|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
51-1535 |
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: 1245.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 51 DFTQCFIDGVILNLSAIFMitFGIRDLVNLCKKKHSgikyrRNWIIVS-----RMAL-VLLEIA-----FVSLASLNISK 119
Cdd:TIGR00957 22 DFTKCFQNTVLAWVPCFYL--WVCFPCYFLYLSRHD-----RGYIQMThlnktKTALgFLLWIVcwadlFYSFWERSHGR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 120 EEAENFTIvsqyASTMLSLFVALALHWIEYDR--SVVANTVLLFYWLFETFGNFAKLINILIRHTYEGIwysgqtgfILT 197
Cdd:TIGR00957 95 APAPVFLV----SPTLLGITMLLATFLIQLERrkGVQSSGIMLTFWLVALVCALAILRSKILLALKEDA--------IVD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 198 LFQVIT-------CASILLLEALPKKPLMPHQHIHQtltrRKPNPYDSANIFSRITFSWMSGLMKTGYEKYLVEADLYKL 270
Cdd:TIGR00957 163 PFRDTTfyiyfalVLSQLVLSCFSDKSPLFSETNHD----PNPCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 271 PRNFSSEELSQKLEKNWENELKQKS----------------------------------------NPSLSWAICRTFGSK 310
Cdd:TIGR00957 239 NKEDTSEMVVPVLVENWKKECKKTRkqpvsavygkkdpskpkgssqldaneevealivksphkprKPSLFKVLYKTFGPY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 311 MLLAAFFKAIHDVLAFTQPQLLRILIKFVTDynserqddhsslqgfennhpQKLPIVRGFLIAFAMFLVGFTQTSVLHQY 390
Cdd:TIGR00957 319 FLMSFCFKAIHDLMMFIGPQILSLLIRFVND--------------------PMAPDWQGYFYTGLLFVCACLQTLILHQY 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 391 FLNVFNTGMYIKSALTALIYQKSLVLSNEASGLSSTGDIVNLMSVDVQKLQDLTQWLNLIWSGPFQIIICLYSLYKLLGN 470
Cdd:TIGR00957 379 FHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGP 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 471 SMWVGVIILVIMMPLNSFLMRIQKKLQKSQMKYKDERTRVISEILNNIKSLKLYAWEKPYREKLEEVRNnKELKNLTKLG 550
Cdd:TIGR00957 459 SVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQ-EELKVLKKSA 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 551 CYMAVTSFQFNIVPFLVSCCTFAVFVYTEDR-ALTTDLVFPALTLFNLLSFPLMIIPMVLNSFIEASVSIGRLFTFFTNE 629
Cdd:TIGR00957 538 YLHAVGTFTWVCTPFLVALITFAVYVTVDENnILDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHE 617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 630 ELQPDSVQRLPkVKNIGDVAINIgDDATFLWQRkpEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKG 709
Cdd:TIGR00957 618 ELEPDSIERRT-IKPGEGNSITV-HNATFTWAR--DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG 693
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 710 FATVHGSVAYVSQVPWIMNGTVKENILFGHRYDAEFYEKTIKACALTIDLAILMDGDKTLVGEKGISLSGGQKARLSLAR 789
Cdd:TIGR00957 694 HVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLAR 773
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 790 AVYARADTYLLDDPLAAVDEHVARHLIEHVLGPNGLLHTKTKVLATNKVSALSIADSIALLDNGEITQQGTYDEITkDAD 869
Cdd:TIGR00957 774 AVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELL-QRD 852
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 870 SPLWKLLNNYGK-KNNGKSNEFGDSSESSVRESSIPVEGEL-------EQLQKLNDLDFGNSDAI*LRRA*DA*LG*IDF 941
Cdd:TIGR00957 853 GAFAEFLRTYAPdEQQGHLEDSWTALVSGEGKEAKLIENGMlvtdvvgKQLQRQLSASSSDSGDQSRHHGSSAELQKAEA 932
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 942 GDDENIAKREHREQ-GKVKWNIYLEYAKAcnpksVCVFILFIVISMFL-----SVMGNVWLKHWSEVNSRYGSNPNAARY 1015
Cdd:TIGR00957 933 KEETWKLMEADKAQtGQVELSVYWDYMKA-----IGLFITFLSIFLFVcnhvsALASNYWLSLWTDDPMVNGTQNNTSLR 1007
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1016 LAIYFALGIGSALATLIQTIVLWVfCTIHASKYLHNLMTNSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTFSQF 1095
Cdd:TIGR00957 1008 LSVYGALGILQGFAVFGYSMAVSI-GGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMF 1086
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1096 FVNAVKVTFTITVICATTWQFIFIIIPLSVFYIYYQQYYLRTSRELRRLDSITRSPIYSHFQETLGGLATVRGYSQQKRF 1175
Cdd:TIGR00957 1087 MGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERF 1166
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1176 SHINQCRIDNNMSAFYPSINANRWLAYRLELIGSIIILGAATLSVfrLKQGTLTAGMVGLSLSYALQITQTLNWIVRMTV 1255
Cdd:TIGR00957 1167 IHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAV--ISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSS 1244
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1256 EVETNIVSVERIKEYADLKSEAPLIVEGHRPPKEWPSQGDIKFNNYSTRYRPELDLVLKHINIHIKPNEKVGIVGRTGAG 1335
Cdd:TIGR00957 1245 EMETNIVAVERLKEYSETEKEAPWQIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAG 1324
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1336 KSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQVFEGTVRENIDPINQYTDEAIWRALELSHLKEHV 1415
Cdd:TIGR00957 1325 KSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFV 1404
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1416 LSMSnDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKDRTILTIAHRLNTI 1495
Cdd:TIGR00957 1405 SALP-DKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTI 1483
|
1530 1540 1550 1560
....*....|....*....|....*....|....*....|
9AYC_A 1496 MDSDRIIVLDNGKVAEFDSPGQLLSdNKSLFYSLCMEAGL 1535
Cdd:TIGR00957 1484 MDYTRVIVLDKGEVAEFGAPSNLLQ-QRGIFYSMAKDAGL 1522
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-1537 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 1015.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 25 MAGNLVSWACKLCRS-------PEGFGPisfygdFTQCFIDGVILNLSAIFMITFGIRDlVNLCKKKHSGIKY--RRNWi 95
Cdd:PLN03130 1 MGFEPLDWYCRPVPNgvwakkvDNAFGA------YTPCATDSLVINISHLVLLGLCLYR-IWLIKKDHKVQRFclRSKW- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 96 ivsRMALVLLEIAFVSLASL-----NISKEEAENFTIVSQYASTMLslfVALALHWIeydrsvvantVLLFYWLFETfgn 170
Cdd:PLN03130 73 ---YNYFLALLAAYCTAEPLfrlvmGISVLNLDGQTSLPPFEIVSL---IVEALTWC----------SMLVMIGVET--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 171 fakliNILIRhtyEGIWY------------SGQTGFILTL--------FQVITCA-------SILLLEALPK-------- 215
Cdd:PLN03130 134 -----KIYIR---EFRWYvrfaviyvlvgdAVMLNLVLSVkeyyssfvLYLYISEvaaqvlfGILLLVYFPNldpypgyt 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 216 ------------KPLMPHQHIhqtltrrkpNPYDSANIFSRITFSWMSGLMKTGYEKYLVEADLYKLPRNFSSEELSQKL 283
Cdd:PLN03130 206 pigsesvddyeyEELPGGEQI---------CPERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSF 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 284 EKNWENELkQKSNPSLSWAICRTFGSKMLLAAFFKAIHDVLAFTQPQLLRILIKfvtdynserqddhsSLQgfennhpQK 363
Cdd:PLN03130 277 QKCWDEEL-KKPKPWLLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLLNLLLE--------------SMQ-------NG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 364 LPIVRGFLIAFAMFLVGFTQTSVLHQYFLNVFNTGMYIKSALTALIYQKSLVLSNEASGLSSTGDIVNLMSVDVQKLQDL 443
Cdd:PLN03130 335 EPAWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQI 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 444 TQWLNLIWSGPFQIIICLYSLYKLLGNSMWVGVIILVIMMPLNSFLMRIQKKLQKSQMKYKDERTRVISEILNNIKSLKL 523
Cdd:PLN03130 415 CQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKC 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 524 YAWEKPYREKLEEVRNNkELKNLTKLGCYMAVTSFQFNIVPFLVSCCTFAVFVYTEDRaLTTDLVFPALTLFNLLSFPLM 603
Cdd:PLN03130 495 YAWENSFQSKVQTVRDD-ELSWFRKAQLLSAFNSFILNSIPVLVTVVSFGVFTLLGGD-LTPARAFTSLSLFAVLRFPLF 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 604 IIPMVLNSFIEASVSIGRLFTFFTNEE--LQPDsvqrlPKVKNiGDVAINIgDDATFLWQRKPEyKVALKNINFQAKKGN 681
Cdd:PLN03130 573 MLPNLITQAVNANVSLKRLEELLLAEErvLLPN-----PPLEP-GLPAISI-KNGYFSWDSKAE-RPTLSNINLDVPVGS 644
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 682 LTCIVGKVGSGKTALLSCMLGDL-FRVKGFATVHGSVAYVSQVPWIMNGTVKENILFGHRYDAEFYEKTIKACALTIDLA 760
Cdd:PLN03130 645 LVAIVGSTGEGKTSLISAMLGELpPRSDASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLD 724
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 761 ILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARHLIEHVLgpNGLLHTKTKVLATNKVSA 840
Cdd:PLN03130 725 LLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCI--KDELRGKTRVLVTNQLHF 802
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 841 LSIADSIALLDNGEITQQGTYDEITKDadSPLW-KLLNNYGKKNNGKSNEFGdssessvressipvegelEQLQKLNDLD 919
Cdd:PLN03130 803 LSQVDRIILVHEGMIKEEGTYEELSNN--GPLFqKLMENAGKMEEYVEENGE------------------EEDDQTSSKP 862
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 920 FGNSDAI*LRRa*DA*LG*IDFGDDENIAKREHREQGKVKWNIYLEYAKACNPKSVcVFILFI--VISMFLSVMGNVWLK 997
Cdd:PLN03130 863 VANGNANNLKK--DSSSKKKSKEGKSVLIKQEERETGVVSWKVLERYKNALGGAWV-VMILFLcyVLTEVFRVSSSTWLS 939
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 998 HWSEVNSRYGSNPNAarYLAIYFALGIGSALATLIQTIVLwVFCTIHASKYLHNLMTNSVLRAPMTFFETTPIGRILNRF 1077
Cdd:PLN03130 940 EWTDQGTPKTHGPLF--YNLIYALLSFGQVLVTLLNSYWL-IMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRF 1016
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1078 SNDIYKVDALLGrTFSQFFVNAVK---VTFTITVICATT--WQfifiIIPLSV-FYIYYQqYYLRTSRELRRLDSITRSP 1151
Cdd:PLN03130 1017 AKDLGDIDRNVA-VFVNMFLGQIFqllSTFVLIGIVSTIslWA----IMPLLVlFYGAYL-YYQSTAREVKRLDSITRSP 1090
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1152 IYSHFQETLGGLATVRGYSQQKRFSHINQCRIDNNMSAFYPSINANRWLAYRLELIGSIIILGAATLSVF---RLKQGTL 1228
Cdd:PLN03130 1091 VYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMqngRAENQAA 1170
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1229 TAGMVGLSLSYALQITQTLNWIVRMTVEVETNIVSVERIKEYADLKSEAPLIVEGHRPPKEWPSQGDIKFNNYSTRYRPE 1308
Cdd:PLN03130 1171 FASTMGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPSEAPLVIENNRPPPGWPSSGSIKFEDVVLRYRPE 1250
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1309 LDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQVFEGTVR 1388
Cdd:PLN03130 1251 LPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVR 1330
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1389 ENIDPINQYTDEAIWRALELSHLKEhVLSMSNDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVET 1468
Cdd:PLN03130 1331 FNLDPFNEHNDADLWESLERAHLKD-VIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT 1409
|
1530 1540 1550 1560 1570 1580
....*....|....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 1469 DKVVQETIRTAFKDRTILTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQLLSDNKSLFYSLCMEAGLVN 1537
Cdd:PLN03130 1410 DALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQSTGAAN 1478
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-1537 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 928.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 25 MAGNLVSWACKLCrsPEGF---GPISFYGDFTQCFIDGVILNLSAIFMITFGI-RDLVNLCKKKHSGIKYRRN------W 94
Cdd:PLN03232 1 MGFEALNWYCKPI--AEGFwekTVDGAFGAYTPCAIDSLVMIVSHSVLLGLCFyRIWIILDNAKAQIYVLRKKyyncvlG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 95 IIVSRMALVLLEIAFVSLASLNISKEEA-ENFTIVSQY--ASTMLSLFVALALHWIEYdrsvvantVLLFYWlFETFGNF 171
Cdd:PLN03232 79 ILACYCVVEPVLRLVMGISLFDMDEETDlPPFEVASLMveAFAWFSMLVLIGLETKQY--------VKEFRW-YVRFGVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 172 ------AKLINIL--IRHTYEG-IWYsgqtgfiltLFQVITCAS----ILLLEALPKKPLMPHQHIHQTLT--------- 229
Cdd:PLN03232 150 yvlvadAVLLDLVlpLKNSINRtALY---------LCISSRCCQalfgILLLVYIPELDPYPGYHILNNESldnveydal 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 230 --RRKPNPYDSANIFSRITFSWMSGLMKTGYEKYLVEADLYKLPRNFSSEELSQKLEKNWENElKQKSNPSLSWAICRTF 307
Cdd:PLN03232 221 rgGENICPERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEE-SRRPKPWLLRALNNSL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 308 GSKMLLAAFFKAIHDVLAFTQPQLLRILikfvtdynserqddhssLQGFENNHPQKLPIVRGFLIAFAMFLVGFTQTsvl 387
Cdd:PLN03232 300 GGRFWLGGIFKIGHDLSQFVGPVILSHL-----------------LQSMQEGDPAWVGYVYAFLIFFGVTFGVLCES--- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 388 hQYFLNVFNTGMYIKSALTALIYQKSLVLSNEASGLSSTGDIVNLMSVDVQKLQDLTQWLNLIWSGPFQIIICLYSLYKL 467
Cdd:PLN03232 360 -QYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQ 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 468 LGNSMWVGVIILVIMMPLNSFLMRIQKKLQKSQMKYKDERTRVISEILNNIKSLKLYAWEKPYREKLEEVRNNkELKNLT 547
Cdd:PLN03232 439 LGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNE-ELSWFR 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 548 KLGCYMAVTSFQFNIVPFLVSCCTFAVFVYTEDRaLTTDLVFPALTLFNLLSFPLMIIPMVLNSFIEASVSIGRLFTFFT 627
Cdd:PLN03232 518 KAQLLSAFNSFILNSIPVVVTLVSFGVFVLLGGD-LTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLL 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 628 NEE--------LQPdsvqrlpkvkniGDVAINIgDDATFLWQRKPEyKVALKNINFQAKKGNLTCIVGKVGSGKTALLSC 699
Cdd:PLN03232 597 SEErilaqnppLQP------------GAPAISI-KNGYFSWDSKTS-KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISA 662
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 700 MLGDLFRVKGFATV-HGSVAYVSQVPWIMNGTVKENILFGHRYDAEFYEKTIKACALTIDLAILMDGDKTLVGEKGISLS 778
Cdd:PLN03232 663 MLGELSHAETSSVViRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNIS 742
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 779 GGQKARLSLARAVYARADTYLLDDPLAAVDEHVARHLIEHVLGPNglLHTKTKVLATNKVSALSIADSIALLDNGEITQQ 858
Cdd:PLN03232 743 GGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDE--LKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEE 820
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 859 GTYDEITKDADSpLWKLLNNYGKKnngksnefgdssessvressipvegELEQLQKLNDLDFGNSDAI*LRRA*DA*LG* 938
Cdd:PLN03232 821 GTFAELSKSGSL-FKKLMENAGKM-------------------------DATQEVNTNDENILKLGPTVTIDVSERNLGS 874
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 939 IDFGDDEN--IAKREHREQGKVKWNIYLEYAKACNPKSVcVFILFI--VISMFLSVMGNVWLKHWSEVNSRYGSNPnaAR 1014
Cdd:PLN03232 875 TKQGKRGRsvLVKQEERETGIISWNVLMRYNKAVGGLWV-VMILLVcyLTTEVLRVSSSTWLSIWTDQSTPKSYSP--GF 951
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1015 YLAIYFALGIGSALATLIQTIVLwVFCTIHASKYLHNLMTNSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTFSQ 1094
Cdd:PLN03232 952 YIVVYALLGFGQVAVTFTNSFWL-ISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNM 1030
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1095 FFVNAVKVTFTITVICATTWQFIFIIIPLSVFYIYYQQYYLRTSRELRRLDSITRSPIYSHFQETLGGLATVRGYSQQKR 1174
Cdd:PLN03232 1031 FMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDR 1110
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1175 FSHINQCRIDNNMSAFYPSINANRWLAYRLELIGSIIILGAATLSVFRLKQGTLTAG---MVGLSLSYALQITQTLNWIV 1251
Cdd:PLN03232 1111 MAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLRNGNAENQAGfasTMGLLLSYTLNITTLLSGVL 1190
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1252 RMTVEVETNIVSVERIKEYADLKSEAPLIVEGHRPPKEWPSQGDIKFNNYSTRYRPELDLVLKHINIHIKPNEKVGIVGR 1331
Cdd:PLN03232 1191 RQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGR 1270
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1332 TGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQVFEGTVRENIDPINQYTDEAIWRALELSHL 1411
Cdd:PLN03232 1271 TGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHI 1350
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1412 KEhVLSMSNDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKDRTILTIAHR 1491
Cdd:PLN03232 1351 KD-VIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHR 1429
|
1530 1540 1550 1560
....*....|....*....|....*....|....*....|....*.
9AYC_A 1492 LNTIMDSDRIIVLDNGKVAEFDSPGQLLSDNKSLFYSLCMEAGLVN 1537
Cdd:PLN03232 1430 LNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPAN 1475
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
316-1534 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 740.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 316 FFKAIHDVLAFTQPQLLRILIKFVtdynserqDDHSSLQGfennhpqklpivRGFLIAFAMFLVGFTQTSVLHQYFLNVF 395
Cdd:PTZ00243 251 PFKLLSDVCTLTLPVLLKYFVKFL--------DADNATWG------------RGLGLVLTLFLTQLIQSVCLHRFYYISI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 396 NTGMYIKSALTALIYQKSLVLSNEASGLS--STGDIVNLMSVDVQKLQDLTQWLNLIWSGPFQIIICLYSLYKLLGNSMW 473
Cdd:PTZ00243 311 RCGLQYRSALNALIFEKCFTISSKSLAQPdmNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCAL 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 474 VGVIILVIMMPLNSFLMRIQKKLQKSQMKYKDERTRVISEILNNIKSLKLYAWEKPYREKLEEVRNnKELKNLTKLGCYM 553
Cdd:PTZ00243 391 MAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRA-RELRYLRDVQLAR 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 554 AVTSFQFNIVPFLVSCCTFAVFvYTEDRALTTDLVFPALTLFNLLSFPLMIIPMVLNSFIEASVSIGRLFTFFTNEELQP 633
Cdd:PTZ00243 470 VATSFVNNATPTLMIAVVFTVY-YLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLECDNATC 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 634 DSVQ------------------------------------RLPKVK---------------------------------- 643
Cdd:PTZ00243 549 STVQdmeeywreqrehstacqlaavlenvdvtafvpvklpRAPKVKtsllsralrmlcceqcrptkrhpspsvvvedtdy 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 644 --------NIGDVAINIGDDATFLWQRKP-------------EYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLG 702
Cdd:PTZ00243 629 gspssasrHIVEGGTGGGHEATPTSERSAktpkmktddffelEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLS 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 703 DLFRVKGFATVHGSVAYVSQVPWIMNGTVKENILFGHRYDAEFYEKTIKACALTIDLAILMDGDKTLVGEKGISLSGGQK 782
Cdd:PTZ00243 709 QFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQK 788
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 783 ARLSLARAVYARADTYLLDDPLAAVDEHVARHLIEHVLgpNGLLHTKTKVLATNKVSALSIADSIALLDNGEITQQGTYD 862
Cdd:PTZ00243 789 ARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF--LGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSA 866
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 863 EItkdADSPLWKLLNNYGKKN----NGKSNEFGDSSESSVRESSIPVEGELEQLQKLNDLDFGNSDAI*LRra*da*lg* 938
Cdd:PTZ00243 867 DF---MRTSLYATLAAELKENkdskEGDADAEVAEVDAAPGGAVDHEPPVAKQEGNAEGGDGAALDAAAGR--------- 934
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 939 idfgddenIAKREHREQGKVKWNIYLEYAKACNPKSVCVFILFI-VISMFLSVMGNVWLKHWSEVNSRYGSNPNAARYLA 1017
Cdd:PTZ00243 935 --------LMTREEKASGSVPWSTYVAYLRFCGGLHAAGFVLATfAVTELVTVSSGVWLSMWSTRSFKLSAATYLYVYLG 1006
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1018 IYFALGIGSALAtliqtivlWVFC---TIHASKYLHNLMTNSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTFSQ 1094
Cdd:PTZ00243 1007 IVLLGTFSVPLR--------FFLSyeaMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLY 1078
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1095 FFVNAVKVTFTITVICATTWQFIFIIIPlsVFYIYYQ--QYYLRTSRELRRLDSITRSPIYSHFQETLGGLATVRGYSQQ 1172
Cdd:PTZ00243 1079 LLQCLFSICSSILVTSASQPFVLVALVP--CGYLYYRlmQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKA 1156
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1173 KRFSHINQCRIDNNMSAFYPSINANRWLAYRLELIGSIIILGAATLSVFR--LKQGTLTAGMVGLSLSYALQITQTLNWI 1250
Cdd:PTZ00243 1157 HLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGVIGtmLRATSQEIGLVSLSLTMAMQTTATLNWL 1236
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1251 VRMTVEVETNIVSVERIKEYAD----------------LKSE--------APLIVEGHRPPKEWP---SQGDIKFNNYST 1303
Cdd:PTZ00243 1237 VRQVATVEADMNSVERLLYYTDevphedmpeldeevdaLERRtgmaadvtGTVVIEPASPTSAAPhpvQAGSLVFEGVQM 1316
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1304 RYRPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQVF 1383
Cdd:PTZ00243 1317 RYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLF 1396
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1384 EGTVRENIDPINQYTDEAIWRALELSHLKEHVLSMSnDGLDAQLTEGGGNLSVGQRQLLCLARAMLVP-SKILVLDQATA 1462
Cdd:PTZ00243 1397 DGTVRQNVDPFLEASSAEVWAALELVGLRERVASES-EGIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFILMDEATA 1475
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
9AYC_A 1463 AVDVETDKVVQETIRTAFKDRTILTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQLLSDNKSLFYSLcMEAG 1534
Cdd:PTZ00243 1476 NIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSM-VEAL 1546
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
234-1526 |
1.30e-177 |
|
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: 572.62 E-value: 1.30e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 234 NPYDSANIFSRITFSWMSGLMKTGYEKYLVEADLYKLPRNFSSEELSQKLEKNWENEL-KQKSNPSLSWAICRTFGSKML 312
Cdd:TIGR01271 4 SPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELaSAKKNPKLLNALRRCFFWRFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 313 LAAFFKAIHDVLAFTQPQLL-RILIKFVTDYNSERQddhsslqgfennhpqklpivRGFLIAFAMFLVGFTQTSVLHQYF 391
Cdd:TIGR01271 84 FYGILLYFGEATKAVQPLLLgRIIASYDPFNAPERE--------------------IAYYLALGLCLLFIVRTLLLHPAI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 392 LNVFNTGMYIKSALTALIYQKSLVLSNEASGLSSTGDIVNLMSVDVQKLQDLTQWLNLIWSGPFQIIICLYSLYKLLGNS 471
Cdd:TIGR01271 144 FGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 472 MWVGVIILVImmplnsfLMRIQKKLQKSQMKYKDERTRVI-------SEILNNIKSLKLYAWEKPYREKLEEVRNNkELK 544
Cdd:TIGR01271 224 GFCGLGFLIL-------LALFQACLGQKMMPYRDKRAGKIserlaitSEIIENIQSVKAYCWEEAMEKIIKNIRQD-ELK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 545 NLTKLGC--YMAVTSFQFNIVpflvscctFAVFVYTEDRALTTDLVFPalTLFNLLSFPLMI-------IPMVLNSFIEA 615
Cdd:TIGR01271 296 LTRKIAYlrYFYSSAFFFSGF--------FVVFLSVVPYALIKGIILR--RIFTTISYCIVLrmtvtrqFPGAIQTWYDS 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 616 SVSIGRLFTFF------------TNEELQPDSV---------QRLPKVK-NIGDVAINIGDDATFLWQRKPEYKVALKNI 673
Cdd:TIGR01271 366 LGAITKIQDFLckeeyktleynlTTTEVEMVNVtaswdegigELFEKIKqNNKARKQPNGDDGLFFSNFSLYVTPVLKNI 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 674 NFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGSVAYVSQVPWIMNGTVKENILFGHRYDAEFYEKTIKAC 753
Cdd:TIGR01271 446 SFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKAC 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 754 ALTIDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARHLIEHVLGPngLLHTKTKVL 833
Cdd:TIGR01271 526 QLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCK--LMSNKTRIL 603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 834 ATNKVSALSIADSIALLDNGEITQQGTYDEI------------------------------------TKDADSPL----- 872
Cdd:TIGR01271 604 VTSKLEHLKKADKILLLHEGVCYFYGTFSELqakrpdfsslllgleafdnfsaerrnsiltetlrrvSIDGDSTVfsgpe 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 873 -------------------------------WKLLNNYGKKNNGKSNEFGDSSESSVRESSIP----------------- 904
Cdd:TIGR01271 684 tikqsfkqpppefaekrkqsiilnpiasarkFSFVQMGPQKAQATTIEDAVREPSERKFSLVPedeqgeeslprgnqyhh 763
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 905 ---------------------VEGELEQLQ----KLNDLDFGNSDAI*L-----RRA*DA*LG*IDFGDDENI----AKR 950
Cdd:TIGR01271 764 glqhqaqrrqsvlqlmthsnrGENRREQLQtsfrKKSSITQQNELASELdiysrRLSKDSVYEISEEINEEDLkecfADE 843
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 951 EHREQGKVKWNIYLEYAKAcNPKSVCVFILFIVIsmFL-----SVMGnVWL-------KHWSEVNSRYGSNP-------- 1010
Cdd:TIGR01271 844 RENVFETTTWNTYLRYITT-NRNLVFVLIFCLVI--FLaevaaSLLG-LWLitdnpsaPNYVDQQHANASSPdvqkpvii 919
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1011 -NAARYLAIYFALGIGSALATL--IQTIVLwVFCTIHASKYLHNLMTNSVLRAPMTFFETTPIGRILNRFSNDIYKVDAL 1087
Cdd:TIGR01271 920 tPTSAYYIFYIYVGTADSVLALgfFRGLPL-VHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDM 998
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1088 LGRT---FSQFFVNAVKVTFTITVIcattWQFIFI-IIPLSVFYIYYQQYYLRTSRELRRLDSITRSPIYSHFQETLGGL 1163
Cdd:TIGR01271 999 LPLTlfdFIQLTLIVLGAIFVVSVL----QPYIFIaAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGL 1074
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1164 ATVRGYSQQKRFSHINQCRIDNNMSAFYPSINANRWLAYRLELIGSIIILGAATLSVFRLKQGtltAGMVGLSLSYALQI 1243
Cdd:TIGR01271 1075 WTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFIAIGTNQDG---EGEVGIILTLAMNI 1151
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1244 TQTLNWIVRMTVEVETNIVSVERIKEYADLKSEAP--------------LIVEGHRPPKEWPSQGDIKFNNYSTRYRPEL 1309
Cdd:TIGR01271 1152 LSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPrpsggggkyqlstvLVIENPHAQKCWPSGGQMDVQGLTAKYTEAG 1231
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1310 DLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIeASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQVFEGTVRE 1389
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRK 1310
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1390 NIDPINQYTDEAIWRALELSHLKEhVLSMSNDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETD 1469
Cdd:TIGR01271 1311 NLDPYEQWSDEEIWKVAEEVGLKS-VIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTL 1389
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 1470 KVVQETIRTAFKDRTILTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQLLSDnKSLF 1526
Cdd:TIGR01271 1390 QIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNE-TSLF 1445
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1294-1515 |
7.67e-133 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 409.96 E-value: 7.67e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1294 GDIKFNNYSTRYRPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKL 1373
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1374 SIIPQDSQVFEGTVRENIDPINQYTDEAIWRALELSHLKEHVLSMSnDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSK 1453
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLP-GGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
9AYC_A 1454 ILVLDQATAAVDVETDKVVQETIRTAFKDRTILTIAHRLNTIMDSDRIIVLDNGKVAEFDSP 1515
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
977-1271 |
8.54e-127 |
|
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: 396.85 E-value: 8.54e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 977 VFILFIVISMFLSVMGNVWLKHWSEVNSRYGSNPNAAR--YLAIYFALGIGSALATLIQTIVLWvFCTIHASKYLHNLMT 1054
Cdd:cd18603 3 LILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDTEQRdyRLGVYGALGLGQAIFVFLGSLALA-LGCVRASRNLHNKLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1055 NSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTFSQFFVNAVKVTFTITVICATTWQFIFIIIPLSVFYIYYQQYY 1134
Cdd:cd18603 82 HNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRFY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1135 LRTSRELRRLDSITRSPIYSHFQETLGGLATVRGYSQQKRFSHINQCRIDNNMSAFYPSINANRWLAYRLELIGSIIILG 1214
Cdd:cd18603 162 VATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVLF 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 1215 AATLSVfrLKQGTLTAGMVGLSLSYALQITQTLNWIVRMTVEVETNIVSVERIKEYA 1271
Cdd:cd18603 242 AALFAV--LSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
964-1529 |
1.32e-124 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 401.85 E-value: 1.32e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 964 LEYAKAcNPKSVCVFILFIVISMFLSVMGNVWLKHWSEVNSRYGSNPNAARYLAIYFALGIGSALATLIQTIVLWVFcTI 1043
Cdd:COG1132 13 LRYLRP-YRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARL-AQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1044 HASKYLHNLMTNSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTFSQFFVNAVKVTFTITVICATTWQ---FIFII 1120
Cdd:COG1132 91 RVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRlalIVLLV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1121 IPLSVF-YIYYQQYYLRTSRELRRldsiTRSPIYSHFQETLGGLATVRGYSQQ----KRFSHINqcriDNNMSAFYPSIN 1195
Cdd:COG1132 171 LPLLLLvLRLFGRRLRKLFRRVQE----ALAELNGRLQESLSGIRVVKAFGREerelERFREAN----EELRRANLRAAR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1196 ANRWLAYRLELIGSIIILGAATLSVFRLKQGTLTAGMVGLSLSYALQITQTLNWIVRMTVEVETNIVSVERIKEYADLKS 1275
Cdd:COG1132 243 LSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1276 EaplIVEGHRPPKEWPSQGDIKFNNYSTRYRPElDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIV 1355
Cdd:COG1132 323 E---IPDPPGAVPLPPVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1356 IDNIAINEIGLYDLRHKLSIIPQDSQVFEGTVRENI---DPinQYTDEAIWRALELSHLKEHVLSMSnDGLDAQLTEGGG 1432
Cdd:COG1132 399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAKAAQAHEFIEALP-DGYDTVVGERGV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1433 NLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKDRTILTIAHRLNTIMDSDRIIVLDNGKVAEF 1512
Cdd:COG1132 476 NLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQ 555
|
570
....*....|....*..
9AYC_A 1513 DSPGQLLSDNkSLFYSL 1529
Cdd:COG1132 556 GTHEELLARG-GLYARL 571
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
975-1271 |
2.12e-119 |
|
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: 376.46 E-value: 2.12e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 975 VCVFILFIVISMFLSVMGNVWLKHWSEVNSRyGSNPNAARYLAIYFALGIGSALATLIQTIVLWVFCTIHASKYLHNLMT 1054
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSS-SPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1055 NSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTFSQFFVNAVKVTFTITVICATTWQFIFIIIPLSVFYIYYQQYY 1134
Cdd:cd18580 80 RSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1135 LRTSRELRRLDSITRSPIYSHFQETLGGLATVRGYSQQKRFSHINQCRIDNNMSAFYPSINANRWLAYRLELIGSIIILG 1214
Cdd:cd18580 160 LRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 1215 AATLSVFRLkqGTLTAGMVGLSLSYALQITQTLNWIVRMTVEVETNIVSVERIKEYA 1271
Cdd:cd18580 240 VALLAVLLR--SSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
313-622 |
1.90e-117 |
|
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: 371.03 E-value: 1.90e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 313 LAAFFKAIHDVLAFTQPQLLRILIKFVTDYNSerqddhsslqgfennhpqklPIVRGFLIAFAMFLVGFTQTSVLHQYFL 392
Cdd:cd18595 1 LAALLKLLSDILLFASPQLLKLLINFVEDPDE--------------------PLWKGYLYAVLLFLVSIIQSLLLHQYFH 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 393 NVFNTGMYIKSALTALIYQKSLVLSNEASGLSSTGDIVNLMSVDVQKLQDLTQWLNLIWSGPFQIIICLYSLYKLLGNSM 472
Cdd:cd18595 61 RCFRLGMRIRTALTSAIYRKALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 473 WVGVIILVIMMPLNSFLMRIQKKLQKSQMKYKDERTRVISEILNNIKSLKLYAWEKPYREKLEEVRnNKELKNLTKLGCY 552
Cdd:cd18595 141 LAGLGVMILLIPLNAVLARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIR-EKELKLLKKAAYL 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
9AYC_A 553 MAVTSFQFNIVPFLVSCCTFAVFVYT-EDRALTTDLVFPALTLFNLLSFPLMIIPMVLNSFIEASVSIGRL 622
Cdd:cd18595 220 NAVSSFLWTCAPFLVSLATFATYVLSdPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
313-622 |
1.31e-111 |
|
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: 354.87 E-value: 1.31e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 313 LAAFFKAIHDVLAFTQPQLLRILIKFVTDYNSErqddhsslqgfennhpqklPIVRGFLIAFAMFLVGFTQTSVLHQYFL 392
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPDE-------------------PLSEGYLLALALFLVSLLQSLLLHQYFF 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 393 NVFNTGMYIKSALTALIYQKSLVLSNEASGLSSTGDIVNLMSVDVQKLQDLTQWLNLIWSGPFQIIICLYSLYKLLGNSM 472
Cdd:cd18579 62 LSFRLGMRVRSALSSLIYRKALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 473 WVGVIILVIMMPLNSFLMRIQKKLQKSQMKYKDERTRVISEILNNIKSLKLYAWEKPYREKLEEVRnNKELKNLTKLGCY 552
Cdd:cd18579 142 LAGLGVLLLLIPLQAFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELR-KKELKALRKFGYL 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 553 MAVTSFQFNIVPFLVSCCTFAVFVYTeDRALTTDLVFPALTLFNLLSFPLMIIPMVLNSFIEASVSIGRL 622
Cdd:cd18579 221 RALNSFLFFSTPVLVSLATFATYVLL-GNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
655-854 |
1.17e-103 |
|
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: 329.04 E-value: 1.17e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 655 DATFLWQRKP-EYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGSVAYVSQVPWIMNGTVKE 733
Cdd:cd03250 5 DASFTWDSGEqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNGTIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 734 NILFGHRYDAEFYEKTIKACALTIDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVAR 813
Cdd:cd03250 85 NILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
9AYC_A 814 HLIEHVLGPNgLLHTKTKVLATNKVSALSIADSIALLDNGE 854
Cdd:cd03250 165 HIFENCILGL-LLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
975-1271 |
6.88e-100 |
|
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: 322.12 E-value: 6.88e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 975 VCVFILFIVISMFLSVMGNVWLKHWSEvnsRYGSNPNAArYLAIYFALGIGSALATLIQTIVLwVFCTIHASKYLHNLMT 1054
Cdd:cd18606 1 LPLLLLLLILSQFAQVFTNLWLSFWTE---DFFGLSQGF-YIGIYAGLGVLQAIFLFLFGLLL-AYLGIRASKRLHNKAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1055 NSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTFSQFFVNAVKVTFTITVICATTWQFIFIIIPLSVFYIYYQQYY 1134
Cdd:cd18606 76 KRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1135 LRTSRELRRLDSITRSPIYSHFQETLGGLATVRGYSQQKRFSHINQCRIDNNMSAFYPSINANRWLAYRLELIGSIIILG 1214
Cdd:cd18606 156 RASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLI 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 1215 AATLSVFRlkQGTLTAGMVGLSLSYALQITQTLNWIVRMTVEVETNIVSVERIKEYA 1271
Cdd:cd18606 236 VALLCVTR--RFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
977-1270 |
1.11e-98 |
|
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: 319.03 E-value: 1.11e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 977 VFILFIVISMFLSVMGNVWLKHWSE----VNSRYGSNPNAARYLAIYFALGIGSALATLIQTIVlWVFCTIHASKYLHNL 1052
Cdd:cd18604 3 LLLLLFVLSQLLSVGQSWWLGIWASayetSSALPPSEVSVLYYLGIYALISLLSVLLGTLRYLL-FFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1053 MTNSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTFSQFFVNAVKVTFTITVICATTWQFIFIIIPLSVFYIYYQQ 1132
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1133 YYLRTSRELRRLDSITRSPIYSHFQETLGGLATVRGYSQQKRFSHINQCRIDNNMSAFYPSINANRWLAYRLELIGSIII 1212
Cdd:cd18604 162 LYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFS 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 1213 LGAATLSVFrlkQGTLTAGMVGLSLSYALQITQTLNWIVRMTVEVETNIVSVERIKEY 1270
Cdd:cd18604 242 FATAALLVY---GPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEY 296
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1020-1529 |
6.04e-97 |
|
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: 329.10 E-value: 6.04e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1020 FALGIGSALATLIQTIVLWV--FCTIHASKYLHNLMTNSV----LRAPMTFFETTPIGRILNRFsNDIYKVDALLGRTFS 1093
Cdd:COG2274 196 WVLAIGLLLALLFEGLLRLLrsYLLLRLGQRIDLRLSSRFfrhlLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1094 QFFVNAVKVTFTITVICATTWQFIFI---IIPLSVFYIYY-QQYYLRTSRELRRLDSITrspiYSHFQETLGGLATVR-- 1167
Cdd:COG2274 275 TALLDLLFVLIFLIVLFFYSPPLALVvllLIPLYVLLGLLfQPRLRRLSREESEASAKR----QSLLVETLRGIETIKal 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1168 GYSQ--QKRFSHINQCRIDNNMSAFYPSINANRWLAYrLELIGSIIILGAATLSVFrlkQGTLTAGMVGLSLSYALQITQ 1245
Cdd:COG2274 351 GAESrfRRRWENLLAKYLNARFKLRRLSNLLSTLSGL-LQQLATVALLWLGAYLVI---DGQLTLGQLIAFNILSGRFLA 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1246 TLNWIVRMTVEVETNIVSVERIKEYADLKSEAPLIVEGHRPPKEwpsQGDIKFNNYSTRYRPELDLVLKHINIHIKPNEK 1325
Cdd:COG2274 427 PVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRL---KGDIELENVSFRYPGDSPPVLDNISLTIKPGER 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1326 VGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQVFEGTVRENI---DPinQYTDEAI 1402
Cdd:COG2274 504 VAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDP--DATDEEI 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1403 WRALELSHLKEHVLSMSNdGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKD 1482
Cdd:COG2274 582 IEAARLAGLHDFIEALPM-GYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKG 660
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
9AYC_A 1483 RTILTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQLLSdNKSLFYSL 1529
Cdd:COG2274 661 RTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLA-RKGLYAEL 706
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1290-1515 |
7.55e-94 |
|
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: 301.64 E-value: 7.55e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1290 WPSQGDIKFNNYSTRYRPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDL 1369
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1370 RHKLSIIPQDSQVFEGTVRENIDPINQYTDEAIWRALELShlkehvlsmsndgldaqltEGGGNLSVGQRQLLCLARAML 1449
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALRVS-------------------EGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 1450 VPSKILVLDQATAAVDVETDKVVQETIRTAFKDRTILTIAHRLNTIMDSDRIIVLDNGKVAEFDSP 1515
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
975-1271 |
1.11e-84 |
|
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: 279.87 E-value: 1.11e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 975 VCVFILFIVISMFLSVMGNVWLKHWSEVNSRYGS-----------NPNAARYLAIYFALGIGSALATLIQTIVLwVFCTI 1043
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWTEANHDVASvvfnitsssleDDEVSYYISVYAGLSLGAVILSLVTNLAG-ELAGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1044 HASKYLHNLMTNSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTFSQFFVNAVKVTFTITVICATTWQFIFIIIPL 1123
Cdd:cd18602 80 RAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1124 SVFYIYYQQYYLRTSRELRRLDSITRSPIYSHFQETLGGLATVRGYSQQKRFSHINQCRIDNNMSAFYPSINANRWLAYR 1203
Cdd:cd18602 160 IIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 1204 LELIGSIIILGAATLSVFRLKQGTLTAGMVGLSLSYALQITQTLNWIVRMTVEVETNIVSVERIKEYA 1271
Cdd:cd18602 240 LDYLGAVIVFLAALSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
976-1270 |
3.45e-84 |
|
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: 277.87 E-value: 3.45e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 976 CVFILFIVISMFLSVMGN-VWLKHW---SEVNSRYGSNPNAARYLAIYFALGIGSALATLIQTiVLWVFCTIHASKYLHN 1051
Cdd:cd18605 1 LILILLSLILMQASRNLIdFWLSYWvshSNNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRA-FLFAYGGLRAARRLHN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1052 LMTNSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTFSQFFVNAVKVTFTITVICATTWQFIFIIIPLSVFYIYYQ 1131
Cdd:cd18605 80 KLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1132 QYYLRTSRELRRLDSITRSPIYSHFQETLGGLATVRGYSQQKRFSHINQCRIDNNMSAFYPSINANRWLAYRLELIGSII 1211
Cdd:cd18605 160 RYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVLI 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1212 ILGAATLSVF-RLKQGTLTAGMVGLSLSYALQITQTLNWIVRMTVEVETNIVSVERIKEY 1270
Cdd:cd18605 240 VTFVALTAVVqHFFGLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQY 299
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1294-1531 |
2.43e-81 |
|
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: 268.32 E-value: 2.43e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1294 GDIKFNNYSTRYRPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKL 1373
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1374 SIIPQDSQVFEGTVRENIDPINQYTDEAIWRALELSHLKEHVLSMSNdGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSK 1453
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPG-GLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 1454 ILVLDQATAAVDVETDKVVQETIRTAFKDRTILTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQLLSDNKSLFYSLCM 1531
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVR 254
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
313-622 |
6.61e-80 |
|
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: 265.47 E-value: 6.61e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 313 LAAFFKAIHDVLAFTQPQLLRILIKFVTDYNSERQDdhsslqgfennhpqkLPIVRGFLIAFAMFLVGFTQTSVLHQYFL 392
Cdd:cd18597 1 LAGLLKLLADVLQVLSPLLLKYLINFVEDAYLGGPP---------------PSIGYGIGYAIGLFLLQLLSSLLLNHFFY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 393 NVFNTGMYIKSALTALIYQKSLVLSNEASGLSSTGDIVNLMSVDVQKLQDLTQWLNLIWSGPFQIIICLYSLYKLLGNSM 472
Cdd:cd18597 66 RSMLTGAQVRAALTKAIYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 473 WVGVIILVIMMPLNSFLMRIQKKLQKSQMKYKDERTRVISEILNNIKSLKLYAWEKPYREKLEEVRnNKELKNLTKLGCY 552
Cdd:cd18597 146 LVGIGVLILSIPLQGFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIR-KKELKYVRKLQIL 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 553 MAVTSFQFNIVPFLVSCCTFAVFVYTeDRALTTDLVFPALTLFNLLSFPLMIIPMVLNSFIEASVSIGRL 622
Cdd:cd18597 225 RSILTAVAFSLPVLASMLSFITYYAT-GHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
974-1271 |
2.55e-75 |
|
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: 253.25 E-value: 2.55e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 974 SVCVFILFI-VISMFLSVMGNVWLKHW----------SEVNSRYGS-----NPNAARYLAIYFALGIGSALATLIQTIVL 1037
Cdd:cd18599 3 VVFLFVLLLfILSVGSTVFSDWWLSYWlkqgsgnttnNVDNSTVDSgnisdNPDLNFYQLVYGGSILVILLLSLIRGFVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1038 wVFCTIHASKYLHNLMTNSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTFSQFFVNAVKVTFTITVICATTWQFI 1117
Cdd:cd18599 83 -VKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWFL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1118 FIIIPLSVFYIYYQQYYLRTSRELRRLDSITRSPIYSHFQETLGGLATVRGYSQQKRFSHINQCRIDNNMSAFYPSINAN 1197
Cdd:cd18599 162 IALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCAM 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
9AYC_A 1198 RWLAYRLELIGSIIILGAATLSVFrlKQGTLTAGMVGLSLSYALQITQTLNWIVRMTVEVETNIVSVERIKEYA 1271
Cdd:cd18599 242 RWLAVRLDILAVLITLITALLVVL--LKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
974-1271 |
4.66e-73 |
|
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: 246.85 E-value: 4.66e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 974 SVCVFILFIVISMF---LSVMGNVWLKHWSEVNSRYGSNP----------------NAARYLAIYFALgIGSALATLIQT 1034
Cdd:cd18601 1 GVFVFILLVLLNIAaqvLYVLSDWWLSYWANLEEKLNDTTdrvqgenstnvdiedlDRDFNLGIYAGL-TAATFVFGFLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1035 IVLWVFCTIHASKYLHNLMTNSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTFSQFFVNAVKVTFTITVICATT- 1113
Cdd:cd18601 80 SLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1114 WQFIFIIiPLSVFYIYYQQYYLRTSRELRRLDSITRSPIYSHFQETLGGLATVRGYSQQKRFSHINQCRIDNNMSAFYPS 1193
Cdd:cd18601 160 WVLIPVI-PLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLF 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 1194 INANRWLAYRLELIGSIIILGAATLSVFrLKQgTLTAGMVGLSLSYALQITQTLNWIVRMTVEVETNIVSVERIKEYA 1271
Cdd:cd18601 239 LATSRWLAVRLDALCALFVTVVAFGSLF-LAE-SLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEYS 314
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
311-622 |
6.66e-73 |
|
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: 245.87 E-value: 6.66e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 311 MLLAAFFKAihdVLAFTQPQLLRILIKFVTDYNSErqddhsslqgfennhpqklPIVRGFLIAFAMFLVGFTQTSVLHQY 390
Cdd:cd18596 2 QALLAVLSS---VLSFAPPFFLNRLLRYLEDPGED-------------------ATVRPWVWVLLLFLGPLLSSLLDQQY 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 391 FLNVFNTGMYIKSALTALIYQKSLVL-------------------SNEASGLSSTGDIVNLMSVDVQKLQDLTQWLNLIW 451
Cdd:cd18596 60 LWIGRRLSVRLRAILTQLIFEKALRRrdksgssksseskkkdkeeDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 452 SGPFQIIICLYSLYKLLGNSMWVGVIILVIMMPLNSFLMRIQKKLQKSQMKYKDERTRVISEILNNIKSLKLYAWEKPYR 531
Cdd:cd18596 140 SAPLQIVIAIVFLYRLLGWSALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 532 EKLEEVRnNKELKNLTKLGCYMAVTSFQFNIVPFLVSCCTFAVFVYTEDRALTTDLVFPALTLFNLLSFPLMIIPMVLNS 611
Cdd:cd18596 220 ERILEAR-EEELKWLRKRFLLDLLLSLLWFLIPILVTVVTFATYTLVMGQELTASVAFTSLALFNMLRGPLNVLPELITQ 298
|
330
....*....|.
