQKVAIARGLMTRP 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 371 DIYLLDDPLSAVDAEVSRHLFELcICQILHEKITI-LVTHQL-QYLKAASQILILKDGKM 428
Cdd:PRK10762 415 KVLILDEPTRGVDVGAKKEIYQL-INQFKAEGLSIiLVSSEMpEVLGMSDRILVMHEGRI 473
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
253-289 |
4.47e-04 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 42.49 E-value: 4.47e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2217293410 253 RPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVH 289
Cdd:COG3709 3 GPGRLIYVVGPSGAGKDSLLAAARARLAADPRLVFAR 39
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
235-440 |
4.89e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.58 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 235 FWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGelapshgLVSVHGRiayVSQQPWVFSGTlrsNILfgK 314
Cdd:PRK11022 13 FGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMG-------LIDYPGR---VMAEKLEFNGQ---DLQ--R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 315 KYEKERYEKV--------------IKAC---------ALK------------KDLQLLEdgdLTVIGDRGT-------TL 352
Cdd:PRK11022 78 ISEKERRNLVgaevamifqdpmtsLNPCytvgfqimeAIKvhqggnkktrrqRAIDLLN---QVGIPDPASrldvyphQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 353 SGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKIT-ILVTHQLQYL-KAASQILILKDGKMVQ 430
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMAlVLITHDLALVaEAAHKIIVMYAGQVVE 234
|
250
....*....|
gi 2217293410 431 KGTYTEFLKS 440
Cdd:PRK11022 235 TGKAHDIFRA 244
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
856-1068 |
5.79e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 856 GVIIFDNVNFMYSPGGplvlkhLTALIksqekvgivGRTGAGKSSLISALFRLSEP-EGKIWID-KILTTEIGLHDLRKK 933
Cdd:PRK10982 10 GVKALDNVNLKVRPHS------IHALM---------GENGAGKSTLLKCLFGIYQKdSGSILFQgKEIDFKSSKEALENG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 934 MSIIPQE--PVLFTGTMrKNL--------DPFNEHtdEELWNalqevQLKETIEDLpgKMDTELAESGSNFSVGQRQLVC 1003
Cdd:PRK10982 75 ISMVHQElnLVLQRSVM-DNMwlgryptkGMFVDQ--DKMYR-----DTKAIFDEL--DIDIDPRAKVATLSVSQMQMIE 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217293410 1004 LARAILRKNQILIIDEATANVDPRTDELIQKKIRE-KFAHCTVLTIAHRLNTIID-SDKIMVLDSGR 1068
Cdd:PRK10982 145 IAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKlKERGCGIVYISHKMEEIFQlCDEITILRDGQ 211
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
887-907 |
6.31e-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: 6.31e-04
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
858-1055 |
7.17e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 42.95 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 858 IIFDNVNFMYSpGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALF---RLSEpeGKIWIDKILTTEIglhdLRKKM 934
Cdd:PRK15056 7 IVVNDVTVTWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMgfvRLAS--GKISILGQPTRQA----LQKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 935 -SIIPQE-------PVLF-----------TGTMRKNldpfNEHTDEELWNALQEVQLKETIEDLPGKMdtelaesgsnfS 995
Cdd:PRK15056 80 vAYVPQSeevdwsfPVLVedvvmmgryghMGWLRRA----KKRDRQIVTAALARVDMVEFRHRQIGEL-----------S 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217293410 996 VGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIRE-KFAHCTVLTIAHRLNTI 1055
Cdd:PRK15056 145 GGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRElRDEGKTMLVSTHNLGSV 205
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
241-435 |
7.90e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.47 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 241 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLG--ELAPSHGLVSVHGR--------------IAYVSQQPWVFSG 304
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKdllelspedragegIFMAFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 305 TlrSNILF-------GKKY-EKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLD 376