9AYC_A 612 FIEASVSIGRL 622
Cdd:cd18596 299 LLQAKVSLDRI 309
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1294-1522 |
3.32e-72 |
|
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: 240.98 E-value: 3.32e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1294 GDIKFNNYSTRYRPElDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKL 1373
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1374 SIIPQDSQVFEGTVRENIDPINQY-TDEAIWRALELSHLKEHVLSMSNdGLDAQLTEGGGNLSVGQRQLLCLARAMLVPS 1452
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNaTDEEVIEAAKEAGAHDFIMKLPN-GYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1453 KILVLDQATAAVDVETDKVVQETIRTAFKDRTILTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQLLSDN 1522
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
974-1522 |
4.01e-72 |
|
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: 252.76 E-value: 4.01e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 974 SVCVFILFIVISMFLS-VMGNVWLKHWSEvnsrygsnPNAARYLAIYFALGIGSALATLIQTIVLwVFCTIHASKYLHNL 1052
Cdd:COG4988 26 GLLSGLLIIAQAWLLAsLLAGLIIGGAPL--------SALLPLLGLLLAVLLLRALLAWLRERAA-FRAAARVKRRLRRR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1053 MTNSVLRAPMTFFETTPIGRILNRFsndIYKVDAL---LGRTFSQFFVNAVkVTFTITVICATT-WQ--FIFII----IP 1122
Cdd:COG4988 97 LLEKLLALGPAWLRGKSTGELATLL---TEGVEALdgyFARYLPQLFLAAL-VPLLILVAVFPLdWLsgLILLVtaplIP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1123 LsvFYIYYQQYYLRTSRelRRLDSITR-SpiySHFQETLGGLATVRGYSQQKR-----------FSHINqcridnnMS-- 1188
Cdd:COG4988 173 L--FMILVGKGAAKASR--RQWRALARlS---GHFLDRLRGLTTLKLFGRAKAeaeriaeasedFRKRT-------MKvl 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1189 --AFyPSINAnrwlayrLELIGSI-IILGAATLsVFRLKQG--TLTAGMVGLSLS---YalqitQTLN-----WIVRMTv 1255
Cdd:COG4988 239 rvAF-LSSAV-------LEFFASLsIALVAVYI-GFRLLGGslTLFAALFVLLLApefF-----LPLRdlgsfYHARAN- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1256 evetNIVSVERIKEYadLKSEAPLIVEGHRPPkEWPSQGDIKFNNYSTRYrPELDLVLKHINIHIKPNEKVGIVGRTGAG 1335
Cdd:COG4988 304 ----GIAAAEKIFAL--LDAPEPAAPAGTAPL-PAAGPPSIELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1336 KSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQVFEGTVRENI---DPinQYTDEAIWRALELSHLK 1412
Cdd:COG4988 376 KSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLrlgRP--DASDEELEAALEAAGLD 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1413 EHVLSMsNDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKDRTILTIAHRL 1492
Cdd:COG4988 454 EFVAAL-PDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRL 532
|
570 580 590
....*....|....*....|....*....|
9AYC_A 1493 NTIMDSDRIIVLDNGKVAEFDSPGQLLSDN 1522
Cdd:COG4988 533 ALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1296-1522 |
5.47e-65 |
|
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: 220.18 E-value: 5.47e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSI 1375
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1376 IPQDSQVFEGTVRENIdpinQY-----TDEAIWRALELSHLKEHVLSMSnDGLDAQLTEGGGNLSVGQRQLLCLARAMLV 1450
Cdd:cd03251 81 VSQDVFLFNDTVAENI----AYgrpgaTREEVEEAARAANAHEFIMELP-EGYDTVIGERGVKLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
9AYC_A 1451 PSKILVLDQATAAVDVETDKVVQETIRTAFKDRTILTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQLLSDN 1522
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
313-622 |
3.90e-64 |
|
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: 220.95 E-value: 3.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 313 LAAFFKAIHDVLAFTQPqllrILIKFVTDYNSERQDDHSSLQGFENNHPQKLP--IVRGFLIAFAMFLVGFTQTSVLHQY 390
Cdd:cd18591 1 LGGILKLLGDLLGFVGP----LCISGIVDYVEENTYSSSNSTDKLSVSYVTVEefFSNGYVLAVILFLALLLQATFSQAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 391 FLNVFNTGMYIKSALTALIYQKSLVLS--NEASGLSSTGDIVNLMSVDVQKLQDLTQWLNLIWSGPFQIIICLYSLYKLL 468
Cdd:cd18591 77 YHIVIREGIRLKTALQAMIYEKALRLSswNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 469 GNSMWVGVIILVIMMPLNSFLMRIQKKLQKSQMKYKDERTRVISEILNNIKSLKLYAWEKPYREKLEEVRnNKELKNLTK 548
Cdd:cd18591 157 GVSALIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEAR-RKELKLLLK 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
9AYC_A 549 LGCYMAVTSFQFNIVPFLVSCCTFAVFVYTEDRALTTDLVFPALTLFNLLSFPLMIIPMVLNSFIEASVSIGRL 622
Cdd:cd18591 236 DAVYWSLMTFLTQASPILVTLVTFGLYPYLEGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1296-1508 |
2.90e-63 |
|
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: 212.63 E-value: 2.90e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSI 1375
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1376 IPQDSQVFEGTVRENIdpinqytdeaiwralelshlkehvlsmsndgldaqltegggnLSVGQRQLLCLARAMLVPSKIL 1455
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
9AYC_A 1456 VLDQATAAVDVETDKVVQETIRTAFKDRTILTIAHRLNTIMDSDRIIVLDNGK 1508
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
315-622 |
3.04e-63 |
|
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: 217.42 E-value: 3.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 315 AFFKAIHDVLAFTQPQLLRILIKFVTDynserqddhsslqgfennhpQKLPIVRGFLIAFAMFLVGFTqTSVLH-QYFLN 393
Cdd:cd18598 3 GLLKLLADVLGFAGPLLLNKLVEFLED--------------------SSEPLSDGYLYALGLVLSSLL-GALLSsHYNFQ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 394 VFNTGMYIKSALTALIYQKSLVLSNEASGLSSTGDIVNLMSVDVQKLQDLTQWLNLIWSGPFQIIICLYSLYKLLGNSMW 473
Cdd:cd18598 62 MNKVSLKVRAALVTAVYRKALRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 474 VGVIILVIMMPLNSFL-MRIQkKLQKSQMKYKDERTRVISEILNNIKSLKLYAWEKPYREKLEEVRnNKELKNLTKLGCY 552
Cdd:cd18598 142 AGLVFALVLIPINKWIaKRIG-ALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELR-AKELKALKGRKYL 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 553 MAVTSFQFNIVPFLVSCCTFAVFVYTEDRaLTTDLVFPALTLFNLLSFPLMIIPMVLNSFIEASVSIGRL 622
Cdd:cd18598 220 DALCVYFWATTPVLISILTFATYVLMGNT-LTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
301-863 |
1.51e-60 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 219.27 E-value: 1.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 301 WAICRTFGSKMLLAAFFKAIHDVLAFTQPQLLRILIkfvtdynserqDDHSSLQGFEnnhpqklPIVRGFLIAFAMFLVG 380
Cdd:COG1132 13 LRYLRPYRGLLILALLLLLLSALLELLLPLLLGRII-----------DALLAGGDLS-------ALLLLLLLLLGLALLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 381 FTqTSVLHQYFLNVFntGMYIKSALTALIYQKSLVLSNEASGLSSTGDIVNLMSVDVQKLQDLTQW-LNLIWSGPFQIII 459
Cdd:COG1132 75 AL-LSYLQRYLLARL--AQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHgLPQLVRSVVTLIG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 460 CLYSLYKL---LGnsmWVGVIILVIMMPLNSFLMRIQKKLQKSQMKYKDERTRVISEILNNIKSLKLYAWEKPYREKLEE 536
Cdd:COG1132 152 ALVVLFVIdwrLA---LIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFRE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 537 VrNNKELKNLTKLGCYMAVTSFqfnIVPFLVSCCTFAVFVY----TEDRALTTDLVFPALTLFNLLSFPLMIIPMVLNSF 612
Cdd:COG1132 229 A-NEELRRANLRAARLSALFFP---LMELLGNLGLALVLLVggllVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 613 IEASVSIGRLFTFFTNEELQPDSVQRLPKVKNIGDVAInigDDATFlwqRKPEYKVALKNINFQAKKGNLTCIVGKVGSG 692
Cdd:COG1132 305 QRALASAERIFELLDEPPEIPDPPGAVPLPPVRGEIEF---ENVSF---SYPGDRPVLKDISLTIPPGETVALVGPSGSG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 693 KTALLSCMLGdLFRVKG--------------FATVHGSVAYVSQVPWIMNGTVKENILFG--HRYDAEFYEKTIKACALT 756
Cdd:COG1132 379 KSTLVNLLLR-FYDPTSgrilidgvdirdltLESLRRQIGVVPQDTFLFSGTIRENIRYGrpDATDEEVEEAAKAAQAHE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 757 iDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARHLIEHVlgpNGLLHTKTKVLATN 836
Cdd:COG1132 458 -FIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL---ERLMKGRTTIVIAH 533
|
570 580
....*....|....*....|....*..
9AYC_A 837 KVSALSIADSIALLDNGEITQQGTYDE 863
Cdd:COG1132 534 RLSTIRNADRILVLDDGRIVEQGTHEE 560
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
1014-1511 |
1.64e-60 |
|
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: 218.80 E-value: 1.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1014 RYLAIYFALGIGSALATLIQ-TIVLWVFCTIHASkyLHNLMTNSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTF 1092
Cdd:TIGR02204 59 RYFAFLLVVALVLALGTAARfYLVTWLGERVVAD--IRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1093 SQFFVNAVKVTFTITVICATTWQ---FIFIIIPLSVFYIYYQQYYLRT-SRELRrlDSITRSPIYShfQETLGGLATVRG 1168
Cdd:TIGR02204 137 SMALRNALMCIGGLIMMFITSPKltsLVLLAVPLVLLPILLFGRRVRKlSRESQ--DRIADAGSYA--GETLGAIRTVQA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1169 YSQQkrfsHINQCRIDNNMSAFYPSinANRWLAYRLELIGSII--ILGAATLSVF----RLKQGTLTAGMVGLSLSYALQ 1242
Cdd:TIGR02204 213 FGHE----DAERSRFGGAVEKAYEA--ARQRIRTRALLTAIVIvlVFGAIVGVLWvgahDVIAGKMSAGTLGQFVFYAVM 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1243 ITQTLNWIVRMTVEVETNIVSVERIKEYADLKSEAPLIVEGHRPPKewPSQGDIKFNNYSTRY--RPELdLVLKHINIHI 1320
Cdd:TIGR02204 287 VAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPV--PLRGEIEFEQVNFAYpaRPDQ-PALDGLNLTV 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1321 KPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQVFEGTVRENIdpinQY--- 1397
Cdd:TIGR02204 364 RPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENI----RYgrp 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1398 --TDEAIWRALELSHLKEHVLSMSnDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQET 1475
Cdd:TIGR02204 440 daTDEEVEAAARAAHAHEFISALP-EGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQA 518
|
490 500 510
....*....|....*....|....*....|....*.
9AYC_A 1476 IRTAFKDRTILTIAHRLNTIMDSDRIIVLDNGKVAE 1511
Cdd:TIGR02204 519 LETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVA 554
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1296-1529 |
3.88e-60 |
|
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: 206.31 E-value: 3.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELDlVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSI 1375
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1376 IPQDSQVFEGTVRENIdpinQY-----TDEAIWRALELSHLKEHVLSMsNDGLDAQLTEGGGNLSVGQRQLLCLARAMLV 1450
Cdd:cd03253 80 VPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEAAKAAQIHDKIMRF-PDGYDTIVGERGLKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 1451 PSKILVLDQATAAVDVETDKVVQETIRTAFKDRTILTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQLLSDNkSLFYSL 1529
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKG-GLYAEM 232
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1296-1529 |
2.29e-55 |
|
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: 192.75 E-value: 2.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRY--RPELdLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKL 1373
Cdd:cd03249 1 IEFKNVSFRYpsRPDV-PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1374 SIIPQDSQVFEGTVRENID-PINQYTDEAIWRALELSHLKEHVLSMSnDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPS 1452
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIRyGKPDATDEEVEEAAKKANIHDFIMSLP-DGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 1453 KILVLDQATAAVDVETDKVVQETIRTAFKDRTILTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQLLSdNKSLFYSL 1529
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMA-QKGVYAKL 234
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1055-1519 |
1.31e-54 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 201.87 E-value: 1.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1055 NSVLRAPMTFFETTPIGRILNRFSNDIYKVDALlgrtfsqfFVNAVKVTF-TITVICAT-------TWQFIFI---IIP- 1122
Cdd:PRK10790 106 DAALRQPLSAFDTQPVGQLISRVTNDTEVIRDL--------YVTVVATVLrSAALIGAMlvamfslDWRMALVaimIFPa 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1123 -LSVFYIYyQQYYLRTSRELRRLdsitRSPIYSHFQETLGGLATVRGYSQQKRFSHinqcRIDNNMSAFYPSinanRWLA 1201
Cdd:PRK10790 178 vLVVMVIY-QRYSTPIVRRVRAY----LADINDGFNEVINGMSVIQQFRQQARFGE----RMGEASRSHYMA----RMQT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1202 YRLE---------LIGSIIILGaaTLSVFrlkqGTLTAGMVGLSLSYALqitqtLNWIVRMT---VEVETN-------IV 1262
Cdd:PRK10790 245 LRLDgfllrpllsLFSALILCG--LLMLF----GFSASGTIEVGVLYAF-----ISYLGRLNeplIELTTQqsmlqqaVV 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1263 SVERIKEYADlkseAPLIVEGH--RPPkewpSQGDIKFNNYSTRYRPElDLVLKHINIHIKPNEKVGIVGRTGAGKSSLT 1340
Cdd:PRK10790 314 AGERVFELMD----GPRQQYGNddRPL----QSGRIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1341 LALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQVFEGTVRENIDPINQYTDEAIWRALELSHLKEHVLSMSn 1420
Cdd:PRK10790 385 SLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLP- 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1421 DGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKDRTILTIAHRLNTIMDSDR 1500
Cdd:PRK10790 464 DGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADT 543
|
490
....*....|....*....
9AYC_A 1501 IIVLDNGKVAEFDSPGQLL 1519
Cdd:PRK10790 544 ILVLHRGQAVEQGTHQQLL 562
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1207-1519 |
3.94e-53 |
|
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: 197.74 E-value: 3.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1207 IGSIIILGAATLSVfrlKQGTLTAG---MVGLslsYALQITQTLN---WIVRmtvEVETNIVSVERikeYADLKSEAPLI 1280
Cdd:COG5265 275 LGLTAMMLMAAQGV---VAGTMTVGdfvLVNA---YLIQLYIPLNflgFVYR---EIRQALADMER---MFDLLDQPPEV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1281 VEGHRPPKEWPSQGDIKFNNYSTRYRPElDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIA 1360
Cdd:COG5265 343 ADAPDAPPLVVGGGEVRFENVSFGYDPE-RPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQD 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1361 INEIGLYDLRHKLSIIPQDSQVFEGTVRENIdpinQY-----TDEAIWRALELSHLKEHVLSMSnDGLDAQLTEGGGNLS 1435
Cdd:COG5265 422 IRDVTQASLRAAIGIVPQDTVLFNDTIAYNI----AYgrpdaSEEEVEAAARAAQIHDFIESLP-DGYDTRVGERGLKLS 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1436 VGQRQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKDRTILTIAHRLNTIMDSDRIIVLDNGKVAEFDSP 1515
Cdd:COG5265 497 GGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTH 576
|
....
9AYC_A 1516 GQLL 1519
Cdd:COG5265 577 AELL 580
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
941-1529 |
1.26e-51 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 195.33 E-value: 1.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 941 FGDDENIAKREHREQGKVKWNIyLEYAKACNPKSVCVFILfivisMFLSVMGNVWLKHWS-EVNSRYGSNPNAARYLAIY 1019
Cdd:TIGR00958 131 AGASEKEAEQGQSETADLLFRL-LGLSGRDWPWLISAFVF-----LTLSSLGEMFIPFYTgRVIDTLGGDKGPPALASAI 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1020 FALGIGSALATLIqtivlwVFCTIHASKYLHNLMT--------NSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRT 1091
Cdd:TIGR00958 205 FFMCLLSIASSVS------AGLRGGSFNYTMARINlriredlfRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLN 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1092 FSQFFVNAVKVTFTITVICATTWQF---IFIIIPLsVFYI--YYQQYYLRTSRELRrlDSITRSPIYShfQETLGGLATV 1166
Cdd:TIGR00958 279 VNVLLRNLVMLLGLLGFMLWLSPRLtmvTLINLPL-VFLAekVFGKRYQLLSEELQ--EAVAKANQVA--EEALSGMRTV 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1167 RGYSQQK----RF-SHINQCRidnnmsafypSINANRWLAYRL-----ELIGSIIILGAATLSVFRLKQGTLTAGMVGLS 1236
Cdd:TIGR00958 354 RSFAAEEgeasRFkEALEETL----------QLNKRKALAYAGylwttSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSF 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1237 LSYALQITQTLNWIVRMTVEVETNIVSVERIKEYADLKSEAPLIVEgHRPPkewPSQGDIKFNNYSTRY--RPELdLVLK 1314
Cdd:TIGR00958 424 LLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGT-LAPL---NLEGLIEFQDVSFSYpnRPDV-PVLK 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1315 HINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQVFEGTVRENID-P 1393
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyG 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1394 INQYTDEAIWRALELSHLKEHVLSMSNdGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQ 1473
Cdd:TIGR00958 579 LTDTPDEEIMAAAKAANAHDFIMEFPN-GYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQ 657
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 1474 ETirTAFKDRTILTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQLLsDNKSLFYSL 1529
Cdd:TIGR00958 658 ES--RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLM-EDQGCYKHL 710
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1294-1509 |
6.50e-51 |
|
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: 179.32 E-value: 6.50e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1294 GDIKFNNYSTRYRPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKL 1373
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1374 SIIPQDSQVFEGTVRENIDPINQY-TDEAIWRALELSHLKEHVLSmSNDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPS 1452
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNK-HPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 1453 KILVLDQATAAVDVETDKVVQETIRTAFKDRTILTIAHRLNTIMDSDRIIVLDNGKV 1509
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
670-864 |
6.89e-51 |
|
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: 181.59 E-value: 6.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 670 LKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGSVAYVSQVPWIMNGTVKENILFGHRYDAEFYEKT 749
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 750 IKACALTIDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARHLIEHVLGPngLLHTK 829
Cdd:cd03291 133 VKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCK--LMANK 210
|
170 180 190
....*....|....*....|....*....|....*
9AYC_A 830 TKVLATNKVSALSIADSIALLDNGEITQQGTYDEI 864
Cdd:cd03291 211 TRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
317-622 |
1.01e-50 |
|
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: 181.64 E-value: 1.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 317 FKAIHDVLAFTQPQLLRILIKFVTDYNSerqddhsslqgfennhpqklPIVRGFLIAFAMFLVGFTQTSVLHQYFLNVFN 396
Cdd:cd18559 5 IKLVLCNHVFSGPSNLWLLLWFDDPVNG--------------------PQEHGQVYLSVLGALAILQGITVFQYSMAVSI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 397 TGMYIKSALTALIYQKSLVLSNEASGLSSTGDIVNLMSVDVQKLQDLTQWLNLIWSGPFQIIICLYSLYKLLGNSMWVGV 476
Cdd:cd18559 65 GGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 477 IILVIMMPLNSFLMRIQKKLQKSQMKYKDERTRVISEILNNIKSLKLYAWEKPYREKLEEVRNNkELKNLTKLGCYMAVT 556
Cdd:cd18559 145 PLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDN-ELAYLPSIVYLRALA 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 557 SFQFNIVPFLVSCCTFAVFVYTEDRA-LTTDLVFPALTLFNLLSFPLMIIPMVLNSFIEASVSIGRL 622
Cdd:cd18559 224 VRLWCVGPCIVLFASFFAYVSRHSLAgLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1034-1539 |
1.15e-50 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 190.17 E-value: 1.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1034 TIVLWVFCTIHASKYLHN----LMTNS---VLRAPMTFFETTPIGRILNRFsndIYKVDALLG---RTFSQFFVNAVKVT 1103
Cdd:PRK13657 69 NIIAGVLVARHADRLAHRrrlaVLTEYferIIQLPLAWHSQRGSGRALHTL---LRGTDALFGlwlEFMREHLATLVALV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1104 FTITVICATTWQFIFIIIPLSVFYIYYQQYYLRTSRELRRLDSITRSPIYSHFQETLGGLATVRGYSQQKRFSHINQCRI 1183
Cdd:PRK13657 146 VLLPLALFMNWRLSLVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1184 DNNMSAFYPSINanrWLAyrlelIGSIIILGAATLSV--------FRLKQGTLTAGMVGLSLSYALQITQTLNWIVRMTV 1255
Cdd:PRK13657 226 DNLLAAQMPVLS---WWA-----LASVLNRAASTITMlailvlgaALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFIN 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1256 EVetnIVSVERIKEYADLKSEAPLIVE--GHRPPKEwpSQGDIKFNNYSTRY---RPELDlvlkHINIHIKPNEKVGIVG 1330
Cdd:PRK13657 298 QV---FMAAPKLEEFFEVEDAVPDVRDppGAIDLGR--VKGAVEFDDVSFSYdnsRQGVE----DVSFEAKPGQTVAIVG 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1331 RTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQVFEGTVRENI-----DPinqyTDEAIWRA 1405
Cdd:PRK13657 369 PTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIrvgrpDA----TDEEMRAA 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1406 LELSHLKEHVLSmSNDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKDRTI 1485
Cdd:PRK13657 445 AERAQAHDFIER-KPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTT 523
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 1486 LTIAHRLNTIMDSDRIIVLDNGKVAE---FDSpgqlLSDNKSLFYSLCMEAGLVNEN 1539
Cdd:PRK13657 524 FIIAHRLSTVRNADRILVFDNGRVVEsgsFDE----LVARGGRFAALLRAQGMLQED 576
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1296-1529 |
2.66e-50 |
|
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: 178.45 E-value: 2.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSI 1375
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1376 IPQDSQVFEGTVRENIDPINQYTD-EAIWRALELSHLKEHVLSMSnDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKI 1454
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSmERVIEAAKLAGAHDFISELP-EGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
9AYC_A 1455 LVLDQATAAVDVETDKVVQETIRTAFKDRTILTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQLLSDNkSLFYSL 1529
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAEN-GLYAYL 233
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
370-864 |
2.44e-49 |
|
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: 188.50 E-value: 2.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 370 FLIAFAMFLVGFTQTSVLHQYFLNVFNTGMYIKsaLTALIYQKSLVLSNEASGLSSTGDIVNLMSvDVQKLQDL--TQWL 447
Cdd:COG2274 198 LAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLR--LSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFltGSLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 448 NLIWSGPFQII----ICLYSlYKLLgnsmWVGVIILVIMMPLNSFLMRIQKKLQKSQMKYKDERTRVISEILNNIKSLKL 523
Cdd:COG2274 275 TALLDLLFVLIflivLFFYS-PPLA----LVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 524 YAWEKPYREKLEEvRNNKELKNLTKLGcymAVTSFQFNIVPFLVSCCTFAVFVY----TEDRALTTDLVFPALTLFNLLS 599
Cdd:COG2274 350 LGAESRFRRRWEN-LLAKYLNARFKLR---RLSNLLSTLSGLLQQLATVALLWLgaylVIDGQLTLGQLIAFNILSGRFL 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 600 FPLMIIPMVLNSFIEASVSIGRLFTFFTNEELQPDSVQRLPKVKNIGDVAInigDDATFlwQRKPEYKVALKNINFQAKK 679
Cdd:COG2274 426 APVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKGDIEL---ENVSF--RYPGDSPPVLDNISLTIKP 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 680 GNLTCIVGKVGSGKTALLSCMLG-----------DLFRVKGF--ATVHGSVAYVSQVPWIMNGTVKENILFGHRyDAEFy 746
Cdd:COG2274 501 GERVAIVGRSGSGKSTLLKLLLGlyeptsgriliDGIDLRQIdpASLRRQIGVVLQDVFLFSGTIRENITLGDP-DATD- 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 747 EKTIKACALT-IDLAI--LMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARHLIEHVlgpN 823
Cdd:COG2274 579 EEIIEAARLAgLHDFIeaLPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENL---R 655
|
490 500 510 520
....*....|....*....|....*....|....*....|.
9AYC_A 824 GLLHTKTKVLATNKVSALSIADSIALLDNGEITQQGTYDEI 864
Cdd:COG2274 656 RLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1294-1526 |
3.42e-49 |
|
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: 176.58 E-value: 3.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1294 GDIKFNNYSTRYRPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEaSEGNIVIDNIAINEIGLYDLRHKL 1373
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1374 SIIPQDSQVFEGTVRENIDPINQYTDEAIWRALELSHLKEhVLSMSNDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSK 1453
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKS-VIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
9AYC_A 1454 ILVLDQATAAVDVETDKVVQETIRTAFKDRTILTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQLLSDnKSLF 1526
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE-KSHF 230
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1061-1522 |
3.43e-49 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 185.61 E-value: 3.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1061 PMTFFETTPIGRILNRFSNDIYKVDAllgrTFSQFFVNAVKVTFTITVICA----TTWQF---IFIIIPLSVFYIYYqqy 1133
Cdd:PRK11176 112 PVSFFDKQSTGTLLSRITYDSEQVAS----SSSGALITVVREGASIIGLFImmfyYSWQLsliLIVIAPIVSIAIRV--- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1134 ylrTSRELRRldsitrspIYSHFQETLGGLAT-----------VRGYSQQK----RFSHINqcridNNM----------- 1187
Cdd:PRK11176 185 ---VSKRFRN--------ISKNMQNTMGQVTTsaeqmlkghkeVLIFGGQEvetkRFDKVS-----NRMrqqgmkmvsas 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1188 SAFYPSInanrwlayrlELIGSI---IILGAATlsvFRLKQGTLTAG--------MVGL-----SLS-------YALQIT 1244
Cdd:PRK11176 249 SISDPII----------QLIASLalaFVLYAAS---FPSVMDTLTAGtitvvfssMIALmrplkSLTnvnaqfqRGMAAC 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1245 QTLNWIVRMTVEVETNIVSVERIKeyadlkseapliveghrppkewpsqGDIKFNNYSTRYRPELDLVLKHINIHIKPNE 1324
Cdd:PRK11176 316 QTLFAILDLEQEKDEGKRVIERAK-------------------------GDIEFRNVTFTYPGKEVPALRNINFKIPAGK 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1325 KVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQVFEGTVRENI--DPINQYTDEAI 1402
Cdd:PRK11176 371 TVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIayARTEQYSREQI 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1403 WRALELSHLKEHVLSMSNdGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKD 1482
Cdd:PRK11176 451 EEAARMAYAMDFINKMDN-GLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKN 529
|
490 500 510 520
....*....|....*....|....*....|....*....|
9AYC_A 1483 RTILTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQLLSDN 1522
Cdd:PRK11176 530 RTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQN 569
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
320-622 |
2.03e-48 |
|
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: 174.74 E-value: 2.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 320 IHDVLAFTQPQLL-RILIKFVTDYNSERQDdhsslqgfennhpqklpivrGFLIAFAMFLVGFTQTSVLHQYFLNVFNTG 398
Cdd:cd18594 8 LEESLKIVQPLLLgRLVAYFVPDSTVTKTE--------------------AYLYALGLSLCAFLRVLLHHPYFFGLHRYG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 399 MYIKSALTALIYQKSLVLSNEASGLSSTGDIVNLMSVDVQKLQDLTQWLNLIWSGPFQIIICLYSLYKLLGNSMWVGVII 478
Cdd:cd18594 68 MQLRIALSSLIYKKTLKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 479 LVIMMPLNSFLMRIQKKLQKSQMKYKDERTRVISEILNNIKSLKLYAWEKPYREKLEEVRnNKELKNLTKLGCYMAVTSF 558
Cdd:cd18594 148 LLLLLPLQAYLGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIR-KKELKLIRKAAYIRAFNMA 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
9AYC_A 559 QFNIVPFLVSCCTFAVFVYTeDRALTTDLVFPALTLFNLLSFPLMI-IPMVLNSFIEASVSIGRL 622
Cdd:cd18594 227 FFFFSPTLVSFATFVPYVLT-GNTLTARKVFTVISLLNALRMTITRfFPESIQTLSESRVSLKRI 290
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
315-622 |
1.71e-47 |
|
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: 172.02 E-value: 1.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 315 AFFKAIHDVLAFTQPQLLRILIKFvtdynserqddhsslqgFENNHpQKLPIVRGFLIAFAMFLVGFTQTSVLHQYFLNV 394
Cdd:cd18593 3 GIFLFLEEAIRVVQPIFLGKLIRY-----------------FEGNG-SSISLTEAYLYAGGVSLCSFLFIITHHPYFFGM 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 395 FNTGMYIKSALTALIYQKSLVLSNEASGLSSTGDIVNLMSVDVQKLQDLTQWLNLIWSGPFQIIICLYSLYKLLGNSMWV 474
Cdd:cd18593 65 QRIGMRLRVACSSLIYRKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 475 GVIILVIMMPLNSFLMRIQKKLQKSQMKYKDERTRVISEILNNIKSLKLYAWEKPYREKLEEVRnNKELKNLTKLGCYMA 554
Cdd:cd18593 145 GLAVLLILIPLQSFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLR-RKEIKKVRRTSFLRA 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 555 VTSFQFNIVPFLVSCCTFAVFVYTEDrALTTDLVFPALTLFNLLSFPLMI-IPMVLNSFIEASVSIGRL 622
Cdd:cd18593 224 LNMGLFFVSSKLILFLTFLAYILLGN-ILTAERVFVTMALYNAVRLTMTLfFPFAIQFGSELSVSIRRI 291
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1058-1529 |
2.26e-45 |
|
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: 175.92 E-value: 2.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1058 LRAPMTFFETTPIGRILNRFS--NDIYK------VDALLGRTFSQF-----FVNAVKVTFTITVICAttwqfifIIIPLS 1124
Cdd:TIGR03797 220 LRLPVSFFRQYSTGDLASRAMgiSQIRRilsgstLTTLLSGIFALLnlglmFYYSWKLALVAVALAL-------VAIAVT 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1125 VFYIYYQQYYLRTSRELR-RLDSITrspiyshfQETLGGLATVR--------------GYSQQKRFsHINQCRIDNNMSA 1189
Cdd:TIGR03797 293 LVLGLLQVRKERRLLELSgKISGLT--------VQLINGISKLRvagaenrafarwakLFSRQRKL-ELSAQRIENLLTV 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1190 FYPSINAnrwlayrlelIGSIIILGAAtlsVFRLKQGTLTAG-------MVGLSLSYALQITQTLnwivrmtVEVETNIV 1262
Cdd:TIGR03797 364 FNAVLPV----------LTSAALFAAA---ISLLGGAGLSLGsflafntAFGSFSGAVTQLSNTL-------ISILAVIP 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1263 SVERIKEYADLKSEapliVEGHRPPkewPSQ--GDIKFNNYSTRYRPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLt 1340
Cdd:TIGR03797 424 LWERAKPILEALPE----VDEAKTD---PGKlsGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTL- 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1341 lalFRMI---EASE-GNIVIDNIAINEIGLYDLRHKLSIIPQDSQVFEGTVRENIDPINQYTDEAIWRALELSHLKEHVL 1416
Cdd:TIGR03797 496 ---LRLLlgfETPEsGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIR 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1417 SMSNdGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIrtafkDR---TILTIAHRLN 1493
Cdd:TIGR03797 573 AMPM-GMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESL-----ERlkvTRIVIAHRLS 646
|
490 500 510
....*....|....*....|....*....|....*.
9AYC_A 1494 TIMDSDRIIVLDNGKVAEFDSPGQLLSdNKSLFYSL 1529
Cdd:TIGR03797 647 TIRNADRIYVLDAGRVVQQGTYDELMA-REGLFAQL 681
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
670-853 |
8.96e-43 |
|
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: 155.95 E-value: 8.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 670 LKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKG-----------------FATVHGSVAYVSQVPWIMNGTVK 732
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGkvhwsnknesepsfeatRSRNRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 733 ENILFGHRYDAEFYEKTIKACALTIDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVA 812
Cdd:cd03290 97 ENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
9AYC_A 813 RHLIEHvlgpnGLLH-----TKTKVLATNKVSALSIADSIALLDNG 853
Cdd:cd03290 177 DHLMQE-----GILKflqddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
311-602 |
9.77e-43 |
|
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: 157.80 E-value: 9.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 311 MLLAAFFKAIHDVLAFTQPQLLRILIKFVTDYNserqDDHSSLQGFennhpqklpivrgFLIAFAMFLVGFTQTSVLHQY 390
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDG----DPETQALNV-------------YSLALLLLGLAQFILSFLQSY 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 391 FLNVfnTGMYIKSALTALIYQKSLVLSNEASGLSSTGDIVNLMSVDVQKLQDLTQWLNLIWSGPFQIIICLYSLYKLLGN 470
Cdd:pfam00664 64 LLNH--TGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGW 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 471 SM-WVGVIILVIMMPLNSFLMRIQKKLQKSQMKYKDERTRVISEILNNIKSLKLYAWEKPYREKLEEVRNNKELKNLTKL 549
Cdd:pfam00664 142 KLtLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKA 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
9AYC_A 550 GCYMAVTSFQFNIVPFLVSCCTFAVFVYTEDRALTTDLVFPALTLFNLLSFPL 602
Cdd:pfam00664 222 VANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
975-1247 |
9.87e-43 |
|
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: 157.80 E-value: 9.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 975 VCVFILFIVISMFLSVMGNVWLKHWSEVNSRYGSNP--NAARYLAIYFALGIGSALATLIQTIvLWVFCTIHASKYLHNL 1052
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPEtqALNVYSLALLLLGLAQFILSFLQSY-LLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1053 MTNSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTFSQFFVNAVKVTFTITVICATTWQFIFIIIPLSVFYIYYQQ 1132
Cdd:pfam00664 80 LFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1133 YYLRTSRELRRLDSITRSPIYSHFQETLGGLATVRGYSQQKRFSHINQCRIDNNMSAFYPSINANRWLAYRLELIGSIII 1212
Cdd:pfam00664 160 VFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSY 239
|
250 260 270
....*....|....*....|....*....|....*
9AYC_A 1213 LGAATLSVFRLKQGTLTAGMVGLSLSYALQITQTL 1247
Cdd:pfam00664 240 ALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1316-1529 |
1.05e-42 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 166.17 E-value: 1.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1316 INIHIKPNEKVGIVGRTGAGKSSLTLALFRMIeASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQVFEGTVRENI---D 1392
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllgN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1393 PinQYTDEAIWRALELSHLKEHVLSMSNdGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETDKVV 1472
Cdd:PRK11174 448 P--DASDEQLQQALENAWVSEFLPLLPQ-GLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV 524
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1473 QETIRTAFKDRTILTIAHRLNTIMDSDRIIVLDNGKVAE---FDSpgqlLSDNKSLFYSL 1529
Cdd:PRK11174 525 MQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQqgdYAE----LSQAGGLFATL 580
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1084-1504 |
1.60e-41 |
|
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: 161.69 E-value: 1.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1084 VDALLGRtFSQFF---VNAVKVTFTI-TVICATTWQ---FIFIIIPL-SVFYI---YYQQyylrtSRELRRLDSITRspI 1152
Cdd:TIGR02857 111 VEALDGY-FARYLpqlVLAVIVPLAIlAAVFPQDWIsglILLLTAPLiPIFMIligWAAQ-----AAARKQWAALSR--L 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1153 YSHFQETLGGLATVRGYSQQKR----FSHINQCRIDNNMS----AFYPSinanrwlaYRLELIGSIIILGAATLSVFRLK 1224
Cdd:TIGR02857 183 SGHFLDRLRGLPTLKLFGRAKAqaaaIRRSSEEYRERTMRvlriAFLSS--------AVLELFATLSVALVAVYIGFRLL 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1225 QGTLT--AGMVGLSLsyALQITQTL-----NWIVRMTvevetnivSVERIKEYADLKSEAPLIVEGHRPpKEWPSQGDIK 1297
Cdd:TIGR02857 255 AGDLDlaTGLFVLLL--APEFYLPLrqlgaQYHARAD--------GVAAAEALFAVLDAAPRPLAGKAP-VTAAPASSLE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1298 FNNYSTRYrPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIP 1377
Cdd:TIGR02857 324 FSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVP 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1378 QDSQVFEGTVRENI---DPinQYTDEAIWRALELSHLKEHVLSMSnDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKI 1454
Cdd:TIGR02857 403 QHPFLFAGTIAENIrlaRP--DASDAEIREALERAGLDEFVAALP-QGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
9AYC_A 1455 LVLDQATAAVDVETDKVVQETIRTAFKDRTILTIAHRLNTIMDSDRIIVL 1504
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
367-863 |
9.73e-41 |
|
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: 159.92 E-value: 9.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 367 VRGFLIAFAMFLVGFTQTSVLHQYFLnvFNTGMYIKSALTALIYQKSLVLSNEASGLSSTGDIVNLMSVDVQKLQD-LTQ 445
Cdd:COG4988 57 LLPLLGLLLAVLLLRALLAWLRERAA--FRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGyFAR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 446 WLNLIWSG---PFQIIICLYSLYkllgnsmWVGVIILVIMMPLNSFLMR-IQKKLQKSQMKYKDERTRVIS---EILNNI 518
Cdd:COG4988 135 YLPQLFLAalvPLLILVAVFPLD-------WLSGLILLVTAPLIPLFMIlVGKGAAKASRRQWRALARLSGhflDRLRGL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 519 KSLKLYAWEKPYREKLEEVrnNKELKNLTklgcyMAVTSFQFN---IVPFLVSCCTFAVFVYTEDRALTTDL-VFPALTL 594
Cdd:COG4988 208 TTLKLFGRAKAEAERIAEA--SEDFRKRT-----MKVLRVAFLssaVLEFFASLSIALVAVYIGFRLLGGSLtLFAALFV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 595 fnllsfpLMIIPMV------LNSF-------IEASvsiGRLFTFFTNEELQPDSVQRLPKVKNIGDVAInigDDATFLWq 661
Cdd:COG4988 281 -------LLLAPEFflplrdLGSFyharangIAAA---EKIFALLDAPEPAAPAGTAPLPAAGPPSIEL---EDVSFSY- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 662 rkPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDL------FRVKG-------FATVHGSVAYVSQVPWIMN 728
Cdd:COG4988 347 --PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLppysgsILINGvdlsdldPASWRRQIAWVPQNPYLFA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 729 GTVKENILFGHRY--DAEFyEKTIKACALTIDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAA 806
Cdd:COG4988 425 GTIRENLRLGRPDasDEEL-EAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAH 503
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 807 VDEHVARHLIEHVLgpnGLLHTKTKVLATNKVSALSIADSIALLDNGEITQQGTYDE 863
Cdd:COG4988 504 LDAETEAEILQALR---RLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEE 557
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
365-622 |
1.00e-40 |
|
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: 152.33 E-value: 1.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 365 PIVRGFLIAFAMFLVGFTQTSVLHQYFLNVFNTGMYIKSALTALIYQKSLVLSNeaSGLSSTGDIVNLMSVDVQKLQDLT 444
Cdd:cd18592 34 SVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKILRLRS--LGDKSVGELINIFSNDGQRLFDAA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 445 QWLNLIWSGPFQIIICL-YSLYkLLGNSMWVGVIILVIMMPLNSFLMRIQKKLQKSQMKYKDERTRVISEILNNIKSLKL 523
Cdd:cd18592 112 VFGPLVIGGPVVLILGIvYSTY-LLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKM 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 524 YAWEKPYREKLEEVRnNKELKNLTKLGCYMAVTSFQFNIVPFLVSCCTFAVFVYTEDRaLTTDLVFPALTLFNLLSFPLM 603
Cdd:cd18592 191 YAWEKPFAKKIADIR-KEERKILEKAGYLQSISISLAPIVPVIASVVTFLAHVALGND-LTAAQAFTVIAVFNSMRFSLR 268
|
250
....*....|....*....
9AYC_A 604 IIPMVLNSFIEASVSIGRL 622
Cdd:cd18592 269 MLPYAVKALAEAKVALQRI 287
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1261-1530 |
4.65e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 158.06 E-value: 4.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1261 IVSVERIKEYADLKseaPLIVEGHRPPKEwPSQGDIKFNNYSTRYRPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLT 1340
Cdd:PRK11160 308 IASARRINEITEQK---PEVTFPTTSTAA-ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1341 LALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQVFEGTVRENI---DPinQYTDEAIWRALE---LSHLKEh 1414
Cdd:PRK11160 384 QLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQqvgLEKLLE- 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1415 vlsmSNDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKDRTILTIAHRLNT 1494
Cdd:PRK11160 461 ----DDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTG 536
|
250 260 270
....*....|....*....|....*....|....*.
9AYC_A 1495 IMDSDRIIVLDNGKVAEFDSPGQLLSdNKSLFYSLC 1530
Cdd:PRK11160 537 LEQFDRICVMDNGQIIEQGTHQELLA-QQGRYYQLK 571
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1071-1492 |
1.21e-39 |
|
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: 155.98 E-value: 1.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1071 GRILNRFSNDIYKVDALLGRTFSQFFVNAVKVTFTITVICATTWQF-IFIIIPLSVFYIYYQQYYLRTSRELRRLDSITR 1149
Cdd:TIGR02868 110 GDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAaLILAAGLLLAGFVAPLVSLRAARAAEQALARLR 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1150 SPIYSHFQETLGGLATVRGYSQQKRFSHINQCRIDNNMSAFYPSINANRWLAYRLELIGSIIILGAATLSVFRLKQGTLT 1229
Cdd:TIGR02868 190 GELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLA 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1230 ----AGMVGLSLSyALQITQTLNWIVRMTVEVETnivSVERIKEYADLKSEAPlIVEGHRPPKEWPSQGDIKFNNYSTRY 1305
Cdd:TIGR02868 270 pvtlAVLVLLPLA-AFEAFAALPAAAQQLTRVRA---AAERIVEVLDAAGPVA-EGSAPAAGAVGLGKPTLELRDLSAGY 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1306 rPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQVFEG 1385
Cdd:TIGR02868 345 -PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDT 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1386 TVRENIDPIN-QYTDEAIWRALELSHLKEHVLSMSnDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATAAV 1464
Cdd:TIGR02868 424 TVRENLRLARpDATDEELWAALERVGLADWLRALP-DGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHL 502
|
410 420
....*....|....*....|....*...
9AYC_A 1465 DVETDKVVQETIRTAFKDRTILTIAHRL 1492
Cdd:TIGR02868 503 DAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1293-1509 |
4.13e-38 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 142.99 E-value: 4.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1293 QGDIKFNNYSTRYRPELD-LVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINeigLYD--- 1368
Cdd:cd03248 9 KGIVKFQNVTFAYPTRPDtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS---QYEhky 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1369 LRHKLSIIPQDSQVFEGTVRENID-PINQYTDEAIWRALELSHLKEHVLSMSnDGLDAQLTEGGGNLSVGQRQLLCLARA 1447
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELA-SGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
9AYC_A 1448 MLVPSKILVLDQATAAVDVETDKVVQETIRTAFKDRTILTIAHRLNTIMDSDRIIVLDNGKV 1509
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1296-1521 |
4.39e-37 |
|
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: 140.16 E-value: 4.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPElDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSI 1375
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1376 IPQ--DSQVFEGTVRENID--PINQ-YTDEAIWR----ALE---LSHLKEHVLSmsndgldaqltegggNLSVGQRQLLC 1443
Cdd:COG1122 80 VFQnpDDQLFAPTVEEDVAfgPENLgLPREEIRErveeALElvgLEHLADRPPH---------------ELSGGQKQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1444 LARAMLVPSKILVLDQATAAVDVETDKVVQETIRT-AFKDRTILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQLLSD 1521
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSD 224
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
978-1270 |
5.95e-37 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 141.58 E-value: 5.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 978 FILFIVISMFL-SVMGNVWLKHWSeVNSRYGSNPNAARYLAIYFALGIGSALaTLIQTIVLWVFCTIHASKYLHNLMTNS 1056
Cdd:cd18559 3 LLIKLVLCNHVfSGPSNLWLLLWF-DDPVNGPQEHGQVYLSVLGALAILQGI-TVFQYSMAVSIGGIFASRAVHLDLYHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1057 VLRAPMTFFETTPIGRILNRFSNDIYKVDALLGrTFSQFFVNAVKVTFTITVICATTWQFIFIIIPLSVFYIYYQQYYLR 1136
Cdd:cd18559 81 ALRSPISFFERTPSGELVNLFSKDLDRVDSMAP-QVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1137 TSRELRRLDSITRSPIYSHFQETLGGLATVRGYSQQKRFSHINQCRIDNNMsAFYPSINANRWLAYRLELIGSIIILGAA 1216
Cdd:cd18559 160 SSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNEL-AYLPSIVYLRALAVRLWCVGPCIVLFAS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
9AYC_A 1217 TLSVFRLKQgtlTAGMVGLSLSYALQITQTLNWIVRMTVEVETNIVSVERIKEY 1270
Cdd:cd18559 239 FFAYVSRHS---LAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLER 289
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
959-1267 |
7.78e-37 |
|
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: 142.25 E-value: 7.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 959 KWNIYLEYAKacNPKSVCVFILFIVISMFLSVMGN-VWLKHWSEVNSRYGSNPNAAR-------------YLAIYFALGI 1024
Cdd:cd18600 2 TWNTYLRYIT--SHKSLIFVLILCLVIFAIEVAASlVGLWLLRSQADRVNTTRPESSsntyavivtftssYYVFYIYVGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1025 G-SALATLIQTIVLWVFCTIHASKYLHNLMTNSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTFSQFFVNAVKVT 1103
Cdd:cd18600 80 AdSLLAMGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1104 FTITVICATTWQFIFIIIPLSVFYIYYQQYYLRTSRELRRLDSITRSPIYSHFQETLGGLATVRGYSQQKRFSHINQCRI 1183
Cdd:cd18600 160 GAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1184 DNNMSAFYPSINANRWLAYRLELIGSIIILGAATLSVFRLKQGtltAGMVGLSLSYALQITQTLNWIVRMTVEVETNIVS 1263
Cdd:cd18600 240 NLHTANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIGTTGDG---EGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRS 316
|
....
9AYC_A 1264 VERI 1267
Cdd:cd18600 317 VSRI 320
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1297-1508 |
1.88e-34 |
|
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: 131.82 E-value: 1.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1297 KFNNYSTRYRPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSII 1376
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1377 PQ--DSQVFEGTVRENI--DPINQYTDEA-----IWRALE---LSHLKEHVLSmsndgldaqltegggNLSVGQRQLLCL 1444
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVafGLENLGLPEEeieerVEEALElvgLEGLRDRSPF---------------TLSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 1445 ARAMLVPSKILVLDQATAAVDVETDKVVQETIRTaFKDR--TILTIAHRLNTIMD-SDRIIVLDNGK 1508
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLKK-LKAEgkTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
425-867 |
2.37e-34 |
|
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: 140.67 E-value: 2.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 425 STGDIVNLMSVDVQKLQDLtqWLNLIwsGPFQI--------IICLYSLYKLLGNSMWVGVIILVIMMPLnsFLMRIQKKL 496
Cdd:COG4987 110 RSGDLLNRLVADVDALDNL--YLRVL--LPLLVallvilaaVAFLAFFSPALALVLALGLLLAGLLLPL--LAARLGRRA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 497 QKSQMKYKDERTRVISEILNNIKSLKLY-AWEKpYREKLEEvRNNKELKNLTKLGCYMAVTSFQFNIVPFLVSCCTFAVF 575
Cdd:COG4987 184 GRRLAAARAALRARLTDLLQGAAELAAYgALDR-ALARLDA-AEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLA 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 576 VYTEDRALTTDLVFPALTLFNLLSF-PLMIIPMVLNSFIEASVSIGRLFTFFTNEELQPDSVQRLPKVkniGDVAINIgD 654
Cdd:COG4987 262 APLVAAGALSGPLLALLVLAALALFeALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAP---GGPSLEL-E 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 655 DATFLW--QRKPeykvALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKG-------------FATVHGSVAY 719
Cdd:COG4987 338 DVSFRYpgAGRP----VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGsitlggvdlrdldEDDLRRRIAV 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 720 VSQVPWIMNGTVKENILFGhRYDAEFyEKTIKACA---LTIDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARAD 796
Cdd:COG4987 414 VPQRPHLFDTTLRENLRLA-RPDATD-EELWAALErvgLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAP 491
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
9AYC_A 797 TYLLDDPLAAVDEHVARHLIEHVLgpnGLLHTKTKVLATNKVSALSIADSIALLDNGEITQQGTYDEITKD 867
Cdd:COG4987 492 ILLLDEPTEGLDAATEQALLADLL---EALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQ 559
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1300-1509 |
2.28e-33 |
|
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: 127.33 E-value: 2.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1300 NYSTRYRPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQD 1379
Cdd:cd03246 5 NVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1380 SQVFEGTVRENIdpinqytdeaiwralelshlkehvlsmsndgldaqltegggnLSVGQRQLLCLARAMLVPSKILVLDQ 1459
Cdd:cd03246 85 DELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
9AYC_A 1460 ATAAVDVETDKVVQETIRTA-FKDRTILTIAHRLNTIMDSDRIIVLDNGKV 1509
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1312-1520 |
7.06e-33 |
|
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: 136.03 E-value: 7.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAI-----NEIGlydlRHklsI--IPQDSQVFE 1384
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLsqwdrEELG----RH---IgyLPQDVELFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1385 GTVRENI----DPinqyTDEAIWRALELSHLKEHVLSMsNDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQA 1460
Cdd:COG4618 420 GTIAENIarfgDA----DPEKVVAAAKLAGVHEMILRL-PDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
9AYC_A 1461 TAAVDVETDKVVQETIRtAFKDR--TILTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQLLS 1520
Cdd:COG4618 495 NSNLDDEGEAALAAAIR-ALKARgaTVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1257-1511 |
7.52e-32 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 132.91 E-value: 7.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1257 VETNIVSVERIKEyadLKSEAPLIVEGHRPPKEWPS--QGDIKFNNYSTRYRPeldlVLKHINIHIKPNEKVGIVGRTGA 1334
Cdd:PRK10789 280 VERGSAAYSRIRA---MLAEAPVVKDGSEPVPEGRGelDVNIRQFTYPQTDHP----ALENVNFTLKPGQMLGICGPTGS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1335 GKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQVFEGTVRENI---DPinQYTDEAIWRALELSHL 1411
Cdd:PRK10789 353 GKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIalgRP--DATQQEIEHVARLASV 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1412 KEHVLSMSnDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKDRTILTIAHR 1491
Cdd:PRK10789 431 HDDILRLP-QGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHR 509
|
250 260
....*....|....*....|
9AYC_A 1492 LNTIMDSDRIIVLDNGKVAE 1511
Cdd:PRK10789 510 LSALTEASEILVMQHGHIAQ 529
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1296-1511 |
1.69e-31 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 122.04 E-value: 1.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGlYDLRHKLSI 1375
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1376 IPQDSQVFEGTVRENIdpinqytdeaiwralelshlkehvlsmsndgldaqltegGGNLSVGQRQLLCLARAMLVPSKIL 1455
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 1456 VLDQATAAVDVETDKVVQETIRTAFKDRTILTIAHRLNTIMDSDRIIVLDNGKVAE 1511
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
667-866 |
9.08e-31 |
|
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: 121.95 E-value: 9.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKG-------------FATVHGSVAYVSQVPWIMNGTVKE 733
Cdd:cd03254 16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGqilidgidirdisRKSLRSMIGVVLQDTFLFSGTIME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 734 NILFGHRYDAEfyEKTIKACALT-IDLAI--LMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEH 810
Cdd:cd03254 96 NIRLGRPNATD--EEVIEAAKEAgAHDFImkLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 811 vARHLIEHVLGPngLLHTKTKVLATNKVSALSIADSIALLDNGEITQQGTYDEITK 866
Cdd:cd03254 174 -TEKLIQEALEK--LMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1312-1518 |
2.32e-30 |
|
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: 120.36 E-value: 2.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEA-----SEGNIVID--NIAINEIGLYDLRHKLSIIPQDSQVFE 1384
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDgkDIYDLDVDVLELRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1385 GTVRENID---PINQY-----TDEAIWRALELSHLKEHVlsmsNDGLDAqlteggGNLSVGQRQLLCLARAMLVPSKILV 1456
Cdd:cd03260 95 GSIYDNVAyglRLHGIklkeeLDERVEEALRKAALWDEV----KDRLHA------LGLSGGQQQRLCLARALANEPEVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 1457 LDQATAAVDVETDKVVQETIRTAFKDRTILTIAH------RLntimdSDRIIVLDNGKVAEFDSPGQL 1518
Cdd:cd03260 165 LDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqqaaRV-----ADRTAFLLNGRLVEFGPTEQI 227
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
762-1506 |
2.53e-30 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 131.30 E-value: 2.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 762 LMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVD---EHVARHLIEHVLGPngllHTKTKVLATNKV 838
Cdd:PTZ00265 565 LPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDnksEYLVQKTINNLKGN----ENRITIIIAHRL 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 839 SALSIADSIALLDNGE-----------------------------------------------ITQQGTYDEITKDADSP 871
Cdd:PTZ00265 641 STIRYANTIFVLSNRErgstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMKNKNGI 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 872 LWKLLNNYGKKNNGKSNEFGDSSESSVRESsipvegeLEQLQKLNDLDFGNSDAI*LR---------RA*DA*LG*IDFG 942
Cdd:PTZ00265 721 YYTMINNQKVSSKKSSNNDNDKDSDMKSSA-------YKDSERGYDPDEMNGNSKHENesasnkkscKMSDENASENNAG 793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 943 DDENIAKREHREQGKVKWNIYLEYAKACNPKSVCVFILF--IVISMFLSVMGNVWLKHWSEV----NSRYGSNPNAARYL 1016
Cdd:PTZ00265 794 GKLPFLRNLFKRKPKAPNNLRIVYREIFSYKKDVTIIALsiLVAGGLYPVFALLYAKYVSTLfdfaNLEANSNKYSLYIL 873
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1017 AIYFALGIGSALATLIQTIVlwvfcTIHASKYLHNLMTNSVLRAPMTFFET---TPiGRILNRFSNDIYKVDALLGRT-- 1091
Cdd:PTZ00265 874 VIAIAMFISETLKNYYNNVI-----GEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINRDVHLLKTGLVNNiv 947
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1092 -FSQF---FVNAVKVTFTITVICATTWQFIFIIIpLSVFYIYYQqyyLRTSREL--RRLDSITRSPIYSHFQETLgglat 1165
Cdd:PTZ00265 948 iFTHFivlFLVSMVMSFYFCPIVAAVLTGTYFIF-MRVFAIRAR---LTANKDVekKEINQPGTVFAYNSDDEIF----- 1018
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1166 vrgysqqKRFSHINQcridnnmSAFYpsiNANRWLAYRLELIGSIIILGAATLSVFRLKQGTLTAGMV-GLSLSYALQIT 1244
Cdd:PTZ00265 1019 -------KDPSFLIQ-------EAFY---NMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLwGFSQSAQLFIN 1081
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1245 QTLNW-----IVRMTVEVET----------------NIVSVERIKEYADLKSEA--PLIVE----------GHRPPKEWP 1291
Cdd:PTZ00265 1082 SFAYWfgsflIRRGTILVDDfmkslftflftgsyagKLMSLKGDSENAKLSFEKyyPLIIRksnidvrdngGIRIKNKND 1161
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1292 SQGDIKFNNYSTRY--RPELDlVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFR------------------------ 1345
Cdd:PTZ00265 1162 IKGKIEIMDVNFRYisRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfknehtndmtneq 1240
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1346 -----------MIEASE-------------------GNIVIDNIAINEIGLYDLRHKLSIIPQDSQVFEGTVRENID-PI 1394
Cdd:PTZ00265 1241 dyqgdeeqnvgMKNVNEfsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKfGK 1320
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1395 NQYTDEAIWRALELSHLKEHVLSMSNDgLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQE 1474
Cdd:PTZ00265 1321 EDATREDVKRACKFAAIDEFIESLPNK-YDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1399
|
890 900 910
....*....|....*....|....*....|....*
9AYC_A 1475 TIrTAFK---DRTILTIAHRLNTIMDSDRIIVLDN 1506
Cdd:PTZ00265 1400 TI-VDIKdkaDKTIITIAHRIASIKRSDKIVVFNN 1433
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1312-1508 |
8.29e-30 |
|
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: 116.58 E-value: 8.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQdsqvfegtvreni 1391
Cdd:cd00267 14 ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1392 dpinqytdeaiwralelshlkehvlsmsndgldaqltegggnLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETDKV 1471
Cdd:cd00267 81 ------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRER 118
|
170 180 190
....*....|....*....|....*....|....*....
9AYC_A 1472 VQETIRTAFKD-RTILTIAHRLNTIMD-SDRIIVLDNGK 1508
Cdd:cd00267 119 LLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1313-1462 |
8.31e-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: 116.21 E-value: 8.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1313 LKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQVF-EGTVRENI 1391
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1392 -------DPINQYTDEAIWRALE---LSHLKEHVLSmsndgldaqltEGGGNLSVGQRQLLCLARAMLVPSKILVLDQAT 1461
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEklgLGDLADRPVG-----------ERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
9AYC_A 1462 A 1462
Cdd:pfam00005 150 A 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1296-1512 |
1.53e-29 |
|
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: 118.38 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELDLV--LKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIG---LYDLR 1370
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1371 HKLSIIPQDSQ-----VFegTVRENI-DPI----NQYTDEAIWRALELshLKEHVlsmsndGLDAQL-----TEgggnLS 1435
Cdd:cd03257 82 KEIQMVFQDPMsslnpRM--TIGEQIaEPLrihgKLSKKEARKEAVLL--LLVGV------GLPEEVlnrypHE----LS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1436 VGQRQLLCLARAMLVPSKILVLDQATAAVDVetdkVVQETIRTAFKD------RTILTIAHRLNTI-MDSDRIIVLDNGK 1508
Cdd:cd03257 148 GGQRQRVAIARALALNPKLLIADEPTSALDV----SVQAQILDLLKKlqeelgLTLLFITHDLGVVaKIADRVAVMYAGK 223
|
....
9AYC_A 1509 VAEF 1512
Cdd:cd03257 224 IVEE 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
663-859 |
1.64e-29 |
|
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: 117.69 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 663 KPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGdLF-------RVKGF-------ATVHGSVAYVSQVPWIMN 728
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAG-LYkptsgsvLLDGTdirqldpADLRRNIGYVPQDVTLFY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 729 GTVKENILFGHRY--DAEFYEKTIKACALTIdLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAA 806
Cdd:cd03245 92 GTLRDNITLGAPLadDERILRAAELAGVTDF-VNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
9AYC_A 807 VDEHVARHLIEHVlgpNGLLHTKTKVLATNKVSALSIADSIALLDNGEITQQG 859
Cdd:cd03245 171 MDMNSEERLKERL---RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1296-1508 |
5.34e-29 |
|
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: 115.64 E-value: 5.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRP---ELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNiaineiglydlrhK 1372
Cdd:cd03250 1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1373 LSIIPQDSQVFEGTVRENI---DPINQytdEAIWRALELSHLKEHvLSMSNDGLDAQLTEGGGNLSVGQRQLLCLARAML 1449
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENIlfgKPFDE---ERYEKVIKACALEPD-LEILPDGDLTEIGEKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
9AYC_A 1450 VPSKILVLDQATAAVDVET-DKVVQETIRTAFKD-RTILTIAHRLNTIMDSDRIIVLDNGK 1508
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVgRHIFENCILGLLLNnKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1296-1525 |
7.57e-29 |
|
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: 123.09 E-value: 7.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEAS---EGNIVIDNIAINEIGLYDLRHK 1372
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1373 LSIIPQD--SQVFEGTVRENID--PINQYT--DEAIWRALELshlkehvlsMSNDGLDAQLTEGGGNLSVGQRQLLCLAR 1446
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAeaLENLGLsrAEARARVLEL---------LEAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1447 AMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKDR--TILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQLLSDNK 1523
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
..
9AYC_A 1524 SL 1525
Cdd:COG1123 236 AL 237
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
622-867 |
2.74e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 122.26 E-value: 2.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 622 LFTFFTNEELQPDSVQRLPKVKniGDVAINIGDdatfLWQRKPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCML 701
Cdd:PRK11174 324 LVTFLETPLAHPQQGEKELASN--DPVTIEAED----LEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 702 GDL-----FRVKG-------FATVHGSVAYVSQVPWIMNGTVKENILFG--HRYDAEFYEKTIKACALTIdLAILMDGDK 767
Cdd:PRK11174 398 GFLpyqgsLKINGielreldPESWRKHLSWVGQNPQLPHGTLRDNVLLGnpDASDEQLQQALENAWVSEF-LPLLPQGLD 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 768 TLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARHLIEhvlGPNGLLHTKTKVLATNKVSALSIADSI 847
Cdd:PRK11174 477 TPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQ---ALNAASRRQTTLMVTHQLEDLAQWDQI 553
|
250 260
....*....|....*....|
9AYC_A 848 ALLDNGEITQQGTYDEITKD 867
Cdd:PRK11174 554 WVMQDGQIVQQGDYAELSQA 573
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
668-850 |
3.92e-28 |
|
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: 120.85 E-value: 3.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 668 VALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDL------FRVKGFATVHGS-------VAYVSQVPWIMNGTVKEN 734
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVdptegsIAVNGVPLADADadswrdqIAWVPQHPFLFAGTIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 735 ILFGHRY--DAEFYEKTIKACALTIdLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVA 812
Cdd:TIGR02857 416 IRLARPDasDAEIREALERAGLDEF-VAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETE 494
|
170 180 190
....*....|....*....|....*....|....*...
9AYC_A 813 RHLIEHVLgpnGLLHTKTKVLATNKVSALSIADSIALL 850
Cdd:TIGR02857 495 AEVLEALR---ALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
591-873 |
6.14e-28 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 120.97 E-value: 6.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 591 ALTLFNLLSF----PLMIIPMV-----LNSFIEASVSIGRLFTFFTNEELQPDSVQRLPKVKNIGDVAINigddaTFLW- 660
Cdd:PRK10789 250 SLTLGQLTSFvmylGLMIWPMLalawmFNIVERGSAAYSRIRAMLAEAPVVKDGSEPVPEGRGELDVNIR-----QFTYp 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 661 -QRKPeykvALKNINFQAKKGNLTCIVGKVGSGKTALLSCML-------GDL-FRVKGFATVH-----GSVAYVSQVPWI 726
Cdd:PRK10789 325 qTDHP----ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQrhfdvseGDIrFHDIPLTKLQldswrSRLAVVSQTPFL 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 727 MNGTVKENILFGhRYDA--EFYEKTIKACALTIDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPL 804
Cdd:PRK10789 401 FSDTVANNIALG-RPDAtqQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 805 AAVDEHvARHLIEHVLGPNGllHTKTKVLATNKVSALSIADSIALLDNGEITQQGTYDEItkdADSPLW 873
Cdd:PRK10789 480 SAVDGR-TEHQILHNLRQWG--EGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQL---AQQSGW 542
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
664-854 |
6.50e-28 |
|
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: 111.71 E-value: 6.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 664 PEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKG-------------FATVHGSVAYVSQVPWIMNGT 730
Cdd:cd03228 12 GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGeilidgvdlrdldLESLRKNIAYVPQDPFLFSGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 731 VKENILfghrydaefyektikacaltidlailmdgdktlvgekgislSGGQKARLSLARAVYARADTYLLDDPLAAVDEH 810
Cdd:cd03228 92 IRENIL-----------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
9AYC_A 811 VARHLIEHVLgpnGLLHTKTKVLATNKVSALSIADSIALLDNGE 854
Cdd:cd03228 131 TEALILEALR---ALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1263-1521 |
6.00e-27 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 117.31 E-value: 6.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1263 SVERIKEYADLKSEAPLIVEGHRPPKEWPSQGD--IKFNNYSTRY---RPELDLVLKHINIHIKPNEKVGIVGRTGAGKS 1337
Cdd:COG1123 226 PPEEILAAPQALAAVPRLGAARGRAAPAAAAAEplLEVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKS 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1338 SLTLALFRMIEASEGNIVIDNIAINEIG---LYDLRHKLSIIPQD--SQVFEG-TVRENI-DPINQYT-------DEAIW 1403
Cdd:COG1123 306 TLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDpySSLNPRmTVGDIIaEPLRLHGllsraerRERVA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1404 RALELSHLKEHVLSMSndgldaqltegGGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVetdkVVQETIRTAFKD- 1482
Cdd:COG1123 386 ELLERVGLPPDLADRY-----------PHELSGGQRQRVAIARALALEPKLLILDEPTSALDV----SVQAQILNLLRDl 450
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
9AYC_A 1483 -----RTILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQLLSD 1521
Cdd:COG1123 451 qrelgLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1312-1524 |
9.99e-27 |
|
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: 110.66 E-value: 9.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSqvfEG------ 1385
Cdd:COG1124 20 VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDP---YAslhprh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1386 TVRENID-PIN----QYTDEAIWRALELSHLKEHVLsmsnDGLDAQLtegggnlSVGQRQLLCLARAMLVPSKILVLDQA 1460
Cdd:COG1124 97 TVDRILAePLRihglPDREERIAELLEQVGLPPSFL----DRYPHQL-------SGGQRQRVAIARALILEPELLLLDEP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
9AYC_A 1461 TAAVDVetdkVVQETIRTAFKD------RTILTIAHRLNTI--MdSDRIIVLDNGKVAEFDSPGQLLSDNKS 1524
Cdd:COG1124 166 TSALDV----SVQAEILNLLKDlreergLTYLFVSHDLAVVahL-CDRVAVMQNGRIVEELTVADLLAGPKH 232
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1312-1520 |
5.55e-26 |
|
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: 108.59 E-value: 5.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQV-FEGTVREN 1390
Cdd:COG1120 16 VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPPApFGLTVREL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1391 I--------DPINQYTDE---AIWRALE---LSHLKehvlsmsndglDAQLTEgggnLSVGQRQLLCLARAMLVPSKILV 1456
Cdd:COG1120 96 ValgryphlGLFGRPSAEdreAVEEALErtgLEHLA-----------DRPVDE----LSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
9AYC_A 1457 LDQATAAVD----VEtdkvVQETIR--TAFKDRTILTIAHRLN-TIMDSDRIIVLDNGKVAEFDSPGQLLS 1520
Cdd:COG1120 161 LDEPTSHLDlahqLE----VLELLRrlARERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
654-875 |
7.26e-26 |
|
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: 107.70 E-value: 7.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 654 DDATFLWQrkPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLS-------------CMLGDLFRVKGFATVHGSVAYV 720
Cdd:cd03251 4 KNVTFRYP--GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNliprfydvdsgriLIDGHDVRDYTLASLRRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 721 SQVPWIMNGTVKENILFG-HRYDAEFYEKTIKACALTIDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYL 799
Cdd:cd03251 82 SQDVFLFNDTVAENIAYGrPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 800 LDDPLAAVD---EHVARHLIEHvlgpngLLHTKTKVLATNKVSALSIADSIALLDNGEITQQGTYDEITkDADSPLWKL 875
Cdd:cd03251 162 LDEATSALDtesERLVQAALER------LMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELL-AQGGVYAKL 233
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
654-866 |
1.20e-25 |
|
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: 107.24 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 654 DDATFLWQRKPEYKVaLKNINFQAKKGNLTCIVGKVGSGKTALLSCML-------------GDLFRVKGFATVHGSVAYV 720
Cdd:cd03249 4 KNVSFRYPSRPDVPI-LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLErfydptsgeilldGVDIRDLNLRWLRSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 721 SQVPWIMNGTVKENILFGhRYDAEFyEKTIKACALT-IDLAI--LMDGDKTLVGEKGISLSGGQKARLSLARAVYARADT 797
Cdd:cd03249 83 SQEPVLFDGTIAENIRYG-KPDATD-EEVEEAAKKAnIHDFImsLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 798 YLLDDPLAAVDEHVaRHLIEHVLgpNGLLHTKTKVLATNKVSALSIADSIALLDNGEITQQGTYDEITK 866
Cdd:cd03249 161 LLLDEATSALDAES-EKLVQEAL--DRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMA 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1296-1521 |
9.10e-25 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 104.96 E-value: 9.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYrPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIG---LYDLRHK 1372
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1373 LSIIPQDSQ-VFEGTVRENI-------DPI-----NQYTDEAIWRALELshLkEHVlsmsndGLDAQLTEGGGNLSVGQR 1439
Cdd:cd03256 80 IGMIFQQFNlIERLSVLENVlsgrlgrRSTwrslfGLFPKEEKQRALAA--L-ERV------GLLDKAYQRADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1440 QLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKDRTILTIA--HRLNTIMD-SDRIIVLDNGKVAeFDSPG 1516
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVslHQVDLAREyADRIVGLKDGRIV-FDGPP 229
|
....*
9AYC_A 1517 QLLSD 1521
Cdd:cd03256 230 AELTD 234
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
654-863 |
9.18e-25 |
|
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: 104.62 E-value: 9.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 654 DDATFlwQRKPEYKVaLKNINFQAKKGNLTCIVGKVGSGKTALLSCmlgdLFRV----KGFATVHG-------------S 716
Cdd:cd03253 4 ENVTF--AYDPGRPV-LKDVSFTIPAGKKVAIVGPSGSGKSTILRL----LFRFydvsSGSILIDGqdirevtldslrrA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 717 VAYVSQVPWIMNGTVKENILFGhRYDA---EFYEKTIKACaltIDLAI--LMDGDKTLVGEKGISLSGGQKARLSLARAV 791
Cdd:cd03253 77 IGVVPQDTVLFNDTIGYNIRYG-RPDAtdeEVIEAAKAAQ---IHDKImrFPDGYDTIVGERGLKLSGGEKQRVAIARAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
9AYC_A 792 YARADTYLLDDPLAAVDEHVARHLIEHVlgpNGLLHTKTKVLATNKVSALSIADSIALLDNGEITQQGTYDE 863
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAAL---RDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEE 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1312-1509 |
1.62e-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: 101.71 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLtlalFRMI----EASEGNIVIDNIAINEIGLyDLRHKLSIIPQDSQVFEG-T 1386
Cdd:cd03230 15 ALDDISLTVEKGEIYGLLGPNGAGKTTL----IKIIlgllKPDSGEIKVLGKDIKKEPE-EVKRRIGYLPEEPSLYENlT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1387 VRENIDpinqytdeaiwralelshlkehvlsmsndgldaqltegggnLSVGQRQLLCLARAMLVPSKILVLDQATAAVDV 1466
Cdd:cd03230 90 VRENLK-----------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDP 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
9AYC_A 1467 ETDKVVQETIRT-AFKDRTILTIAHRLNTIMD-SDRIIVLDNGKV 1509
Cdd:cd03230 129 ESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
1015-1267 |
1.63e-24 |
|
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: 105.33 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1015 YLAIYFALGIGSALATLIQTIVLWVFctihASKYLHNLMT---NSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRT 1091
Cdd:cd07346 41 IALLLLLLALLRALLSYLRRYLAARL----GQRVVFDLRRdlfRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1092 FSQFFVNAVKVTFTITVICATTWQ---FIFIIIPLSVFYIYYQQYYLR-TSRELRRldsiTRSPIYSHFQETLGGLATVR 1167
Cdd:cd07346 117 LLQLLSDVLTLIGALVILFYLNWKltlVALLLLPLYVLILRYFRRRIRkASREVRE----SLAELSAFLQESLSGIRVVK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1168 GYSQQK----RFSHINQCRIDNNM------SAFYPSINAnrwlayrLELIGSIIILGAATLSVFrlkQGTLTAGMVGLSL 1237
Cdd:cd07346 193 AFAAEEreieRFREANRDLRDANLraarlsALFSPLIGL-------LTALGTALVLLYGGYLVL---QGSLTIGELVAFL 262
|
250 260 270
....*....|....*....|....*....|
9AYC_A 1238 SYALQITQTLNWIVRMTVEVETNIVSVERI 1267
Cdd:cd07346 263 AYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1296-1525 |
3.22e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 103.92 E-value: 3.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSI 1375
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1376 IPQ--DSQVFEGTVRENID---PINQYTDEAIWRALElsHLKEHVlsmsndGLDAQLTEGGGNLSVGQRQLLCLARAMLV 1450
Cdd:PRK13632 88 IFQnpDNQFIGATVEDDIAfglENKKVPPKKMKDIID--DLAKKV------GMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 1451 PSKILVLDQATAAVDVETDKVVQETIRTAFKDR--TILTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQLLSDNKSL 1525
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEIL 236
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1312-1521 |
6.55e-24 |
|
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: 101.74 E-value: 6.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYD-LRHKLSIIPQDSQVFEG-TVRE 1389
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1390 NIdpinqytdEAIWRALELSHLK---EHVLSMSNDgLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQAT---AA 1463
Cdd:cd03224 95 NL--------LLGAYARRRAKRKarlERVYELFPR-LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSeglAP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
9AYC_A 1464 VDVETdkvVQETIRTaFKDR--TILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQLLSD 1521
Cdd:cd03224 166 KIVEE---IFEAIRE-LRDEgvTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
426-869 |
6.96e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 109.04 E-value: 6.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 426 TGDIVNLMSVDVQKLQD-LTQWLN-LIWSGpfqiiICLYSLYKLLGNSMWVGVIILVIMMPL--------NSFLMRIQKK 495
Cdd:TIGR00958 257 TGELTSRLSSDTQTMSRsLSLNVNvLLRNL-----VMLLGLLGFMLWLSPRLTMVTLINLPLvflaekvfGKRYQLLSEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 496 LQKSQMKykdeRTRVISEILNNIKSLKLYAWEK----PYREKLEEVRNNKELKNLTKLGcYMAVTSFqfnivpflvscct 571
Cdd:TIGR00958 332 LQEAVAK----ANQVAEEALSGMRTVRSFAAEEgeasRFKEALEETLQLNKRKALAYAG-YLWTTSV------------- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 572 FAVFVYTEDRALTTDLVFP-ALTLFNLLSFplMIIPMVLNSFIEASVSI-----------GRLFTFFTNE-ELQPDSVQR 638
Cdd:TIGR00958 394 LGMLIQVLVLYYGGQLVLTgKVSSGNLVSF--LLYQEQLGEAVRVLSYVysgmmqavgasEKVFEYLDRKpNIPLTGTLA 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 639 LPKVKniGDVAINigdDATFLWQRKPEYKVaLKNINFQAKKGNLTCIVGKVGSGKTALLScMLGDLFRVKGfATV----- 713
Cdd:TIGR00958 472 PLNLE--GLIEFQ---DVSFSYPNRPDVPV-LKGLTFTLHPGEVVALVGPSGSGKSTVAA-LLQNLYQPTG-GQVlldgv 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 714 ----------HGSVAYVSQVPWIMNGTVKENILFGHRY--DAEFYEKTIKACALTIdLAILMDGDKTLVGEKGISLSGGQ 781
Cdd:TIGR00958 544 plvqydhhylHRQVALVGQEPVLFSGSVRENIAYGLTDtpDEEIMAAAKAANAHDF-IMEFPNGYDTEVGEKGSQLSGGQ 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 782 KARLSLARAVYARADTYLLDDPLAAVDEHVarhliEHVLGPNGLLHTKTKVLATNKVSALSIADSIALLDNGEITQQGTY 861
Cdd:TIGR00958 623 KQRIAIARALVRKPRVLILDEATSALDAEC-----EQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTH 697
|
....*...
9AYC_A 862 DEITKDAD 869
Cdd:TIGR00958 698 KQLMEDQG 705
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
667-864 |
7.90e-24 |
|
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: 102.24 E-value: 7.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHG------------SVAYVSQ---VPWIMngTV 731
Cdd:COG4555 14 VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPDergLYDRL--TV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 732 KENIlfghRYDAEFY----EKTIKACALTIDLAILMDGDKTLVGEkgisLSGGQKARLSLARAVYARADTYLLDDPLAAV 807
Cdd:COG4555 92 RENI----RYFAELYglfdEELKKRIEELIELLGLEEFLDRRVGE----LSTGMKKKVALARALVHDPKVLLLDEPTNGL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 808 DEHVARHLIEHV--LGPNGllhtKTKVLATNKVSALS-IADSIALLDNGEITQQGTYDEI 864
Cdd:COG4555 164 DVMARRLLREILraLKKEG----KTVLFSSHIMQEVEaLCDRVVILHKGKVVAQGSLDEL 219
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1296-1532 |
7.90e-24 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 102.09 E-value: 7.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELdlVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEiglydLRHKLSI 1375
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1376 IPQDSQVFEG---TVRE-----------NIDPINQYTDEAIWRALE---LSHLKehvlsmsndglDAQLteggGNLSVGQ 1438
Cdd:COG1121 80 VPQRAEVDWDfpiTVRDvvlmgrygrrgLFRRPSRADREAVDEALErvgLEDLA-----------DRPI----GELSGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1439 RQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRT-AFKDRTILTIAHRLNTIMD-SDRIIVLDNGKVAeFDSPG 1516
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLVA-HGPPE 223
|
250
....*....|....*..
9AYC_A 1517 QLL-SDNKSLFYSLCME 1532
Cdd:COG1121 224 EVLtPENLSRAYGGPVA 240
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1117-1538 |
1.03e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 109.68 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1117 IFIIIPLSVFYIyyQQYYLRTSRELRRLDSitRSPIyshFQETLGGLATVRGYSQQKRFSHINQCRIDNNMSAFYpsiNA 1196
Cdd:PLN03232 450 LFLLIPLQTLIV--RKMRKLTKEGLQWTDK--RVGI---INEILASMDTVKCYAWEKSFESRIQGIRNEELSWFR---KA 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1197 NRWLAYRLELIGSI-IILGAATLSVFRLKQGTLTAGMVGLSLSYALQITQTLNWIVRMTVEVETNIVSVERIKEYadLKS 1275
Cdd:PLN03232 520 QLLSAFNSFILNSIpVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEEL--LLS 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1276 EAPLIVEGhrPPKEwPSQGDIKFNNYSTRYRPELDL-VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNI 1354
Cdd:PLN03232 598 EERILAQN--PPLQ-PGAPAISIKNGYFSWDSKTSKpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSS 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1355 VidniaineiglyDLRHKLSIIPQDSQVFEGTVRENIDPINQYTDEAIWRALELSHLkEHVLSMSNDGLDAQLTEGGGNL 1434
Cdd:PLN03232 675 V------------VIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTAL-QHDLDLLPGRDLTEIGERGVNI 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1435 SVGQRQLLCLARAMLVPSKILVLDQATAAVDVE-TDKVVQETIRTAFKDRTILTIAHRLNTIMDSDRIIVLDNGKVAEfD 1513
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKE-E 820
|
410 420
....*....|....*....|....*
9AYC_A 1514 SPGQLLSDNKSLFYSLCMEAGLVNE 1538
Cdd:PLN03232 821 GTFAELSKSGSLFKKLMENAGKMDA 845
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1296-1520 |
2.39e-23 |
|
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: 100.35 E-value: 2.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRY--RPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLtLALFRMIEA-SEGNIVI---DNIAINEIGLYDL 1369
Cdd:cd03258 2 IELKNVSKVFgdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTL-IRCINGLERpTSGSVLVdgtDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1370 RHKLSIIPQDSQVFEG-TVRENID-PI---NQYTDEAIWRALELSHLkehVlsmsndGLDAQLTEGGGNLSVGQRQLLCL 1444
Cdd:cd03258 81 RRRIGMIFQHFNLLSSrTVFENVAlPLeiaGVPKAEIEERVLELLEL---V------GLEDKADAYPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 1445 ARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKDR--TILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQLLS 1520
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFA 230
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
663-864 |
3.81e-23 |
|
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: 99.87 E-value: 3.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 663 KPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHG-------------SVAYVSQVPWIMNG 729
Cdd:cd03252 11 KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 730 TVKENILFGHryDAEFYEKTIKACALTIDLAILM---DGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAA 806
Cdd:cd03252 91 SIRDNIALAD--PGMSMERVIEAAKLAGAHDFISelpEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 807 VDEHVARHLIEHVlgpNGLLHTKTKVLATNKVSALSIADSIALLDNGEITQQGTYDEI 864
Cdd:cd03252 169 LDYESEHAIMRNM---HDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
654-859 |
6.20e-23 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 98.76 E-value: 6.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 654 DDATFLWQRKPeykvALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDL------FRVKGF--ATVHGSVAYVSQ--- 722
Cdd:cd03235 3 EDLTVSYGGHP----VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLkptsgsIRVFGKplEKERKRIGYVPQrrs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 723 VPWIMNGTVKENILFGHRYDAEFYEKTIKACALTIDLAIlmdgdkTLVGEKGI------SLSGGQKARLSLARAVYARAD 796
Cdd:cd03235 79 IDRDFPISVRDVVLMGLYGHKGLFRRLSKADKAKVDEAL------ERVGLSELadrqigELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
9AYC_A 797 TYLLDDPLAAVDEHVARHLIEHVLGPNGllHTKTKVLATNKVSALS-IADSIALLdNGEITQQG 859
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRR--EGMTILVVTHDLGLVLeYFDRVLLL-NRTVVASG 213
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
403-835 |
1.66e-22 |
|
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: 103.59 E-value: 1.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 403 SALTALIYQKSLVLSNEASGLSSTGDIVNLMSVDVQKLQDLTqwlnLIWSGPFQIIICLYSLYKLL-GNSMWVGVIILVI 481
Cdd:TIGR02868 86 GALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLY----VRVIVPAGVALVVGAAAVAAiAVLSVPAALILAA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 482 MMPLNSFLM-----RIQKKLQKSQMKYKDERTRVISEILNNIKSLKLYAWEKPYREKLEEVrnNKEL------------- 543
Cdd:TIGR02868 162 GLLLAGFVAplvslRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEA--DRELtraerraaaatal 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 544 -KNLTKLGCYMAVTSFQFNIVPFL----VSCCTFAVFVYTedralttdlvfpALTLFNLLSfPLmiiPMVLNSFIEASVS 618
Cdd:TIGR02868 240 gAALTLLAAGLAVLGALWAGGPAVadgrLAPVTLAVLVLL------------PLAAFEAFA-AL---PAAAQQLTRVRAA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 619 IGRLFTFFTNEELQPDSVQRLPKVKNIGDVAINIgDDATFLWqrkPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLS 698
Cdd:TIGR02868 304 AERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLEL-RDLSAGY---PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 699 CMLGDLFRVKGFATVHGS-------------VAYVSQVPWIMNGTVKENILFGhRYDA--EFYEKTIKACALTIDLAILM 763
Cdd:TIGR02868 380 TLAGLLDPLQGEVTLDGVpvssldqdevrrrVSVCAQDAHLFDTTVRENLRLA-RPDAtdEELWAALERVGLADWLRALP 458
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
9AYC_A 764 DGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARHLIEHVLGPnglLHTKTKVLAT 835
Cdd:TIGR02868 459 DGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA---LSGRTVVLIT 527
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1312-1510 |
1.77e-22 |
|
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: 95.57 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYD-LRHKLSIIPQdsqvfegtvren 1390
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1391 idpinqytdeaiwralelshlkehvlsmsndgldaqltegggnLSVGQRQLLCLARAMLVPSKILVLDQATAAVDV-ETD 1469
Cdd:cd03216 83 -------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPaEVE 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....
9AYC_A 1470 KVVqETIRtAFKDR--TILTIAHRLNTIMD-SDRIIVLDNGKVA 1510
Cdd:cd03216 120 RLF-KVIR-RLRAQgvAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
611-864 |
2.21e-22 |
|
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: 103.29 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 611 SFIEASVSIGRLFTFFTNEELQPDSVQrLPKVKniGDVAInigDDATFlwqRKP-EYKVALKNINFQAKKGNLTCIVGKV 689
Cdd:COG4618 297 QFVSARQAYRRLNELLAAVPAEPERMP-LPRPK--GRLSV---ENLTV---VPPgSKRPILRGVSFSLEPGEVLGVIGPS 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 690 GSGKTALLSCMLGDLfrvkgfATVHGSV-------------------AYVSQVPWIMNGTVKENI-LFGhryDAEFyEKT 749
Cdd:COG4618 368 GSGKSTLARLLVGVW------PPTAGSVrldgadlsqwdreelgrhiGYLPQDVELFDGTIAENIaRFG---DADP-EKV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 750 IKACALT-IDLAILM--DGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARHLIEhvlgpnGLL 826
Cdd:COG4618 438 VAAAKLAgVHEMILRlpDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAA------AIR 511
|
250 260 270 280
....*....|....*....|....*....|....*....|..
9AYC_A 827 HTK----TKVLATNKVSALSIADSIALLDNGEITQQGTYDEI 864
Cdd:COG4618 512 ALKargaTVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEV 553
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1296-1508 |
2.68e-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: 95.72 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELdlVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVID--NIAINEIGLYDLRHKL 1373
Cdd:cd03229 1 LELKNVSKRYGQKT--VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgeDLTDLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1374 SIIPQDSQVFEG-TVRENIdpinqytdeaiwralelshlkehvlsmsndgldaqlTEGggnLSVGQRQLLCLARAMLVPS 1452
Cdd:cd03229 79 GMVFQDFALFPHlTVLENI------------------------------------ALG---LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 1453 KILVLDQATAAVDVETDKVVQETIRTAFKD--RTILTIAHRLNTIMD-SDRIIVLDNGK 1508
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1312-1509 |
3.52e-22 |
|
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: 95.19 E-value: 3.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQdsqvfegtvreni 1391
Cdd:cd03214 14 VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1392 dpinqytdeAIwRALELSHLKEHVLSMsndgldaqltegggnLSVGQRQLLCLARAMLVPSKILVLDQATAAVD----VE 1467
Cdd:cd03214 81 ---------AL-ELLGLAHLADRPFNE---------------LSGGERQRVLLARALAQEPPILLLDEPTSHLDiahqIE 135
|
170 180 190 200
....*....|....*....|....*....|....*....|...
9AYC_A 1468 TDKVVQETIRTafKDRTILTIAHRLN-TIMDSDRIIVLDNGKV 1509
Cdd:cd03214 136 LLELLRRLARE--RGKTVVMVLHDLNlAARYADRVILLKDGRI 176
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
667-859 |
4.14e-22 |
|
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: 96.05 E-value: 4.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGdLFRV-KGFATVHG-----------SVAYVSQ----VPWImngT 730
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAG-LERPdSGEILIDGrdvtgvpperrNIGMVFQdyalFPHL---T 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 731 VKENILFGHRyDAEFYEKTIKAcalTIDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEH 810
Cdd:cd03259 89 VAENIAFGLK-LRGVPKAEIRA---RVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
9AYC_A 811 VARHLIEHVLGpnglLHTKTK---VLATNKVS-ALSIADSIALLDNGEITQQG 859
Cdd:cd03259 165 LREELREELKE----LQRELGittIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1296-1522 |
4.19e-22 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 96.80 E-value: 4.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELdlVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAI---NEIGLYDLRHK 1372
Cdd:cd03261 1 IELRGLTKSFGGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1373 LSIIPQDSQVFEG-TVRENID-PINQYT--DEAIWRALELSHLkEHVlsmsndGLDAQLTEGGGNLSVGQRQLLCLARAM 1448
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAfPLREHTrlSEEEIREIVLEKL-EAV------GLRGAEDLYPAELSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 1449 LVPSKILVLDQATAAVDVETDKVVQETIRT--AFKDRTILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQLL-SDN 1522
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRaSDD 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1297-1510 |
5.96e-22 |
|
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: 95.68 E-value: 5.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1297 KFNNYSTRYRPELdlVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIaineiGLYDLRHKLSII 1376
Cdd:cd03235 1 EVEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1377 PQDSQV---FEGTVRE-----------NIDPINQYTDEAIWRALE---LSHLKehvlsmsndglDAQLTEgggnLSVGQR 1439
Cdd:cd03235 74 PQRRSIdrdFPISVRDvvlmglyghkgLFRRLSKADKAKVDEALErvgLSELA-----------DRQIGE----LSGGQQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
9AYC_A 1440 QLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRT-AFKDRTILTIAHRLNTIMDS-DRIIVLDNGKVA 1510
Cdd:cd03235 139 QRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYfDRVLLLNRTVVA 211
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
979-1267 |
9.01e-22 |
|
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: 97.47 E-value: 9.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 979 ILFIVISMFLSVMGNVWLKH-----WSEVNSRYGSNPNA-ARYLAIYFALGIGSALATLIQTIVLwVFCTIHASKYLHNL 1052
Cdd:cd18547 5 IILAIISTLLSVLGPYLLGKaidliIEGLGGGGGVDFSGlLRILLLLLGLYLLSALFSYLQNRLM-ARVSQRTVYDLRKD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1053 MTNSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTFSQFFVNAVKVTFTITVICATTWQF---IFIIIPLSVFYIY 1129
Cdd:cd18547 84 LFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLtliVLVTVPLSLLVTK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1130 Y-----QQYYLRTSRELRRLDsitrspiySHFQETLGGLATVRGYSQQ----KRFSHINQCRIDNNMSA-FY-----PSI 1194
Cdd:cd18547 164 FiakrsQKYFRKQQKALGELN--------GYIEEMISGQKVVKAFNREeeaiEEFDEINEELYKASFKAqFYsgllmPIM 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
9AYC_A 1195 NanrwlayrleLIGSIIILGAATLSVFRLKQGTLTAGMVGLSLSYALQITQTLNWIVRMTVEVETNIVSVERI 1267
Cdd:cd18547 236 N----------FINNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1296-1525 |
1.10e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 97.01 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSI 1375
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1376 IPQ--DSQVFEGTVRENI----DPINQYTDEAIWR---ALELSHLKEHvlsmsndgldaqLTEGGGNLSVGQRQLLCLAR 1446
Cdd:PRK13635 86 VFQnpDNQFVGATVQDDVafglENIGVPREEMVERvdqALRQVGMEDF------------LNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1447 AMLVPSKILVLDQATAAVDVETDKVVQETIRTaFKDR---TILTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQLLSDNK 1523
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQ-LKEQkgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGH 232
|
..
9AYC_A 1524 SL 1525
Cdd:PRK13635 233 ML 234
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
667-868 |
1.56e-21 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 95.13 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHG------------SVAYVSQVPWIMNG-TVKE 733
Cdd:COG1131 13 KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALYPDlTVRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 734 NIlfghRYDAEFYEKTIKACALTIDLAI----LMDGDKTLVGekgiSLSGGQKARLSLARAVYARADTYLLDDPLAAVDE 809
Cdd:COG1131 93 NL----RFFARLYGLPRKEARERIDELLelfgLTDAADRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
9AYC_A 810 HVARHLIEHV--LGPNGllhtKTKVLATNKVS-ALSIADSIALLDNGEITQQGTYDEITKDA 868
Cdd:COG1131 165 EARRELWELLreLAAEG----KTVLLSTHYLEeAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1296-1519 |
1.71e-21 |
|
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: 95.45 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYrPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSI 1375
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1376 IPQDSQVF-EGTVRENID---PINQYTDEAI-WRALELSHLKehvlsmsndGLD-AQLTEG-GGNLSVGQRQLLCLARAM 1448
Cdd:cd03295 80 VIQQIGLFpHMTVEENIAlvpKLLKWPKEKIrERADELLALV---------GLDpAEFADRyPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
9AYC_A 1449 LVPSKILVLDQATAAVDVETDKVVQETIRTAFKD--RTILTIAHRLN-TIMDSDRIIVLDNGKVAEFDSPGQLL 1519
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1312-1509 |
2.10e-21 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 94.13 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAIN--EIGLYDLRHKLSIIPQDSQVFEG-TVR 1388
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddKKNINELRQKVGMVFQQFNLFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1389 ENID--PI---NQYTDEAIWRALELshLKEhVlsmsndGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATAA 1463
Cdd:cd03262 95 ENITlaPIkvkGMSKAEAEERALEL--LEK-V------GLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
9AYC_A 1464 VDVETDKVVQETIRTAFKD-RTILTIAHRLNTIMD-SDRIIVLDNGKV 1509
Cdd:cd03262 166 LDPELVGEVLDVMKDLAEEgMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1296-1520 |
2.43e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 95.95 E-value: 2.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELD-LVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLS 1374
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1375 IIPQ--DSQVFEGTVRENIdpinQYTDEAiwRALELSHLKEHVL-SMSNDGLDAQLTEGGGNLSVGQRQLLCLARAMLVP 1451
Cdd:PRK13650 85 MVFQnpDNQFVGATVEDDV----AFGLEN--KGIPHEEMKERVNeALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
9AYC_A 1452 SKILVLDQATAAVDVETDKVVQETIRTAFKDR--TILTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQLLS 1520
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1313-1507 |
4.43e-21 |
|
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: 93.55 E-value: 4.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1313 LKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDL----RHKLSIIPQDSQVFEGTVR 1388
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1389 ENI---DPINQYTDEAIWRALELshlkEHVLSMSNDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVD 1465
Cdd:cd03290 97 ENItfgSPFNKQRYKAVTDACSL----QPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
9AYC_A 1466 VE-TDKVVQETIRTAFKD--RTILTIAHRLNTIMDSDRIIVLDNG 1507
Cdd:cd03290 173 IHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1296-1509 |
4.84e-21 |
|
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: 93.32 E-value: 4.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYR--PELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLtlalFRMI----EASEGNIVIDNIAINEIGLYDL 1369
Cdd:cd03255 1 IELKNLSKTYGggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTL----LNILggldRPTSGEVRVDGTDISKLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1370 ----RHKLSIIPQDSQVFEG-TVRENIDPINQYT----DEAIWRALELshLkEHVlsmsndGLDAQLTEGGGNLSVGQRQ 1440
Cdd:cd03255 77 aafrRRHIGFVFQSFNLLPDlTALENVELPLLLAgvpkKERRERAEEL--L-ERV------GLGDRLNHYPSELSGGQQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
9AYC_A 1441 LLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIR--TAFKDRTILTIAHRLNTIMDSDRIIVLDNGKV 1509
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1296-1521 |
5.77e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 94.67 E-value: 5.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYrPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIG-LYDLRHKLS 1374
Cdd:PRK13644 2 IRLENVSYSY-PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1375 IIPQ--DSQVFEGTVRENIdpinQYTDEAIwrALELSHLKEHV-LSMSNDGLDAQLTEGGGNLSVGQRQLLCLARAMLVP 1451
Cdd:PRK13644 81 IVFQnpETQFVGRTVEEDL----AFGPENL--CLPPIEIRKRVdRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
9AYC_A 1452 SKILVLDQATAAVDVETDKVVQETIRTAF-KDRTILTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQLLSD 1521
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1296-1517 |
1.46e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 92.04 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELDlVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEI---GLYDLRHK 1372
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1373 LSIIPQDSQVFEG-TVRENIdpinqytdeAIwrALELSHLKEH--------VLSMSndGLDAQLTEGGGNLSVGQRQLLC 1443
Cdd:COG2884 81 IGVVFQDFRLLPDrTVYENV---------AL--PLRVTGKSRKeirrrvreVLDLV--GLSDKAKALPHELSGGEQQRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1444 LARAMLVPSKILVLDQATAAVDVETdkvVQETIRtAFKD-----RTILtIA-HRLNtIMDS--DRIIVLDNGKVAEFDSP 1515
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPET---SWEIME-LLEEinrrgTTVL-IAtHDLE-LVDRmpKRVLELEDGRLVRDEAR 221
|
..