Cdd:PRK09580 93 V--SNQFFlqtalnaVRSYrGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217293410 377 DPLSAVDAEVSRHLFELCICQILHEKITILVTHQ---LQYLKaASQILILKDGKMVQKGTYT 435
Cdd:PRK09580 171 ESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYqriLDYIK-PDYVHVLYQGRIVKSGDFT 231
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
888-1075 |
8.25e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.26 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 888 VGIVGRTGAGKSSLISALF-----RLSEPEGKIWIDKILT----TEIG-----LHDLRKKMSIIPQE----PVLFTGTMR 949
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSgelipNLGDYEEEPSWDEVLKrfrgTELQnyfkkLYNGEIKVVHKPQYvdliPKVFKGKVR 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 950 KNLdpfnEHTDEElwNALQEVqlketIEDLpgKMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTD 1029
Cdd:PRK13409 182 ELL----KKVDER--GKLDEV-----VERL--GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQR 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2217293410 1030 ELIQKKIREKFAHCTVLTIAHRLnTIID--SDKIMVLdsgrlkeYDEP 1075
Cdd:PRK13409 249 LNVARLIRELAEGKYVLVVEHDL-AVLDylADNVHIA-------YGEP 288
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
590-794 |
1.24e-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: 42.04 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 590 VATVLFGIARSLLVFYVLVNSSQ----TLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQTLL 665
Cdd:cd18551 43 VALFLLQAVLSALSSYLLGRTGErvvlDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 666 qVVGVVSVAVAVIPW-------IAIPLVPLGIIFI--FLRRYFLETSRDVKRLEsttrspvfSHLSSSLQGLWTIRAYKA 736
Cdd:cd18551 123 -TVVGAVVLMFLLDWvltlvtlAVVPLAFLIILPLgrRIRKASKRAQDALGELS--------AALERALSAIRTVKASNA 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217293410 737 EERCQELFDAHQDlhsEAWFLFLTTSRWFAV-----RLdAICAMFVIIVAFGSLILAK-TLDAG 794
Cdd:cd18551 194 EERETKRGGEAAE---RLYRAGLKAAKIEALigplmGL-AVQLALLVVLGVGGARVASgALTVG 253
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
882-1065 |
1.69e-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: 42.46 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 882 IKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIwidkiltteiglhDLRKKMSIIPQEPV-LFTGTMRKNLdpFNEHT 959
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPdEGEV-------------DEDLKISYKPQYISpDYDGTVEEFL--RSANT 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 960 D--------EELWNALQevqlketIEDLpgkMDTELAE-SGsnfsvGQRQLVCLARAILRKNQILIIDEATANVDP---- 1026
Cdd:COG1245 428 DdfgssyykTEIIKPLG-------LEKL---LDKNVKDlSG-----GELQRVAIAACLSRDADLYLLDEPSAHLDVeqrl 492
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2217293410 1027 RTDELIQKKIREKFAhcTVLTIAHRLnTIID--SDKIMVLD 1065
Cdd:COG1245 493 AVAKAIRRFAENRGK--TAMVVDHDI-YLIDyiSDRLMVFE 530
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
528-830 |
1.87e-03 |
|
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: 41.70 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 528 WIVFIFLILLNTAAQVAYVLqdwwlsywankqsMLNVTVNGGGNVTEKLDLNWYLGIYSGLTVATVLFGIARSLLVFYVL 607
Cdd:cd18543 1 LILALLAALLATLAGLAIPL-------------LTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 608 VNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLlpLTFLDF-IQTLLQVVGVVSVAVAVIPWIA---- 682
Cdd:cd18543 68 LGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRF--LAFGPFlLGNLLTLVVGLVVMLVLSPPLAlval 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 683 IPLVPLGIIFIFLRRYFLETSRDVKRLESTtrspVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLhseawfLFLTTS 762
Cdd:cd18543 146 ASLPPLVLVARRFRRRYFPASRRAQDQAGD----LATVVEESVTGIRVVKAFGRERRELDRFEAAARR------LRATRL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 763 RwfAVRLDAICAMF---------VIIVAFGS-LILAKTLDAGQVgLALSyalTLMGMFQWCVRQSAEVENM----MISVE 828
Cdd:cd18543 216 R--AARLRARFWPLlealpelglAAVLALGGwLVANGSLTLGTL-VAFS---AYLTMLVWPVRMLGWLLAMaqraRAAAE 289
|
..
gi 2217293410 829 RV 830
Cdd:cd18543 290 RV 291
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
565-787 |
2.01e-03 |
|
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: 41.70 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 565 TVNGGGNVtekLDLNWYLGIYSGLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSK 644
Cdd:cd18576 25 AALGGGDT---ASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 645 DIGHLDDLLPLTFLDFIQTLLQVVGVVSVAVAVIP----WIAIPLVPLGIIFIFLRRYFLETSRDVK-RLESTTrspvfS 719
Cdd:cd18576 102 DVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWkltlLMLATVPVVVLVAVLFGRRIRKLSKKVQdELAEAN-----T 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217293410 720 HLSSSLQGLWTIRAYKAEERCQELFDAHQDlhsEAWFLFLTTSRWfavrlDAICAMFVIIVAFGSLIL 787
Cdd:cd18576 177 IVEETLQGIRVVKAFTREDYEIERYRKALE---RVVKLALKRARI-----RALFSSFIIFLLFGAIVA 236
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
351-437 |
2.63e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 351 TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVsrhLFELCICQILHEKITILVTHQLQYLKA-ASQILILKDGKMV 429
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA---VLWLETYLLKWPKTFIVVSHAREFLNTvVTDILHLHGQKLV 420
|
....*....
gi 2217293410 430 Q-KGTYTEF 437
Cdd:PLN03073 421 TyKGDYDTF 429
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
224-435 |
3.70e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.40 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 224 KKMVHVQDFTAfwdKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGElaPSHGLVSvhGRIAYVSQQPWVFS 303
Cdd:CHL00131 5 KPILEIKNLHA---SVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PAYKILE--GDILFKGESILDLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 304 GTLRSN--ILFGKKYEKE------------RYEKVIKACALKK--DLQLLE--DGDLTVIGDRGTTL--------SGGQK 357
Cdd:CHL00131 78 PEERAHlgIFLAFQYPIEipgvsnadflrlAYNSKRKFQGLPEldPLEFLEiiNEKLKLVGMDPSFLsrnvnegfSGGEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 358 ARVNLARAVYQDADIYLLDDPLSAVDAEVSRhlfelCICQILH-----EKITILVTHQ---LQYLKaASQILILKDGKMV 429
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLDIDALK-----IIAEGINklmtsENSIILITHYqrlLDYIK-PDYVHVMQNGKII 231
|
....*.
gi 2217293410 430 QKGTYT 435
Cdd:CHL00131 232 KTGDAE 237
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
334-433 |
3.73e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 334 LQLLEDGDLTVI--GDRGTTLSGGQKARVNLARAVYQDAD---IYLLDDPLSAVDAEVSRHLFELcICQILHEKITILVT 408
Cdd:TIGR00630 810 LQTLCDVGLGYIrlGQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEV-LQRLVDKGNTVVVI 888
|
90 100 110
....*....|....*....|....*....|..
gi 2217293410 409 -HQLQYLKAASQILIL------KDGKMVQKGT 433
Cdd:TIGR00630 889 eHNLDVIKTADYIIDLgpeggdGGGTVVASGT 920
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
259-426 |
4.04e-03 |
|
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: 39.90 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 259 AVVGPVGAGKSSLLSAVL----GELAPS----HGLVSVHG---RIAYVsqqpwvfsgTLRSNILFGKKYEKERYEKVIKA 327
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKyaltGELPPNskggAHDPKLIRegeVRAQV---------KLAFENANGKKYTITRSLAILEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 328 CAlkkdlqLLEDGDLTVIGDRG-TTLSGGQKA------RVNLARAVYQDADIYLLDDPLSAVDAE-VSRHLFELcICQIL 399
Cdd:cd03240 97 VI------FCHQGESNWPLLDMrGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEnIEESLAEI-IEERK 169
|
170 180 190
....*....|....*....|....*....|
gi 2217293410 400 HEKI--TILVTHQLQYLKAASQIL-ILKDG 426
Cdd:cd03240 170 SQKNfqLIVITHDEELVDAADHIYrVEKDG 199
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
801-902 |
4.06e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 801 SYALTLMGMFQWCVRQSAEVENMMISVERvIEYTDLEKEAP-WEYQKRPPPAWPHEGVIIFDNVNFMYsPGGPLVLKHLT 879
Cdd:PLN03073 452 SHMQAFIDKFRYNAKRASLVQSRIKALDR-LGHVDAVVNDPdYKFEFPTPDDRPGPPIISFSDASFGY-PGGPLLFKNLN 529
|
90 100
....*....|....*....|...