9AYC_A 1516 GQ 1517
Cdd:COG2884 222 GV 223
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
473-864 |
2.07e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 97.40 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 473 WVGVIILVIMMPLNSFLMR--------IQKKLQKSQmkykDERTRVISEILNNIKSLKLYAWEKPYREKLEEVRNNKELK 544
Cdd:PRK11176 165 WQLSLILIVIAPIVSIAIRvvskrfrnISKNMQNTM----GQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQ 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 545 NLTklgcyMAVTSFQFNIVPFLVSCCTFAVFVYtedrALTTDLVFPALT----------LFNLLSfPLMIIPMVLNSFIE 614
Cdd:PRK11176 241 GMK-----MVSASSISDPIIQLIASLALAFVLY----AASFPSVMDTLTagtitvvfssMIALMR-PLKSLTNVNAQFQR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 615 ASVSIGRLFTFFTNEELQPDSVQRLPKVKniGDVAInigDDATFLWQRKPEykVALKNINFQAKKGNLTCIVGKVGSGKT 694
Cdd:PRK11176 311 GMAACQTLFAILDLEQEKDEGKRVIERAK--GDIEF---RNVTFTYPGKEV--PALRNINFKIPAGKTVALVGRSGSGKS 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 695 ALLS-------------CMLGDLFRVKGFATVHGSVAYVSQVPWIMNGTVKENILF--GHRYDAEFYEKTIKAcALTIDL 759
Cdd:PRK11176 384 TIANlltrfydidegeiLLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYarTEQYSREQIEEAARM-AYAMDF 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 760 AILMD-GDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARhLIEHVLgpNGLLHTKTKVLATNKV 838
Cdd:PRK11176 463 INKMDnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESER-AIQAAL--DELQKNRTSLVIAHRL 539
|
410 420
....*....|....*....|....*.
9AYC_A 839 SALSIADSIALLDNGEITQQGTYDEI 864
Cdd:PRK11176 540 STIEKADEILVVEDGEIVERGTHAEL 565
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
654-864 |
2.27e-20 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 92.07 E-value: 2.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 654 DDATFLWQRKPeykvALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHG--------SVAYVSQ--- 722
Cdd:COG1121 10 ENLTVSYGGRP----VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVPQrae 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 723 VPWIMNGTVKENILFG--------HRYDAEFYEKTIKACALT--IDLAilmdgdKTLVGEkgisLSGGQKARLSLARAVY 792
Cdd:COG1121 86 VDWDFPITVRDVVLMGrygrrglfRRPSRADREAVDEALERVglEDLA------DRPIGE----LSGGQQQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 793 ARADTYLLDDPLAAVDEHVARHLIEhvlgpngLLHT-----KTKVLAT---NKVSALsiADSIALLdNGEITQQGTYDEI 864
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYE-------LLRElrregKTILVVThdlGAVREY--FDRVLLL-NRGLVAHGPPEEV 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1296-1510 |
2.28e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 93.19 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELDL---VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINE--IGLYDLR 1370
Cdd:PRK13637 3 IKIENLTHIYMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1371 HKLSIIPQ--DSQVFEGTVRENID--PINqytdeaiwRALELSHLKEHVL-SMSNDGLDAQ--LTEGGGNLSVGQRQLLC 1443
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAfgPIN--------LGLSEEEIENRVKrAMNIVGLDYEdyKDKSPFELSGGQKRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1444 LARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKDR--TILTIAHRLNTIMD-SDRIIVLDNGKVA 1510
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKlADRIIVMNKGKCE 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
670-805 |
2.29e-20 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 89.24 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 670 LKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDL-------------FRVKGFATVHGSVAYVSQVPWIMNG-TVKENI 735
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLsptegtilldgqdLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
9AYC_A 736 LFGhRYDAEFYEKTIKAcalTIDLAI----LMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLA 805
Cdd:pfam00005 81 RLG-LLLKGLSKREKDA---RAEEALeklgLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1312-1521 |
3.88e-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: 3.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLtlalFRMI----EASEGNIVIDNIAINEIGLYDL-RHKLSIIPQDSQVFEG- 1385
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTL----FNLIsgflRPTSGSVLFDGEDITGLPPHEIaRLGIGRTFQIPRLFPEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1386 TVRENID-PINQYTDEAIWRALELSHLKEH------VLSMSndGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLD 1458
Cdd:cd03219 91 TVLENVMvAAQARTGSGLLLARARREEREAreraeeLLERV--GLADLADRPAGELSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 1459 QATAAV-DVETDKVVqETIRT-AFKDRTILTIAHRLNTIMD-SDRIIVLDNGKV-AEfDSPGQLLSD 1521
Cdd:cd03219 169 EPAAGLnPEETEELA-ELIRElRERGITVLLVEHDMDVVMSlADRVTVLDQGRViAE-GTPDEVRNN 233
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
662-864 |
6.78e-20 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 90.82 E-value: 6.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 662 RKPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLScMLGDLFR-VKGFATVHG-------------SVAYVSQVPWIM 727
Cdd:cd03295 9 RYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMK-MINRLIEpTSGEIFIDGedireqdpvelrrKIGYVIQQIGLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 728 -NGTVKENI-----LFG---HRYDAEFYEktikacaltidLAILMD-GDKTLVGEKGISLSGGQKARLSLARAVYARADT 797
Cdd:cd03295 88 pHMTVEENIalvpkLLKwpkEKIRERADE-----------LLALVGlDPAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 798 YLLDDPLAAVDEHVARHLIEHVLGPNGLLHtKTKVLATNKV-SALSIADSIALLDNGEITQQGTYDEI 864
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELG-KTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1296-1525 |
9.27e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 90.97 E-value: 9.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSI 1375
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1376 IPQDsqvfegtvrenidPINQYT------DEAIwrALE---LSHLKEHVL---SMSNDGLDAQLTEGGGNLSVGQRQLLC 1443
Cdd:PRK13648 88 VFQN-------------PDNQFVgsivkyDVAF--GLEnhaVPYDEMHRRvseALKQVDMLERADYEPNALSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1444 LARAMLVPSKILVLDQATAAVDVETDKVVQETIR--TAFKDRTILTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQLLSD 1521
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
|
....
9AYC_A 1522 NKSL 1525
Cdd:PRK13648 233 AEEL 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1312-1513 |
2.81e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.16 E-value: 2.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNiaiNEIGLYD----LRHKLSIIPQDSQVFEG-T 1386
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG---EPVRFRSprdaQAAGIAIIHQELNLVPNlS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1387 VRENI----DP-----INqytdeaiWRALE------LSHLKEHVlsmsnDgLDAQLteggGNLSVGQRQLLCLARAMLVP 1451
Cdd:COG1129 96 VAENIflgrEPrrgglID-------WRAMRrrarelLARLGLDI-----D-PDTPV----GDLSVAQQQLVEIARALSRD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 1452 SKILVLDQATAA-VDVETDKVVqETIRTaFKDR--TILTIAHRLNTIMD-SDRIIVLDNGK-VAEFD 1513
Cdd:COG1129 159 ARVLILDEPTASlTEREVERLF-RIIRR-LKAQgvAIIYISHRLDEVFEiADRVTVLRDGRlVGTGP 223
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1312-1518 |
3.18e-19 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 88.94 E-value: 3.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIE-----ASEGNIVID--NIAINEIGLYDLRHKLSIIPQDSQVFE 1384
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlipgaRVEGEILLDgeDIYDPDVDVVELRRRVGMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1385 GTVRENID---PINQYT-----DEAIWRALELSHLKEHVlsmsNDGLDAQltegGGNLSVGQRQLLCLARAMLVPSKILV 1456
Cdd:COG1117 106 KSIYDNVAyglRLHGIKskselDEIVEESLRKAALWDEV----KDRLKKS----ALGLSGGQQQRLCIARALAVEPEVLL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 1457 LDQATAAVD-VETDKvVQETIRTAFKDRTILTIAHRlntiMD-----SDRIIVLDNGKVAEFDSPGQL 1518
Cdd:COG1117 178 MDEPTSALDpISTAK-IEELILELKKDYTIVIVTHN----MQqaarvSDYTAFFYLGELVEFGPTEQI 240
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1311-1508 |
4.74e-19 |
|
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: 87.15 E-value: 4.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1311 LVLKHINIHIKPNEKVGIVGRTGAGKSSLtlalFRMI----EASEGNIVIDNIAINEIGLyDLRHKLSIIPQDSQVFEG- 1385
Cdd:COG4133 16 LLFSGLSFTLAAGEALALTGPNGSGKTTL----LRILagllPPSAGEVLWNGEPIRDARE-DYRRRLAYLGHADGLKPEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1386 TVRENID------PINQyTDEAIWRALE---LSHLkEHVLsmsndgldaqltegGGNLSVGQRQLLCLARAMLVPSKILV 1456
Cdd:COG4133 91 TVRENLRfwaalyGLRA-DREAIDEALEavgLAGL-ADLP--------------VRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
9AYC_A 1457 LDQATAAVDVETDKVVQETIRtAFKDR--TILTIAHRLNTImDSDRIIVLDNGK 1508
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIA-AHLARggAVLLTTHQPLEL-AAARVLDLGDFK 206
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1296-1524 |
5.38e-19 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 90.14 E-value: 5.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELDLV--LKHINIHIKPNEKVGIVGRTGAGKSslTLAlfRMI----EASEGNIVIDNI---AINEIGL 1366
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKS--TLI--RCInlleRPTSGSVLVDGVdltALSEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1367 YDLRHKLSIIPQDSQVFEG-TVRENID-P--INQYTDEAIW-RALELSHLkehVlsmsndGLD-------AQltegggnL 1434
Cdd:COG1135 78 RAARRKIGMIFQHFNLLSSrTVAENVAlPleIAGVPKAEIRkRVAELLEL---V------GLSdkadaypSQ-------L 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1435 SVGQRQLLCLARAmLVPS-KILVLDQATAAVDVETdkvvqeTirtafkdRTILT----IAHRLN-TI------MD----- 1497
Cdd:COG1135 142 SGGQKQRVGIARA-LANNpKVLLCDEATSALDPET------T-------RSILDllkdINRELGlTIvlitheMDvvrri 207
|
250 260
....*....|....*....|....*..
9AYC_A 1498 SDRIIVLDNGKVAEFDSPGQLLSDNKS 1524
Cdd:COG1135 208 CDRVAVLENGRIVEQGPVLDVFANPQS 234
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
655-855 |
6.28e-19 |
|
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: 87.53 E-value: 6.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 655 DATFLWQRKPEYKVaLKNINFQAKKGNLTCIVGKVGSGKTALLScMLGDLFRVKGFATV--------------HGSVAYV 720
Cdd:cd03248 16 NVTFAYPTRPDTLV-LQDVSFTLHPGEVTALVGPSGSGKSTVVA-LLENFYQPQGGQVLldgkpisqyehkylHSKVSLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 721 SQVPWIMNGTVKENILFGHRyDAEFYEKTIKACALTIDLAI--LMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTY 798
Cdd:cd03248 94 GQEPVLFARSLQDNIAYGLQ-SCSFECVKEAAQKAHAHSFIseLASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 799 LLDDPLAAVDEHvARHLIEHVLgpNGLLHTKTKVLATNKVSALSIADSIALLDNGEI 855
Cdd:cd03248 173 ILDEATSALDAE-SEQQVQQAL--YDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1263-1506 |
8.14e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 93.56 E-value: 8.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1263 SVERIKEYADLKSEAPLiVEGHRPPKEWPSQGDIKFNNYSTRYRPELDL-VLKHINIHIKPNEKVGIVGRTGAGKSSLTL 1341
Cdd:PTZ00265 351 SLEATNSLYEIINRKPL-VENNDDGKKLKDIKKIQFKNVRFHYDTRKDVeIYKDLNFTLTEGKTYAFVGESGCGKSTILK 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1342 ALFRMIEASEGNIVI-DNIAINEIGLYDLRHKLSIIPQDSQVFEGTVRENI----------DPINQYTDE---------- 1400
Cdd:PTZ00265 430 LIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdlEALSNYYNEdgndsqenkn 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1401 --AIWRALELSHLKEHVLSMSNDGL--------------------------------DAQLTEGGGN---LSVGQRQLLC 1443
Cdd:PTZ00265 510 krNSCRAKCAGDLNDMSNTTDSNELiemrknyqtikdsevvdvskkvlihdfvsalpDKYETLVGSNaskLSGGQKQRIS 589
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
9AYC_A 1444 LARAMLVPSKILVLDQATAAVDVETDKVVQETIRT--AFKDRTILTIAHRLNTIMDSDRIIVLDN 1506
Cdd:PTZ00265 590 IARAIIRNPKILILDEATSSLDNKSEYLVQKTINNlkGNENRITIIIAHRLSTIRYANTIFVLSN 654
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
654-854 |
8.51e-19 |
|
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: 86.75 E-value: 8.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 654 DDATFLWQRKPEYkvALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHG-------------SVAYV 720
Cdd:cd03225 3 KNLSFSYPDGARP--ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 721 SQVP--WIMNGTVKENILFG----HRYDAEFYEKTIKACALTiDLAILMDgdktlvgEKGISLSGGQKARLSLARAVYAR 794
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGlenlGLPEEEIEERVEEALELV-GLEGLRD-------RSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
9AYC_A 795 ADTYLLDDPLAAVDEHVARHLIEHVLGpnglLHT--KTKVLATNKVS-ALSIADSIALLDNGE 854
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKK----LKAegKTIIIVTHDLDlLLELADRVIVLEDGK 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
667-855 |
8.95e-19 |
|
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: 85.53 E-value: 8.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGsvayvsQVPWIMNGTVKENI--LFGhryDAE 744
Cdd:cd03230 13 KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG------KDIKKEPEEVKRRIgyLPE---EPS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 745 FYEKtikacaLTidlailmdgdktlvGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARHLIEHVLGPNG 824
Cdd:cd03230 84 LYEN------LT--------------VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKK 143
|
170 180 190
....*....|....*....|....*....|..
9AYC_A 825 llHTKTKVLATNKVS-ALSIADSIALLDNGEI 855
Cdd:cd03230 144 --EGKTILLSSHILEeAERLCDRVAILNNGRI 173
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
621-864 |
9.96e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 91.95 E-value: 9.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 621 RLFTFFTNEELQPDSVQRlPKVKNIGDVAINIG-DDATFLWQRKPEykvALKNINFQAKKGNLTCIVGKVGSGKTALLSC 699
Cdd:PRK13657 305 KLEEFFEVEDAVPDVRDP-PGAIDLGRVKGAVEfDDVSFSYDNSRQ---GVEDVSFEAKPGQTVAIVGPTGAGKSTLINL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 700 mlgdLFRV----KGFATVHG-------------SVAYVSQVPWIMNGTVKENILFGhRYDA---EFYEKTIKACALTIDL 759
Cdd:PRK13657 381 ----LQRVfdpqSGRILIDGtdirtvtraslrrNIAVVFQDAGLFNRSIEDNIRVG-RPDAtdeEMRAAAERAQAHDFIE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 760 AILmDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARHLIEHVlgpNGLLHTKTKVLATNKVS 839
Cdd:PRK13657 456 RKP-DGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAAL---DELMKGRTTFIIAHRLS 531
|
250 260
....*....|....*....|....*
9AYC_A 840 ALSIADSIALLDNGEITQQGTYDEI 864
Cdd:PRK13657 532 TVRNADRILVFDNGRVVESGSFDEL 556
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
669-864 |
1.76e-18 |
|
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: 86.08 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 669 ALKNINFQAKKGNLTCIVGKVGSGKTALLSCM-----LGDLFRVKGFATVHGS---------------VAYVSQVPWIMN 728
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKdiydldvdvlelrrrVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 729 GTVKENILFG---HRYDAEFYEKTIKACALTIdlAILMD--GDKTlvgeKGISLSGGQKARLSLARAVYARADTYLLDDP 803
Cdd:cd03260 95 GSIYDNVAYGlrlHGIKLKEELDERVEEALRK--AALWDevKDRL----HALGLSGGQQQRLCLARALANEPEVLLLDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
9AYC_A 804 LAAVDEhVARHLIEHVLGpnGLLHTKTKVLAT-NKVSALSIADSIALLDNGEITQQGTYDEI 864
Cdd:cd03260 169 TSALDP-ISTAKIEELIA--ELKKEYTIVIVThNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
667-872 |
2.03e-18 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 86.02 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGS----------------VAYVSQvpwimNG- 729
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrrMGMLFQ-----SGa 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 730 -----TVKENILFGHRYDAEFYEKTIKACAL-TIDLAILMDGDKTLVGEkgisLSGGQKARLSLARAVYARADTYLLDDP 803
Cdd:cd03261 88 lfdslTVFENVAFPLREHTRLSEEEIREIVLeKLEAVGLRGAEDLYPAE----LSGGMKKRVALARALALDPELLLYDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 804 LAAVDEHVARHLIEHVLGPNGLLHTkTKVLATNKV-SALSIADSIALLDNGEITQQGTYDEItKDADSPL 872
Cdd:cd03261 164 TAGLDPIASGVIDDLIRSLKKELGL-TSIMVTHDLdTAFAIADRIAVLYDGKIVAEGTPEEL-RASDDPL 231
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1312-1511 |
2.91e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 85.48 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSL--TLALfrMIEASEGNIVIDNIAI---NEIGLYDLR-HKLSIIPQDSQVFEG 1385
Cdd:COG1136 23 ALRGVSLSIEAGEFVAIVGPSGSGKSTLlnILGG--LDRPTSGEVLIDGQDIsslSERELARLRrRHIGFVFQFFNLLPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1386 -TVRENI----DPINQYTDEAIWRALELshLkEHVlsmsndGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQA 1460
Cdd:COG1136 101 lTALENValplLLAGVSRKERRERAREL--L-ERV------GLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
9AYC_A 1461 TAAVDVETDKVVQETIRTAFKD--RTILTIAHRLNTIMDSDRIIVLDNGKVAE 1511
Cdd:COG1136 172 TGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1305-1512 |
3.01e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 90.64 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1305 YRPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSltlaLFRMI----EASEGNIVIDNIAineiglydlrhKLSIIPQDS 1380
Cdd:COG4178 371 RTPDGRPLLEDLSLSLKPGERLLITGPSGSGKST----LLRAIaglwPYGSGRIARPAGA-----------RVLFLPQRP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1381 QVFEGTVRENI---DPINQYTDEAIWRALE---LSHLKEHvlsmsndgLDAQlTEGGGNLSVGQRQLLCLARAMLVPSKI 1454
Cdd:COG4178 436 YLPLGTLREALlypATAEAFSDAELREALEavgLGHLAER--------LDEE-ADWDQVLSLGEQQRLAFARLLLHKPDW 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 1455 LVLDQATAAVDVETDKVVQETIRTAFKDRTILTIAHRlNTIMD-SDRIIVLDNGKVAEF 1512
Cdd:COG4178 507 LFLDEATSALDEENEAALYQLLREELPGTTVISVGHR-STLAAfHDRVLELTGDGSWQL 564
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1296-1521 |
5.13e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 86.29 E-value: 5.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELD----LVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNI-AINEIGLYDLR 1370
Cdd:PRK13633 5 IKCKNVSYKYESNEEstekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLdTSDEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1371 HKLSIIPQ--DSQVFEGTVREN---------IDP--INQYTDEAIwRALELSHLKEHVLSMsndgldaqltegggnLSVG 1437
Cdd:PRK13633 85 NKAGMVFQnpDNQIVATIVEEDvafgpenlgIPPeeIRERVDESL-KKVGMYEYRRHAPHL---------------LSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1438 QRQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKDR--TILTIAHRLNTIMDSDRIIVLDNGKVAEFDSP 1515
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGTP 228
|
....*.
9AYC_A 1516 GQLLSD 1521
Cdd:PRK13633 229 KEIFKE 234
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
667-864 |
5.34e-18 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 85.48 E-value: 5.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHG-------------SVAYVSQ---VPWimNGT 730
Cdd:COG1120 14 RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAYVPQeppAPF--GLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 731 VKENILFG--------HRYDAEFYEKTIKACALTiDLAILMDgdkTLVGEkgisLSGGQKARLSLARAVYARADTYLLDD 802
Cdd:COG1120 92 VRELVALGryphlglfGRPSAEDREAVEEALERT-GLEHLAD---RPVDE----LSGGERQRVLIARALAQEPPLLLLDE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
9AYC_A 803 PLAAVDehvARHLIEhVLgpnGLLHT------KTKVLAT---NkvSALSIADSIALLDNGEITQQGTYDEI 864
Cdd:COG1120 164 PTSHLD---LAHQLE-VL---ELLRRlarergRTVVMVLhdlN--LAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1296-1525 |
7.73e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 85.65 E-value: 7.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELDLV---LKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAIN----EIGLYD 1368
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1369 LRHKLSIIPQ--DSQVFEGTVRENID--PIN--QYTDEAIWRALELshlkehvlsMSNDGLDAQLTEGGG-NLSVGQRQL 1441
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEfgPKNfgFSEDEAKEKALKW---------LKKVGLSEDLISKSPfELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1442 LCLARAMLVPSKILVLDQATAAVDVETdkvvQETIRTAFKD-----RTILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSP 1515
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEG----RKEMMQLFKDyqkagHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASP 229
|
250
....*....|
9AYC_A 1516 GQLLSDNKSL 1525
Cdd:PRK13641 230 KEIFSDKEWL 239
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1296-1513 |
8.50e-18 |
|
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: 83.72 E-value: 8.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPelDLVLKHINIHIKPNEKVGIVGRTGAGKSSLtlalFRMI----EASEGNIVIDNIAINEIGLYdlRH 1371
Cdd:cd03259 1 LELKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTL----LRLIagleRPDSGEILIDGRDVTGVPPE--RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1372 KLSIIPQDSQVFEG-TVRENID--PINQYTDEAIWRALELSHLkEHVlsmsndGLDAQLTEGGGNLSVGQRQLLCLARAM 1448
Cdd:cd03259 73 NIGMVFQDYALFPHlTVAENIAfgLKLRGVPKAEIRARVRELL-ELV------GLEGLLNRYPHELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 1449 LVPSKILVLDQATAAVDVETDKVVQETIRTAFKDR--TILTIAHRLNTIMD-SDRIIVLDNGKVAEFD 1513
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1296-1511 |
9.24e-18 |
|
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: 83.68 E-value: 9.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELD--LVLKHINIHIKPNEKVGIVGRTGAGKSSltlaLFRMI----EASEGNIVIDNIAINEIGlydl 1369
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKST----LLRIIagleRPTSGEVLVDGEPVTGPG---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1370 rHKLSIIPQDSQVFE-GTVRENIdpinqytdeAIwrALEL-----SHLKEHVLSMSND-GLDAQLTEGGGNLSVGQRQLL 1442
Cdd:cd03293 73 -PDRGYVFQQDALLPwLTVLDNV---------AL--GLELqgvpkAEARERAEELLELvGLSGFENAYPHQLSGGMRQRV 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
9AYC_A 1443 CLARAMLVPSKILVLDQATAAVDVETDKVVQETI-RTAFKDR-TILTIAHRLN-TIMDSDRIIVLDN--GKVAE 1511
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELlDIWRETGkTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
663-859 |
1.02e-17 |
|
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: 82.36 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 663 KPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGS------------VAYVSQVPWIMNGT 730
Cdd:cd03247 11 PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVLNQRPYLFDTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 731 VKENIlfghrydaefyektikacaltidlailmdgdktlvgekGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEH 810
Cdd:cd03247 91 LRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPI 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
9AYC_A 811 VARHLIEHVLgpnGLLHTKTKVLATNKVSALSIADSIALLDNGEITQQG 859
Cdd:cd03247 133 TERQLLSLIF---EVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
667-869 |
1.29e-17 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 83.54 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHG-------------SVAYVSQVPWIM--NGTV 731
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknlrelrrKVGLVFQNPDDQlfAPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 732 KENILFG---HRYDAEFYEKTIKACALTIDLAILMDgdktlvgeKGI-SLSGGQKARLSLARAVYARADTYLLDDPLAAV 807
Cdd:COG1122 94 EEDVAFGpenLGLPREEIRERVEEALELVGLEHLAD--------RPPhELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
9AYC_A 808 DEHVARHLIEHVLGpnglLHT--KTKVLATNKVS-ALSIADSIALLDNGEITQQGTYDEITKDAD 869
Cdd:COG1122 166 DPRGRRELLELLKR----LNKegKTVIIVTHDLDlVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
663-852 |
2.64e-17 |
|
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: 82.52 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 663 KPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHG--------SVAYVSQ----VPWImngT 730
Cdd:cd03293 13 GGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvtgpgpDRGYVFQqdalLPWL---T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 731 VKENILFG----HRYDAEFYEKTIKACALtidlailmdgdktlVGEKGIS------LSGGQKARLSLARAVYARADTYLL 800
Cdd:cd03293 90 VLDNVALGlelqGVPKAEARERAEELLEL--------------VGLSGFEnayphqLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
9AYC_A 801 DDPLAAVDEHVARHLIEHVLgpnGLLHT--KTKVLATNKVS-ALSIADSIALLDN 852
Cdd:cd03293 156 DEPFSALDALTREQLQEELL---DIWREtgKTVLLVTHDIDeAVFLADRVVVLSA 207
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1296-1526 |
2.93e-17 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 82.77 E-value: 2.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRpelDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEigLYDLRHKLSI 1375
Cdd:cd03299 1 LKVENLSKDWK---EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN--LPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1376 IPQDSQVFEG-TVRENIdpinQYTdeAIWRALELSHLKEHVLSMSND-GLDAQLTEGGGNLSVGQRQLLCLARAMLVPSK 1453
Cdd:cd03299 76 VPQNYALFPHmTVYKNI----AYG--LKKRKVDKKEIERKVLEIAEMlGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 1454 ILVLDQATAAVDVETDKVVQETIRTAFK--DRTILTIAHRLNTI-MDSDRIIVLDNGKVAEFDSPGQLLSDNKSLF 1526
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKKPKNEF 225
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
664-860 |
5.22e-17 |
|
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: 81.77 E-value: 5.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 664 PEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCmlgdLFRV----KGFATVHG-------------SVAYVSQVPWI 726
Cdd:cd03244 14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLA----LFRLvelsSGSILIDGvdiskiglhdlrsRISIIPQDPVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 727 MNGTVKENI-LFGHRYDAEFYEkTIKACALTIDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLA 805
Cdd:cd03244 90 FSGTIRSNLdPFGEYSDEELWQ-ALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
9AYC_A 806 AVDEHVARHLIEhvlgpngLLHTKTKvlatnKVSALSIA---------DSIALLDNGEITQQGT 860
Cdd:cd03244 169 SVDPETDALIQK-------TIREAFK-----DCTVLTIAhrldtiidsDRILVLDKGRVVEFDS 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
410-863 |
5.78e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 86.42 E-value: 5.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 410 YQKSLVLSneASGLSS--TGDIVNLMSVDVQKLQDLtqWLNLI--WSGPFQIIICLY--------SLYKLLGNSMwvgVI 477
Cdd:PRK11160 100 FSKLLPLS--PAGLARyrQGDLLNRLVADVDTLDHL--YLRLIspLVAALVVILVLTiglsffdlTLALTLGGIL---LL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 478 ILVIMMPLNSFL-MRIQKKLQKSQMKYkdeRTRVIsEILNNIKSLKLYAWEKPYREKLEEV-----RNNKELKNLTKL-- 549
Cdd:PRK11160 173 LLLLLPLLFYRLgKKPGQDLTHLRAQY---RVQLT-EWLQGQAELTLFGAEDRYRQQLEQTeqqwlAAQRRQANLTGLsq 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 550 GCYMAVTSFQFNIVPFLVScctFAVFVYTEDRALTTDLVFPALTLFNLLsfplMIIPMV-------------LNSFIEAS 616
Cdd:PRK11160 249 ALMILANGLTVVLMLWLAA---GGVGGNAQPGALIALFVFAALAAFEAL----MPVAGAfqhlgqviasarrINEITEQK 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 617 VSIgrlfTFFTNEELQPDSVqrlpkvknigdvAINIgDDATFLWQRKPEykVALKNINFQAKKGNLTCIVGKVGSGKTAL 696
Cdd:PRK11160 322 PEV----TFPTTSTAAADQV------------SLTL-NNVSFTYPDQPQ--PVLKGLSLQIKAGEKVALLGRTGCGKSTL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 697 LS------------CMLGDLfRVKGF--ATVHGSVAYVSQVPWIMNGTVKENILFG--HRYDAEFYEktikacALT-IDL 759
Cdd:PRK11160 383 LQlltrawdpqqgeILLNGQ-PIADYseAALRQAISVVSQRVHLFSATLRDNLLLAapNASDEALIE------VLQqVGL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 760 AILMDGDKTL---VGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARH----LIEHVLGpngllhtKTKV 832
Cdd:PRK11160 456 EKLLEDDKGLnawLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQilelLAEHAQN-------KTVL 528
|
490 500 510
....*....|....*....|....*....|.
9AYC_A 833 LATNKVSALSIADSIALLDNGEITQQGTYDE 863
Cdd:PRK11160 529 MITHRLTGLEQFDRICVMDNGQIIEQGTHQE 559
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
1013-1267 |
6.50e-17 |
|
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: 83.21 E-value: 6.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1013 ARYLAIYFALGIGSALATLIQTIVL-WVfctihASKYLHNL---MTNSVLRAPMTFFETTPIGRILNRFSNDIYKVDALL 1088
Cdd:cd18544 41 LLLALLYLGLLLLSFLLQYLQTYLLqKL-----GQRIIYDLrrdLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1089 GRTFSQFFVNAVKVTFTITVICATTWQ---FIFIIIPLSVFYIYYQQYYLRTS-RELRRLdsitRSPIYSHFQETLGGLA 1164
Cdd:cd18544 116 TSGLVTLIGDLLLLIGILIAMFLLNWRlalISLLVLPLLLLATYLFRKKSRKAyREVREK----LSRLNAFLQESISGMS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1165 TVRGYSQQKR----FSHINQCRIDNNM------SAFYPSInanrwlayrlELIGSIIIlgAATLSVF--RLKQGTLTAGM 1232
Cdd:cd18544 192 VIQLFNREKRefeeFDEINQEYRKANLksiklfALFRPLV----------ELLSSLAL--ALVLWYGggQVLSGAVTLGV 259
|
250 260 270
....*....|....*....|....*....|....*.
9AYC_A 1233 VGLSLSYALQITQTLNWIV-RMTVeVETNIVSVERI 1267
Cdd:cd18544 260 LYAFIQYIQRFFRPIRDLAeKFNI-LQSAMASAERI 294
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1296-1535 |
8.74e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 82.54 E-value: 8.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELDLVLKHINIHIKPNEKVGIVGRTGAGKSS---LTLALFRMIEASEGNIVIDNIAINEIGLYDLRHK 1372
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1373 LSIIPQ--DSQVFEGTVRENIdpinQYTDEAiwRALELSHLKEHVLSMSND--GLDAQLTEGGgNLSVGQRQLLCLARAM 1448
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDV----AFGLEN--RAVPRPEMIKIVRDVLADvgMLDYIDSEPA-NLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1449 LVPSKILVLDQATAAVDVETDKVVQETIRTAFKDR--TILTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQLLSDNkslf 1526
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV---- 234
|
....*....
9AYC_A 1527 ySLCMEAGL 1535
Cdd:PRK13640 235 -EMLKEIGL 242
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
661-819 |
1.08e-16 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 80.25 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 661 QRKPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLScMLGDLFRV-KGFATVHG-------------SVAYVSQVPWI 726
Cdd:COG4619 7 SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLR-ALADLDPPtSGEIYLDGkplsampppewrrQVAYVPQEPAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 727 MNGTVKENILFGHRYDAEFYEKTiKACALtidLAILMDGDKTLvgEKGIS-LSGGQKARLSLARAVYARADTYLLDDPLA 805
Cdd:COG4619 86 WGGTVRDNLPFPFQLRERKFDRE-RALEL---LERLGLPPDIL--DKPVErLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170
....*....|....
9AYC_A 806 AVDEHVARHLIEHV 819
Cdd:COG4619 160 ALDPENTRRVEELL 173
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1312-1509 |
1.30e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 81.67 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLtlalFRMI----EASEGNIVIDNIAINEIGLYDlRHKLsiIpqdSQVFE--- 1384
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTL----LNAIagslPPDSGSILIDGKDVTKLPEYK-RAKY--I---GRVFQdpm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1385 -GT-----VRENIdpinqytdeAI------WRAL-------ELSHLKEHVLSMSNdGLDAQLTEGGGNLSVGQRQLLCLA 1445
Cdd:COG1101 91 mGTapsmtIEENL---------ALayrrgkRRGLrrgltkkRRELFRELLATLGL-GLENRLDTKVGLLSGGQRQALSLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
9AYC_A 1446 RAMLVPSKILVLDQATAAVD-------VE-TDKVVQEtirtafKDRTILTIAHRLNTIMD-SDRIIVLDNGKV 1509
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDpktaalvLElTEKIVEE------NNLTTLMVTHNMEQALDyGNRLIMMHEGRI 227
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1298-1507 |
1.37e-16 |
|
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: 81.83 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1298 FNNYSTRYRPeldlVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIvidniaineiglydlRH--KLSI 1375
Cdd:cd03291 42 FSNLCLVGAP----VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI---------------KHsgRISF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1376 IPQDSQVFEGTVRENID---PINQYTDEAIWRALELshlkEHVLSMSNDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPS 1452
Cdd:cd03291 103 SSQFSWIMPGTIKENIIfgvSYDEYRYKSVVKACQL----EEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 1453 KILVLDQATAAVDVETDKVVQET-IRTAFKDRTILTIAHRLNTIMDSDRIIVLDNG 1507
Cdd:cd03291 179 DLYLLDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
667-859 |
1.73e-16 |
|
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: 79.02 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGS-------------VAYVSQVpwimngtvke 733
Cdd:cd03214 12 RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaslspkelarkIAYVPQA---------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 734 nilfghrydaefyektIKACALTiDLAilmdgdktlvgEKGI-SLSGGQKARLSLARAVYARADTYLLDDPLAAVDehvA 812
Cdd:cd03214 82 ----------------LELLGLA-HLA-----------DRPFnELSGGERQRVLLARALAQEPPILLLDEPTSHLD---I 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
9AYC_A 813 RHLIEhVLgpnGLLHT------KTKVLATNKVS-ALSIADSIALLDNGEITQQG 859
Cdd:cd03214 131 AHQIE-LL---ELLRRlarergKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1309-1509 |
3.12e-16 |
|
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: 78.24 E-value: 3.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1309 LDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYD-LRHKLSIIPQDSQ----VF 1383
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDRKreglVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1384 EGTVRENIdpinqytdeaiwralELSHLkehvLSmsndgldaqltegGGNLsvgqrQLLCLARAMLVPSKILVLDQATAA 1463
Cdd:cd03215 92 DLSVAENI---------------ALSSL----LS-------------GGNQ-----QKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
9AYC_A 1464 VDVETDKVVQETIRtAFKDR--TILTIAHRLNTIMD-SDRIIVLDNGKV 1509
Cdd:cd03215 135 VDVGAKAEIYRLIR-ELADAgkAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1296-1510 |
4.25e-16 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 78.95 E-value: 4.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELDLV--LKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLyDLRHKL 1373
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA-EARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1374 SIIPQDSQVFEG-TVRENIdpinQY--------TDEAIWRALELSHLkehvLSMsNDGLDAQltegGGNLSVGQRQLLCL 1444
Cdd:cd03266 81 GFVSDSTGLYDRlTARENL----EYfaglyglkGDELTARLEELADR----LGM-EELLDRR----VGGFSTGMRQKVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 1445 ARAMLVPSKILVLDQATAAVDVETDKVVQETIRtAFKD--RTILTIAHRLNTIMD-SDRIIVLDNGKVA 1510
Cdd:cd03266 148 ARALVHDPPVLLLDEPTTGLDVMATRALREFIR-QLRAlgKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1313-1515 |
4.42e-16 |
|
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: 83.20 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1313 LKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEaSEGNIVIDNIAINEIG---LYDLRHKLSIIPQD---------- 1379
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDpfgslsprmt 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1380 -SQ-VFEGTVRENIDPINQYTDEAIWRALelshlkEHVlsmsndGLDAQL-----TEgggnLSVGQRQLLCLARAMLVPS 1452
Cdd:COG4172 381 vGQiIAEGLRVHGPGLSAAERRARVAEAL------EEV------GLDPAArhrypHE----FSGGQRQRIAIARALILEP 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 1453 KILVLDQATAAVDVetdkVVQETIRTAFKD------RTILTIAHRLNTI--MdSDRIIVLDNGKVAE-------FDSP 1515
Cdd:COG4172 445 KLLVLDEPTSALDV----SVQAQILDLLRDlqrehgLAYLFISHDLAVVraL-AHRVMVMKDGKVVEqgpteqvFDAP 517
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
667-854 |
8.06e-16 |
|
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: 76.51 E-value: 8.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGSvayvsQVPWIMNGTVKENILFGHrydaefy 746
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK-----DIAKLPLEELRRRIGYVP------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 747 ektikacaltidlailmdgdktlvgekgiSLSGGQKARLSLARAVYARADTYLLDDPLAAVDEH----VARHLIEHvlgp 822
Cdd:cd00267 80 -----------------------------QLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPAsrerLLELLREL---- 126
|
170 180 190
....*....|....*....|....*....|...
9AYC_A 823 ngLLHTKTKVLATNKVS-ALSIADSIALLDNGE 854
Cdd:cd00267 127 --AEEGRTVIIVTHDPElAELAADRVIVLKDGK 157
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
667-854 |
1.18e-15 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 76.46 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHG---------------SVAYVSQVPWIMNG-T 730
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelpplrrRIGMVFQDFALFPHlT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 731 VKENILFGhrydaefyektikacaltidlailmdgdktlvgekgisLSGGQKARLSLARAVYARADTYLLDDPLAAVDEH 810
Cdd:cd03229 93 VLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPI 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
9AYC_A 811 VARHLIEhvlgpngLL------HTKTKVLATNKVS-ALSIADSIALLDNGE 854
Cdd:cd03229 135 TRREVRA-------LLkslqaqLGITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1295-1525 |
1.31e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 79.29 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1295 DIKFNNYSTRYR---PELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAI----NEIGLY 1367
Cdd:PRK13634 2 DITFQKVEHRYQyktPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1368 DLRHKLSIIPQ--DSQVFEGTVRENI--DPIN--QYTDEAIWRA---LELSHLKEHVLSMSNdgldaqlteggGNLSVGQ 1438
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEKDIcfGPMNfgVSEEDAKQKAremIELVGLPEELLARSP-----------FELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1439 RQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKDR--TILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSP 1515
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTP 230
|
250
....*....|
9AYC_A 1516 GQLLSDNKSL 1525
Cdd:PRK13634 231 REIFADPDEL 240
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
668-864 |
1.32e-15 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 80.12 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 668 VALKNINFQAKKGNLTCIVGKVGSGKTALLSCM--L-----GDLF----RVKGFATVHGSVAYVSQVPWI---MngTVKE 733
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIagLedptsGEILiggrDVTDLPPKDRNIAMVFQSYALyphM--TVYE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 734 NILFG---HRYDAEFYEKTIKACALTIDLAILMDgdkTLVGEkgisLSGGQKARLSLARAVYARADTYLLDDPLAAVD-- 808
Cdd:COG3839 95 NIAFPlklRKVPKAEIDRRVREAAELLGLEDLLD---RKPKQ----LSGGQRQRVALGRALVREPKVFLLDEPLSNLDak 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
9AYC_A 809 --EHVARHLIEhvlgpnglLHTKTK---VLAT-NKVSALSIADSIALLDNGEITQQGTYDEI 864
Cdd:COG3839 168 lrVEMRAEIKR--------LHRRLGtttIYVThDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
668-864 |
1.77e-15 |
|
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: 78.45 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 668 VALKNINFQAKKGNLTCIVGKVGSGKTALLSCM-------LGDLF-----------------RVKGFATVHGSVAYVSQV 723
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCInrlieptSGKVLidgqdiaamsrkelrelRRKKISMVFQSFALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 724 pwimngTVKENILFG----HRYDAEFYEKTIKAcaltIDLAILMDGDKTLVGEkgisLSGGQKARLSLARAVYARADTYL 799
Cdd:cd03294 118 ------TVLENVAFGlevqGVPRAEREERAAEA----LELVGLEGWEHKYPDE----LSGGMQQRVGLARALAVDPDILL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 800 LDDPLAAVDEHVARHLIEHVLGPNGLLHtKTKVLATNKVS-ALSIADSIALLDNGEITQQGTYDEI 864
Cdd:cd03294 184 MDEAFSALDPLIRREMQDELLRLQAELQ-KTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
669-864 |
2.32e-15 |
|
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: 81.10 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 669 ALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDL---FRVKGFATVHG-------------SVAYVSQVPWI-MNG-T 730
Cdd:COG1123 21 AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphgGRISGEVLLDGrdllelsealrgrRIGMVFQDPMTqLNPvT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 731 VKENILFGHRYD----AEFYEKTIKACALTidlailmdGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAA 806
Cdd:COG1123 101 VGDQIAEALENLglsrAEARARVLELLEAV--------GLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 807 VDEHVARHLIEHVLGPNGLLHTkTKVLATNKVS-ALSIADSIALLDNGEITQQGTYDEI 864
Cdd:COG1123 173 LDVTTQAEILDLLRELQRERGT-TVLLITHDLGvVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
661-859 |
2.61e-15 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 76.93 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 661 QRKPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALL---SCMLGDLFRVKGFATVHG----------SVAYVSQ----V 723
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLdaiSGRVEGGGTTSGQILFNGqprkpdqfqkCVAYVRQddilL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 724 PWImngTVKENILF-----GHRYDAEFYEKTIKACALTIDLAILMDGDKTLVGekgisLSGGQKARLSLARAVYARADTY 798
Cdd:cd03234 94 PGL---TVRETLTYtailrLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKG-----ISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
9AYC_A 799 LLDDPLAAVDEHVArhliehvlgpNGLLHTKTKVLATNKVSALSIA----------DSIALLDNGEITQQG 859
Cdd:cd03234 166 ILDEPTSGLDSFTA----------LNLVSTLSQLARRNRIVILTIHqprsdlfrlfDRILLLSSGEIVYSG 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1312-1515 |
2.92e-15 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 78.56 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEA---SEGNIVIDNIAINEIGLYDLRH----KLSIIPQDSQ--- 1381
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDPMtsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1382 --VFegTVRENI-DPINQYTD----EAIWRALELshLKEhV-LSMSNDGLDA---QltegggnLSVGQRQLLCLARAMLV 1450
Cdd:COG0444 100 npVM--TVGDQIaEPLRIHGGlskaEARERAIEL--LER-VgLPDPERRLDRyphE-------LSGGMRQRVMIARALAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1451 PSKILVLDQATAAVDVetdkVVQETIRTAFKDR------TILTIAHRLNTI--MdSDRIIVLDNGKVAE-------FDSP 1515
Cdd:COG0444 168 EPKLLIADEPTTALDV----TIQAQILNLLKDLqrelglAILFITHDLGVVaeI-ADRVAVMYAGRIVEegpveelFENP 242
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1312-1521 |
2.96e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 77.50 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQV-FEGTVRE- 1389
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1390 ----------NIDPINQYTDEAIwRALELSHLKehvlsmsndglDAQLTEgggnLSVGQRQLLCLARAmLV-------PS 1452
Cdd:PRK13548 97 vamgraphglSRAEDDALVAAAL-AQVDLAHLA-----------GRDYPQ----LSGGEQQRVQLARV-LAqlwepdgPP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
9AYC_A 1453 KILVLDQATAAVDVETDKVVQETIRTAFKDR--TILTIAHRLN-TIMDSDRIIVLDNGKVAEFDSPGQLLSD 1521
Cdd:PRK13548 160 RWLLLDEPTSALDLAHQHHVLRLARQLAHERglAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLTP 231
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
667-859 |
3.73e-15 |
|
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: 76.14 E-value: 3.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLG-------DLF----RVKGFATVHGSVAYVSQ----VPwimNGTV 731
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGleeptsgRIYiggrDVTDLPPKDRDIAMVFQnyalYP---HMTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 732 KENILFG---HRYDAEFYEKTIKACALTIDLAILMDgdktlvgEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVD 808
Cdd:cd03301 90 YDNIAFGlklRKVPKDEIDERVREVAELLQIEHLLD-------RKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 809 EHVARHL------IEHVLGpngllhtKTKVLAT-NKVSALSIADSIALLDNGEITQQG 859
Cdd:cd03301 163 AKLRVQMraelkrLQQRLG-------TTTIYVThDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1296-1525 |
4.16e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 77.44 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELDL-VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLS 1374
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1375 IIPQ--DSQVFEGTVRENIdpINQYTDEAIWRALELSHLKEHVLSMsnDGLDAQLTEgGGNLSVGQRQLLCLARAMLVPS 1452
Cdd:PRK13642 85 MVFQnpDNQFVGATVEDDV--AFGMENQGIPREEMIKRVDEALLAV--NMLDFKTRE-PARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1453 KILVLDQATAAVD----VETDKVVQEtirtaFKDR---TILTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQLLSDNKSL 1525
Cdd:PRK13642 160 EIIILDESTSMLDptgrQEIMRVIHE-----IKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDM 234
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
670-866 |
4.35e-15 |
|
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: 76.61 E-value: 4.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 670 LKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGS-----------VAYVSQ----VPwimNGTVKEN 734
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQnyalFP---HMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 735 ILFGHR---YDAEFYEKTIKACALTIDLAILMDgdktlvgEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHV 811
Cdd:cd03299 92 IAYGLKkrkVDKKEIERKVLEIAEMLGIDHLLN-------RKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 812 ARHLIEHVlgpnGLLHTKTKVLAT----NKVSALSIADSIALLDNGEITQQGTYDEITK 866
Cdd:cd03299 165 KEKLREEL----KKIRKEFGVTVLhvthDFEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1296-1511 |
4.80e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 78.30 E-value: 4.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELDLV--LKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNI---AINEIGLYDLR 1370
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1371 HKLSIIPQ-----DSQvfegTVRENI-----------DPINQYTDEaiwrALELSHLKEHvlsmsNDGLDAQltegggnL 1434
Cdd:PRK11153 82 RQIGMIFQhfnllSSR----TVFDNValplelagtpkAEIKARVTE----LLELVGLSDK-----ADRYPAQ-------L 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1435 SVGQRQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKDR--TILTIAHRlntiMD-----SDRIIVLDNG 1507
Cdd:PRK11153 142 SGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELglTIVLITHE----MDvvkriCDRVAVIDAG 217
|
....
9AYC_A 1508 KVAE 1511
Cdd:PRK11153 218 RLVE 221
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
668-808 |
5.00e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.13 E-value: 5.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 668 VALKNINFQAKKGNLTCIVGKVGSGKTALLSCM--LGDL---FRVKGFATVHGSVAYVSQV---------------PWIM 727
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLipgFRVEGKVTFHGKNLYAPDVdpvevrrrigmvfqkPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 728 NGTVKENILFGHRYDA------EFYEKTIKAcaltidlAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLD 801
Cdd:PRK14243 104 PKSIYDNIAYGARINGykgdmdELVERSLRQ-------AALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
....*..
9AYC_A 802 DPLAAVD 808
Cdd:PRK14243 177 EPCSALD 183
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
669-864 |
6.60e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 77.88 E-value: 6.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 669 ALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLG----DlfrvKGFATVHG------------SVAYVSQ----VPwimN 728
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGletpD----SGRIVLNGrdlftnlpprerRVGFVFQhyalFP---H 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 729 GTVKENILFGHRyDAEFYEKTIKACALTidlaiLMDgdktLVGEKGIS------LSGGQKARLSLARAVYARADTYLLDD 802
Cdd:COG1118 90 MTVAENIAFGLR-VRPPSKAEIRARVEE-----LLE----LVQLEGLAdrypsqLSGGQRQRVALARALAVEPEVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 803 PLAAVDEHVARHLiEHVLgpnGLLHTKTK---VLAT-NKVSALSIADSIALLDNGEITQQGTYDEI 864
Cdd:COG1118 160 PFGALDAKVRKEL-RRWL---RRLHDELGgttVFVThDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1312-1523 |
6.67e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 76.33 E-value: 6.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINeiGLYDLRHKLSIIPQDSQ----VFEG-- 1385
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITID--TARSLSQQKGLIRQLRQhvgfVFQNfn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1386 -----TVRENI--DPI---NQYTDEAIWRALELshlkehvlsMSNDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKIL 1455
Cdd:PRK11264 96 lfphrTVLENIieGPVivkGEPKEEATARAREL---------LAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1456 VLDQATAAVDVETDKVVQETIRT-AFKDRTILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQLLSDNK 1523
Cdd:PRK11264 167 LFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFADPQ 236
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1313-1518 |
8.74e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 75.97 E-value: 8.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1313 LKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLY-------DLRHKLSIIPQDSQVFEG 1385
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYsprtdtvDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1386 TVRENID---PINQYTDEAIwraleLSHLKEHVLSMSN--DGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQA 1460
Cdd:PRK14239 101 SIYENVVyglRLKGIKDKQV-----LDEAVEKSLKGASiwDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 1461 TAAVDVETDKVVQETIRTAFKDRTILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQL 1518
Cdd:PRK14239 176 TSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQM 234
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1313-1525 |
1.24e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 76.04 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1313 LKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAIN--EIGLYDLRHKLSIIPQ--DSQVFEGTVR 1388
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysRKGLMKLRESVGMVFQdpDNQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1389 ENID--PIN-----QYTDEAIWRALE---LSHLKE---HVLSMsndgldaqltegggnlsvGQRQLLCLARAMLVPSKIL 1455
Cdd:PRK13636 102 QDVSfgAVNlklpeDEVRKRVDNALKrtgIEHLKDkptHCLSF------------------GQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
9AYC_A 1456 VLDQATAAVD----VETDKVVQETIRTAfkDRTILTIAHRLNTI-MDSDRIIVLDNGKVAEFDSPGQLLSDNKSL 1525
Cdd:PRK13636 164 VLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVFAEKEML 236
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
667-853 |
1.24e-14 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 75.51 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHG--------SVAYVSQ----VPWImngTVKEN 734
Cdd:COG1116 24 VTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpDRGVVFQepalLPWL---TVLDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 735 ILFG----HRYDAEFYEKTIKAcaltidLAilmdgdktLVGEKGIS------LSGGQKARLSLARAVYARADTYLLDDPL 804
Cdd:COG1116 101 VALGlelrGVPKAERRERAREL------LE--------LVGLAGFEdayphqLSGGMRQRVAIARALANDPEVLLMDEPF 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
9AYC_A 805 AAVDEHVARHLIEHVLGpnglLHTKTK---VLATNKVS-ALSIADSIALLDNG 853
Cdd:COG1116 167 GALDALTRERLQDELLR----LWQETGktvLFVTHDVDeAVFLADRVVVLSAR 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1296-1522 |
1.34e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 74.79 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELdlvlKHINIHIKPNEKVGIVGRTGAGKSSLtLAL---FrmIEASEGNIVIDNIAINEIGLYDlRhK 1372
Cdd:COG3840 2 LRLDDLTYRYGDFP----LRFDLTIAAGERVAILGPSGAGKSTL-LNLiagF--LPPDSGRILWNGQDLTALPPAE-R-P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1373 LSIIPQDSQVFEG-TVRENI----DPINQYTDEAiwRAlELSHLKEHVlsmsndGLDAQLTEGGGNLSVGQRQLLCLARA 1447
Cdd:COG3840 73 VSMLFQENNLFPHlTVAQNIglglRPGLKLTAEQ--RA-QVEQALERV------GLAGLLDRLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1448 MLVPSKILVLDQATAAVD--------VETDKVVQETirtafkDRTILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQL 1518
Cdd:COG3840 144 LVRKRPILLLDEPFSALDpalrqemlDLVDELCRER------GLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAAL 217
|
....
9AYC_A 1519 LSDN 1522
Cdd:COG3840 218 LDGE 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1296-1521 |
1.53e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 75.13 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELdlVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAIN--EIGLYDLRHKL 1373
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1374 SIIPQDSQVF-EGTVRENI--DPIN---QYTDEAIWRALELshlkehvlsMSNDGLDAQLTEGGGNLSVGQRQLLCLARA 1447
Cdd:PRK09493 80 GMVFQQFYLFpHLTALENVmfGPLRvrgASKEEAEKQAREL---------LAKVGLAERAHHYPSELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 1448 MLVPSKILVLDQATAAVDVETDKVVQETIRT-AFKDRTILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQLLSD 1521
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRHEVLKVMQDlAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
667-864 |
1.68e-14 |
|
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: 74.58 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLScMLGdlfrvkGFAT------------VHGSVAYVSQVPWIM------- 727
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLR-LIA------GFETptsgeilldgkdITNLPPHKRPVNTVFqnyalfp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 728 NGTVKENILFGHRYdAEFYEKTIKA-CALTIDLaILMDGdktLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAA 806
Cdd:cd03300 86 HLTVFENIAFGLRL-KKLPKAEIKErVAEALDL-VQLEG---YANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
9AYC_A 807 VDEHVARHL------IEHVLGpngllhtKTKVLATNKVS-ALSIADSIALLDNGEITQQGTYDEI 864
Cdd:cd03300 161 LDLKLRKDMqlelkrLQKELG-------ITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1296-1525 |
1.81e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 75.50 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYrPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDN--IAINEIGLYDLRHKL 1373
Cdd:PRK13639 2 LETRDLKYSY-PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1374 SIIPQ--DSQVFEGTVRENI--DPINqytdeaiwraLELShlKEHVLSMSNDGLDAQLTEGGGN-----LSVGQRQLLCL 1444
Cdd:PRK13639 81 GIVFQnpDDQLFAPTVEEDVafGPLN----------LGLS--KEEVEKRVKEALKAVGMEGFENkpphhLSGGQKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1445 ARAMLVPSKILVLDQATAAVD-VETDKVVQETIRTAFKDRTILTIAHRLNTI-MDSDRIIVLDNGKVAEFDSPGQLLSDN 1522
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDpMGASQIMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
...
9AYC_A 1523 KSL 1525
Cdd:PRK13639 229 ETI 231
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
659-865 |
2.00e-14 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 74.08 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 659 LWQR-KPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHG------------SVAYVSQ--- 722
Cdd:cd03263 6 LTKTyKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYCPQfda 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 723 VPWIMngTVKENILFGHRYDAEFYEKTIKACALTIDLAILMDGDKTLVGEkgisLSGGQKARLSLARAVYARADTYLLDD 802
Cdd:cd03263 86 LFDEL--TVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRART----LSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 803 PLAAVDeHVARHLIEHVLgpNGLLHTKTKVLAT---NKVSALsiADSIALLDNGEITQQGTYDEIT 865
Cdd:cd03263 160 PTSGLD-PASRRAIWDLI--LEVRKGRSIILTThsmDEAEAL--CDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1296-1509 |
2.06e-14 |
|
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: 73.98 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYrPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINeiGLYD-----LR 1370
Cdd:cd03292 1 IEFINVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS--DLRGraipyLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1371 HKLSIIPQDSQVF-EGTVRENIDPINQYTDE----------AIWRALELSHlKEHVLSMSndgldaqltegggnLSVGQR 1439
Cdd:cd03292 78 RKIGVVFQDFRLLpDRNVYENVAFALEVTGVppreirkrvpAALELVGLSH-KHRALPAE--------------LSGGEQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
9AYC_A 1440 QLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKDRTILTIAHRLNTIMD--SDRIIVLDNGKV 1509
Cdd:cd03292 143 QRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDttRHRVIALERGKL 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
668-864 |
2.16e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 76.68 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 668 VALKNINFQAKKGNLTCIVGKVGSGKTALLScMLGdlfrvkGFATV-HGS-----------------VAYVSQvpwimNG 729
Cdd:COG3842 19 TALDDVSLSIEPGEFVALLGPSGCGKTTLLR-MIA------GFETPdSGRilldgrdvtglppekrnVGMVFQ-----DY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 730 ------TVKENILFG---HRYDAEFYEKTIKACaltidLAIL-MDG-DKTLVGEkgisLSGGQKARLSLARAVYARADTY 798
Cdd:COG3842 87 alfphlTVAENVAFGlrmRGVPKAEIRARVAEL-----LELVgLEGlADRYPHQ----LSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 799 LLDDPLAAVDEHVARHLIEHVLGpnglLHTKTK---VLAT-NKVSALSIADSIALLDNGEITQQGTYDEI 864
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRR----LQRELGitfIYVThDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1312-1511 |
2.35e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 74.56 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIE-----ASEGNIVIDNIAINEIGLYDLRHKLSIIPQ------DS 1380
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQipnpipNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1381 QVFE----GTVRENIDPINQYTDEAIWRALELSHLKEHVlsmsNDGLDAQltegGGNLSVGQRQLLCLARAMLVPSKILV 1456
Cdd:PRK14247 98 SIFEnvalGLKLNRLVKSKKELQERVRWALEKAQLWDEV----KDRLDAP----AGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
9AYC_A 1457 LDQATAAVDVETDKVVQETIRTAFKDRTILTIAH------RLntimdSDRIIVLDNGKVAE 1511
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVE 225
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
668-864 |
2.76e-14 |
|
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: 74.30 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 668 VALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHG-----------SVAYVSQ-VPWIMNGTVKENI 735
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatdvpvqerNVGFVFQhYALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 736 LFGHRY---DAEFYEKTIKACALtiDLAILMDGDKtLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVA 812
Cdd:cd03296 96 AFGLRVkprSERPPEAEIRAKVH--ELLKLVQLDW-LADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
9AYC_A 813 RHLIEHVLGPNGLLHTKTKVLATNKVSALSIADSIALLDNGEITQQGTYDEI 864
Cdd:cd03296 173 KELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1312-1517 |
3.45e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.44 E-value: 3.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIeASEGNIVIDNIAINEIG---LYDLRHKLSIIPQD--SQVfegT 1386
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDpnSSL---N 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1387 VRENIDPINQYTDEAIWRALELSHLKEHVLS-MSNDGLDAQLTEG-GGNLSVGQRQLLCLARAMLVPSKILVLDQATAAV 1464
Cdd:PRK15134 377 PRLNVLQIIEEGLRVHQPTLSAAQREQQVIAvMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1465 dvetDKVVQETIRTAFKDrtiLTIAHRLNTIMDS----------DRIIVLDNGKVAE-------FDSPGQ 1517
Cdd:PRK15134 457 ----DKTVQAQILALLKS---LQQKHQLAYLFIShdlhvvralcHQVIVLRQGEVVEqgdcervFAAPQQ 519
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
311-622 |
3.67e-14 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 74.89 E-value: 3.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 311 MLLAAFFKAIHDVLAFTQPQLLRILIKFVTdynseRQDDHSSLqgfennhpqklpivrgFLIAFAMFLVGFTQT--SVLH 388
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVI-----PAGDLSLL----------------LWIALLLLLLALLRAllSYLR 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 389 QYFLNVFntGMYIKSALTALIYQKSLVLSNEASGLSSTGDIVNLMSVDVQKLQDLTQW-LNLIWSGPFQIIICLYSLYKL 467
Cdd:cd07346 60 RYLAARL--GQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSgLLQLLSDVLTLIGALVILFYL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 468 lgNsmW----VGVIILVIMMPLNSFLMRIQKKLQKSQMKYKDERTRVISEILNNIKSLKLYAWEKPYREKLEEvRNNKEL 543
Cdd:cd07346 138 --N--WkltlVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFRE-ANRDLR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 544 KNLTKLgcyMAVTSFQFNIVPFLVSCCTFAVFVYTEDRALTTDLVFPALTLF----NLLSFPLMIIPMVLNSFIEASVSI 619
Cdd:cd07346 213 DANLRA---ARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGELVAFlaylGMLFGPIQRLANLYNQLQQALASL 289
|
...
9AYC_A 620 GRL 622
Cdd:cd07346 290 ERI 292
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
670-855 |
3.93e-14 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 71.86 E-value: 3.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 670 LKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGS-------------VAYVSQVPWIMNGTVKENIL 736
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGYLPQDDELFSGSIAENIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 737 fghrydaefyektikacaltidlailmdgdktlvgekgislSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARHLI 816
Cdd:cd03246 98 -----------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALN 136
|
170 180 190
....*....|....*....|....*....|....*....
9AYC_A 817 EHVLGPNglLHTKTKVLATNKVSALSIADSIALLDNGEI 855
Cdd:cd03246 137 QAIAALK--AAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
1007-1267 |
4.32e-14 |
|
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: 74.77 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1007 GSNPNAARYLAIY-FALGIGSALATLIQTIVLwVFCTIHASKYLHNLMTNSVLRAPMTFFETTPIGRILNRFSNDIYKVD 1085
Cdd:cd18552 32 EKDLEALLLVPLAiIGLFLLRGLASYLQTYLM-AYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1086 ALLGRTFSQFFVNAVKVTFTITVICATTWQ---FIFIIIPLSVFYIYYQQYYLR--TSRELRRLDSITrspiySHFQETL 1160
Cdd:cd18552 111 NALTSALTVLVRDPLTVIGLLGVLFYLDWKltlIALVVLPLAALPIRRIGKRLRkiSRRSQESMGDLT-----SVLQETL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1161 GGLATVRGYS----QQKRFSHINQCRIDNNM-----SAFYPSINanrwlayrlELIGSIIILGAATLSVFRLKQGTLTAG 1231
Cdd:cd18552 186 SGIRVVKAFGaedyEIKRFRKANERLRRLSMkiaraRALSSPLM---------ELLGAIAIALVLWYGGYQVISGELTPG 256
|
250 260 270
....*....|....*....|....*....|....*.
9AYC_A 1232 MVGLSLSYALQITQTLNWIVRMTVEVETNIVSVERI 1267
Cdd:cd18552 257 EFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
667-872 |
4.76e-14 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 73.48 E-value: 4.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGdLFRV-KGFATVHG----------------SVAYVSQvpwimNG 729
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIG-LLRPdSGEILVDGqditglsekelyelrrRIGMLFQ-----GG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 730 ------TVKENILFGHRYDAEFYEKTIKacaltiDLAILmdgdK-TLVGEKGI------SLSGGQKARLSLARAVYARAD 796
Cdd:COG1127 92 alfdslTVFENVAFPLREHTDLSEAEIR------ELVLE----KlELVGLPGAadkmpsELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 797 TYLLDDPLAAVDEHVARHLIEHVLGPNGLLHTkTKVLATNKV-SALSIADSIALLDNGEITQQGTYDEItKDADSPL 872
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDELIRELRDELGL-TSVVVTHDLdSAFAIADRVAVLADGKIIAEGTPEEL-LASDDPW 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1312-1513 |
6.12e-14 |
|
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: 72.95 E-value: 6.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDN-----IAINeIGL-YDLrhklsiipqdsqvfeg 1385
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvsslLGLG-GGFnPEL---------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1386 TVRENI-----------DPINQYTDEAIwralELSHLKEHvlsmsndgLDAQLteggGNLSVGQRQLLCLARAMLVPSKI 1454
Cdd:cd03220 100 TGRENIylngrllglsrKEIDEKIDEII----EFSELGDF--------IDLPV----KTYSSGMKARLAFAIATALEPDI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
9AYC_A 1455 LVLDQATAAVDVETDKVVQETIRTAFKD-RTILTIAHRLNTIMD-SDRIIVLDNGKVAEFD 1513
Cdd:cd03220 164 LLIDEVLAVGDAAFQEKCQRRLRELLKQgKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
662-859 |
6.48e-14 |
|
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: 72.92 E-value: 6.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 662 RKPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHG----------------SVAYVSQVPw 725
Cdd:cd03257 13 TGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirrkEIQMVFQDP- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 726 iMNG-----TVKENI-----LFGHRYDAEFYEKTIkacaltIDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARA 795
Cdd:cd03257 92 -MSSlnprmTIGEQIaeplrIHGKLSKKEARKEAV------LLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
9AYC_A 796 DTYLLDDPLAAVDEHVARHLIEhvlgpngLLHT------KTKVLATNKVSALS-IADSIALLDNGEITQQG 859
Cdd:cd03257 165 KLLIADEPTSALDVSVQAQILD-------LLKKlqeelgLTLLFITHDLGVVAkIADRVAVMYAGKIVEEG 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
672-859 |
6.58e-14 |
|
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: 72.33 E-value: 6.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 672 NINFQAKkGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGSVAYVSQVPWIM------------------NGTVKE 733
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLppqqrkiglvfqqyalfpHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 734 NILFGHRYDAEfYEKTIKACALTIDLAIlmdgdKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVAR 813
Cdd:cd03297 95 NLAFGLKRKRN-REDRISVDELLDLLGL-----DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
9AYC_A 814 HLIEHVLGPNGLLHTKTKVLATNKVSALSIADSIALLDNGEITQQG 859
Cdd:cd03297 169 QLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1296-1491 |
7.21e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 71.03 E-value: 7.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTrYRPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLtlalFRMI----EASEGNIVIDniaineiglydLRH 1371
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSL----FRALaglwPWGSGRIGMP-----------EGE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1372 KLSIIPQDSQVFEGTVRENIdpinQYTdeaiWralelshlkEHVLSMsndgldaqltegggnlsvGQRQLLCLARAMLVP 1451
Cdd:cd03223 65 DLLFLPQRPYLPLGTLREQL----IYP----W---------DDVLSG------------------GEQQRLAFARLLLHK 109
|
170 180 190 200
....*....|....*....|....*....|....*....|..
9AYC_A 1452 SKILVLDQATAAVDVETdkvvQETIRTAFKDR--TILTIAHR 1491
Cdd:cd03223 110 PKFVFLDEATSALDEES----EDRLYQLLKELgiTVISVGHR 147
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1313-1509 |
8.33e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.83 E-value: 8.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1313 LKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVID---------NIAIneiglydlRHKLSIIPQDSQVF 1383
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkpvrirspRDAI--------ALGIGMVHQHFMLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1384 EG-TVRENI----DPINqytdeaiWRALELSHLKEHVLSMSND-GLDAQLTEGGGNLSVGQRQ----LLCLARAmlvpSK 1453
Cdd:COG3845 93 PNlTVAENIvlglEPTK-------GGRLDRKAARARIRELSERyGLDVDPDAKVEDLSVGEQQrveiLKALYRG----AR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
9AYC_A 1454 ILVLDQATAavdV----ETDKVVqETIRtAFKD--RTILTIAHRLNTIMD-SDRIIVLDNGKV 1509
Cdd:COG3845 162 ILILDEPTA---VltpqEADELF-EILR-RLAAegKSIIFITHKLREVMAiADRVTVLRRGKV 219
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
990-1267 |
8.37e-14 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 74.09 E-value: 8.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 990 VMGNVWLKHWSEVNSRYGSNPNAARYLA--IYFALGIGSALATLIQTIVL-----WVFCTIHASKYLHnlmtnsVLRAPM 1062
Cdd:cd18564 29 VLGDKPLPGLLGLAPLLGPDPLALLLLAaaALVGIALLRGLASYAGTYLTalvgqRVVLDLRRDLFAH------LQRLSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1063 TFFETTPIGRILNRFSNDIYKVDALLGRTFSQFFVNAVKVTFTITVICATTWQF---IFIIIPLSVFYIYYqqYYLRT-- 1137
Cdd:cd18564 103 SFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLaliALAVAPLLLLAARR--FSRRIke 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1138 -SRELRRLDSItrspIYSHFQETLGGLATVRGYSQQ----KRFSHINQCRIDNNMSAfypsinanRWLAYRLELIGSIII 1212
Cdd:cd18564 181 aSREQRRREGA----LASVAQESLSAIRVVQAFGREeheeRRFARENRKSLRAGLRA--------ARLQALLSPVVDVLV 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1213 lGAATLSV-----FRLKQGTLTAGMVGLSLSYALQITQTLNWIVRMTVEVETNIVSVERI 1267
Cdd:cd18564 249 -AVGTALVlwfgaWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
661-859 |
9.74e-14 |
|
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: 72.18 E-value: 9.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 661 QRKPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGSVAYVSQVPWIMNG--TVKENILFG 738
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGGGFNPelTGRENIYLN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 739 HR-------YDAEFYEKTIKACALT--IDLAIlmdgdKTlvgekgisLSGGQKARLSLARAVYARADTYLLDDPLAAVDE 809
Cdd:cd03220 109 GRllglsrkEIDEKIDEIIEFSELGdfIDLPV-----KT--------YSSGMKARLAFAIATALEPDILLIDEVLAVGDA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
9AYC_A 810 H----VARHLIEHVlgpnglLHTKTKVLATNKVSAL-SIADSIALLDNGEITQQG 859
Cdd:cd03220 176 AfqekCQRRLRELL------KQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
668-819 |
1.06e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 71.11 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 668 VALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHG--SVAYVSQ---VPWIMNGTVKENI---LFGH 739
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQrseVPDSLPLTVRDLVamgRWAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 740 -----RYDAEFYEKTIKACAlTIDLAILmdgDKTLVGEkgisLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARH 814
Cdd:NF040873 86 rglwrRLTRDDRAAVDDALE-RVGLADL---AGRQLGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
|
....*
9AYC_A 815 LIEHV 819
Cdd:NF040873 158 IIALL 162
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
660-855 |
1.23e-13 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 71.75 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 660 WQRKPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHG-----------------SVAYVSQ 722
Cdd:cd03255 10 YGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdisklsekelaafrrrHIGFVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 723 ----VPwimNGTVKENILFGHRYDAEFYeKTIKACALT----IDLAILMDgdkTLVGEkgisLSGGQKARLSLARAVYAR 794
Cdd:cd03255 90 sfnlLP---DLTALENVELPLLLAGVPK-KERRERAEEllerVGLGDRLN---HYPSE----LSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
9AYC_A 795 ADTYLLDDPLAAVDEHVARHLIEHVLGPNGLLHTkTKVLATNKVSALSIADSIALLDNGEI 855
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEAGT-TIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
670-819 |
1.43e-13 |
|
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: 71.36 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 670 LKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKG------------FATVHGSVAYVSQVPWIMNG-TVKENIL 736
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGevlwngepirdaREDYRRRLAYLGHADGLKPElTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 737 F-----GHRYDAEfyekTIKACALTIDLAILMDgdkTLVGEkgisLSGGQKARLSLARAVYARADTYLLDDPLAAVDEH- 810
Cdd:COG4133 98 FwaalyGLRADRE----AIDEALEAVGLAGLAD---LPVRQ----LSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAg 166
|
170
....*....|..
9AYC_A 811 ---VARHLIEHV 819
Cdd:COG4133 167 valLAELIAAHL 178
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1296-1495 |
1.62e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 72.38 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYrpELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEAS-----EGNIVIDNIAINE--IGLYD 1368
Cdd:PRK14258 8 IKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYErrVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1369 LRHKLSIIPQDSQVFEGTVRENIdpinQYTDEAI-WR-ALELSHLKEHVLSMSN--DGLDAQLTEGGGNLSVGQRQLLCL 1444
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNV----AYGVKIVgWRpKLEIDDIVESALKDADlwDEIKHKIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
9AYC_A 1445 ARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAF--KDRTILTIAHRLNTI 1495
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQV 214
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1312-1521 |
1.75e-13 |
|
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: 71.81 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLtlalFRMI----EASEGNIVIDNIAINEIGLYDlRHKLSII--PQDSQVFEG 1385
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTT----FYMIvglvKPDSGKILLDGQDITKLPMHK-RARLGIGylPQEASIFRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1386 -TVRENIDPINQYTDEAIWralELSHLKEHVLSmsndglDAQLTE----GGGNLSVGQRQLLCLARAMLVPSKILVLDQA 1460
Cdd:cd03218 90 lTVEENILAVLEIRGLSKK---EREEKLEELLE------EFHITHlrksKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
9AYC_A 1461 TAAVDVETDKVVQETIRTaFKDRTI---LTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQLLSD 1521
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKI-LKDRGIgvlITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1312-1524 |
1.84e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 72.00 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIA------INEIGLYDLRHKLSIIPQDSQVFEG 1385
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlyfgkdIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1386 -TVRENID-PINQY---TDEAIWRALELSHLKEHVLSMSNDGLDAQLTEgggnLSVGQRQLLCLARAMLVPSKILVLDQA 1460
Cdd:PRK14246 105 lSIYDNIAyPLKSHgikEKREIKKIVEECLRKVGLWKEVYDRLNSPASQ----LSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
9AYC_A 1461 TAAVDVETDKVVQETIRTAFKDRTILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQLLSDNKS 1524
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1313-1507 |
1.92e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.82 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1313 LKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEiglydLRHKLS------IIPQD-SQVFEG 1385
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNK-----LDHKLAaqlgigIIYQElSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1386 TVRENIdPINQYTDEAIW--RALELSHLKEHVLSMSND-GLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATA 1462
Cdd:PRK09700 96 TVLENL-YIGRHLTKKVCgvNIIDWREMRVRAAMMLLRvGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
9AYC_A 1463 AV-DVETDKVVQETIRTAFKDRTILTIAHRLNTIMD-SDRIIVLDNG 1507
Cdd:PRK09700 175 SLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1312-1527 |
1.93e-13 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 72.04 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNividNIAI--NEIG---LYDLRHKLSII-PQDSQVFEG 1385
Cdd:COG1119 18 ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGN----DVRLfgERRGgedVWELRKRIGLVsPALQLRFPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1386 --TVRE--------NIDPINQYTDEAIWRA------LELSHLKEHVLsmsndgldaqlteggGNLSVGQRQLLCLARAML 1449
Cdd:COG1119 94 deTVLDvvlsgffdSIGLYREPTDEQRERArellelLGLAHLADRPF---------------GTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1450 VPSKILVLDQATAAVDVETDKVVQETIRT--AFKDRTILTIAHRLNTIMDS-DRIIVLDNGKVAEFDSPGQLL-SDNKSL 1525
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVLtSENLSE 238
|
..
9AYC_A 1526 FY 1527
Cdd:COG1119 239 AF 240
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1296-1526 |
1.99e-13 |
|
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: 71.60 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYR--PELDlvlkHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNiaineiglydlRHKL 1373
Cdd:cd03296 3 IEVRNVSKRFGdfVALD----DVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG-----------EDAT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1374 SIIPQDSQ---VFEG-------TVRENI------DPINQYTDEAIWRA-----LELSHLkehvlsmsnDGLDAQLTEggg 1432
Cdd:cd03296 68 DVPVQERNvgfVFQHyalfrhmTVFDNVafglrvKPRSERPPEAEIRAkvhelLKLVQL---------DWLADRYPA--- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1433 NLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTaFKDRTILT---IAHRLNTIMD-SDRIIVLDNGK 1508
Cdd:cd03296 136 QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRR-LHDELHVTtvfVTHDQEEALEvADRVVVMNKGR 214
|
250
....*....|....*...
9AYC_A 1509 VAEFDSPGQLLSDNKSLF 1526
Cdd:cd03296 215 IEQVGTPDEVYDHPASPF 232
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1296-1526 |
2.20e-13 |
|
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: 71.50 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYrpELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLtlalFRMI----EASEGNIVIDNIAINEIGLYdlRH 1371
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLIagfeTPTSGEILLDGKDITNLPPH--KR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1372 KLSIIPQDSQVFEG-TVRENI--------DPINQyTDEAIWRALELSHLKEHVLSMSNDgldaqltegggnLSVGQRQLL 1442
Cdd:cd03300 73 PVNTVFQNYALFPHlTVFENIafglrlkkLPKAE-IKERVAEALDLVQLEGYANRKPSQ------------LSGGQQQRV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1443 CLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKDR--TILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQLL 1519
Cdd:cd03300 140 AIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEIY 219
|
....*..
9AYC_A 1520 SDNKSLF 1526
Cdd:cd03300 220 EEPANRF 226
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
646-864 |
2.93e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 74.37 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 646 GDVAInigDDATFLWQRKpeyKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKG-------------FAT 712
Cdd:PRK10790 339 GRIDI---DNVSFAYRDD---NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGeirldgrplsslsHSV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 713 VHGSVAYVSQVPWIMNGTVKENILFGHrydaEFYEKTIKACALTIDLAILM----DGDKTLVGEKGISLSGGQKARLSLA 788
Cdd:PRK10790 413 LRQGVAMVQQDPVVLADTFLANVTLGR----DISEEQVWQALETVQLAELArslpDGLYTPLGEQGNNLSVGQKQLLALA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 789 RAVYARADTYLLDDPLAAVD---EHVARHLIEHVLGpngllHTKTKVLAtNKVSALSIADSIALLDNGEITQQGTYDEI 864
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDsgtEQAIQQALAAVRE-----HTTLVVIA-HRLSTIVEADTILVLHRGQAVEQGTHQQL 561
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1296-1525 |
4.11e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 71.73 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYR---PELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAIN----EIGLYD 1368
Cdd:PRK13646 3 IRFDNVSYTYQkgtPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1369 LRHKLSIIPQ--DSQVFEGTVRENID--------PINQYTDEAIWRALELShLKEHVLSMSNdgldaqlteggGNLSVGQ 1438
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIfgpknfkmNLDEVKNYAHRLLMDLG-FSRDVMSQSP-----------FQMSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1439 RQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRT--AFKDRTILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSP 1515
Cdd:PRK13646 151 MRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSP 230
|
250
....*....|
9AYC_A 1516 GQLLSDNKSL 1525
Cdd:PRK13646 231 KELFKDKKKL 240
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1312-1520 |
4.61e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.95 E-value: 4.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQV-FEGTVREN 1390
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1391 I-----------DPINQYTDEAIWRALELSHLKEHVlsmsndglDAQLTEgggnLSVGQRQLLCLARAMLVPSKILVLDQ 1459
Cdd:PRK09536 98 VemgrtphrsrfDTWTETDRAAVERAMERTGVAQFA--------DRPVTS----LSGGERQRVLLARALAQATPVLLLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 1460 ATAAVD----VETDKVVQETIRTafkDRTILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQLLS 1520
Cdd:PRK09536 166 PTASLDinhqVRTLELVRRLVDD---GKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLT 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1312-1509 |
4.94e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.56 E-value: 4.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSltlaLFRMI----EASEGNIVIDNiaineiglyDLRhkLSIIPQDSQVFEG-T 1386
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKST----LLKILagelEPDSGEVSIPK---------GLR--IGYLPQEPPLDDDlT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1387 VRENI--------DPINQY---------TDEAIWRALELSHLKEH------------VLS---MSNDGLDAQLTEgggnL 1434
Cdd:COG0488 78 VLDTVldgdaelrALEAELeeleaklaePDEDLERLAELQEEFEAlggweaearaeeILSglgFPEEDLDRPVSE----L 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1435 SVGQRQLLCLARAMLVPSKILVLDQATAAVDVETdkvVQ--ETIRTAFKdRTILTIAH-R--LNTImdSDRIIVLDNGKV 1509
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwlEEFLKNYP-GTVLVVSHdRyfLDRV--ATRILELDRGKL 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1309-1521 |
7.83e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 72.37 E-value: 7.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1309 LDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRH----KLSIIPQDSQVF- 1383
Cdd:PRK10070 40 LSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMp 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1384 EGTVREN----IDPINQYTDEAIWRALElshlkehvlSMSNDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQ 1459
Cdd:PRK10070 120 HMTVLDNtafgMELAGINAEERREKALD---------ALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
9AYC_A 1460 ATAAVD--VETDKVVQETIRTAFKDRTILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQLLSD 1521
Cdd:PRK10070 191 AFSALDplIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1312-1515 |
9.70e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 69.73 E-value: 9.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVID-NIA-INEIGLydlrhklsiipqdsqVFEG--TV 1387
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNgRVSaLLELGA---------------GFHPelTG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1388 RENI-----------DPINQYTDEAIwralELSHLKEHvlsmsndgLDAQLteggGNLSVGQRQLLCLARAMLVPSKILV 1456
Cdd:COG1134 106 RENIylngrllglsrKEIDEKFDEIV----EFAELGDF--------IDQPV----KTYSSGMRARLAFAVATAVDPDILL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
9AYC_A 1457 LDQATAAVDVETDKVVQETIRtAFKD--RTILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSP 1515
Cdd:COG1134 170 VDEVLAVGDAAFQKKCLARIR-ELREsgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDP 230
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1296-1535 |
1.25e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.15 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELDlVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSI 1375
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1376 IPQ--DSQVFEGTVRENI--DPINqytdeaiwraLELShlKEHVLSMSNDGLDA----QLTEGGG-NLSVGQRQLLCLAR 1446
Cdd:PRK13647 84 VFQdpDDQVFSSTVWDDVafGPVN----------MGLD--KDEVERRVEEALKAvrmwDFRDKPPyHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1447 AMLVPSKILVLDQATAAVDVETDKVVQETI-RTAFKDRTILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPgQLLSDNKs 1524
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILdRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDK-SLLTDED- 229
|
250
....*....|.
9AYC_A 1525 lfysLCMEAGL 1535
Cdd:PRK13647 230 ----IVEQAGL 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1312-1520 |
1.34e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 72.14 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRM--IEASEGNIV---------------------------------I 1356
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtlepeeV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1357 DNIAINEIGLYDLRHKLSIIPQDSQVFEG--TVRENI----DPINQYTDEAIWRALELshlkehvLSMSNdgLDAQLTEG 1430
Cdd:TIGR03269 95 DFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNVlealEEIGYEGKEAVGRAVDL-------IEMVQ--LSHRITHI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1431 GGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKDRTILTI--AHRLNTIMD-SDRIIVLDNG 1507
Cdd:TIGR03269 166 ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVltSHWPEVIEDlSDKAIWLENG 245
|
250
....*....|...
9AYC_A 1508 KVAEFDSPGQLLS 1520
Cdd:TIGR03269 246 EIKEEGTPDEVVA 258
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1296-1511 |
1.39e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 71.02 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELdlVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYdLRHKLSI 1375
Cdd:PRK13536 42 IDLAGVSKSYGDKA--VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARL-ARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1376 IPQ-DSQVFEGTVRENIDPINQY-------TDEAIWRALELSHLKEHVlsmsndglDAQLTEgggnLSVGQRQLLCLARA 1447
Cdd:PRK13536 119 VPQfDNLDLEFTVRENLLVFGRYfgmstreIEAVIPSLLEFARLESKA--------DARVSD----LSGGMKRRLTLARA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
9AYC_A 1448 MLVPSKILVLDQATAAVDVETDKVVQETIRTAF-KDRTILTIAHrlntIMDS-----DRIIVLDNG-KVAE 1511
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTH----FMEEaerlcDRLCVLEAGrKIAE 253
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
668-867 |
1.57e-12 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 69.00 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 668 VALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLG--------------DLFRVKGFATVHGSVAYVSQVPWIMNG-TVK 732
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGflrptsgsvlfdgeDITGLPPHEIARLGIGRTFQIPRLFPElTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 733 ENILFGHRYD---------AEFYEKTIKACALTI-DLAILMDGDKTLVGEkgisLSGGQKARLSLARAVYARADTYLLDD 802
Cdd:cd03219 94 ENVMVAAQARtgsglllarARREEREARERAEELlERVGLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 803 PLAAVD-----------EHVARH-----LIEHVLGpngllhtktkvlatnkvSALSIADSIALLDNGEITQQGTYDEITK 866
Cdd:cd03219 170 PAAGLNpeeteelaeliRELRERgitvlLVEHDMD-----------------VVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
.
9AYC_A 867 D 867
Cdd:cd03219 233 N 233
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1312-1523 |
1.64e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 69.74 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEG-----NIVIDNIAI-NEIGLYDLRHKLSIIPQDSQVFEG 1385
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1386 TVRENIDP---INQYTDEAIWRALELSHLKEHVLSmsnDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATA 1462
Cdd:PRK14271 116 SIMDNVLAgvrAHKLVPRKEFRGVAQARLTEVGLW---DAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
9AYC_A 1463 AVDVETDKVVQETIRTAFKDRTILTIAHRL-NTIMDSDRIIVLDNGKVAEFDSPGQLLSDNK 1523
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSSPK 254
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1311-1513 |
1.78e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.63 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1311 LVLKHINIHIKPNEKVGIVGRTGAGKSSltlaLFRMI----EASEGNIVI-DNIainEIGLYDlrhklsiipQDSQVFEG 1385
Cdd:COG0488 329 TLLDDLSLRIDRGDRIGLIGPNGAGKST----LLKLLagelEPDSGTVKLgETV---KIGYFD---------QHQEELDP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1386 --TVRENIDPINQYTDEAiwralelshlkeHVLSMSNDGL---DAQLTEgGGNLSVGQRQLLCLARAMLVPSKILVLDQA 1460
Cdd:COG0488 393 dkTVLDELRDGAPGGTEQ------------EVRGYLGRFLfsgDDAFKP-VGVLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
9AYC_A 1461 TAAVDVETdkvvqetiRTAFKDR------TILTIAH-R--LNTImdSDRIIVLDNGKVAEFD 1513
Cdd:COG0488 460 TNHLDIET--------LEALEEAlddfpgTVLLVSHdRyfLDRV--ATRILEFEDGGVREYP 511
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1315-1524 |
1.85e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.46 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1315 HINIHIKPNEKVGIVGRTGAGKSSLtLALFR-MIEASEGNIVIDNiaINEIGLYDLRHKLSIIPQDSQVFEG-TVRENI- 1391
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTL-LNLIAgFLTPASGSLTLNG--QDHTTTPPSRRPVSMLFQENNLFSHlTVAQNIg 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1392 ---DPinqytdeaiwrALELSHLKEHVLS--MSNDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVD- 1465
Cdd:PRK10771 94 lglNP-----------GLKLNAAQREKLHaiARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDp 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 1466 ---VETDKVVQETIRTafKDRTILTIAHRLNtimDSDRI----IVLDNGKVAEFDSPGQLLSDNKS 1524
Cdd:PRK10771 163 alrQEMLTLVSQVCQE--RQLTLLMVSHSLE---DAARIaprsLVVADGRIAWDGPTDELLSGKAS 223
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1312-1521 |
1.90e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 70.26 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYD----------------LRHKLSI 1375
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHelitnpyskkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1376 IPQ--DSQVFEGTVRENI--DPIN--QYTDEAIWRA---LELSHLKEHVLSMSNDGLdaqltegggnlSVGQRQLLCLAR 1446
Cdd:PRK13631 121 VFQfpEYQLFKDTIEKDImfGPVAlgVKKSEAKKLAkfyLNKMGLDDSYLERSPFGL-----------SGGQKRRVAIAG 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 1447 AMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKD-RTILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQLLSD 1521
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANnKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTD 266
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
669-867 |
2.29e-12 |
|
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: 68.23 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 669 ALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLG--------------DLFRVKGFATVHGSVAYVSQVPWIM-NGTVKE 733
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGllpprsgsirfdgrDITGLPPHERARAGIGYVPEGRRIFpELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 734 NILFG--HRYDAEFYEKTIKACALtidLAILMDGDKTLVGekgiSLSGGQKARLSLARAVYARADTYLLDDP---LA-AV 807
Cdd:cd03224 95 NLLLGayARRRAKRKARLERVYEL---FPRLKERRKQLAG----TLSGGEQQMLAIARALMSRPKLLLLDEPsegLApKI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
9AYC_A 808 DEHVARHLIEhvlgpngLLHTKTKVLAT--NKVSALSIADSIALLDNGEITQQGTYDEITKD 867
Cdd:cd03224 168 VEEIFEAIRE-------LRDEGVTILLVeqNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1312-1510 |
2.44e-12 |
|
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: 67.19 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSL--TLALFRMIEASEGNIVIDNIainEIGLYDLRHKLSIIPQDSQVFEG-TVR 1388
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLlnALAGRRTGLGVSGEVLINGR---PLDKRSFRKIIGYVPQDDILHPTlTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1389 enidpinqytdEAIWRALELShlkehvlsmsndgldaqltegggNLSVGQRQLLCLARAMLV-PSkILVLDQATAAVDVE 1467
Cdd:cd03213 101 -----------ETLMFAAKLR-----------------------GLSGGERKRVSIALELVSnPS-LLFLDEPTSGLDSS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
9AYC_A 1468 TDKVVQETIRT-AFKDRTILTIAHRLNTIMDS--DRIIVLDNGKVA 1510
Cdd:cd03213 146 SALQVMSLLRRlADTGRTIICSIHQPSSEIFElfDKLLLLSQGRVI 191
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
652-885 |
2.48e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 69.27 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 652 IGDDATFLWQRKPEYKV-ALKNINFQAKKGNLTCIVGKVGSGKTALL------------SCMLGD------LFRVKGFAT 712
Cdd:PRK13645 8 ILDNVSYTYAKKTPFEFkALNNTSLTFKKNKVTCVIGTTGSGKSTMIqltngliisetgQTIVGDyaipanLKKIKEVKR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 713 VHGSVAYVSQVP--WIMNGTVKENILFGHRYDAEFYEKTIKACALTIDLAILmdgDKTLVGEKGISLSGGQKARLSLARA 790
Cdd:PRK13645 88 LRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQL---PEDYVKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 791 VYARADTYLLDDPLAAVDEHVARHLIEHVLGPNGLLHTKTKVLATNKVSALSIADSIALLDNGEITQQGTYDEI------ 864
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIfsnqel 244
|
250 260
....*....|....*....|....
9AYC_A 865 -TK-DADSP-LWKLLnnYGKKNNG 885
Cdd:PRK13645 245 lTKiEIDPPkLYQLM--YKLKNKG 266
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1296-1521 |
2.74e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 68.37 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELdlVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYD-LRHKLS 1374
Cdd:PRK11614 6 LSFDKVSAHYGKIQ--ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1375 IIPQDSQVFEG-TVRENIDPINQYTD-----EAIWRALEL-SHLKEhvlsmsndgldaQLTEGGGNLSVGQRQLLCLARA 1447
Cdd:PRK11614 84 IVPEGRRVFSRmTVEENLAMGGFFAErdqfqERIKWVYELfPRLHE------------RRIQRAGTMSGGEQQMLAIGRA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 1448 MLVPSKILVLDQATAAVdveTDKVVQETIRTAFKDR----TILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQLLSD 1521
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGL---APIIIQQIFDTIEQLReqgmTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALLAN 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1310-1478 |
3.07e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.59 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1310 DLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSiiPQDSQVFEGTVRE 1389
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1390 NID---PINQYTDEAIWRALE---LSHLkEHVLsmsndgldaqltegGGNLSVGQRQLLCLARAMLVPSKILVLDQATAA 1463
Cdd:PRK13539 93 NLEfwaAFLGGEELDIAAALEavgLAPL-AHLP--------------FGYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170
....*....|....*
9AYC_A 1464 VDVETDKVVQETIRT 1478
Cdd:PRK13539 158 LDAAAVALFAELIRA 172
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
668-864 |
3.70e-12 |
|
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: 67.39 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 668 VALKNINFQAKKGNLTCIVGKVGSGKTALLScMLGDLFRV-KGFATVHG------------SVAYVSQVPWIMNG-TVKE 733
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIK-MLTTLLKPtSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGWE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 734 NI-LFGHRYDAEFYEKTIKAcALTIDLAILMDGDKTLVGekgiSLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVA 812
Cdd:cd03265 93 NLyIHARLYGVPGAERRERI-DELLDFVGLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
9AYC_A 813 RHLIEHVLGPNGlLHTKTKVLATNKV-SALSIADSIALLDNGEITQQGTYDEI 864
Cdd:cd03265 168 AHVWEYIEKLKE-EFGMTILLTTHYMeEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
670-856 |
4.50e-12 |
|
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: 66.90 E-value: 4.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 670 LKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHG----------SVAYVSQVP--WIMNGTVKENILF 737
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQDVdyQLFTDSVREELLL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 738 GHRYDAEFYEKTikACAL-TIDLAILMDgdktlvgEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVD----EHVA 812
Cdd:cd03226 96 GLKELDAGNEQA--ETVLkDLDLYALKE-------RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDyknmERVG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
9AYC_A 813 RhLIEHVLGpngllHTKTKVLATNKVS-ALSIADSIALLDNGEIT 856
Cdd:cd03226 167 E-LIRELAA-----QGKAVIVITHDYEfLAKVCDRVLLLANGAIV 205
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
664-868 |
5.13e-12 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 67.59 E-value: 5.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 664 PEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGS----------------VAYVSQ-VPWI 726
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrrqIGMIFQqFNLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 727 MNGTVKENILFGhRYDAE---------FYEKTIKACALTIDLAILMDGDKTLVGEkgisLSGGQKARLSLARAVYARADT 797
Cdd:cd03256 91 ERLSVLENVLSG-RLGRRstwrslfglFPKEEKQRALAALERVGLLDKAYQRADQ----LSGGQQQRVAIARALMQQPKL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
9AYC_A 798 YLLDDPLAAVDEHVARHLIEHVLGPNgLLHTKTKVLATNKVS-ALSIADSIALLDNGEITQQGTYDEITKDA 868
Cdd:cd03256 166 ILADEPVASLDPASSRQVMDLLKRIN-REEGITVIVSLHQVDlAREYADRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
662-876 |
6.15e-12 |
|
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: 69.93 E-value: 6.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 662 RKPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLG--------------DLFRVKG--FATVHGSVAYVSQ--- 722
Cdd:COG1123 273 RGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGllrptsgsilfdgkDLTKLSRrsLRELRRRVQMVFQdpy 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 723 ---VPWImngTVKENILFGHRYDAEFYEKTIKACALTidlaiLMDgdktLVG-EKGI------SLSGGQKARLSLARAVY 792
Cdd:COG1123 353 sslNPRM---TVGDIIAEPLRLHGLLSRAERRERVAE-----LLE----RVGlPPDLadryphELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 793 ARADTYLLDDPLAAVDEHVARHLIEHVLGpnglLHTKTKV--------LATnkvsALSIADSIALLDNGEITQQGTYDEI 864
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRD----LQRELGLtylfishdLAV----VRYIADRVAVMYDGRIVEDGPTEEV 492
|
250
....*....|..
9AYC_A 865 TKDADSPLWKLL 876
Cdd:COG1123 493 FANPQHPYTRAL 504
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
654-859 |
7.55e-12 |
|
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: 66.36 E-value: 7.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 654 DDATFLWQRKPeykvalKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHG---SVAYVSQVPWIMngT 730
Cdd:cd03298 4 DKIRFSYGEQP------MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvTAAPPADRPVSM--L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 731 VKENILFGH---------------RYDAEfYEKTIKACALTIDLAILMdgdKTLVGEkgisLSGGQKARLSLARAVYARA 795
Cdd:cd03298 76 FQENNLFAHltveqnvglglspglKLTAE-DRQAIEVALARVGLAGLE---KRLPGE----LSGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 796 DTYLLDDPLAAVDEHVARHLIEHVLGpnglLHTKTK---VLATNKVS-ALSIADSIALLDNGEITQQG 859
Cdd:cd03298 148 PVLLLDEPFAALDPALRAEMLDLVLD----LHAETKmtvLMVTHQPEdAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
1014-1267 |
7.83e-12 |
|
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: 67.88 E-value: 7.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1014 RYLAIYFALGIGSALATLIQTIVL-WVfctihASKYLHNL---MTNSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLG 1089
Cdd:cd18545 41 IIALLFLALNLVNWVASRLRIYLMaKV-----GQRILYDLrqdLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1090 RTFSQFFVNAVKVTFTITVICATTWQF---IFIIIPLSVFYIYYQQYYLRTS-RELRRldsiTRSPIYSHFQETLGGLAT 1165
Cdd:cd18545 116 NGLINLIPDLLTLVGIVIIMFSLNVRLalvTLAVLPLLVLVVFLLRRRARKAwQRVRK----KISNLNAYLHESISGIRV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1166 VRGYSQQK----RFSHINQCRIDNNMSA------FYPSINAnrwlayrLELIGSIIILGaatLSVFRLKQGTLTAGMVGL 1235
Cdd:cd18545 192 IQSFAREDeneeIFDELNRENRKANMRAvrlnalFWPLVEL-------ISALGTALVYW---YGGKLVLGGAITVGVLVA 261
|
250 260 270
....*....|....*....|....*....|..