gi 2217293410 880 ALIKSQEKVGIVGRTGAGKSSLI 902
Cdd:PLN03073 530 FGIDLDSRIAMVGPNGIGKSTIL 552
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
888-1075 |
5.27e-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: 40.92 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 888 VGIVGRTGAGKSSLISALF-----RLSEPEGKIWIDKILT----TEIGLH--DLRK---KMSIIPQE----PVLFTGTMR 949
Cdd:COG1245 102 TGILGPNGIGKSTALKILSgelkpNLGDYDEEPSWDEVLKrfrgTELQDYfkKLANgeiKVAHKPQYvdliPKVFKGTVR 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 950 KNLdpfnEHTDEelwnalqEVQLKETIEDLpgKMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDP--- 1026
Cdd:COG1245 182 ELL----EKVDE-------RGKLDELAEKL--GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIyqr 248
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2217293410 1027 -RTDELIQKKIREKFAhctVLTIAHRLnTIID--SDKIMVLdsgrlkeYDEP 1075
Cdd:COG1245 249 lNVARLIRELAEEGKY---VLVVEHDL-AILDylADYVHIL-------YGEP 289
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
874-1038 |
7.57e-03 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 39.24 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 874 VLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHdLRKKMSI--IPQEPVLFTG-TMR 949
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPdSGRIFLDGEDITHLPMH-KRARLGIgyLPQEASIFRKlTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 950 KNLDPFNEHTDeelwnaLQEVQLKETIEDLpgkMD----TELAES-GSNFSVGQRQLVCLARAILRKNQILIIDEATANV 1024
Cdd:COG1137 97 DNILAVLELRK------LSKKEREERLEEL---LEefgiTHLRKSkAYSLSGGERRRVEIARALATNPKFILLDEPFAGV 167
|
170
....*....|....
gi 2217293410 1025 DPRTDELIQKKIRE 1038
Cdd:COG1137 168 DPIAVADIQKIIRH 181
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
5-206 |
7.90e-03 |
|
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: 39.79 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 5 KTTTGQIVNLLSNDVNKFDQV--TVFLHFLWAGpLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKLFSSLR--- 79
Cdd:cd18580 92 TTPSGRILNRFSKDIGLIDEElpLALLDFLQSL-FSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYLRTSRQLRrle 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 80 --SKTATFTdarirTMNEVITGIRIIKMYAWEKSF-----SNLITNLRkkeiSKILRSSCLRGMNL-ASFFSAskIIVFV 151
Cdd:cd18580 171 seSRSPLYS-----HFSETLSGLSTIRAFGWQERFieenlRLLDASQR----AFYLLLAVQRWLGLrLDLLGA--LLALV 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217293410 152 TFTTYVLLGSVITASrvFVAVTLYGAVRLTVTLFFpsAIERVSE---AIVSIRRIQTF 206
Cdd:cd18580 240 VALLAVLLRSSISAG--LVGLALTYALSLTGSLQW--LVRQWTEletSMVSVERILEY 293
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
245-384 |
9.19e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.21 E-value: 9.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 245 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSH--GLVSVHG---------RIAYVSQQPWVFSG--TLRSNIL 311
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYieGDIRISGfpkkqetfaRISGYCEQNDIHSPqvTVRESLI 975
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217293410 312 FGK--KYEKE--RYEKVIkacALKKDLQLLEDGDL--TVIGDRGTT-LSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 384
Cdd:PLN03140 976 YSAflRLPKEvsKEEKMM---FVDEVMELVELDNLkdAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
|
| |