9AYC_A 1236 SLSYALQITQTLNWIVRMTVEVETNIVSVERI 1267
Cdd:cd18545 262 FIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1311-1492 |
8.44e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 67.50 E-value: 8.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1311 LVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYD-------LRHKLSIIPQDSQVF 1383
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLYApdvdpveVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1384 EGTVRENID---PINQYT---DEAIWRALELSHLKEHVlsmsndglDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVL 1457
Cdd:PRK14243 104 PKSIYDNIAygaRINGYKgdmDELVERSLRQAALWDEV--------KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190
....*....|....*....|....*....|....*
9AYC_A 1458 DQATAAVDVETDKVVQETIRTAFKDRTILTIAHRL 1492
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1312-1490 |
1.29e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 66.79 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEAS-----EGNIVI--DNIAINEIGLYDLRHKLSIIPQDSQVFE 1384
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLfgRNIYSPDVDPIEVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1385 G-TVRENIdPINQYTDEAIWRALELSHLKEHVLSMSN--DGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQAT 1461
Cdd:PRK14267 99 HlTIYDNV-AIGVKLNGLVKSKKELDERVEWALKKAAlwDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180
....*....|....*....|....*....
9AYC_A 1462 AAVDVETDKVVQETIRTAFKDRTILTIAH 1490
Cdd:PRK14267 178 ANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1310-1467 |
1.29e-11 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 65.46 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1310 DLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQVFEGTVRE 1389
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1390 NID---PINQYTDEAIWRALE---LSHLkEHVLSmsndgldaqlteggGNLSVGQRQLLCLARAMLVPSKILVLDQATAA 1463
Cdd:TIGR01189 93 NLHfwaAIHGGAQRTIEDALAavgLTGF-EDLPA--------------AQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
....
9AYC_A 1464 VDVE 1467
Cdd:TIGR01189 158 LDKA 161
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1312-1521 |
1.69e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 66.63 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEI---GLYDLRHKLSIIPQDSQVF---EG 1385
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSISAvnpRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1386 TVRENID-PINQYTD----EAIWRALELSHLKEHVLSMSnDGLDAQltegggnLSVGQRQLLCLARAMLVPSKILVLDQA 1460
Cdd:PRK10419 107 TVREIIRePLRHLLSldkaERLARASEMLRAVDLDDSVL-DKRPPQ-------LSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 1461 TAAVD-------VETDKVVQETIRTAFkdrtiLTIAHRLNTIMD-SDRIIVLDNGKVAE---------FDSP-GQLLSD 1521
Cdd:PRK10419 179 VSNLDlvlqagvIRLLKKLQQQFGTAC-----LFITHDLRLVERfCQRVMVMDNGQIVEtqpvgdkltFSSPaGRVLQN 252
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
667-808 |
1.74e-11 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 66.42 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGSV--------AYVSQ----VPWImngTVKEN 734
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVFQkdalLPWL---NVLDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 735 ILFGHRYdaefyEKTIKACALTIDLAILmdgdkTLVGEKGI------SLSGGQKARLSLARAVYARADTYLLDDPLAAVD 808
Cdd:COG4525 97 VAFGLRL-----RGVPKAERRARAEELL-----ALVGLADFarrriwQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1312-1524 |
1.83e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.15 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAIN-------EIGLYD------LRHKLSIIPQ 1378
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLKVADknqlrlLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1379 DSQVFEG-TVRENIdpinqytDEAIWRALELSHLKEH---VLSMSNDGLD-AQLTEGGGNLSVGQRQLLCLARAMLVPSK 1453
Cdd:PRK10619 100 HFNLWSHmTVLENV-------MEAPIQVLGLSKQEAReraVKYLAKVGIDeRAQGKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 1454 ILVLDQATAAVDVEtdkVVQETIRT----AFKDRTILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQLLSDNKS 1524
Cdd:PRK10619 173 VLLFDEPTSALDPE---LVGEVLRImqqlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1010-1267 |
1.88e-11 |
|
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: 66.76 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1010 PNAARYLAIYFALGIgsALATLIQTIVLWVFCTI------HASKYLHNLMTNSVLRAPMTFFETTPIGRILNRFSNDIYK 1083
Cdd:cd18563 35 PGGNTSLLLLLVLGL--AGAYVLSALLGILRGRLlarlgeRITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1084 VDALLGRTFSQFFVNAVKVTFTITVICATTWQ---FIFIIIPLSVFYIYYQQYYLRT--SRELRRLDSITrspiySHFQE 1158
Cdd:cd18563 113 LQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKlalLVLIPVPLVVWGSYFFWKKIRRlfHRQWRRWSRLN-----SVLND 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1159 TLGGLATVRGYSQQK----RFSHINQ------CRIDNNMSAFYPSINAnrwlayrLELIGSIIILGAATLSVFrlkQGTL 1228
Cdd:cd18563 188 TLPGIRVVKAFGQEKreikRFDEANQelldanIRAEKLWATFFPLLTF-------LTSLGTLIVWYFGGRQVL---SGTM 257
|
250 260 270
....*....|....*....|....*....|....*....
9AYC_A 1229 TAGMVGLSLSYALQITQTLNWIVRMTVEVETNIVSVERI 1267
Cdd:cd18563 258 TLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
1014-1267 |
2.09e-11 |
|
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: 66.43 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1014 RYLAIYFALGIGSALATLIQTivlWVFCTI--HASKYLHNLMTNSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRT 1091
Cdd:cd18557 37 ELALILLAIYLLQSVFTFVRY---YLFNIAgeRIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1092 FSQFFVNAVKVTFTITVICATTWQ---FIFIIIPL-SVFYIYYQQYYLRTSRELRrlDSITRSPiySHFQETLGGLATVR 1167
Cdd:cd18557 114 LSQLLRNILQVIGGLIILFILSWKltlVLLLVIPLlLIASKIYGRYIRKLSKEVQ--DALAKAG--QVAEESLSNIRTVR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1168 GYSQQ----KRFS-HINQCRIDNNMSAfypsinanRWLAYrLELIGSIIILGAATLSVF---RL-KQGTLTAGMVGLSLS 1238
Cdd:cd18557 190 SFSAEekeiRRYSeALDRSYRLARKKA--------LANAL-FQGITSLLIYLSLLLVLWyggYLvLSGQLTVGELTSFIL 260
|
250 260
....*....|....*....|....*....
9AYC_A 1239 YALQITQTLNWIVRMTVEVETNIVSVERI 1267
Cdd:cd18557 261 YTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1312-1507 |
2.39e-11 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 65.15 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVID------NIA-INEIGLYDLRHK--------LSII 1376
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggwvDLAqASPREILALRRRtigyvsqfLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1377 PQDSQ---VFEGTVRENIDPinqytDEAIWRALE-LSHL--KEHVLSMSNdgldaqlteggGNLSVGQRQLLCLARAMLV 1450
Cdd:COG4778 106 PRVSAldvVAEPLLERGVDR-----EEARARARElLARLnlPERLWDLPP-----------ATFSGGEQQRVNIARGFIA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
9AYC_A 1451 PSKILVLDQATAAVDVETDKVVQETIRTAfKDR--TILTIAHRLNTiMD--SDRIIVLDNG 1507
Cdd:COG4778 170 DPPLLLLDEPTASLDAANRAVVVELIEEA-KARgtAIIGIFHDEEV-REavADRVVDVTPF 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1296-1521 |
2.60e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 66.30 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELDLV---LKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIG----LYD 1368
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFAsraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1369 LRHKLSIIPQ--DSQVFEGTVRENIDPINQYTDEAIWRALELSHLKEHVLSMSNDGLDAQLTEgggnLSVGQRQLLCLAR 1446
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFE----LSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1447 AMLVPSKILVLDQATAAVD----VETDKVVQETIRTAfkdRTILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQLLSD 1521
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDpkarIEMMQLFESIHQSG---QTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
668-864 |
2.83e-11 |
|
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: 65.30 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 668 VALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLG--------------DLFRVKGFATVHGS--VAYVSQVPWIMNG-T 730
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGlerptsgsvlvdgtDLTLLSGKELRKARrrIGMIFQHFNLLSSrT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 731 VKENILF----GHRYDAEFYEKTikacaltidLAILmdgdkTLVG--EKGIS----LSGGQKARLSLARAVYARADTYLL 800
Cdd:cd03258 99 VFENVALpleiAGVPKAEIEERV---------LELL-----ELVGleDKADAypaqLSGGQKQRVGIARALANNPKVLLC 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 801 DDPLAAVDEHVARHLIEHVLGPN---GLlhtkTKVLATNKVSAL-SIADSIALLDNGEITQQGTYDEI 864
Cdd:cd03258 165 DEATSALDPETTQSILALLRDINrelGL----TIVLITHEMEVVkRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
661-866 |
3.21e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.10 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 661 QRKPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGSVAyvsqvpWI------MNG--TVK 732
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVS------ALlelgagFHPelTGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 733 ENILFG---HRYDAEFYEKTIKACaltIDLAILmdGD------KTlvgekgisLSGGQKARLSLARAVYARADTYLLDDP 803
Cdd:COG1134 107 ENIYLNgrlLGLSRKEIDEKFDEI---VEFAEL--GDfidqpvKT--------YSSGMRARLAFAVATAVDPDILLVDEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 804 LAAVDEHV---ARHLIEHVLGpngllHTKTKVLATNKVSAL-SIADSIALLDNGEITQQGTYDEITK 866
Cdd:COG1134 174 LAVGDAAFqkkCLARIRELRE-----SGRTVIFVSHSMGAVrRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
664-860 |
3.28e-11 |
|
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: 64.36 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 664 PEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCmlgdLFRV----KGFATVHG-------------SVAYVSQVPWI 726
Cdd:cd03369 18 PDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILA----LFRFleaeEGKIEIDGidistipledlrsSLTIIPQDPTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 727 MNGTVKENI-LFGHRYDAEFYEktikacALTidlailmdgdktlVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLA 805
Cdd:cd03369 94 FSGTIRSNLdPFDEYSDEEIYG------ALR-------------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
9AYC_A 806 AVDEHvARHLIEHVlgpnglLHTKtkvlaTNKVSALSIA---------DSIALLDNGEITQQGT 860
Cdd:cd03369 155 SIDYA-TDALIQKT------IREE-----FTNSTILTIAhrlrtiidyDKILVMDAGEVKEYDH 206
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1319-1515 |
3.59e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 66.29 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1319 HIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIG---LYDLRHKLSIIPQDSQ--------VFEgTV 1387
Cdd:COG4608 40 DIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDPYaslnprmtVGD-II 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1388 RENIDpINQYTD--EAIWRALELshlkehvlsMSNDGLDAQLT-----EgggnLSVGQRQLLCLARAMLVPSKILVLDQA 1460
Cdd:COG4608 119 AEPLR-IHGLASkaERRERVAEL---------LELVGLRPEHAdryphE----FSGGQRQRIGIARALALNPKLIVCDEP 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
9AYC_A 1461 TAAVDVEtdkvVQETIRTAFKDR------TILTIAHRLNT---ImdSDRIIVLDNGKVAE-------FDSP 1515
Cdd:COG4608 185 VSALDVS----IQAQVLNLLEDLqdelglTYLFISHDLSVvrhI--SDRVAVMYLGKIVEiaprdelYARP 249
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1304-1520 |
3.75e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.41 E-value: 3.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1304 RYRPELdlVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAIN--EIGLYDLRHKLSIIPQD-- 1379
Cdd:PRK13638 10 RYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDysKRGLLALRQQVATVFQDpe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1380 SQVFEGTVRENI-----------DPINQYTDEAIwRALELSHLKEHVLSMsndgldaqltegggnLSVGQRQLLCLARAM 1448
Cdd:PRK13638 88 QQIFYTDIDSDIafslrnlgvpeAEITRRVDEAL-TLVDAQHFRHQPIQC---------------LSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
9AYC_A 1449 LVPSKILVLDQATAAVDVETDKVVQETI-RTAFKDRTILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQLLS 1520
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIrRIVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFA 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1296-1508 |
3.88e-11 |
|
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: 62.47 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYrpELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLtlalfrmieasegnividniaineiglydlrhkLSI 1375
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTL---------------------------------LKL 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1376 IPQDSQVFEGTVRENidpinqytdeaiwRALELSHLkehvlsmsndgldAQltegggnLSVGQRQLLCLARAMLVPSKIL 1455
Cdd:cd03221 46 IAGELEPDEGIVTWG-------------STVKIGYF-------------EQ-------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 1456 VLDQATAAVDVETDKVVQETIRTafKDRTILTIAH-R--LNTImdSDRIIVLDNGK 1508
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEALKE--YPGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
670-870 |
4.15e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 66.65 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 670 LKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGS-----------VAYVSQ-VPWIMNGTVKENILF 737
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQhYALFRHMTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 738 G-------HRYDAEFYEKTIKACALTIDLAILMDGDKTlvgekgiSLSGGQKARLSLARAVYARADTYLLDDPLAAVDEH 810
Cdd:PRK10851 98 GltvlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPA-------QLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
9AYC_A 811 VARHLIEHVLGpnglLHTK---TKVLAT-NKVSALSIADSIALLDNGEITQQGTYDEITKDADS 870
Cdd:PRK10851 171 VRKELRRWLRQ----LHEElkfTSVFVThDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPAT 230
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
667-864 |
4.26e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 65.18 E-value: 4.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCM--LGDLfrvKGFATVHGSVAY---------------------VSQV 723
Cdd:PRK14239 18 KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDL---NPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 724 PWIMNGTVKENILFGHRYDA--------EFYEKTIKAcaltidlAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARA 795
Cdd:PRK14239 95 PNPFPMSIYENVVYGLRLKGikdkqvldEAVEKSLKG-------ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 796 DTYLLDDPLAAVDEHVARHLIEHVLgpnGLLHTKTKVLATNKVSALS-IADSIALLDNGEITQQGTYDEI 864
Cdd:PRK14239 168 KIILLDEPTSALDPISAGKIEETLL---GLKDDYTMLLVTRSMQQASrISDRTGFFLDGDLIEYNDTKQM 234
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1315-1510 |
4.42e-11 |
|
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: 64.05 E-value: 4.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1315 HINIHIKPNEKVGIVGRTGAGKSSLtLALFRMIE-ASEGNIVIDNIAINEIGLYDlrHKLSIIPQDSQVFEG-TVRENID 1392
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTL-LNLIAGFEtPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHlTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1393 ----P---INQYTDEAIWRALElshlkehvlSMSNDGLDAQLTeggGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVD 1465
Cdd:cd03298 93 lglsPglkLTAEDRQAIEVALA---------RVGLAGLEKRLP---GELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
9AYC_A 1466 VETDKVVQETIRTAFKDR--TILTIAHRLNTIMD-SDRIIVLDNGKVA 1510
Cdd:cd03298 161 PALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
672-873 |
4.53e-11 |
|
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: 66.28 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 672 NINFQAKKGNLTCIVGKVGSGKTALLSCMLGdLFRV-KGFATVHGSV-----------------AYVSQ----VPWImng 729
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAG-LERPdSGRIRLGGEVlqdsargiflpphrrriGYVFQearlFPHL--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 730 TVKENILFGHRYdaefyektIKACALTIDLAILMD--GDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAV 807
Cdd:COG4148 93 SVRGNLLYGRKR--------APRAERRISFDEVVEllGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 808 DEhvARH-----LIEHvlgpnglLHTKTK--VL----ATNKVSALsiADSIALLDNGEITQQGTYDEITKDADSPLW 873
Cdd:COG4148 165 DL--ARKaeilpYLER-------LRDELDipILyvshSLDEVARL--ADHVVLLEQGRVVASGPLAEVLSRPDLLPL 230
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1296-1520 |
4.88e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 65.21 E-value: 4.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELDlVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSI 1375
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1376 IPQ--DSQVFEGTVRENI--DPINQYTDEAiwralELSHLKEHVLSMSndGLDAQLTEGGGNLSVGQRQLLCLARAMLVP 1451
Cdd:PRK13652 83 VFQnpDDQIFSPTVEQDIafGPINLGLDEE-----TVAHRVSSALHML--GLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
9AYC_A 1452 SKILVLDQATAAVDVETdkvVQETIR--TAFKDR---TILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQLLS 1520
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQG---VKELIDflNDLPETygmTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFL 227
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1313-1516 |
5.05e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.28 E-value: 5.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1313 LKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVI----------------------DNIA--INEIGLY- 1367
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeqdlivarlqqdpprnvegtvyDFVAegIEEQAEYl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1368 ----DLRHKLSIIPQDSQVFE-GTVRENIDPINqytdeaIWRaLElSHLKEHVLSMSNDGlDAQLTEgggnLSVGQRQLL 1442
Cdd:PRK11147 99 kryhDISHLVETDPSEKNLNElAKLQEQLDHHN------LWQ-LE-NRINEVLAQLGLDP-DAALSS----LSGGWLRKA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 1443 CLARAMLVPSKILVLDQATAAVDVETDKVVqETIRTAFKDrTILTIAHRLNTI--MdSDRIIVLDNGKVAEFdsPG 1516
Cdd:PRK11147 166 ALGRALVSNPDVLLLDEPTNHLDIETIEWL-EGFLKTFQG-SIIFISHDRSFIrnM-ATRIVDLDRGKLVSY--PG 236
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
1010-1231 |
5.22e-11 |
|
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: 65.54 E-value: 5.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1010 PNAARYLAIYFALGIgsALATLIQTIVLWV--FCTIHASKYLHNLMT----NSVLRAPMTFFETTPIGRILNRFsNDIYK 1083
Cdd:cd18570 34 PSGDINLLNIISIGL--ILLYLFQSLLSYIrsYLLLKLSQKLDIRLIlgyfKHLLKLPLSFFETRKTGEIISRF-NDANK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1084 VDALLGRTFSQFFVNAVKVTFTITVICATTWQ---FIFIIIPLSVFYIY-YQQYYLRTSRELRRLDSITrspiYSHFQET 1159
Cdd:cd18570 111 IREAISSTTISLFLDLLMVIISGIILFFYNWKlflITLLIIPLYILIILlFNKPFKKKNREVMESNAEL----NSYLIES 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
9AYC_A 1160 LGGLATVRGYSQQKRFSHINQCRIDNNMSAFYPS---INANRWLAYRLELIGSIIILGAATLSVFrlkQGTLTAG 1231
Cdd:cd18570 187 LKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLgklSNLQSSIKGLISLIGSLLILWIGSYLVI---KGQLSLG 258
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1312-1537 |
6.43e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 65.94 E-value: 6.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLtlaLfRMI----EASEGNIVID------NIAINE--IGL----YDL-RHKls 1374
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTL---L-RIIagleTPDSGRIVLNgrdlftNLPPRErrVGFvfqhYALfPHM-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1375 iipqdsqvfegTVRENID---PINQYTDEAIwRA-----LELSHLkehvlsmsnDGLD----AQLtegggnlSVGQRQLL 1442
Cdd:COG1118 91 -----------TVAENIAfglRVRPPSKAEI-RArveelLELVQL---------EGLAdrypSQL-------SGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1443 CLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKD--RTILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQLL 1519
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDElgGTTVFVTHDQEEALElADRVVVMNQGRIEQVGTPDEVY 222
|
250
....*....|....*....
9AYC_A 1520 SDNKSLF-YSLcmeAGLVN 1537
Cdd:COG1118 223 DRPATPFvARF---LGCVN 238
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1313-1518 |
7.33e-11 |
|
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: 63.54 E-value: 7.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1313 LKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNI-AINEIGlyDLRHKLSIIPQDSQVFEG-TVREN 1390
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHdVVREPR--EVRRRIGIVFQDLSVDDElTGWEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1391 I-----------DPINQYTDEAIwRALELSHLKEHVLSmsndgldaqltegggNLSVGQRQLLCLARAMLVPSKILVLDQ 1459
Cdd:cd03265 94 LyiharlygvpgAERRERIDELL-DFVGLLEAADRLVK---------------TYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 1460 ATAAVDVETDKVVQETIRTAFK--DRTILTIAHrlntIMD-----SDRIIVLDNGKVAEFDSPGQL 1518
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEefGMTILLTTH----YMEeaeqlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1312-1513 |
7.81e-11 |
|
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: 63.43 E-value: 7.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSltlaLFRMI----EASEGNIVIDNIAINEIGLYDlrHKLSIIPQDSQVF-EGT 1386
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTT----TLRMIagleEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQNYALYpHMT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1387 VRENI-----------DPINQYTDEAIwRALELSHLkehvlsmsndgLDAQLTEgggnLSVGQRQLLCLARAMLVPSKIL 1455
Cdd:cd03301 89 VYDNIafglklrkvpkDEIDERVREVA-ELLQIEHL-----------LDRKPKQ----LSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
9AYC_A 1456 VLDQATAAVDVEtdkvVQETIRTAFK------DRTILTIAHRLNTIMD-SDRIIVLDNGKVAEFD 1513
Cdd:cd03301 153 LMDEPLSNLDAK----LRVQMRAELKrlqqrlGTTTIYVTHDQVEAMTmADRIAVMNDGQIQQIG 213
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
978-1267 |
9.77e-11 |
|
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: 64.42 E-value: 9.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 978 FILFIVISMFLSVMGNVWLKHWSEVNSRY---GSNPNAARYLAIYFALgigsalaTLIQTIVLWVFCTI------HASKY 1048
Cdd:cd18540 4 LILLIILMLLVALLDAVFPLLTKYAIDHFitpGTLDGLTGFILLYLGL-------ILIQALSVFLFIRLagkiemGVSYD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1049 LHNLMTNSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTFSQFFVNAVKVTFTITVICATTWQ---FIFIIIP-LS 1124
Cdd:cd18540 77 LRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKlalIVLAVVPvLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1125 VFYIYYQQYYLRTSRELRRLDS-ITrspiySHFQETLGGLATVRGYSQQKR----FSHINQcridnNMsaFYPSINANRW 1199
Cdd:cd18540 157 VVSIYFQKKILKAYRKVRKINSrIT-----GAFNEGITGAKTTKTLVREEKnlreFKELTE-----EM--RRASVRAARL 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
9AYC_A 1200 LAYRLELIGSIIILGAATLSVF---RLKQGTLTAGMVGLSLSYALQITQTLNWIVRMTVEVETNIVSVERI 1267
Cdd:cd18540 225 SALFLPIVLFLGSIATALVLWYggiLVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
978-1515 |
1.10e-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: 65.97 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 978 FILFIVISMfLSVMGNVWLKHWseVNSRYGSNPNAARYLAIYFALGIgsALATLIQTIVLWVFCTIhASKYLHNL---MT 1054
Cdd:COG4615 15 LLLALLLGL-LSGLANAGLIAL--INQALNATGAALARLLLLFAGLL--VLLLLSRLASQLLLTRL-GQHAVARLrlrLS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1055 NSVLRAPMTFFETTPIGRILNRFSNDIykvdallgRTFSQFFVNAVK-VTFTITVICATT------WQ---FIFIIIPLS 1124
Cdd:COG4615 89 RRILAAPLERLERIGAARLLAALTEDV--------RTISQAFVRLPElLQSVALVLGCLAylawlsPPlflLTLVLLGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1125 VFYIYYQQY----YLRTSRELR-RLdsitrspiYSHFQETLGGLATVRGYSQQKRF-------SHINQCRiDNNMSAFYP 1192
Cdd:COG4615 161 VAGYRLLVRrarrHLRRAREAEdRL--------FKHFRALLEGFKELKLNRRRRRAffdedlqPTAERYR-DLRIRADTI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1193 SINANRW-----LAyrleLIGSIIILGAATLSVFrlkQGTLTA-GMVGLSLSYAL-QITQTLNWIVRMTVEVEtNIVSVE 1265
Cdd:COG4615 232 FALANNWgnllfFA----LIGLILFLLPALGWAD---PAVLSGfVLVLLFLRGPLsQLVGALPTLSRANVALR-KIEELE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1266 RiKEYADlkSEAPLIVEGHRPPKEWPSqgdIKFNNYSTRYRPELD---LVLKHINIHIKPNEKVGIVGRTGAGKSslTLA 1342
Cdd:COG4615 304 L-ALAAA--EPAAADAAAPPAPADFQT---LELRGVTYRYPGEDGdegFTLGPIDLTIRRGELVFIVGGNGSGKS--TLA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1343 -----LFRmieASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQVFEgtvrENIDPINQYTDEAIWRALELSHLkEHVLS 1417
Cdd:COG4615 376 klltgLYR---PESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD----RLLGLDGEADPARARELLERLEL-DHKVS 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1418 MSNDGLDAQltegggNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKDR--TILTIAHrlnti 1495
Cdd:COG4615 448 VEDGRFSTT------DLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVFYTELLPELKARgkTVIAISH----- 516
|
570 580
....*....|....*....|....*.
9AYC_A 1496 mD------SDRIIVLDNGKVAEFDSP 1515
Cdd:COG4615 517 -DdryfdlADRVLKMDYGKLVELTGP 541
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
667-855 |
1.10e-10 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 62.93 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCM-------LGDL--------FRVKGFATVHGSVAYVSQ----VPwim 727
Cdd:cd03262 13 FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlleepdSGTIiidglkltDDKKNINELRQKVGMVFQqfnlFP--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 728 NGTVKENILFGHRYdaefYEKTIKACALTIDLAILmdgdkTLVG--EKG----ISLSGGQKARLSLARAVYARADTYLLD 801
Cdd:cd03262 90 HLTVLENITLAPIK----VKGMSKAEAEERALELL-----EKVGlaDKAdaypAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 802 DPLAAVDEhvarHLIEHVLGP-NGLLHTK-TKVLATNKVS-ALSIADSIALLDNGEI 855
Cdd:cd03262 161 EPTSALDP----ELVGEVLDVmKDLAEEGmTMVVVTHEMGfAREVADRVIFMDDGRI 213
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
664-869 |
1.11e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 64.33 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 664 PEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDL---------------FRVKGFATVHGSVAYVSQVP--WI 726
Cdd:PRK13639 12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILkptsgevlikgepikYDKKSLLEVRKTVGIVFQNPddQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 727 MNGTVKENILFGH---RYDAEFYEKTIKAcALTidlAILMDGDKTLVGEKgisLSGGQKARLSLARAVYARADTYLLDDP 803
Cdd:PRK13639 92 FAPTVEEDVAFGPlnlGLSKEEVEKRVKE-ALK---AVGMEGFENKPPHH---LSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 804 LAAVDEHVARHLIE--HVLGPNGLlhtkTKVLATNKVSALSI-ADSIALLDNGEITQQGTYDEITKDAD 869
Cdd:PRK13639 165 TSGLDPMGASQIMKllYDLNKEGI----TIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1313-1520 |
1.18e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.04 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1313 LKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAInEIGLYDLR-HKLSIIPQD-----------S 1380
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSYRsQRIRMIFQDpstslnprqriS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1381 QVFEGTVRENIDPINQYTDEAIWRAL-ELSHLKEHVLSMSNdgldaqltegggNLSVGQRQLLCLARAMLVPSKILVLDQ 1459
Cdd:PRK15112 108 QILDFPLRLNTDLEPEQREKQIIETLrQVGLLPDHASYYPH------------MLAPGQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 1460 ATAAVDVETDKVV-------QETIRTAFkdrtILTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQLLS 1520
Cdd:PRK15112 176 ALASLDMSMRSQLinlmlelQEKQGISY----IYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1294-1525 |
1.27e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 64.26 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1294 GDIKFNNYSTRYRPELDLVLKHIN---IHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAI-------NE 1363
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFEFKALNntsLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkkiKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1364 IGlyDLRHKLSIIPQ--DSQVFEGTVRENI--DPINQYTD--EAIWRALELSHLkehvLSMSNDGLDAQLTEgggnLSVG 1437
Cdd:PRK13645 85 VK--RLRKEIGLVFQfpEYQLFQETIEKDIafGPVNLGENkqEAYKKVPELLKL----VQLPEDYVKRSPFE----LSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1438 QRQLLCLARAMLVPSKILVLDQATAAVDV--ETDKV-VQETIRTAFKDRTILtIAHRLNTIMD-SDRIIVLDNGKVAEFD 1513
Cdd:PRK13645 155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPkgEEDFInLFERLNKEYKKRIIM-VTHNMDQVLRiADEVIVMHEGKVISIG 233
|
250
....*....|..
9AYC_A 1514 SPGQLLSDNKSL 1525
Cdd:PRK13645 234 SPFEIFSNQELL 245
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
670-863 |
1.30e-10 |
|
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: 66.00 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 670 LKNINFQAKKGNLTCIVGKVGSGKTAL--LscmlgdLFRvkgF--------------------ATVHGSVAYVSQVPWIM 727
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLarL------LFR---FydvtsgrilidgqdirdvtqASLRAAIGIVPQDTVLF 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 728 NGTVKENILFGhRYDA--EFYEKTIKACALTIDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLA 805
Cdd:COG5265 445 NDTIAYNIAYG-RPDAseEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATS 523
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 806 AVDEH-----------VARHliehvlgpngllHTkTKVLAtNKVSALSIADSIALLDNGEITQQGTYDE 863
Cdd:COG5265 524 ALDSRteraiqaalreVARG------------RT-TLVIA-HRLSTIVDADEILVLEAGRIVERGTHAE 578
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1296-1525 |
1.81e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 63.95 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELDLVLK---HINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVI------DNIAINEIGL 1366
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdekNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1367 Y------------------DLRHKLSIIPQ--DSQVFEGTVRENI--DPINQYTD--EAIWRA---LELSHLKEHVLSMS 1419
Cdd:PRK13651 83 VleklviqktrfkkikkikEIRRRVGVVFQfaEYQLFEQTIEKDIifGPVSMGVSkeEAKKRAakyIELVGLDESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1420 NdgldaqlteggGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKD-RTILTIAHRLNTIMD- 1497
Cdd:PRK13651 163 P-----------FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEw 231
|
250 260
....*....|....*....|....*...
9AYC_A 1498 SDRIIVLDNGKVAEFDSPGQLLSDNKSL 1525
Cdd:PRK13651 232 TKRTIFFKDGKIIKDGDTYDILSDNKFL 259
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1305-1504 |
1.93e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 62.42 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1305 YRPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQVFE 1384
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1385 GTVREN-IDPI---NQYTDEAIWRA-LELSHLKEHVLSMSndgldaqLTEgggnLSVGQRQLLCLARAMLVPSKILVLDQ 1459
Cdd:PRK10247 95 DTVYDNlIFPWqirNQQPDPAIFLDdLERFALPDTILTKN-------IAE----LSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
9AYC_A 1460 ATAAVDVETDKVVQETIRTAFKDRTI--LTIAHRLNTIMDSDRIIVL 1504
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQNIavLWVTHDKDEINHADKVITL 210
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1312-1523 |
2.46e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.60 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYD-LRHKLSIIPQDSQVFEG-TVRE 1389
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRRlSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1390 NIDPINQYTDEAIW-----RALELshLKEHVLSMSNDGLdaqltegGGNLSVGQRQLLCLARAMLVPSKILVLDQATAAV 1464
Cdd:PRK10895 98 NLMAVLQIRDDLSAeqredRANEL--MEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 1465 D----VETDKVVQEtirtaFKDR--TILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQLLSDNK 1523
Cdd:PRK10895 169 DpisvIDIKRIIEH-----LRDSglGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
667-815 |
2.50e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.81 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGSVAYVSQVPWIM------NG-----TVKENI 735
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAChylghrNAmkpalTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 736 LFGhrydAEFY---EKTIKACALTIDLAILMDgdktlvgEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEH-- 810
Cdd:PRK13539 95 EFW----AAFLggeELDIAAALEAVGLAPLAH-------LPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAav 163
|
170
....*....|.
9AYC_A 811 ------VARHL 815
Cdd:PRK13539 164 alfaelIRAHL 174
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
670-871 |
2.58e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 62.42 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 670 LKNINFQAKKGNLTCIVGKVGSGKTALLSCM-------LGDLfRVKGFaTVHGSVAYVSQV--------------PWImn 728
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDL-IVDGL-KVNDPKVDERLIrqeagmvfqqfylfPHL-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 729 gTVKENILFGHRYdaefYEKTIKACALTIDLAILmdgDKTLVGEKG----ISLSGGQKARLSLARAVYARADTYLLDDPL 804
Cdd:PRK09493 93 -TALENVMFGPLR----VRGASKEEAEKQARELL---AKVGLAERAhhypSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
9AYC_A 805 AAVDEHVaRHLIEHV---LGPNGLlhtkTKVLATNKVS-ALSIADSIALLDNGEITQQGTYDEITKDADSP 871
Cdd:PRK09493 165 SALDPEL-RHEVLKVmqdLAEEGM----TMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQ 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
667-859 |
2.63e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 62.46 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCM------LGDLFRVkGFATVHGSVAYVSQVPWIMN-----GTVKENI 735
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpEAGTIRV-GDITIDTARSLSQQKGLIRQlrqhvGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 736 -LFGHRYDAE-------FYEKTIKACALTIDLAILMDgdktlVGEKGIS------LSGGQKARLSLARAVYARADTYLLD 801
Cdd:PRK11264 95 nLFPHRTVLEniiegpvIVKGEPKEEATARARELLAK-----VGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
9AYC_A 802 DPLAAVDEhvarHLIEHVLGP-NGLLHTK-TKVLATNKVS-ALSIADSIALLDNGEITQQG 859
Cdd:PRK11264 170 EPTSALDP----ELVGEVLNTiRQLAQEKrTMVIVTHEMSfARDVADRAIFMDQGRIVEQG 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
669-864 |
3.12e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 62.90 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 669 ALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGS-------------VAYVSQVP--WIMNGTVKE 733
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfVGLVFQNPddQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 734 NILFGhRYDAEFYEKTIKAcalTIDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVAR 813
Cdd:PRK13652 99 DIAFG-PINLGLDEETVAH---RVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVK 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
9AYC_A 814 HLIEHVlgpNGLLHT--KTKVLATNKVSAL-SIADSIALLDNGEITQQGTYDEI 864
Cdd:PRK13652 175 ELIDFL---NDLPETygMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
720-869 |
3.13e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.44 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 720 VSQVPWIMNGTVKENILFGhRYDAEFyEKTIKACALT-IDLAI--LMDGDKTLVGEKGISLSGGQKARLSLARAVYARAD 796
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFG-KEDATR-EDVKRACKFAaIDEFIesLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPK 1378
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 797 TYLLDDPLAAVDEHvARHLIEHVLGPNGLLHTKTKVLATNKVSALSIADSIALLDN----GEITQ-QGTYDEITKDAD 869
Cdd:PTZ00265 1379 ILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSVQD 1455
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1312-1510 |
3.17e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.69 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLyDLRHKLSI--IPQDSQVFEG-TVR 1388
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP-AKAHQLGIylVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1389 ENID---PINQYTDEAIWRAL-EL-SHLKehvlsmsndgLDAQltegGGNLSVGQRQLLCLARAMLVPSKILVLDQATAA 1463
Cdd:PRK15439 105 ENILfglPKRQASMQKMKQLLaALgCQLD----------LDSS----AGSLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
9AYC_A 1464 VD-VETDKVVQETIRTAFKDRTILTIAHRLNTIMD-SDRIIVLDNGKVA 1510
Cdd:PRK15439 171 LTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIA 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1313-1508 |
3.30e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.37 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1313 LKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAIN-EIGLYDLRHKLSIIPQD-SQVFEGTVREN 1390
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1391 I------------DPINQYTD-EAIWRALelshlkehvlsmsndGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVL 1457
Cdd:PRK10982 94 MwlgryptkgmfvDQDKMYRDtKAIFDEL---------------DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 1458 DQATAAVdveTDKVVQE--TIRTAFKDR--TILTIAHRLNTIMD-SDRIIVLDNGK 1508
Cdd:PRK10982 159 DEPTSSL---TEKEVNHlfTIIRKLKERgcGIVYISHKMEEIFQlCDEITILRDGQ 211
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1312-1520 |
4.04e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.54 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLAL---FRMIEASEGNIVIDNIAIN-----EIGLYDLRHKLSIIPQDSQ-V 1382
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagdLTGGGAPRGARVTGDVTLNgeplaAIDAPRLARLRAVLPQAAQpA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1383 FEGTVRENI-----------DPINQYTDEAIWRALELShlkehvlsmSNDGLDAQ--LTEGGGNLSVGQ--RQLLCL--A 1445
Cdd:PRK13547 96 FAFSAREIVllgrypharraGALTHRDGEIAWQALALA---------GATALVGRdvTTLSGGELARVQfaRVLAQLwpP 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 1446 RAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKDRTI--LTIAHRLN-TIMDSDRIIVLDNGKVAEFDSPGQLLS 1520
Cdd:PRK13547 167 HDAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgvLAIVHDPNlAARHADRIAMLADGAIVAHGAPADVLT 244
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
667-869 |
4.05e-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: 61.79 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLG--------------DLFRVKGFATVHGSVAYVSQVPWIMNG-TV 731
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGlvkpdsgkilldgqDITKLPMHKRARLGIGYLPQEASIFRKlTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 732 KENI---LFGHRYDAEfyEKTIKACALTIDLAIlmdgdKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVD 808
Cdd:cd03218 93 EENIlavLEIRGLSKK--EREEKLEELLEEFHI-----THLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 809 -------EHVARHLIEHVLGpngllhtktkVLAT--NKVSALSIADSIALLDNGEITQQGTYDEITKDAD 869
Cdd:cd03218 166 piavqdiQKIIKILKDRGIG----------VLITdhNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1312-1509 |
5.24e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.00 E-value: 5.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIglydlRHKLSIIPQDSQVFegtvreni 1391
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLMFQDARLL-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1392 dPINQYTD------EAIWRALELSHLkEHVlsmsndGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVD 1465
Cdd:PRK11247 94 -PWKKVIDnvglglKGQWRDAALQAL-AAV------GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
9AYC_A 1466 VETDKVVQETIRTAFKDR--TILTIAHRLN-TIMDSDRIIVLDNGKV 1509
Cdd:PRK11247 166 ALTRIEMQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
668-858 |
5.51e-10 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 61.21 E-value: 5.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 668 VALKNINFQAKKGNLTCIVGKVGSGKTALLSCmLGDLFRV-KGFATVHG-----------------SVAYVSQ----VPW 725
Cdd:COG1136 22 TALRGVSLSIEAGEFVAIVGPSGSGKSTLLNI-LGGLDRPtSGEVLIDGqdisslserelarlrrrHIGFVFQffnlLPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 726 ImngTVKENILFGHRYdAEFYEKTIKACALTIdLAILMDGDKT--LVGEkgisLSGGQKARLSLARAVYARADTYLLDDP 803
Cdd:COG1136 101 L---TALENVALPLLL-AGVSRKERRERAREL-LERVGLGDRLdhRPSQ----LSGGQQQRVAIARALVNRPKLILADEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
9AYC_A 804 LAAVDEHVARHLIEhvlgpngLLHT------KTKVLATNKVSALSIADSIALLDNGEITQQ 858
Cdd:COG1136 172 TGNLDSKTGEEVLE-------LLRElnrelgTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1296-1511 |
5.72e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 62.52 E-value: 5.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELdlVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYdLRHKLSI 1375
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1376 IPQ-DSQVFEGTVRENIDPINQY-------TDEAIWRALELSHLKEHVlsmsndglDAQLTEgggnLSVGQRQLLCLARA 1447
Cdd:PRK13537 85 VPQfDNLDPDFTVRENLLVFGRYfglsaaaARALVPPLLEFAKLENKA--------DAKVGE----LSGGMKRRLTLARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
9AYC_A 1448 MLVPSKILVLDQATAAVDVETDKVVQETIRTAF-KDRTILTIAH------RLntimdSDRIIVLDNG-KVAE 1511
Cdd:PRK13537 153 LVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHfmeeaeRL-----CDRLCVIEEGrKIAE 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1313-1508 |
6.19e-10 |
|
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: 63.69 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1313 LKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEAS--EGNIVIDNIAINEIGLYDLRHK-LSIIPQD-SQVFEGTVR 1388
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTERAgIVIIHQElTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1389 ENIDPINQYT--------DEAIWRALELshLKEHVLSMSNDGLDAqlteggGNLSVGQRQLLCLARAMLVPSKILVLDQA 1460
Cdd:TIGR02633 97 ENIFLGNEITlpggrmayNAMYLRAKNL--LRELQLDADNVTRPV------GDYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
9AYC_A 1461 TAAVDVETDKVVQETIRTaFKDRTI--LTIAHRLNTIMD-SDRIIVLDNGK 1508
Cdd:TIGR02633 169 SSSLTEKETEILLDIIRD-LKAHGVacVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
664-869 |
6.47e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 61.99 E-value: 6.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 664 PEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHG---------------SVAYVSQVP--WI 726
Cdd:PRK13637 17 PFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkKVGLVFQYPeyQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 727 MNGTVKENILFGHR----YDAEFYEKTIKACALT-IDLAILMDgdktlvgEKGISLSGGQKARLSLARAVYARADTYLLD 801
Cdd:PRK13637 97 FEETIEKDIAFGPInlglSEEEIENRVKRAMNIVgLDYEDYKD-------KSPFELSGGQKRRVAIAGVVAMEPKILILD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
9AYC_A 802 DPLAAVDEHvARhliEHVLGPNGLLHTK---TKVLATNKVSALS-IADSIALLDNGEITQQGTYDEITKDAD 869
Cdd:PRK13637 170 EPTAGLDPK-GR---DEILNKIKELHKEynmTIILVSHSMEDVAkLADRIIVMNKGKCELQGTPREVFKEVE 237
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
637-869 |
8.34e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 62.18 E-value: 8.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 637 QRLPKVKN--IGDVAINIGDDATFLWQRKPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLS------------CMLG 702
Cdd:PRK13631 7 KKKLKVPNplSDDIILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglikskygtIQVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 703 DLF-----------------RVKGFATVHGSVAYVSQVP--WIMNGTVKENILFGhryDAEFYEKTIKACALTIDLAILM 763
Cdd:PRK13631 87 DIYigdkknnhelitnpyskKIKNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFG---PVALGVKKSEAKKLAKFYLNKM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 764 DGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARHLIEHVLGPNGllHTKTKVLATNKV-SALS 842
Cdd:PRK13631 164 GLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKA--NNKTVFVITHTMeHVLE 241
|
250 260
....*....|....*....|....*..
9AYC_A 843 IADSIALLDNGEITQQGTYDEITKDAD 869
Cdd:PRK13631 242 VADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
670-864 |
8.68e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 61.08 E-value: 8.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 670 LKNINFQAKKGNLTCIVGKVGSGKTALLSCM--LGDLF---RVKGFATVHGS-------------VAYVSQVP-WIMNGT 730
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYpeaRVSGEVYLDGQdifkmdvielrrrVQMVFQIPnPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 731 VKENILFGHRYD------AEFYEKTIKAcaltIDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPL 804
Cdd:PRK14247 99 IFENVALGLKLNrlvkskKELQERVRWA----LEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
9AYC_A 805 AAVD-EHVARhlIEHVlgpngLLHTK---TKVLATN-KVSALSIADSIALLDNGEITQQGTYDEI 864
Cdd:PRK14247 175 ANLDpENTAK--IESL-----FLELKkdmTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1312-1520 |
9.63e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 61.18 E-value: 9.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQVFEG-TVREN 1390
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1391 I----DPINQY------TDEA-IWRALELSHLKEHVlsmsndglDAQLTEgggnLSVGQRQLLCLARAMLVPSKILVLDQ 1459
Cdd:PRK11231 97 VaygrSPWLSLwgrlsaEDNArVNQAMEQTRINHLA--------DRRLTD----LSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 1460 ATAAVD----VETDKVVQEtIRTAFKdrTILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQLLS 1520
Cdd:PRK11231 165 PTTYLDinhqVELMRLMRE-LNTQGK--TVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
1017-1231 |
1.08e-09 |
|
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: 61.35 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1017 AIYFALGIGSALATLIQTIVL-WVfctihASKYLHNLMTNS---VLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTF 1092
Cdd:cd18546 43 AAYLAVVLAGWVAQRAQTRLTgRT-----GERLLYDLRLRVfahLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1093 SQFFVNAVKVTFTITVICATTWQF----IFIIIPLSVFYIYYQQYYLRTSRELRrlDSITRspIYSHFQETLGGLATVRG 1168
Cdd:cd18546 118 VQLVVSLLTLVGIAVVLLVLDPRLalvaLAALPPLALATRWFRRRSSRAYRRAR--ERIAA--VNADLQETLAGIRVVQA 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 1169 YSQQ----KRFSHINQCRIDNNMSAfypsINANRWLAYRLELIGSIIIlgAATLSV--FRLKQGTLTAG 1231
Cdd:cd18546 194 FRRErrnaERFAELSDDYRDARLRA----QRLVAIYFPGVELLGNLAT--AAVLLVgaWRVAAGTLTVG 256
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
668-859 |
1.09e-09 |
|
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: 60.07 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 668 VALKNINFQAKKGNLTCIVGKVGSGKTALLScMLGDLFR-------VKGFATVHGSVAYVSQVPWIMNG-------TVKE 733
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLR-MLAGLLEpdagfatVDGFDVVKEPAEARRRLGFVSDStglydrlTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 734 NIlfghRYDAEFYekTIKACALTIDLAILMD--GDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHV 811
Cdd:cd03266 98 NL----EYFAGLY--GLKGDELTARLEELADrlGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
9AYC_A 812 ARHLIEHV--LGPNGllhtKTKVLATNKVS-ALSIADSIALLDNGEITQQG 859
Cdd:cd03266 172 TRALREFIrqLRALG----KCILFSTHIMQeVERLCDRVVVLHRGRVVYEG 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
662-871 |
1.21e-09 |
|
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: 60.59 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 662 RKPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGdLFRV-KGFATVHGS-------------VAYVSQVP--- 724
Cdd:COG1124 13 QGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAG-LERPwSGEVTFDGRpvtrrrrkafrrrVQMVFQDPyas 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 725 ----WIMNGTVKENILFGHRYDAEfyeKTIKACALTIDLailmdgDKTLVGEKGISLSGGQKARLSLARAVYARADTYLL 800
Cdd:COG1124 92 lhprHTVDRILAEPLRIHGLPDRE---ERIAELLEQVGL------PPSFLDRYPHQLSGGQRQRVAIARALILEPELLLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 801 DDPLAAVDEHVARHLIEhvlgpngLL------HTKTKVLATNKVSALS-IADSIALLDNGEITQQGTYDEITKDADSP 871
Cdd:COG1124 163 DEPTSALDVSVQAEILN-------LLkdlreeRGLTYLFVSHDLAVVAhLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
667-803 |
1.32e-09 |
|
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: 58.23 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHG--SVAYVSQvpwimngtvkenilfghrydae 744
Cdd:cd03221 13 KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGStvKIGYFEQ---------------------- 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 745 fyektikacaltidlailmdgdktlvgekgisLSGGQKARLSLARAVYARADTYLLDDP 803
Cdd:cd03221 71 --------------------------------LSGGEKMRLALAKLLLENPNLLLLDEP 97
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
667-803 |
1.60e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.39 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDL-------FRVKGFatvhgSVAYVSQ-VPWIMNGTVKENILFG 738
Cdd:COG0488 11 RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELepdsgevSIPKGL-----RIGYLPQePPLDDDLTVLDTVLDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 739 H--------RYDaEFYEKTIKACALTIDLAIL------MDG-------DKTLVG--------EKGIS-LSGGQKARLSLA 788
Cdd:COG0488 86 DaelraleaELE-ELEAKLAEPDEDLERLAELqeefeaLGGweaearaEEILSGlgfpeedlDRPVSeLSGGWRRRVALA 164
|
170
....*....|....*
9AYC_A 789 RAVYARADTYLLDDP 803
Cdd:COG0488 165 RALLSEPDLLLLDEP 179
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
670-855 |
2.05e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.08 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 670 LKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGdLFRVKGFATVHGSvAYVSQV--------------PWimnGTVKENI 735
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-LETPSAGELLAGT-APLAEAredtrlmfqdarllPW---KKVIDNV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 736 LFGHRYDaeFYEKTIKACAlTIDLAilmdgDKTlvGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEhVAR-- 813
Cdd:PRK11247 103 GLGLKGQ--WRDAALQALA-AVGLA-----DRA--NEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA-LTRie 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
9AYC_A 814 --HLIEHVLGPNGLlhtkTKVLATNKVS-ALSIADSIALLDNGEI 855
Cdd:PRK11247 172 mqDLIESLWQQHGF----TVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1313-1508 |
2.13e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.87 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1313 LKHINIHIKPNEKVGIVGRTGAGKSSLtlalfrMIEAS--------EGNIVIDNIAINEIGLYDLRHK-LSIIPQD-SQV 1382
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTL------MKVLSgvyphgtyEGEIIFEGEELQASNIRDTERAgIAIIHQElALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1383 FEGTVRENIDPINQYT-------DEAIWRALELshLKEHvlsmsndGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKIL 1455
Cdd:PRK13549 95 KELSVLENIFLGNEITpggimdyDAMYLRAQKL--LAQL-------KLDINPATPVGNLGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 1456 VLDQATAAV-DVETDkVVQETIRTaFKDRTI--LTIAHRLNTIMD-SDRIIVLDNGK 1508
Cdd:PRK13549 166 ILDEPTASLtESETA-VLLDIIRD-LKAHGIacIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
654-808 |
2.18e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 60.28 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 654 DDATFLWQRKpeyKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGS----------VAYVSQ- 722
Cdd:PRK15056 10 NDVTVTWRNG---HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVPQs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 723 --VPWIMNGTVKENILFGhRYD-------AEFYEKTIKACALT-IDLailMDGDKTLVGEkgisLSGGQKARLSLARAVY 792
Cdd:PRK15056 87 eeVDWSFPVLVEDVVMMG-RYGhmgwlrrAKKRDRQIVTAALArVDM---VEFRHRQIGE----LSGGQKKRVFLARAIA 158
|
170
....*....|....*.
9AYC_A 793 ARADTYLLDDPLAAVD 808
Cdd:PRK15056 159 QQGQVILLDEPFTGVD 174
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
670-859 |
2.23e-09 |
|
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: 58.81 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 670 LKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGdlfRVKGFATVHGSVAYVSQVPWIMNGTVKENILFGHRYDAEFYEKT 749
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 750 IKAcalTIDLAILMDGDKTLVGekgisLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARHLIEhvlgpngLLHTK 829
Cdd:cd03233 100 VRE---TLDFALRCKGNEFVRG-----ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILK-------CIRTM 164
|
170 180 190
....*....|....*....|....*....|....*...
9AYC_A 830 TKVL-ATNKVSAL-------SIADSIALLDNGEITQQG 859
Cdd:cd03233 165 ADVLkTTTFVSLYqasdeiyDLFDKVLVLYEGRQIYYG 202
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1312-1511 |
2.96e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.82 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIE--ASEGNIVIDNIAINEiglydlrhKLSIIpqdsqvfegtvrE 1389
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGR--------EASLI------------D 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1390 NIDPINQYTDeaiwrALElshlkehVLSMSndGL-DAQL-----TEgggnLSVGQRQLLCLARAMLVPSKILVLDQATAA 1463
Cdd:COG2401 105 AIGRKGDFKD-----AVE-------LLNAV--GLsDAVLwlrrfKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
9AYC_A 1464 VDVETDKVVQETIRTAFKDR--TILTIAHRLNTIMD--SDRIIVLDNGKVAE 1511
Cdd:COG2401 167 LDRQTAKRVARNLQKLARRAgiTLVVATHHYDVIDDlqPDLLIFVGYGGVPE 218
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
671-859 |
3.31e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 60.81 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 671 KNINFQAKKGNLTCIVGKVGSGKTALLSCMLG-------DLF----RVKGFATVHGSVAYVSQ----VPWImngTVKENI 735
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGleditsgDLFigekRMNDVPPAERGVGMVFQsyalYPHL---SVAENM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 736 LFGHRY---DAEFYEKTIKACALTIDLAILMDgdktlvgEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDE--- 809
Cdd:PRK11000 97 SFGLKLagaKKEEINQRVNQVAEVLQLAHLLD-------RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalr 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 810 -----HVARhliehvlgpnglLHTK---TKVLAT-NKVSALSIADSIALLDNGEITQQG 859
Cdd:PRK11000 170 vqmriEISR------------LHKRlgrTMIYVThDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
667-859 |
4.47e-09 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 58.36 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGnLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGS------------VAYVSQ-VPWIMNGTVKE 733
Cdd:cd03264 13 KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrIGYLPQeFGVYPNFTVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 734 NIlfghRYDAEFYE---KTIKA-CALTIDLAILMDGDKTLVGekgiSLSGGQKARLSLARAVYARADTYLLDDPLAAVD- 808
Cdd:cd03264 92 FL----DYIAWLKGipsKEVKArVDEVLELVNLGDRAKKKIG----SLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDp 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
9AYC_A 809 -EHVA-RHLIEhvlgpnGLLHTKTKVLATNKVSAL-SIADSIALLDNGEITQQG 859
Cdd:cd03264 164 eERIRfRNLLS------ELGEDRIVILSTHIVEDVeSLCNQVAVLNKGKLVFEG 211
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1306-1535 |
5.64e-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: 61.18 E-value: 5.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1306 RPELDlvlkHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAInEIGLYDLRHKLSIIPQDSQVFEG 1385
Cdd:TIGR01257 943 RPAVD----RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHH 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1386 -TVRENIDPINQYTDEAiWRALELshlkEHVLSMSNDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATAAV 1464
Cdd:TIGR01257 1018 lTVAEHILFYAQLKGRS-WEEAQL----EMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
9AYC_A 1465 DVETDKVVQETIRTAFKDRTILTIAHRLNTI-MDSDRIIVLdngkvaefdSPGQLLSDNKSLFYSLCMEAGL 1535
Cdd:TIGR01257 1093 DPYSRRSIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAII---------SQGRLYCSGTPLFLKNCFGTGF 1155
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
668-869 |
5.97e-09 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 58.51 E-value: 5.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 668 VALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLG--------------DLFRVKGFATVHGSVAYVSQVPWIMNG-TVK 732
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGfyrptsgrilfdgrDITGLPPHRIARLGIARTFQNPRLFPElTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 733 ENILFGH----------------RYDAEFYEKTIKACAL--TIDLAILMDgdkTLVGekgiSLSGGQKARLSLARAVYAR 794
Cdd:COG0411 98 ENVLVAAharlgrgllaallrlpRARREEREARERAEELleRVGLADRAD---EPAG----NLSYGQQRRLEIARALATE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 795 ADTYLLDDPLAAVDEHVARHLIEHVLgpngllhtktKVLATNKVSAL----------SIADSIALLDNGEITQQGTYDEI 864
Cdd:COG0411 171 PKLLLLDEPAAGLNPEETEELAELIR----------RLRDERGITILliehdmdlvmGLADRIVVLDFGRVIAEGTPAEV 240
|
....*
9AYC_A 865 TKDAD 869
Cdd:COG0411 241 RADPR 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1296-1521 |
7.31e-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: 60.20 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYRPELDLVLK---HINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVI----DNIAINEIGlYD 1368
Cdd:TIGR03269 280 IKVRNVSKRYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPG-PD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1369 LRHK----LSIIPQDSQVF-EGTVRENIdpinqytDEAIWRAL--ELSHLKE-HVLSM---SNDGLDAQLTEGGGNLSVG 1437
Cdd:TIGR03269 359 GRGRakryIGILHQEYDLYpHRTVLDNL-------TEAIGLELpdELARMKAvITLKMvgfDEEKAEEILDKYPDELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1438 QRQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKD--RTILTIAHRLNTIMD-SDRIIVLDNGKVAEFDS 1514
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGD 511
|
....*..
9AYC_A 1515 PGQLLSD 1521
Cdd:TIGR03269 512 PEEIVEE 518
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
669-869 |
7.64e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.98 E-value: 7.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 669 ALKNINFQAKKGNLTCIVGKVGSGKTALL------------SCMLGDLF-----RVKGFATVHGSVAYVSQVP--WIMNG 729
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLqhlngllqptegKVTVGDIVvsstsKQKEIKPVRKKVGVVFQFPesQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 730 TVKENILFGHRYDAEFYEKTIKACALTIDLAILmdgDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDE 809
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGL---ADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 810 HVARHLIE-----HVLGpngllhtKTKVLATNKVSALS-IADSIALLDNGEITQQGTYDEITKDAD 869
Cdd:PRK13643 178 KARIEMMQlfesiHQSG-------QTVVLVTHLMDDVAdYADYVYLLEKGHIISCGTPSDVFQEVD 236
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
664-867 |
1.11e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 58.07 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 664 PEYKVALKNINFQAKKGNLTCIVGKVGSGKTAlLSCMLGDLFR-------VKGFAT--------VHGSVAYVSQVP--WI 726
Cdd:PRK13644 12 PDGTPALENINLVIKKGEYIGIIGKNGSGKST-LALHLNGLLRpqkgkvlVSGIDTgdfsklqgIRKLVGIVFQNPetQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 727 MNGTVKENILFGHRydaefyektiKACALTIDLAILMDgdkTLVGEKGI---------SLSGGQKARLSLARAVYARADT 797
Cdd:PRK13644 91 VGRTVEEDLAFGPE----------NLCLPPIEIRKRVD---RALAEIGLekyrhrspkTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
9AYC_A 798 YLLDDPLAAVDEHVARHLIEHVlgpnGLLHTKTK--VLATNKVSALSIADSIALLDNGEITQQGTYDEITKD 867
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERI----KKLHEKGKtiVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1313-1518 |
1.16e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.54 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1313 LKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYD-LRHKLSIIPQDSQ-VFEGTVREN 1390
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQELHlVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1391 ID----P-----INQytDEAIWRALE-LSHLKEHVlsmsnDGlDAQLteggGNLSVGQRQLLCLARAMLVPSKILVLDQA 1460
Cdd:PRK11288 100 LYlgqlPhkggiVNR--RLLNYEAREqLEHLGVDI-----DP-DTPL----KYLSIGQRQMVEIAKALARNARVIAFDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
9AYC_A 1461 TAAVDV-ETD---KVVQEtIRTafKDRTILTIAHRLNTIMD-SDRIIVLDNG-KVAEFDSPGQL 1518
Cdd:PRK11288 168 TSSLSArEIEqlfRVIRE-LRA--EGRVILYVSHRMEEIFAlCDAITVFKDGrYVATFDDMAQV 228
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
670-808 |
1.18e-08 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 57.11 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 670 LKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDL---FRVKGFATVHGS-----------VAYVSQVPWI---MNgtVK 732
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLspaFSASGEVLLNGRrltalpaeqrrIGILFQDDLLfphLS--VG 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 733 ENILFG--HRYDAEFYEKTIKAcALT-IDLAILMDGDKTlvgekgiSLSGGQKARLSLARAVYARADTYLLDDPLAAVD 808
Cdd:COG4136 95 ENLAFAlpPTIGRAQRRARVEQ-ALEeAGLAGFADRDPA-------TLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1322-1510 |
1.18e-08 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 56.92 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1322 PNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAineigLYDLRHKLSIIPQD---SQVFEG-------TVRENI 1391
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV-----LFDSRKKINLPPQQrkiGLVFQQyalfphlNVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1392 ---------DPINQYTDEaIWRALELSHLKEhvlsmsndgldaqltEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATA 1462
Cdd:cd03297 97 afglkrkrnREDRISVDE-LLDLLGLDHLLN---------------RYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
9AYC_A 1463 AVDVETDKVVQETIRTAFKDRTI--LTIAHRLNTI-MDSDRIIVLDNGKVA 1510
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNLNIpvIFVTHDLSEAeYLADRIVVMEDGRLQ 211
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
668-815 |
1.20e-08 |
|
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: 56.60 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 668 VALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGfaTV--------------HGSVAYVSQVPWIMNG-TVK 732
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSG--EVrwngtplaeqrdepHENILYLGHLPGLKPElSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 733 ENILFGHRydaeFYEKTIKACALTIDLAILMDGDKTLVGekgiSLSGGQKARLSLARAVYARADTYLLDDPLAAVD---- 808
Cdd:TIGR01189 92 ENLHFWAA----IHGGAQRTIEDALAAVGLTGFEDLPAA----QLSAGQQRRLALARLWLSRRPLWILDEPTTALDkagv 163
|
170
....*....|.
9AYC_A 809 ----EHVARHL 815
Cdd:TIGR01189 164 allaGLLRAHL 174
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
654-870 |
1.23e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 57.84 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 654 DDATFLWQRKPEYkvALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGD--------LFR-----VKGFATVHGSVAYV 720
Cdd:PRK13648 11 KNVSFQYQSDASF--TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIekvksgeiFYNnqaitDDNFEKLRKHIGIV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 721 SQVP--WIMNGTVKENILFGHRYDAEFYEKTIKACALTI-DLAILMDGDktlvgEKGISLSGGQKARLSLARAVYARADT 797
Cdd:PRK13648 89 FQNPdnQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALkQVDMLERAD-----YEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 798 YLLDDPLAAVDEHVARHLIEHVlgpngllhtkTKVLATNKVSALSI---------ADSIALLDNGEITQQGTYDEITKDA 868
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLV----------RKVKSEHNITIISIthdlseameADHVIVMNKGTVYKEGTPTEIFDHA 233
|
..
9AYC_A 869 DS 870
Cdd:PRK13648 234 EE 235
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1296-1521 |
1.31e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 57.83 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTRYR---PELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIG----LYD 1368
Cdd:PRK13649 3 INLQNVSYTYQagtPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1369 LRHKLSIIPQ--DSQVFEGTVRENI--DPIN--QYTDEAIWRALElshlKEHVLSMSNDGLDAQLTEgggnLSVGQRQLL 1442
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVafGPQNfgVSQEEAEALARE----KLALVGISESLFEKNPFE----LSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1443 CLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKD-RTILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQLLS 1520
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIFQ 234
|
.
9AYC_A 1521 D 1521
Cdd:PRK13649 235 D 235
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
667-813 |
1.75e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.51 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHgsvayVSQVPWIMNGTVKENIlfGHRYDaeFY 746
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----VPDNQFGREASLIDAI--GRKGD--FK 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 747 EKT--IKACALTiDlAILMdgdKTLVGEkgisLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVAR 813
Cdd:COG2401 114 DAVelLNAVGLS-D-AVLW---LRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
669-864 |
1.88e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 58.31 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 669 ALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHG-SVAYVS--QVPWIM---------NGTVKENIL 736
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvDLSHVPpyQRPINMmfqsyalfpHMTVEQNIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 737 FGHRYD----AEFYEKTIKACALtidlaILMdgdKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHV- 811
Cdd:PRK11607 114 FGLKQDklpkAEIASRVNEMLGL-----VHM---QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLr 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 812 --ARHLIEHVLGPNGLlhtkTKVLAT-NKVSALSIADSIALLDNGEITQQGTYDEI 864
Cdd:PRK11607 186 drMQLEVVDILERVGV----TCVMVThDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
979-1231 |
2.00e-08 |
|
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: 57.42 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 979 ILFIVISMFLSVMGNVWLKHW-SEVNSRYGSNPNAARYLAIYFALGIGSALATliqtiVLWVFCTIHAS----KYLHNLM 1053
Cdd:cd18541 5 ILFLILVDLLQLLIPRIIGRAiDALTAGTLTASQLLRYALLILLLALLIGIFR-----FLWRYLIFGASrrieYDLRNDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1054 TNSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTFSQfFVNAvkVTFTITVICATTWQ------FIFIIIPLSVFY 1127
Cdd:cd18541 80 FAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILY-LVDA--LFLGVLVLVMMFTIspkltlIALLPLPLLALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1128 IYY--QQYYLRTSRELRRLDSITrspiySHFQETLGGLATVRGYSQ----QKRFSHINQCRIDNNM------SAFYPSIN 1195
Cdd:cd18541 157 VYRlgKKIHKRFRKVQEAFSDLS-----DRVQESFSGIRVIKAFVQeeaeIERFDKLNEEYVEKNLrlarvdALFFPLIG 231
|
250 260 270
....*....|....*....|....*....|....*.
9AYC_A 1196 AnrwlayrLELIGSIIILGAATLSVFrlkQGTLTAG 1231
Cdd:cd18541 232 L-------LIGLSFLIVLWYGGRLVI---RGTITLG 257
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1020-1267 |
2.36e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 57.49 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1020 FALGIGSALATLIQTivlWVFCTIhASKYLHNL---MTNSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTFSQFF 1096
Cdd:cd18550 46 VAVAVASALLGVVQT---YLSARI-GQGVMYDLrvqLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1097 VNAVKVTFTITVICATTWQ---FIFIIIPLsvfyiyyqqYYLRTSRELRRLDSITR------SPIYSHFQETL--GGLAT 1165
Cdd:cd18550 122 SNVVTLVATLVAMLALDWRlalLSLVLLPL---------FVLPTRRVGRRRRKLTReqqeklAELNSIMQETLsvSGALL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1166 VRGYSQQK----RFSHINQ----CRIDNNMsafypsinANRWLAYRLELIGSI---IILGAATLSVFrlkQGTLTAGMVG 1234
Cdd:cd18550 193 VKLFGREDdeaaRFARRSRelrdLGVRQAL--------AGRWFFAALGLFTAIgpaLVYWVGGLLVI---GGGLTIGTLV 261
|
250 260 270
....*....|....*....|....*....|...
9AYC_A 1235 LSLSYALQITQTLNWIVRMTVEVETNIVSVERI 1267
Cdd:cd18550 262 AFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1312-1511 |
2.43e-08 |
|
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: 56.29 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLtLALFRMIE-ASEGNIVIDNIAI---NEIGLYDLR-HKLSIIPQDSQVFEG- 1385
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTL-LGLLAGLDrPTSGTVRLAGQDLfalDEDARARLRaRHVGFVFQSFQLLPTl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1386 TVRENI--------DPinqytdEAIWRALELshLkEHVlsmsndGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVL 1457
Cdd:COG4181 106 TALENVmlplelagRR------DARARARAL--L-ERV------GLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 1458 DQATAAVDVETDKVVQETIRTAFKDR--TILTIAHRLNTIMDSDRIIVLDNGKVAE 1511
Cdd:COG4181 171 DEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
667-867 |
2.44e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 57.02 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKT-------ALLSCMLGDLFrVKGFAT--------VHGSVAYVSQVP--WIMNG 729
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKStiakhmnALLIPSEGKVY-VDGLDTsdeenlwdIRNKAGMVFQNPdnQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 730 TVKENILFGHRydaefyektikacaltiDLAILMDGDKTLVGE--KGIS-----------LSGGQKARLSLARAVYARAD 796
Cdd:PRK13633 102 IVEEDVAFGPE-----------------NLGIPPEEIRERVDEslKKVGmyeyrrhaphlLSGGQKQRVAIAGILAMRPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
9AYC_A 797 TYLLDDPLAAVDEHVARHLIEHVLGPNGLLHTkTKVLATNKVSALSIADSIALLDNGEITQQGTYDEITKD 867
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNTIKELNKKYGI-TIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
1020-1245 |
3.11e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 57.09 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1020 FALGIGSALATLIQTIVLWV--FCTIHASKYLHNLMTNSV----LRAPMTFFETTPIGRILNRFSNdIYKVDALLGRTFS 1093
Cdd:cd18567 42 TVLAIGFGLLLLLQALLSALrsWLVLYLSTSLNLQWTSNLfrhlLRLPLSYFEKRHLGDIVSRFGS-LDEIQQTLTTGFV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1094 QFFVNAVKVTFTITVICATTWQFIFIIIPLSVFYIYYQQYYLRTSRELrRLDSITRSPIY-SHFQETLGGLATVRGYSQQ 1172
Cdd:cd18567 121 EALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLRLALYPPLRRA-TEEQIVASAKEqSHFLETIRGIQTIKLFGRE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1173 KRfshinqcRIDNNMSAFYPSINANRWLAyRLELIGS-----------IIILGAATLSVFrlkQGTLTAGMVGLSLSYAL 1241
Cdd:cd18567 200 AE-------REARWLNLLVDAINADIRLQ-RLQILFSaangllfglenILVIYLGALLVL---DGEFTVGMLFAFLAYKD 268
|
....
9AYC_A 1242 QITQ 1245
Cdd:cd18567 269 QFSS 272
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
659-859 |
3.27e-08 |
|
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: 56.19 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 659 LWQRKPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGSV------AYVSQVPWIM----- 727
Cdd:cd03267 26 LFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrrkKFLRRIGVVFgqktq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 728 ---NGTVKENILFGHR-YDAEF--YEKTIKACALTIDLAILMDgdkTLVGEkgisLSGGQKARLSLARAVYARADTYLLD 801
Cdd:cd03267 106 lwwDLPVIDSFYLLAAiYDLPParFKKRLDELSELLDLEELLD---TPVRQ----LSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
9AYC_A 802 DPLAAVDEHVARHLIEHVLGPNGLlhTKTKVLATN----KVSALsiADSIALLDNGEITQQG 859
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKEYNRE--RGTTVLLTShymkDIEAL--ARRVLVIDKGRLLYDG 236
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1312-1511 |
3.44e-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: 55.23 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSL--TLALFRMIEASEGNIVIDNIAINEIGLYDlRHKLSII--PQDSQVFEG-T 1386
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLakTIMGHPKYEVTEGEILFKGEDITDLPPEE-RARLGIFlaFQYPPEIPGvK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1387 VRENIDPINqytdeaiwralelshlkehvlsmsndgldaqltEGggnLSVGQRQLLCLARAMLVPSKILVLDQATAAVDV 1466
Cdd:cd03217 94 NADFLRYVN---------------------------------EG---FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
9AYC_A 1467 ETDKVVQETIRT-AFKDRTILTIAH--RLNTIMDSDRIIVLDNGKVAE 1511
Cdd:cd03217 138 DALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVK 185
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
670-866 |
3.48e-08 |
|
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: 56.79 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 670 LKNINFQAKKGNLTCIVGKVGSGKTALLSCMLgDLFRVKGFATVHG-------------SVAYVSQVPWIMNGTVKENI- 735
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwrkAFGVIPQKVFIFSGTFRKNLd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 736 LFGHRYDAEFYEKTIKACALTIDLAILMDGDKTLVgEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDE---HVA 812
Cdd:cd03289 99 PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLV-DGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPityQVI 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
9AYC_A 813 RHLIEHVLGpngllhTKTKVLATNKVSALSIADSIALLDNGEITQqgtYDEITK 866
Cdd:cd03289 178 RKTLKQAFA------DCTVILSEHRIEAMLECQRFLVIEENKVRQ---YDSIQK 222
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
670-871 |
3.51e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.58 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 670 LKNINFQAKKGNLTCIVGKVGSGKTALLSCmLGDLFRVKGFATVHGSVAYVSQV---------------------PWIMN 728
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNiyerrvnlnrlrrqvsmvhpkPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 729 GTVKENILFGHRYDA--------EFYEKTIKAcaltidlAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLL 800
Cdd:PRK14258 102 MSVYDNVAYGVKIVGwrpkleidDIVESALKD-------ADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
9AYC_A 801 DDPLAAVDEhVARHLIEHVLGPNGLLHTKTKVLATNKVSALS-IADSIALLDNGE--ITQQGTYDEITKDADSP 871
Cdd:PRK14258 175 DEPCFGLDP-IASMKVESLIQSLRLRSELTMVIVSHNLHQVSrLSDFTAFFKGNEnrIGQLVEFGLTKKIFNSP 247
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
1015-1267 |
3.64e-08 |
|
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: 56.67 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1015 YLAIYFALGIGSALATLIQTIVLWVFCTiHASKYLHNLMTNSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTFSQ 1094
Cdd:cd18542 41 LALLILGVALLRGVFRYLQGYLAEKASQ-KVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1095 FFVNAVKVTFTITVICATTWQF---IFIIIPLSVFYIYY-----QQYYLRTSRELRRLDSItrspiyshFQETLGGLATV 1166
Cdd:cd18542 120 LVRAVLLFIGALIIMFSINWKLtliSLAIIPFIALFSYVffkkvRPAFEEIREQEGELNTV--------LQENLTGVRVV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1167 RGYSQQK----RFSHINQ------CRIDNNMSAFYPSINAnrwlayrLELIGSIIILGAATLSVFrlkQGTLTAGMVGLS 1236
Cdd:cd18542 192 KAFAREDyeieKFDKENEeyrdlnIKLAKLLAKYWPLMDF-------LSGLQIVLVLWVGGYLVI---NGEITLGELVAF 261
|
250 260 270
....*....|....*....|....*....|....*
9AYC_A 1237 LSYALQitqtLNWIVRM----TVEVETNIVSVERI 1267
Cdd:cd18542 262 ISYLWM----LIWPVRQlgrlINDMSRASASAERI 292
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
657-871 |
3.90e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 56.13 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 657 TFLWQRKPEYKVaLKNINFQAKKGNLTCIVGKVGSGKTALLSCMlgDLFRVKGFATVHGSVAYVSQVP------------ 724
Cdd:PRK10619 9 IDLHKRYGEHEV-LKGVSLQANAGDVISIIGSSGSGKSTFLRCI--NFLEKPSEGSIVVNGQTINLVRdkdgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 725 ------------------WiMNGTVKENIL------FGHRyDAEFYEKTIKACAltiDLAIlmdgDKTLVGEKGISLSGG 780
Cdd:PRK10619 86 qlrllrtrltmvfqhfnlW-SHMTVLENVMeapiqvLGLS-KQEARERAVKYLA---KVGI----DERAQGKYPVHLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 781 QKARLSLARAVYARADTYLLDDPLAAVD-EHVARHL-IEHVLGPNGllhtKTKVLATNKVS-ALSIADSIALLDNGEITQ 857
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDpELVGEVLrIMQQLAEEG----KTMVVVTHEMGfARHVSSHVIFLHQGKIEE 232
|
250
....*....|....
9AYC_A 858 QGTYDEITKDADSP 871
Cdd:PRK10619 233 EGAPEQLFGNPQSP 246
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1306-1518 |
4.10e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.94 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1306 RPELDLVlKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDN----------IAINEIGLYDLRH---- 1371
Cdd:PRK10261 26 QQKIAAV-RNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRHvrga 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1372 KLSIIPQDSQvfegTVRENIDPINQYTDEAIWRALELSHlkEHVLSMSNDGLD--------AQLTEGGGNLSVGQRQLLC 1443
Cdd:PRK10261 105 DMAMIFQEPM----TSLNPVFTVGEQIAESIRLHQGASR--EEAMVEAKRMLDqvripeaqTILSRYPHQLSGGMRQRVM 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 1444 LARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKDRT--ILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQL 1518
Cdd:PRK10261 179 IAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQI 256
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
667-864 |
4.40e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 57.26 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLscmlgdlfR-VKGFATV-HGSVAY----VSQVP--------------WI 726
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVL--------RlIAGFETPdSGRIMLdgqdITHVPaenrhvntvfqsyaLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 727 MNGTVKENILFGHRY----DAEFYEKTIKACALtIDLAILMDgdktlvgEKGISLSGGQKARLSLARAVYARADTYLLDD 802
Cdd:PRK09452 99 PHMTVFENVAFGLRMqktpAAEITPRVMEALRM-VQLEEFAQ-------RKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 803 PLAAVDeHVARHLIEHVLGPnglLHTK---TKVLAT-NKVSALSIADSIALLDNGEITQQGTYDEI 864
Cdd:PRK09452 171 SLSALD-YKLRKQMQNELKA---LQRKlgiTFVFVThDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
669-864 |
4.88e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 56.18 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 669 ALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHG-------------SVAYVSQVP--WIMNGTVKE 733
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseetvwdvrrQVGMVFQNPdnQFVGATVQD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 734 NILFGHRYDAEFYEKTIKacalTIDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDehvar 813
Cdd:PRK13635 102 DVAFGLENIGVPREEMVE----RVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD----- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 814 hliehvlgPNGllhtKTKVLAT-------NKVSALSI---------ADSIALLDNGEITQQGTYDEI 864
Cdd:PRK13635 173 --------PRG----RREVLETvrqlkeqKGITVLSIthdldeaaqADRVIVMNKGEILEEGTPEEI 227
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1320-1505 |
5.34e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1320 IKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIvidniaineiglyDLRHKLSIIPQ----DsqvFEGTVRENIDPIN 1395
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-------------DPELKISYKPQyikpD---YDGTVEDLLRSIT 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1396 QYTDEAIW-----RALELSHLkehvlsmsndgLDAQLTEgggnLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETDK 1470
Cdd:PRK13409 426 DDLGSSYYkseiiKPLQLERL-----------LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRL 490
|
170 180 190
....*....|....*....|....*....|....*...
9AYC_A 1471 VVQETIR--TAFKDRTILTIAHRLNTI-MDSDRIIVLD 1505
Cdd:PRK13409 491 AVAKAIRriAEEREATALVVDHDIYMIdYISDRLMVFE 528
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1320-1512 |
5.36e-08 |
|
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: 55.49 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1320 IKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAIneiglydlrhklSIIPQDSQV-FEGTVRE---NIDPI- 1394
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV------------SYKPQYIKAdYEGTVRDllsSITKDf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1395 ---NQYTDEaIWRALELSHLkehvlsmsndgLDAQLTEgggnLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETDKV 1471
Cdd:cd03237 90 ythPYFKTE-IAKPLQIEQI-----------LDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLM 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
9AYC_A 1472 VQETIR--TAFKDRTILTIAHRLNTI-MDSDRIIVLDnGKVAEF 1512
Cdd:cd03237 154 ASKVIRrfAENNEKTAFVVEHDIIMIdYLADRLIVFE-GEPSVN 196
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1014-1220 |
6.34e-08 |
|
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: 350019 [Multi-domain] Cd Length: 289 Bit Score: 55.95 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1014 RYLAIYFALGIGSALATLIQT-IVLW----VFCTIHASKYLHnlmtnsVLRAPMTFFETTPIGRILNRFSNDIYKVDALL 1088
Cdd:cd18575 37 RAFLLLLAVALVLALASALRFyLVSWlgerVVADLRKAVFAH------LLRLSPSFFETTRTGEVLSRLTTDTTLIQTVV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1089 GRTFSQFFVNAVKVTFTITVICATTWQ---FIFIIIPLSVFYIyyqqyyLRTSRELRRLDSITRSPI---YSHFQETLGG 1162
Cdd:cd18575 111 GSSLSIALRNLLLLIGGLVMLFITSPKltlLVLLVIPLVVLPI------ILFGRRVRRLSRASQDRLadlSAFAEETLSA 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 1163 LATVRGYSQQKRFSHINQCRIDNNMSAfypsinANRWLAYRLELIGSIIILGAATLSV 1220
Cdd:cd18575 185 IKTVQAFTREDAERQRFATAVEAAFAA------ALRRIRARALLTALVIFLVFGAIVF 236
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
667-810 |
7.26e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.72 E-value: 7.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALL-------SCMLGD-LFRVKGFATV-----HGSVAYVSQVPWIMNGTVKE 733
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLkivasliSPTSGTlLFEGEDISTLkpeiyRQQVSYCAQTPTLFGDTVYD 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 734 NILFGHrydaEFYEKTIKACALTIDLAILMDGDKTLvgEKGIS-LSGGQKARLSLARAVYARADTYLLDDPLAAVDEH 810
Cdd:PRK10247 100 NLIFPW----QIRNQQPDPAIFLDDLERFALPDTIL--TKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1322-1511 |
8.26e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.17 E-value: 8.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1322 PNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIG---LYDLRHKLSIIPQD---SQVFEGTVRENI-DPI 1394
Cdd:PRK10261 349 PGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDpyaSLDPRQTVGDSImEPL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1395 NQYT----DEAIWRA---LELSHLK-EHVLSMSNDgldaqltegggnLSVGQRQLLCLARAMLVPSKILVLDQATAAVDV 1466
Cdd:PRK10261 429 RVHGllpgKAAAARVawlLERVGLLpEHAWRYPHE------------FSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
9AYC_A 1467 ETDKVVQETIRTAFKDRTI--LTIAHRLNTIMD-SDRIIVLDNGKVAE 1511
Cdd:PRK10261 497 SIRGQIINLLLDLQRDFGIayLFISHDMAVVERiSHRVAVMYLGQIVE 544
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1011-1176 |
8.41e-08 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 55.56 E-value: 8.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1011 NAARYLAIYFA-LGIGSALATLIQTiVLWVFCTIHASKYLHNLMTNSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLG 1089
Cdd:cd18577 44 DDVNKYALYFVyLGIGSFVLSYIQT-ACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1090 RTFSQFFVNAvkVTFTITVICA----------TTWQFIFIIIPLSVFYIYYQQYYLRTSRELRRLDSITrspiyshfQET 1159
Cdd:cd18577 123 EKLGLLIQSL--STFIAGFIIAfiyswkltlvLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIA--------EEA 192
|
170
....*....|....*..
9AYC_A 1160 LGGLATVRGYSQQKRFS 1176
Cdd:cd18577 193 LSSIRTVKAFGGEEKEI 209
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
664-819 |
8.83e-08 |
|
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: 53.31 E-value: 8.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 664 PEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLScMLGDLFRV-KGFATVHGS--VAYVSQVPWIMNGTVKENILfgHR 740
Cdd:cd03223 11 PDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFR-ALAGLWPWgSGRIGMPEGedLLFLPQRPYLPLGTLREQLI--YP 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 741 YDAEfyektikacaltidlailmdgdktlvgekgisLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARHLIEHV 819
Cdd:cd03223 88 WDDV--------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL 134
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
618-820 |
9.20e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 56.74 E-value: 9.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 618 SIGRLFTFFTN-EELQ-PDSVQRLPKVKNIGDVAInigDDATFlwqRKPEYKVALKNINFQAKKGNLTCIVGKVGSGKTA 695
Cdd:COG4178 331 TVDRLAGFEEAlEAADaLPEAASRIETSEDGALAL---EDLTL---RTPDGRPLLEDLSLSLKPGERLLITGPSGSGKST 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 696 LLSCM--L-----GDLFRVKGfatvhGSVAYVSQVPWIMNGTVKENILFGH---RYDAEFYEKTIKACALTiDLAILMDg 765
Cdd:COG4178 405 LLRAIagLwpygsGRIARPAG-----ARVLFLPQRPYLPLGTLREALLYPAtaeAFSDAELREALEAVGLG-HLAERLD- 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
9AYC_A 766 dktLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARHLIEHVL 820
Cdd:COG4178 478 ---EEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR 529
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1312-1511 |
1.07e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 54.64 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSL--TLALFRMIEASEGNIVIDNI----AINEIGLYDLRHKLSIIPQDSQVFEG 1385
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLlrVLNLLEMPRSGTLNIAGNHFdfskTPSDKAIRELRRNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1386 -TVRENIdpInqytdEAIWRALELShlKEHVLSMSNDGLDA-QLTEGGG----NLSVGQRQLLCLARAMLVPSKILVLDQ 1459
Cdd:PRK11124 97 lTVQQNL--I-----EAPCRVLGLS--KDQALARAEKLLERlRLKPYADrfplHLSGGQQQRVAIARALMMEPQVLLFDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
9AYC_A 1460 ATAAVDVE-TDKVV------QETIRTafkdRTILT----IAHRLNTimdsdRIIVLDNGKVAE 1511
Cdd:PRK11124 168 PTAALDPEiTAQIVsiirelAETGIT----QVIVTheveVARKTAS-----RVVYMENGHIVE 221
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1320-1505 |
1.14e-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: 56.33 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1320 IKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIvidniaineiglyDLRHKLSIIPQD-SQVFEGTVRENI-DPINQY 1397
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-------------DEDLKISYKPQYiSPDYDGTVEEFLrSANTDD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1398 TDEAIWRALELSHLKEHVLsmsndgLDAQLTEgggnLSVGQRQLL----CLARamlvPSKILVLDQATAAVDVETDKVVQ 1473
Cdd:COG1245 430 FGSSYYKTEIIKPLGLEKL------LDKNVKD----LSGGELQRVaiaaCLSR----DADLYLLDEPSAHLDVEQRLAVA 495
|
170 180 190
....*....|....*....|....*....|....*
9AYC_A 1474 ETIR--TAFKDRTILTIAHRLNTI-MDSDRIIVLD 1505
Cdd:COG1245 496 KAIRrfAENRGKTAMVVDHDIYLIdYISDRLMVFE 530
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
976-1175 |
1.18e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 55.54 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 976 CVFILF-IVISMFLSVMGNVWLKH-WSEVNsrygsnpnaaRYLAIYFALGIGSALATLIQtivlWVFCTIHASKYLHNL- 1052
Cdd:cd18578 23 AVFPVFaILFSKLISVFSLPDDDElRSEAN----------FWALMFLVLAIVAGIAYFLQ----GYLFGIAGERLTRRLr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1053 --MTNSVLRAPMTFF---ETTPiGRILNRFSNDIYKVDALLGRTFSQFFVNAVKVTFTITVICATTWQF---IFIIIPLS 1124
Cdd:cd18578 89 klAFRAILRQDIAWFddpENST-GALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLalvGLATVPLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
9AYC_A 1125 VFYIYYQQYYLrTSRELRRLDSITRSPIYSHfqETLGGLATVRGYSQQKRF 1175
Cdd:cd18578 168 LLAGYLRMRLL-SGFEEKNKKAYEESSKIAS--EAVSNIRTVASLTLEDYF 215
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
667-860 |
1.19e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.83 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDL--------FRVKGFATVHGS----------------VAYVSQ 722
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgARVTGDVTLNGEplaaidaprlarlravLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 723 VPWIMngTVKENILFGHrydaefYEKTIKACALT------IDLAILMDGDKTLVGEKGISLSGGQKARLSLARAV----- 791
Cdd:PRK13547 94 PAFAF--SAREIVLLGR------YPHARRAGALThrdgeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 792 ---YARADTY-LLDDPLAAVD-EHVARhliehvlgpngLLHTKTKVLATNKVSALSI----------ADSIALLDNGEIT 856
Cdd:PRK13547 166 phdAAQPPRYlLLDEPTAALDlAHQHR-----------LLDTVRRLARDWNLGVLAIvhdpnlaarhADRIAMLADGAIV 234
|
....
9AYC_A 857 QQGT 860
Cdd:PRK13547 235 AHGA 238
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1058-1247 |
1.34e-07 |
|
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: 54.80 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1058 LRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTFSQFFVNAVKVTFTITVICATTWQ---FIFIIIP-LSVFYIYYQQY 1133
Cdd:cd18576 80 QRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKltlLMLATVPvVVLVAVLFGRR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1134 YLRTSRElrRLDSITRSpiYSHFQETLGGLATVRGYSQQ----KRFSHINQcridnnmSAFYPSINANRWLAyrleLIGS 1209
Cdd:cd18576 160 IRKLSKK--VQDELAEA--NTIVEETLQGIRVVKAFTREdyeiERYRKALE-------RVVKLALKRARIRA----LFSS 224
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
9AYC_A 1210 IIILGAATLSVFRL-------KQGTLTAGMVGLSLSYALQITQTL 1247
Cdd:cd18576 225 FIIFLLFGAIVAVLwyggrlvLAGELTAGDLVAFLLYTLFIAGSI 269
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1314-1523 |
1.65e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 55.10 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1314 KHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVI---DNIAINEIGLYDLRHKLSIIPQD---SQVFEGTV 1387
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlgkDLLGMKDDEWRAVRSDIQMIFQDplaSLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1388 RENI-DPINQYTDEaiwraLELSHLKEHVLS-MSNDGLDAQLTegggN-----LSVGQRQLLCLARAMLVPSKILVLDQA 1460
Cdd:PRK15079 118 GEIIaEPLRTYHPK-----LSRQEVKDRVKAmMLKVGLLPNLI----NrypheFSGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 1461 TAAVDVETDKVVQETIRTAFKDR--TILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQLLSDNK 1523
Cdd:PRK15079 189 VSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1285-1511 |
1.69e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.75 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1285 RPPKEWPSqgdIKFNNYSTRYrPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEI 1364
Cdd:PRK10522 315 QAFPDWQT---LELRNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1365 GLYDLRHKLSIIPQDSQVFEGTvrenIDPINQYTDEAI---WraleLSHLK-EHVLSMSndglDAQLTEggGNLSVGQRQ 1440
Cdd:PRK10522 391 QPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALvekW----LERLKmAHKLELE----DGRISN--LKLSKGQKK 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
9AYC_A 1441 LLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKD--RTILTIAHRLNTIMDSDRIIVLDNGKVAE 1511
Cdd:PRK10522 457 RLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
667-808 |
1.75e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 54.32 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGSV--------AYVSQ----VPWImngTVKEN 734
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPvegpgaerGVVFQneglLPWR---NVQDN 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
9AYC_A 735 ILFGHRYDAEFYEKTIKACALTIDLAILMDGDKTLVGEkgisLSGGQKARLSLARAVYARADTYLLDDPLAAVD 808
Cdd:PRK11248 91 VAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQ----LSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
668-856 |
1.77e-07 |
|
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: 52.43 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 668 VALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGsvayvsqvpwimngtvkENILFGHRYDAEfye 747
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-----------------KEVSFASPRDAR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 748 ktikacaltidlailmdgdktlvgEKGIS----LSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARHLIEHV--LG 821
Cdd:cd03216 74 ------------------------RAGIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIrrLR 129
|
170 180 190
....*....|....*....|....*....|....*.
9AYC_A 822 PNGllhtKTKVLATNKVS-ALSIADSIALLDNGEIT 856
Cdd:cd03216 130 AQG----VAVIFISHRLDeVFEIADRVTVLRDGRVV 161
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
667-859 |
2.07e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 54.43 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHG---------SVAYVSQVPWIMN----GTVKE 733
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpsrarhARQRVGVVPQFDNldpdFTVRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 734 NILFGHRYDAEFYEKTIKACALTIDLAILMDGDKTLVGEkgisLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHvAR 813
Cdd:PRK13537 100 NLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ-AR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
9AYC_A 814 HLIEHVLgpNGLLHT-KTKVLATNKV-SALSIADSIALLDNGEITQQG 859
Cdd:PRK13537 175 HLMWERL--RSLLARgKTILLTTHFMeEAERLCDRLCVIEEGRKIAEG 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
667-863 |
2.07e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 55.46 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLF----RVKGFATVHgsVAYVSQVPWIMNG--TVKENIlfgHR 740
Cdd:COG0488 328 KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEpdsgTVKLGETVK--IGYFDQHQEELDPdkTVLDEL---RD 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 741 YDAEFYEKTIKACaltidLAILM-DGDK--TLVGekgiSLSGGQKARLSLARAVYARADTYLLDDP--------LAAVDE 809
Cdd:COG0488 403 GAPGGTEQEVRGY-----LGRFLfSGDDafKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPtnhldietLEALEE 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 810 HVA------------RHLIEhvlgpngllhtktkvlatnkvsalSIADSIALLDNGEITQ-QGTYDE 863
Cdd:COG0488 474 ALDdfpgtvllvshdRYFLD------------------------RVATRILEFEDGGVREyPGGYDD 516
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1314-1510 |
2.24e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.44 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1314 KHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYD-LRHKLSIIPQDSQV----FEGTVR 1388
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDRQSsglyLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1389 ENIDPINqYTDEAIW--------------RAL--ELSHLKEHVLSMSndgldaqltegGGNlsvgQRQLLcLARAMLVPS 1452
Cdd:PRK15439 360 WNVCALT-HNRRGFWikparenavleryrRALniKFNHAEQAARTLS-----------GGN----QQKVL-IAKCLEASP 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1453 KILVLDQATAAVDVETDKVVQETIRTAFKDRT-ILTIAHRLNTIMD-SDRIIVLDNGKVA 1510
Cdd:PRK15439 423 QLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVaVLFISSDLEEIEQmADRVLVMHQGEIS 482
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1313-1523 |
2.36e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 53.86 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1313 LKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMI---EASEGNIVIDNIAINEIGLY--DLR----HKLSIIPQDSQVF 1383
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGRLarDIRksraNTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1384 EGTVRENIdPINQYTDEAIWRALeLSHL----KEHVL-SMSNDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLD 1458
Cdd:PRK09984 100 RLSVLENV-LIGALGSTPFWRTC-FSWFtreqKQRALqALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 1459 QATAAVDVETDKVVQETIRTAFKDR--TILTIAHRLNTIMD-SDRIIVLDNGKVAeFDSPGQLLSDNK 1523
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALRyCERIVALRQGHVF-YDGSSQQFDNER 244
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
777-864 |
2.42e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 55.04 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 777 LSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARHLIEHVLGPNGLlHTKTKVLATNKV-SALSIADSIALLDNGEI 855
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAK-HQRTIVFISHDLdEAMRIGDRIAIMQNGEV 243
|
....*....
9AYC_A 856 TQQGTYDEI 864
Cdd:PRK10070 244 VQVGTPDEI 252
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1312-1526 |
2.80e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 54.32 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLT-------------------------------------LALFRMIEasegni 1354
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLriiaglehqtsghirfhgtdvsrlhardrkvgfvfqhYALFRHMT------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1355 VIDNIAINeiglydlrhkLSIIPQDSqvfegtvRENIDPINQytdeAIWRALE---LSHLKEHVLSmsndgldaqltegg 1431
Cdd:PRK10851 91 VFDNIAFG----------LTVLPRRE-------RPNAAAIKA----KVTQLLEmvqLAHLADRYPA-------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1432 gNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAFKDR--TILTIAHRLNTIMD-SDRIIVLDNGK 1508
Cdd:PRK10851 136 -QLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEAMEvADRVVVMSQGN 214
|
250
....*....|....*...
9AYC_A 1509 VAEFDSPGQLLSDNKSLF 1526
Cdd:PRK10851 215 IEQAGTPDQVWREPATRF 232
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
1007-1250 |
3.00e-07 |
|
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: 53.70 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1007 GSNPNAARYLAIYFALGIGSALATLIQtivlwVFCTIHASKYLHNLMTN----SVLRAPMTFFETTPIGRILNRFSNDIY 1082
Cdd:cd18572 30 GSREAFYRAVLLLLLLSVLSGLFSGLR-----GGCFSYAGTRLVRRLRRdlfrSLLRQDIAFFDATKTGELTSRLTSDCQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1083 KVDALLGRTFSQFFVNAVKVTFTITVICATTWQF---IFIIIPLsVFYIY--YQQYYLRTSRELRrlDSITRSpiYSHFQ 1157
Cdd:cd18572 105 KVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLtllAFITVPV-IALITkvYGRYYRKLSKEIQ--DALAEA--NQVAE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1158 ETLGGLATVRGYS----QQKRFSH-INQCRIDNNMSAFYPSINAnrWLAYRLELIGSIIILGAATLSVF--RLKQGTLTA 1230
Cdd:cd18572 180 EALSNIRTVRSFAteerEARRYERaLDKALKLSVRQALAYAGYV--AVNTLLQNGTQVLVLFYGGHLVLsgRMSAGQLVT 257
|
250 260
....*....|....*....|
9AYC_A 1231 GMVglslsYALQITQTLNWI 1250
Cdd:cd18572 258 FML-----YQQQLGEAFQSL 272
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
669-859 |
3.02e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.59 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 669 ALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGSVAYVSQVPWIMN---------------GTVKE 733
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSkvglvfqdpddqvfsSTVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 734 NILFGHRY----DAEFYEKTIKACAltidlAILMdgdKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDE 809
Cdd:PRK13647 100 DVAFGPVNmgldKDEVERRVEEALK-----AVRM---WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
9AYC_A 810 HVARHLIE--HVLGPNGllhtKTKVLATNKVS-ALSIADSIALLDNGEITQQG 859
Cdd:PRK13647 172 RGQETLMEilDRLHNQG----KTVIVATHDVDlAAEWADQVIVLKEGRVLAEG 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1316-1509 |
3.11e-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: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1316 INIHIKPNEKVGIVGRTGAGKSSLTLALFRMIE-ASEGNIVIDNIAIN-EIGLYDLRHKLSIIPQDSQ----VFEGTVRE 1389
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDiRNPAQAIRAGIAMVPEDRKrhgiVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1390 NI--DPINQYTDEA-IWRALELSHLKEHVLSMSNDGLDAQLTEGGgnLSVGQRQLLCLARAMLVPSKILVLDQATAAVDV 1466
Cdd:TIGR02633 359 NItlSVLKSFCFKMrIDAAAELQIIGSAIQRLKVKTASPFLPIGR--LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
9AYC_A 1467 ----ETDKVVQETIRTAFkdrTILTIAHRLNTIMD-SDRIIVLDNGKV 1509
Cdd:TIGR02633 437 gakyEIYKLINQLAQEGV---AIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
1021-1169 |
3.29e-07 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the 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 the ABC_6TM exporter 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.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 53.85 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1021 ALGIGSALATLIQTiVLWVFCTIHASKYLHNLMTNSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTFSQFFVNAV 1100
Cdd:cd18784 44 LLAIASSVAAGIRG-GLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLV 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
9AYC_A 1101 KVTFTITVICATTWQ---FIFIIIPLsVFYI--YYQQYYLRTSRELRrlDSITRSPiySHFQETLGGLATVRGY 1169
Cdd:cd18784 123 KAIGVIVFMFKLSWQlslVTLIGLPL-IAIVskVYGDYYKKLSKAVQ--DSLAKAN--EVAEETISSIRTVRSF 191
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
664-869 |
5.26e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 53.29 E-value: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 664 PEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHG-----------------SVAYVSQVP-- 724
Cdd:PRK13641 17 PMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkKVSLVFQFPea 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 725 WIMNGTVKENILFGHRyDAEFYEKTIKACALTIDLAILMDGDktLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPL 804
Cdd:PRK13641 97 QLFENTVLKDVEFGPK-NFGFSEDEAKEKALKWLKKVGLSED--LISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 805 AAVDEHVARHLIEHVLGPNGLLHtkTKVLATNKVSALS-IADSIALLDNGEITQQGTYDEITKDAD 869
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKAGH--TVILVTHNMDDVAeYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
773-869 |
5.60e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 52.34 E-value: 5.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 773 KGISLSGGQKARLSLARAVYARADTYLLDDPLAAVD-------EHVARHLIEHVLGpngllhtktkVLAT--NKVSALSI 843
Cdd:COG1137 133 KAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpiavadiQKIIRHLKERGIG----------VLITdhNVRETLGI 202
|
90 100
....*....|....*....|....*.
9AYC_A 844 ADSIALLDNGEITQQGTYDEITKDAD 869
Cdd:COG1137 203 CDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
664-817 |
5.78e-07 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 52.02 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 664 PEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGD------LFRVKGFATVH---GSVAYVSQ--------VPWI 726
Cdd:cd03292 11 PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEelptsgTIRVNGQDVSDlrgRAIPYLRRkigvvfqdFRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 727 MNGTVKENILFGHRYDAEFYEKTIKACALTIDLAILMDGDKTLVGEkgisLSGGQKARLSLARAVYARADTYLLDDPLAA 806
Cdd:cd03292 91 PDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAE----LSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170
....*....|.
9AYC_A 807 VDEHVARHLIE 817
Cdd:cd03292 167 LDPDTTWEIMN 177
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
670-859 |
8.26e-07 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 53.31 E-value: 8.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 670 LKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHG-------------SVAYVSQVPWI-MNGTVKENI 735
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASVPQDTSLsFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 736 LFG---HRYDAEFYEKTIKAcalTIDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVA 812
Cdd:PRK09536 99 EMGrtpHRSRFDTWTETDRA---AVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
9AYC_A 813 RHLIEHV--LGPNGllhtKTKVLATNKVS-ALSIADSIALLDNGEITQQG 859
Cdd:PRK09536 176 VRTLELVrrLVDDG----KTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
667-867 |
9.80e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 52.11 E-value: 9.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTA---LLSCML-------------GDLFRVKGFATVHGSVAYVSQVP--WIMN 728
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLlpddnpnskitvdGITLTAKTVWDIREKVGIVFQNPdnQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 729 GTVKENILFGHRYDAEFYEKTIKACALTIDLAILMDGDKTlvgeKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVD 808
Cdd:PRK13640 100 ATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDS----EPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
9AYC_A 809 ----EHVARhLIEHVLGPNGLlhtkTKVLATNKVSALSIADSIALLDNGEITQQGTYDEITKD 867
Cdd:PRK13640 176 pagkEQILK-LIRKLKKKNNL----TVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
1013-1231 |
1.04e-06 |
|
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: 52.05 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1013 ARYLAIYFALGIGSALATLIQTIVLWVFctihASKYLHNL---MTNSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLG 1089
Cdd:cd18551 36 GGLLALLVALFLLQAVLSALSSYLLGRT----GERVVLDLrrrLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELIT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1090 RTFSQFFVNAVKVTFTITVICATTWQ---FIFIIIPLSVFYIYY-----QQYYLRTSRELRRLDsitrspiySHFQETLG 1161
Cdd:cd18551 112 SGLPQLVTGVLTVVGAVVLMFLLDWVltlVTLAVVPLAFLIILPlgrriRKASKRAQDALGELS--------AALERALS 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 1162 GLATVRGYSQQKRFSHINQCRIDNnmsAFYPSINANRWLAyrleLIGSIIILG--AATLSVF-----RLKQGTLTAG 1231
Cdd:cd18551 184 AIRTVKASNAEERETKRGGEAAER---LYRAGLKAAKIEA----LIGPLMGLAvqLALLVVLgvggaRVASGALTVG 253
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
660-817 |
1.09e-06 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 51.01 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 660 WQRKPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFR--VKGFATVHG----------SVAYVSQvpwim 727
Cdd:cd03213 15 SSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGrpldkrsfrkIIGYVPQ----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 728 ngtvkENILFGHRydaefyekTIKAcalTIDLAILMDGdktlvgekgisLSGGQKARLSLARAVYARADTYLLDDPLAAV 807
Cdd:cd03213 90 -----DDILHPTL--------TVRE---TLMFAAKLRG-----------LSGGERKRVSIALELVSNPSLLFLDEPTSGL 142
|
170
....*....|
9AYC_A 808 DEHVARHLIE 817
Cdd:cd03213 143 DSSSALQVMS 152
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
654-867 |
1.21e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 52.09 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 654 DDATFLWQRKPEY-KVALKNINFQAKKGNLTCIVGKVGSGKTALL------------SCMLGDL-----FRVKGFATVHG 715
Cdd:PRK13646 6 DNVSYTYQKGTPYeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIqninallkpttgTVTVDDItithkTKDKYIRPVRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 716 SVAYVSQVP--WIMNGTVKENILFGHR-YDAEFYEKTIKACALTIDLAILMDgdktLVGEKGISLSGGQKARLSLARAVY 792
Cdd:PRK13646 86 RIGMVFQFPesQLFEDTVEREIIFGPKnFKMNLDEVKNYAHRLLMDLGFSRD----VMSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 793 ARADTYLLDDPLAAVDEHvARHLIEHVLGPNGLLHTKTKVLATNKVSALS-IADSIALLDNGEITQQGTYDEITKD 867
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQ-SKRQVMRLLKSLQTDENKTIILVSHDMNEVArYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1312-1509 |
1.58e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.18 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLT--LALFRMIEASEGNIVIDNIAINEIGLyDLRHKLSI---------IPQDS 1380
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSkvIAGHPAYKILEGDILFKGESILDLEP-EERAHLGIflafqypieIPGVS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1381 ------------QVFEGtvRENIDPINQYtdEAIWRALELSHLKEHVLSMS-NDGldaqltegggnLSVGQR---QLLCL 1444
Cdd:CHL00131 101 nadflrlaynskRKFQG--LPELDPLEFL--EIINEKLKLVGMDPSFLSRNvNEG-----------FSGGEKkrnEILQM 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 1445 AramLVPSKILVLDQATAAVDVETDKVVQETIRT-AFKDRTILTIAH--RLNTIMDSDRIIVLDNGKV 1509
Cdd:CHL00131 166 A---LLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKI 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
667-864 |
2.10e-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: 52.11 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGdlfrVKGFATVHGSVAY-VSQVP---WI------------MNGT 730
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRG----MDQYEPTSGRIIYhVALCEkcgYVerpskvgepcpvCGGT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 731 VK-ENILFGHRYDAEFYEKTiKACALTIDLAILMDGDKTLV-------------GEKGI--------------------- 775
Cdd:TIGR03269 89 LEpEEVDFWNLSDKLRRRIR-KRIAIMLQRTFALYGDDTVLdnvlealeeigyeGKEAVgravdliemvqlshrithiar 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 776 SLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARhLIEHVLGPNGLLHTKTKVLATNKVSALS-IADSIALLDNGE 854
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEEAVKASGISMVLTSHWPEVIEdLSDKAIWLENGE 246
|
250
....*....|
9AYC_A 855 ITQQGTYDEI 864
Cdd:TIGR03269 247 IKEEGTPDEV 256
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
667-816 |
2.24e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 51.76 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGS------------VAYVSQVPWI-MNGTVKE 733
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVpvpararlararIGVVPQFDNLdLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 734 NILFGHRYdaeFYEKTIKACALT---IDLAILMDGDKTLVGEkgisLSGGQKARLSLARAVYARADTYLLDDPLAAVDEH 810
Cdd:PRK13536 134 NLLVFGRY---FGMSTREIEAVIpslLEFARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPH 206
|
....*.
9AYC_A 811 vARHLI 816
Cdd:PRK13536 207 -ARHLI 211
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1311-1508 |
2.45e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 50.76 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1311 LVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINeiGLYD---LRHKLSIIPQDSQVF-EGT 1386
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE--GLPGhqiARMGVVRTFQHVRLFrEMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1387 VRENIdPINQYT--------------------DEAIWRAlelSHLKEHVlsmsndGLDAQLTEGGGNLSVGQRQLLCLAR 1446
Cdd:PRK11300 97 VIENL-LVAQHQqlktglfsgllktpafrraeSEALDRA---ATWLERV------GLLEHANRQAGNLAYGQQRRLEIAR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 1447 AMLVPSKILVLDQATAAVDVETDKVVQETI---RTAFkDRTILTIAHRLNTIMD-SDRIIVLDNGK 1508
Cdd:PRK11300 167 CMVTQPEILMLDEPAAGLNPKETKELDELIaelRNEH-NVTVLLIEHDMKLVMGiSDRIYVVNQGT 231
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1310-1514 |
2.48e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 51.41 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1310 DLVLKhINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVidniaINEIGLYDLRHKLSIIP---------QDS 1380
Cdd:PRK11144 12 DLCLT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIV-----LNGRVLFDAEKGICLPPekrrigyvfQDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1381 QVF-----EGTVRENIDPINQYTDEAIWRALELSHLkehvlsmsndgldaqLTEGGGNLSVGQRQLLCLARAMLVPSKIL 1455
Cdd:PRK11144 86 RLFphykvRGNLRYGMAKSMVAQFDKIVALLGIEPL---------------LDRYPGSLSGGEKQRVAIGRALLTAPELL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 1456 VLDQATAAVDVETDKVV-------QETIRTAfkdrtILTIAHRLNTIMD-SDRIIVLDNGKVAEFDS 1514
Cdd:PRK11144 151 LMDEPLASLDLPRKRELlpylerlAREINIP-----ILYVSHSLDEILRlADRVVVLEQGKVKAFGP 212
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
663-860 |
2.52e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 52.71 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 663 KPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHG-----SVAYVSQVpwiMNGTVKENILF 737
Cdd:TIGR01257 939 EPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietNLDAVRQS---LGMCPQHNILF 1015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 738 GHRYDAE---FYE----KTIKACALTIDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEH 810
Cdd:TIGR01257 1016 HHLTVAEhilFYAqlkgRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
9AYC_A 811 VARHLIEHVLGPNGllhTKTKVLATNKVSALSI-ADSIALLDNGEITQQGT 860
Cdd:TIGR01257 1096 SRRSIWDLLLKYRS---GRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT 1143
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
669-867 |
2.78e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 51.00 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 669 ALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDL---------------FRVKGFATVHGSVAYVSQVP--WIMNGTV 731
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILkpssgrilfdgkpidYSRKGLMKLRESVGMVFQDPdnQLFSASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 732 KENILFGhRYDAEFYEKTIKAcalTIDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHV 811
Cdd:PRK13636 101 YQDVSFG-AVNLKLPEDEVRK---RVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 812 ARHLIEHVLGPNGLLHTkTKVLATNKVSALSI-ADSIALLDNGEITQQGTYDEITKD 867
Cdd:PRK13636 177 VSEIMKLLVEMQKELGL-TIIIATHDIDIVPLyCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1315-1506 |
2.83e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.80 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1315 HINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIG-------LYdLRHKLSIIPqdsqvfEGTV 1387
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRdeyhqdlLY-LGHQPGIKT------ELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1388 RENID---PINQ-YTDEAIWRALELSHLK--EHVLSmsndgldaqlteggGNLSVGQRQLLCLARAMLVPSKILVLDQAT 1461
Cdd:PRK13538 92 LENLRfyqRLHGpGDDEALWEALAQVGLAgfEDVPV--------------RQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
9AYC_A 1462 AAVDVETDKVVQETIRtAFKDR---TILTIAHRLNTIMDSDRIIVLDN 1506
Cdd:PRK13538 158 TAIDKQGVARLEALLA-QHAEQggmVILTTHQDLPVASDKVRKLRLGQ 204
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1313-1513 |
2.90e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.93 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1313 LKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYD-LRHKLSIIPQDSQ----VFEGTV 1387
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISEDRKrdglVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1388 REN--IDPINQYTDEAIwralELSHLKEHV--------LSMSNDGLDAQLteggGNLSVGQRQLLCLARAMLVPSKILVL 1457
Cdd:PRK10762 348 KENmsLTALRYFSRAGG----SLKHADEQQavsdfirlFNIKTPSMEQAI----GLLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1458 DQATAAVDVETDKVVQETIrTAFKDR--TILTIAHRLNTIMD-SDRIIVLDNGKV-AEFD 1513
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLI-NQFKAEglSIILVSSEMPEVLGmSDRILVMHEGRIsGEFT 478
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
667-815 |
3.17e-06 |
|
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: 49.80 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKG------------FATVHGSVAYVSQVPWIMNG-TVKE 733
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGrvllnggpldfqRDSIARGLLYLGHAPGIKTTlSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 734 NILFGHRYDAEfyEKTIKACAlTIDLAILMDgdkTLVGekgiSLSGGQKARLSLARAVYARADTYLLDDPLAAVD----- 808
Cdd:cd03231 93 NLRFWHADHSD--EQVEEALA-RVGLNGFED---RPVA----QLSAGQQRRVALARLLLSGRPLWILDEPTTALDkagva 162
|
170
....*....|
9AYC_A 809 ---EHVARHL 815
Cdd:cd03231 163 rfaEAMAGHC 172
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1312-1520 |
3.26e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 50.37 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQVFEGTVRENI 1391
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1392 DPINQYTDEAI---WRALELSHLKEhvlSMSNDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVET 1468
Cdd:PRK10253 102 VARGRYPHQPLftrWRKEDEEAVTK---AMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 1469 D----KVVQETIRTafKDRTILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQLLS 1520
Cdd:PRK10253 179 QidllELLSELNRE--KGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIVT 233
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1324-1512 |
4.12e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.47 E-value: 4.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1324 EKVGIVGRTGAGKSSLTLALFRMIE-ASEGNIVIDN--IAINEIgLYDLRHKLSIIPQDSQ----VFEGTVRENID--PI 1394
Cdd:PRK13549 289 EILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGkpVKIRNP-QQAIAQGIAMVPEDRKrdgiVPVMGVGKNITlaAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1395 NQYTD-EAIWRALELSHLKEHVLSMSNDGLDAQLTEGggNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDV----ETD 1469
Cdd:PRK13549 368 DRFTGgSRIDDAAELKTILESIQRLKVKTASPELAIA--RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVgakyEIY 445
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
9AYC_A 1470 KV----VQETIrtafkdrTILTIAHRLNTIMD-SDRIIVLDNGKV-AEF 1512
Cdd:PRK13549 446 KLinqlVQQGV-------AIIVISSELPEVLGlSDRVLVMHEGKLkGDL 487
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
667-864 |
4.66e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 50.09 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALL-----------------SCMLG--DLFRVKGFATVHGSVAYVSQVPWIM 727
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLrtlnrmndkvsgyrysgDVLLGgrSIFNYRDVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 728 NGTVKENILFGHRYDAEFYEKTIKACALTIDLAI-LMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAA 806
Cdd:PRK14271 114 PMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVgLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 807 VDEHVARHLIEHVlgpNGLLHTKTKVLAT-NKVSALSIADSIALLDNGEITQQGTYDEI 864
Cdd:PRK14271 194 LDPTTTEKIEEFI---RSLADRLTVIIVThNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
673-838 |
5.12e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.08 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 673 INFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGS----------VAYVSQVPWI-MNGTVKENILFG--- 738
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsrfMAYLGHLPGLkADLSTLENLHFLcgl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 739 HRYDAefyeKTIKACALTIdlAILMDGDKTLVGEkgisLSGGQKARLSLARAVYARADTYLLDDPLAAVDEH----VARH 814
Cdd:PRK13543 110 HGRRA----KQMPGSALAI--VGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEgitlVNRM 179
|
170 180
....*....|....*....|....
9AYC_A 815 LIEHVLGPNGLLHTKTKVLATNKV 838
Cdd:PRK13543 180 ISAHLRGGGAALVTTHGAYAAPPV 203
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
669-877 |
5.98e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 49.63 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 669 ALKNINFQAKKGNLTCIVGKVGSGKTALLSCM----------------LGDLFRVKG-----FATVHGSVAYVSQVPWIM 727
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLsglitgdksagshielLGRTVQREGrlardIRKSRANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 728 NG-TVKENILFGH-------RYDAEFYEKTIKACALTidlAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYL 799
Cdd:PRK09984 99 NRlSVLENVLIGAlgstpfwRTCFSWFTREQKQRALQ---ALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVIL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 800 LDDPLAAVDEHVARHLIEHVLGPN---GLlhtkTKVLATNKVS-ALSIADSIALLDNGEITQQGTYDEITKDADSPLWKL 875
Cdd:PRK09984 176 ADEPIASLDPESARIVMDTLRDINqndGI----TVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNERFDHLYRS 251
|
..
9AYC_A 876 LN 877
Cdd:PRK09984 252 IN 253
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
670-837 |
6.91e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.79 E-value: 6.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 670 LKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGS------VAYVSQVPWI-------MNGTVKENIL 736
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlCTYQKQLCFVghrsginPYLTLRENCL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 737 fghrYDAEFyektiKACALTID-LAILMDGDKTLVGEKGIsLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARHL 815
Cdd:PRK13540 97 ----YDIHF-----SPGAVGITeLCRLFSLEHLIDYPCGL-LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170 180
....*....|....*....|....*.
9AYC_A 816 I----EHVLGPNGLLHTKTKVLATNK 837
Cdd:PRK13540 167 ItkiqEHRAKGGAVLLTSHQDLPLNK 192
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
670-872 |
6.97e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 49.46 E-value: 6.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 670 LKNINFQAKKGNLTCIVGKVGSGKTALLSCM-----LGDLFRVKGFATVHGSVAYVSQVPWIM----------------N 728
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIEvrrevgmvfqypnpfpH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 729 GTVKENILFGHRYD--AEFYEKTIKACALTIDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAA 806
Cdd:PRK14267 100 LTIYDNVAIGVKLNglVKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 807 VDEhVARHLIEHVLGPngLLHTKTKVLATNK-VSALSIADSIALLDNGEITQQGTYDEITKDADSPL 872
Cdd:PRK14267 180 IDP-VGTAKIEELLFE--LKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHEL 243
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
668-867 |
8.22e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 50.40 E-value: 8.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 668 VALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDL------FRVKG----FATVHGS----VAYVSQ----VPWImng 729
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYqpdsgeILLDGepvrFRSPRDAqaagIAIIHQelnlVPNL--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 730 TVKENILFGH------RYD-AEFYEKTIKACA---LTIDLAilmdgdkTLVGEkgisLSGGQKARLSLARAVYARADTYL 799
Cdd:COG1129 95 SVAENIFLGReprrggLIDwRAMRRRARELLArlgLDIDPD-------TPVGD----LSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 800 LDDPLAAVDEHVARHLIEHVlgpngllhtktKVLATNKVS----------ALSIADSIALLDNGEITQQGTYDEITKD 867
Cdd:COG1129 164 LDEPTASLTEREVERLFRII-----------RRLKAQGVAiiyishrldeVFEIADRVTVLRDGRLVGTGPVAELTED 230
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1312-1526 |
8.96e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 49.72 E-value: 8.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLtLALFRMIEA-SEGNIVIDNiaineiglYDLRHKlSIIPQD-SQVFEG---- 1385
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTV-LRLVAGLEKpTEGQIFIDG--------EDVTHR-SIQQRDiCMVFQSyalf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1386 ---TVRENI-----------DPINQYTDEAiwraLELSHLkehvlsmsnDGLDAQLTEgggNLSVGQRQLLCLARAMLVP 1451
Cdd:PRK11432 91 phmSLGENVgyglkmlgvpkEERKQRVKEA----LELVDL---------AGFEDRYVD---QISGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 1452 SKILVLDQATAAVDVETDKVVQETIRTAFK--DRTILTIAH-RLNTIMDSDRIIVLDNGKVAEFDSPGQLLSDNKSLF 1526
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
401-818 |
9.29e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 50.52 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 401 IKSALTALIYQKSL------VLSNEASGLSstgDIVNLMSVDVQKLQDLTQWLNLIWSGPFQIIIcLYSlYKLLGNSMWV 474
Cdd:TIGR00954 166 FRVRLTRYLYSKYLsgftfyKVSNLDSRIQ---NPDQLLTQDVEKFCDSVVELYSNLTKPILDVI-LYS-FKLLTALGSV 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 475 GV-IILVIMMPLNSFLMRIQKKLQKSQM---KYKDERTRVISEILNNIKSLKLYAWEKPYREKLEEVRN------NKELK 544
Cdd:TIGR00954 241 GPaGLFAYLFATGVVLTKLRPPIGKLTVeeqALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETVMSSFYrlvehlNLIIK 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 545 nlTKLGCYMA---VTSFQFNIVPFLVscCTFAVFVYTEDRALTTDLVFPALTLFNllSFPLMI-IPMVLNSFIEASVSIG 620
Cdd:TIGR00954 321 --FRFSYGFLdniVAKYTWSAVGLVA--VSIPIFDKTHPAFLEMSEEELMQEFYN--NGRLLLkAADALGRLMLAGRDMT 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 621 RL--FTFFTNEELQP-DSVQRL-------PKVKNIGDVAIN----------IGDDATFLWQR----KPEYKVALKNINFQ 676
Cdd:TIGR00954 395 RLagFTARVDTLLQVlDDVKSGnfkrprvEEIESGREGGRNsnlvpgrgivEYQDNGIKFENiplvTPNGDVLIESLSFE 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 677 AKKGNLTCIVGKVGSGKTALLScMLGDLFRVK-GFATV--HGSVAYVSQVPWIMNGTVKENILFGHRYDaEFYEKTIKAC 753
Cdd:TIGR00954 475 VPSGNNLLICGPNGCGKSSLFR-ILGELWPVYgGRLTKpaKGKLFYVPQRPYMTLGTLRDQIIYPDSSE-DMKRRGLSDK 552
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
9AYC_A 754 ALtIDLAILMDGDKTLVGEKGIS--------LSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARHLIEH 818
Cdd:TIGR00954 553 DL-EQILDNVQLTHILEREGGWSavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRL 624
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
777-862 |
9.52e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 48.86 E-value: 9.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 777 LSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARHL--IEHVLGPNGLlhtkTKVLATNKVS-ALSIADSIALLDNG 853
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIvsIIRELAETGI----TQVIVTHEVEvARKTASRVVYMENG 217
|
....*....
9AYC_A 854 EITQQGTYD 862
Cdd:PRK11124 218 HIVEQGDAS 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
680-864 |
1.01e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 49.02 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 680 GNLTCIVGKVGSGKTALLScMLG-----------------DLFRVKGFATvhgSVAYV-SQVPWIMNGTVKENILFGH-- 739
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLK-MLGrhqppsegeilldaqplESWSSKAFAR---KVAYLpQQLPAAEGMTVRELVAIGRyp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 740 ------RYDAEFYEKtikacaltIDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDehvar 813
Cdd:PRK10575 113 whgalgRFGAADREK--------VEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD----- 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 814 hlIEHVLGPNGLLH--------TKTKVLATNKVSAlSIADSIALLDNGEITQQGTYDEI 864
Cdd:PRK10575 180 --IAHQVDVLALVHrlsqerglTVIAVLHDINMAA-RYCDYLVALRGGEMIAQGTPAEL 235
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
669-868 |
1.10e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 50.02 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 669 ALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGS--------------VAYVSQ------VpwIMN 728
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVPEdrkgegL--VLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 729 GTVKENI------------LFGHRYDAEFYEKTIKacaltiDLAILMDGDKTLVGekgiSLSGG--QKArlSLARAVYAR 794
Cdd:COG1129 345 LSIRENItlasldrlsrggLLDRRRERALAEEYIK------RLRIKTPSPEQPVG----NLSGGnqQKV--VLAKWLATD 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 795 ADTYLLDDPLAAVDehV-ARHLIEHVLgpNGLLHTKTKVLAtnkVS-----ALSIADSIALLDNGEITQQGTYDEITKDA 868
Cdd:COG1129 413 PKVLILDEPTRGID--VgAKAEIYRLI--RELAAEGKAVIV---ISselpeLLGLSDRILVMREGRIVGELDREEATEEA 485
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
777-864 |
1.40e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 48.50 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 777 LSGGQKARLSLARAVYARADTYLLDDPLAAVDEhVARHLIEHVLgpNGLLHTKTKVLAT-NKVSALSIADSIALLDNGEI 855
Cdd:PRK14246 154 LSGGQQQRLTIARALALKPKVLLMDEPTSMIDI-VNSQAIEKLI--TELKNEIAIVIVShNPQQVARVADYVAFLYNGEL 230
|
....*....
9AYC_A 856 TQQGTYDEI 864
Cdd:PRK14246 231 VEWGSSNEI 239
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
1061-1231 |
1.86e-05 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis 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: 349993 [Multi-domain] Cd Length: 295 Bit Score: 48.22 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1061 PMTFFETTPIGRILNRFSNDIYKVDALLGRTFSQFFVNAVKVTFTITVICATTWQ---FIFIIIPLSVFYIYYQQYYLR- 1136
Cdd:cd18549 89 SFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPltlIVFALLPLMIIFTIYFNKKMKk 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1137 TSRELRRldsiTRSPIYSHFQETLGGLATVRGYS----QQKRFSHINQ------CRIDNNMSAFYPSINAnrwlayrLEL 1206
Cdd:cd18549 169 AFRRVRE----KIGEINAQLEDSLSGIRVVKAFAneeyEIEKFDEGNDrfleskKKAYKAMAYFFSGMNF-------FTN 237
|
170 180
....*....|....*....|....*
9AYC_A 1207 IGSIIILGAATLSVFrlkQGTLTAG 1231
Cdd:cd18549 238 LLNLVVLVAGGYFII---KGEITLG 259
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
670-864 |
2.01e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 48.17 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 670 LKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGS-------------VAYVSQVP--WIMNGTVKEN 734
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGElltaenvwnlrrkIGMVFQNPdnQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 735 ILFGHRYDAEFYEKTIKacalTIDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEhVARH 814
Cdd:PRK13642 103 VAFGMENQGIPREEMIK----RVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDP-TGRQ 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
9AYC_A 815 LIEHVLGPNGLLHTKTKVLATNKVSALSIADSIALLDNGEITQQGTYDEI 864
Cdd:PRK13642 178 EIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1322-1508 |
2.07e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1322 PNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAIN--------EIGLYDLRHKLSIIPQDsqvfegTVRENI-- 1391
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssqEAGIGIIHQELNLIPQL------TIAENIfl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1392 --DPINQYTdeAI-WRALE------LSHLKehvLSMSNDGLdaqltegGGNLSVGQRQLLCLARAMLVPSKILVLDQATA 1462
Cdd:PRK10762 103 grEFVNRFG--RIdWKKMYaeadklLARLN---LRFSSDKL-------VGELSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
9AYC_A 1463 AV-DVETD---KVVQEtirTAFKDRTILTIAHRLNTIMD-SDRIIVLDNGK 1508
Cdd:PRK10762 171 ALtDTETEslfRVIRE---LKSQGRGIVYISHRLKEIFEiCDDVTVFRDGQ 218
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
669-869 |
2.18e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.20 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 669 ALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGS-----------------VAYVSQVP--WIMNG 729
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitstsknkdikqirkkVGLVFQFPesQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 730 TVKENILFGHRydaEFYEKTIKACALTIDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDE 809
Cdd:PRK13649 102 TVLKDVAFGPQ---NFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
9AYC_A 810 HVARHLIEHVLGpnglLHTK--TKVLATNKVSALS-IADSIALLDNGEITQQGTYDEITKDAD 869
Cdd:PRK13649 179 KGRKELMTLFKK----LHQSgmTIVLVTHLMDDVAnYADFVYVLEKGKLVLSGKPKDIFQDVD 237
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
670-867 |
2.41e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 47.58 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 670 LKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGS--------------VAYVSQVPWIMNG-TVKEN 734
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplhararrgIGYLPQEASIFRRlSVYDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 735 IL--FGHRYDAEFYEKTIKACALTIDLAIlmdgdKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVA 812
Cdd:PRK10895 99 LMavLQIRDDLSAEQREDRANELMEEFHI-----EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 813 ---RHLIEHVLGPN-GLLHTKTKVLATnkvsaLSIADSIALLDNGEITQQGTYDEITKD 867
Cdd:PRK10895 174 idiKRIIEHLRDSGlGVLITDHNVRET-----LAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
667-860 |
2.95e-05 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 47.46 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHG-------------SVAYVSQV-----PWimn 728
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHsslsfPF--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 729 gTVKENILFGhRYD-----AEFYEKTIKACALTiDLAILMDGDKTlvgekgiSLSGGQKARLSLARA---VYARADTY-- 798
Cdd:PRK13548 92 -TVEEVVAMG-RAPhglsrAEDDALVAAALAQV-DLAHLAGRDYP-------QLSGGEQQRVQLARVlaqLWEPDGPPrw 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
9AYC_A 799 -LLDDPLAAVDehvARHLIeHVLgpnGLLHTKTK-----VLAtnkV------SALsIADSIALLDNGEITQQGT 860
Cdd:PRK13548 162 lLLDEPTSALD---LAHQH-HVL---RLARQLAHerglaVIV---VlhdlnlAAR-YADRIVLLHQGRLVADGT 224
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1296-1491 |
3.14e-05 |
|
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: 48.59 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1296 IKFNNYSTrYRPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLtlalFRMIEasegnividniaineiGLYDLRHKLSI 1375
Cdd:TIGR00954 452 IKFENIPL-VTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSL----FRILG----------------ELWPVYGGRLT 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1376 IPQDSQVF---------EGTVRENI---DPINQ-----YTDEAIWRALELSHLkEHVLSmSNDGLDAqLTEGGGNLSVGQ 1438
Cdd:TIGR00954 511 KPAKGKLFyvpqrpymtLGTLRDQIiypDSSEDmkrrgLSDKDLEQILDNVQL-THILE-REGGWSA-VQDWMDVLSGGE 587
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
9AYC_A 1439 RQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAfkDRTILTIAHR 1491
Cdd:TIGR00954 588 KQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHR 638
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1017-1257 |
3.37e-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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 47.56 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1017 AIYFALGIGSALATLIQTIVLWVFctihASKYLHNLMT---NSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTFS 1093
Cdd:cd18565 58 GLTVAAFLLESLFQYLSGVLWRRF----AQRVQHDLRTdtyDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGAN 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1094 QFFVNAVKVTFTITVICATTWQ---FIFIIIPLSVFY-IYYQQYYLRTSRELRRldsiTRSPIYSHFQETLGGLATVRGY 1169
Cdd:cd18565 134 SIIRVVVTVLGIGAILFYLNWQlalVALLPVPLIIAGtYWFQRRIEPRYRAVRE----AVGDLNARLENNLSGIAVIKAF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1170 SQQ----KRFSHINQCRIDNNMSA------FYPSINAnrwlayrLELIGSIIILGAATLSVF---RLKQGTLTAGmvglS 1236
Cdd:cd18565 210 TAEdferERVADASEEYRDANWRAirlraaFFPVIRL-------VAGAGFVATFVVGGYWVLdgpPLFTGTLTVG----T 278
|
250 260
....*....|....*....|.
9AYC_A 1237 LSYALQITQTLNWIVRMTVEV 1257
Cdd:cd18565 279 LVTFLFYTQRLLWPLTRLGDL 299
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
1056-1174 |
3.87e-05 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 47.51 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1056 SVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTFSQFFVNAVKVTFTITVICATTWQ---FIFIIIP-LSVFYIYYQ 1131
Cdd:cd18573 83 SILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKltlVMLLVVPpIAVGAVFYG 162
|
90 100 110 120
....*....|....*....|....*....|....*....|....
9AYC_A 1132 QYYLRTSRELR-RLDSITRSPiyshfQETLGGLATVRGYSQQKR 1174
Cdd:cd18573 163 RYVRKLSKQVQdALADATKVA-----EERLSNIRTVRAFAAERK 201
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1247-1517 |
4.63e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1247 LNWIVRMTVEVETNIVSVER--IKEYADLKSEAPLIVEghRPPKEWPSQGDIKF---NNYSTRYRPELDLVLKHINIHIK 1321
Cdd:TIGR00956 710 LKRAKKAGETSASNKNDIEAgeVLGSTDLTDESDDVND--EKDMEKESGEDIFHwrnLTYEVKIKKEKRVILNNVDGWVK 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1322 PNEKVGIVGRTGAGKSSLTLALFRMIeaSEGNIVIDNIAINEIGLyDLRHKLSI---IPQDSQVFEGTVRE--------- 1389
Cdd:TIGR00956 788 PGTLTALMGASGAGKTTLLNVLAERV--TTGVITGGDRLVNGRPL-DSSFQRSIgyvQQQDLHLPTSTVREslrfsaylr 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1390 -----NIDPINQYTDEAIwRALELSHLKEHVLSMSNDGldaqltegggnLSVGQRQLLCLArAMLV--PSKILVLDQATA 1462
Cdd:TIGR00956 865 qpksvSKSEKMEYVEEVI-KLLEMESYADAVVGVPGEG-----------LNVEQRKRLTIG-VELVakPKLLLFLDEPTS 931
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 1463 AVDVETDKVVQETIR-TAFKDRTIL-TIAHRLNTIMDS-DRIIVLDNG-KVAEFDSPGQ 1517
Cdd:TIGR00956 932 GLDSQTAWSICKLMRkLADHGQAILcTIHQPSAILFEEfDRLLLLQKGgQTVYFGDLGE 990
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1299-1493 |
5.23e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 46.35 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1299 NNYSTRYRpELDL---VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEI---GLYDLR-H 1371
Cdd:PRK11629 9 DNLCKRYQ-EGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRnQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1372 KLSIIPQDSQVF-EGTVRENID-PI---NQYTDEAIWRALELshlkehvlsMSNDGLDAQLTEGGGNLSVGQRQLLCLAR 1446
Cdd:PRK11629 88 KLGFIYQFHHLLpDFTALENVAmPLligKKKPAEINSRALEM---------LAAVGLEHRANHRPSELSGGERQRVAIAR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 1447 AmLVPSKILVL-DQATAAVDVET-DKVVQ---ETIR---TAFKDRT-ILTIAHRLN 1493
Cdd:PRK11629 159 A-LVNNPRLVLaDEPTGNLDARNaDSIFQllgELNRlqgTAFLVVThDLQLAKRMS 213
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1322-1507 |
5.57e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.06 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1322 PNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIipqdsqvfegtvrenidpinqytdea 1401
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIV-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1402 iwralelshlkehvlsmsndgldaqlTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIRTAF- 1480
Cdd:smart00382 55 --------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLl 108
|
170 180 190
....*....|....*....|....*....|....*....
9AYC_A 1481 ------KDRTILTIAHRLNTIMD------SDRIIVLDNG 1507
Cdd:smart00382 109 lllkseKNLTVILTTNDEKDLGPallrrrFDRRIVLLLI 147
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
1055-1267 |
6.33e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. 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. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 46.78 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1055 NSVLRAPMTFFETTPIGRILNRFS-NDiyKVDALLGRTFSQFFVNAVKVTFTITVICATTWQF----IFIIIPLSVFYIY 1129
Cdd:cd18568 83 KHLLSLPLSFFASRKVGDIITRFQeNQ--KIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLtlivLAFIPLYVLLTLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1130 YQQYYLRTSRELRRLDSITrspiYSHFQETLGGLATVRGYSQQKRFSHINQCRIDNNMSAFYPSINanrwLAYRLELI-- 1207
Cdd:cd18568 161 SSPKLKRNSREIFQANAEQ----QSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQK----LSIVLQLIss 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 1208 -----GSIIILGAATLSVFrlkQGTLTAG-MVGLSLSYALqITQTLNWIVRMTVEVETNIVSVERI 1267
Cdd:cd18568 233 linhlGTIAVLWYGAYLVI---SGQLTIGqLVAFNMLFGS-VINPLLALVGLWDELQETRISVERL 294
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1434-1520 |
7.46e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.39 E-value: 7.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1434 LSVGQRQLLCLARAMLVPSKILVLDQATAAVDVetdkVVQETIRTAFKD------RTILTIAHRLNTIMD-SDRIIVLDN 1506
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDV----SVQAQILQLLRElqqelnMGLLFITHNLSIVRKlADRVAVMQN 232
|
90
....*....|....
9AYC_A 1507 GKVAEFDSPGQLLS 1520
Cdd:PRK15134 233 GRCVEQNRAATLFS 246
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1313-1511 |
7.97e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.09 E-value: 7.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1313 LKHINIHIKPNEKVGIVGRTGAGKSSLTLAL---------------------FRMIEASEG-NIVIdniaineiglydLR 1370
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLsgvyphgsyegeilfdgevcrFKDIRDSEAlGIVI------------IH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1371 HKLSIIPQDSqvfegtVRENIDPINQYT-------DEAIWRALELshlkehvlsMSNDGLDAQLTEGGGNLSVGQRQLLC 1443
Cdd:NF040905 85 QELALIPYLS------IAENIFLGNERAkrgvidwNETNRRAREL---------LAKVGLDESPDTLVTDIGVGKQQLVE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
9AYC_A 1444 LARAMLVPSKILVLDQATAAVDVETDKVVQETIRtAFKDR--TILTIAHRLNTIMD-SDRIIVLDNGKVAE 1511
Cdd:NF040905 150 IAKALSKDVKLLILDEPTAALNEEDSAALLDLLL-ELKAQgiTSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1328-1511 |
8.17e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 46.50 E-value: 8.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1328 IVGRTGAGKSslTLA-LFRMIEA-SEGNIVIDNIAI---NEIGLYDLRHKLSIIPQD-----------SQVFEgtvreni 1391
Cdd:PRK11308 46 VVGESGCGKS--TLArLLTMIETpTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNpygslnprkkvGQILE------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1392 DP--INqyTDeaiwraLELSHLKEHVLSM-SNDGLDaqlTEGGGN----LSVGQRQLLCLARAMLVPSKILVLDQATAAV 1464
Cdd:PRK11308 117 EPllIN--TS------LSAAERREKALAMmAKVGLR---PEHYDRyphmFSGGQRQRIAIARALMLDPDVVVADEPVSAL 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
9AYC_A 1465 DVETDKVV-------QETIRTAFkdrtiLTIAHRLNTIMD-SDRIIVLDNGKVAE 1511
Cdd:PRK11308 186 DVSVQAQVlnlmmdlQQELGLSY-----VFISHDLSVVEHiADEVMVMYLGRCVE 235
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
425-621 |
8.37e-05 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 46.24 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 425 STGDIVNLMSVDVQKLQDLTQW-LNLIWSGPFQIIICLYSLYKLLGNSMWVGVIILVIMMPLNSFLMRIQKKLQKSQMKY 503
Cdd:cd18548 94 GTSSLITRLTNDVTQVQNFVMMlLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 504 KDERTRVISEILNNIKSLKLYAWEKPYREKLEEVrnNKELKNLT-KLGCYMAVTsfqFNIVPFLVSCCTFAVFVYTEDRA 582
Cdd:cd18548 174 LDRLNRVVRENLTGIRVIRAFNREDYEEERFDKA--NDDLTDTSlKAGRLMALL---NPLMMLIMNLAIVAILWFGGHLI 248
|
170 180 190 200
....*....|....*....|....*....|....*....|...
9AYC_A 583 LTTDLVFPALTLF----NLLSFPLMIIPMVLNSFIEASVSIGR 621
Cdd:cd18548 249 NAGSLQVGDLVAFinylMQILMSLMMLSMVFVMLPRASASAKR 291
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
1064-1267 |
1.05e-04 |
|
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: 46.26 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1064 FFETTPIGRILNRFSNDIYKVDALLGRTFSQFFVNAVKVTFTITVICATTWQFIFIIIPLSVFYIYYQQYYLRTSRELRR 1143
Cdd:cd18554 96 YYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1144 LDSITRSPIYSHFQETLGGLATVRGYSQQKRfshiNQCRIDNNMSAFYP-SINANRWLAYRLELIGSIIILG---AATLS 1219
Cdd:cd18554 176 ERSQALAEVQGFLHERIQGMSVIKSFALEKH----EQKQFDKRNGHFLTrALKHTRWNAKTFSAVNTITDLApllVIGFA 251
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
9AYC_A 1220 VFRLKQGTLTAGMVGLSLSYALQITQTLNWIVRMTVEVETNIVSVERI 1267
Cdd:cd18554 252 AYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
426-567 |
1.19e-04 |
|
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: 46.01 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 426 TGDIVNLMSVDVQKLQD-LTQWLNLIWSGPFQIIICLYSLYKLlgnSMWVGVIILVIMMPL-------NSFLMRIQKKLQ 497
Cdd:cd18557 92 TGELTSRLSSDTSVLQSaVTDNLSQLLRNILQVIGGLIILFIL---SWKLTLVLLLVIPLLliaskiyGRYIRKLSKEVQ 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
9AYC_A 498 KSQMKykdeRTRVISEILNNIKSLKLYAWE----KPYREKLEEVRNNKELKNLTkLGCYMAVTSFQFNIVPFLV 567
Cdd:cd18557 169 DALAK----AGQVAEESLSNIRTVRSFSAEekeiRRYSEALDRSYRLARKKALA-NALFQGITSLLIYLSLLLV 237
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
424-559 |
1.22e-04 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 46.00 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 424 SSTGDIVNLMSVDVQKL-----QDLTQWL-NLIwsgpfQIIICLYSLYKL---LGNSMWVGVIILVIMMPL-NSFLMRIQ 493
Cdd:cd18574 96 HRTGELVNRLTADVQEFkssfkQCVSQGLrSVT-----QTVGCVVSLYLIspkLTLLLLVIVPVVVLVGTLyGSFLRKLS 170
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 494 KKLQKSQMKykdeRTRVISEILNNIKSLKLYAWEKPYREKLEEVRNNKELKNlTKLGCYMAVtsFQ 559
Cdd:cd18574 171 RRAQAQVAK----ATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLN-EKLGLGIGI--FQ 229
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1315-1520 |
1.30e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 45.95 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1315 HINIHIKPNEKVGIVGRTGAGKSSLTLALFRmIEASEGNIVIDNIAINEIGLYDL---------RHKLSIIPQDSQV--- 1382
Cdd:PRK15093 25 RVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVTADRMRFDDIDLLRLsprerrklvGHNVSMIFQEPQScld 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1383 -FEGTVRENIDPINQYTDEAIW---------RALELSH---LKEHVLSMSNdgLDAQLTEgggnlsvGQRQLLCLARAML 1449
Cdd:PRK15093 104 pSERVGRQLMQNIPGWTYKGRWwqrfgwrkrRAIELLHrvgIKDHKDAMRS--FPYELTE-------GECQKVMIAIALA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
9AYC_A 1450 VPSKILVLDQATAAVDVETDKVVQETIRTAFKDR--TILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQLLS 1520
Cdd:PRK15093 175 NQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELVT 248
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1314-1532 |
1.36e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.32 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1314 KHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYD-LRHKLSIIPQ---DSQVFEG-TVR 1388
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDaVKKGMAYITEsrrDNGFFPNfSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1389 ENIDPINQYTDEAIWRALELSHLKEH---------VLSMSNDGLDAQLTEgggnLSVGQRQLLCLARAMLVPSKILVLDQ 1459
Cdd:PRK09700 360 QNMAISRSLKDGGYKGAMGLFHEVDEqrtaenqreLLALKCHSVNQNITE----LSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
9AYC_A 1460 ATAAVDVETDKVVQETIRT-AFKDRTILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSPGQLLSDNKSLFYSLCME 1532
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITvCDRIAVFCEGRLTQILTNRDDMSEEEIMAWALPQE 510
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1316-1515 |
1.40e-04 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 45.98 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1316 INIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYdlRHKLSIIPQDSQVF-EGTVRENI--- 1391
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPINMMFQSYALFpHMTVEQNIafg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1392 --------DPINQYTDEAiwraLELSHLKEHVLSMSNdgldaqltegggNLSVGQRQLLCLARAMLVPSKILVLDQATAA 1463
Cdd:PRK11607 116 lkqdklpkAEIASRVNEM----LGLVHMQEFAKRKPH------------QLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
9AYC_A 1464 VDVE-TDKVVQETIRTAfkDR---TILTIAHRLNTIMD-SDRIIVLDNGKVAEFDSP 1515
Cdd:PRK11607 180 LDKKlRDRMQLEVVDIL--ERvgvTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEP 234
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
641-867 |
1.49e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 45.46 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 641 KVKNIgdvainigddaTFLWQRK-PEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLF-------------- 705
Cdd:PRK13651 4 KVKNI-----------VKIFNKKlPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLpdtgtiewifkdek 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 706 -----------------------RVKGFATVHGSVAYVSQVP--WIMNGTVKENILFGHRYDAEFYEKTIKACALTIDLA 760
Cdd:PRK13651 73 nkkktkekekvleklviqktrfkKIKKIKEIRRRVGVVFQFAeyQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 761 ILmdgDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARHLIE--HVLGPNGllhtKTKVLATNKV 838
Cdd:PRK13651 153 GL---DESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEifDNLNKQG----KTIILVTHDL 225
|
250 260 270
....*....|....*....|....*....|
9AYC_A 839 -SALSIADSIALLDNGEITQQGTYDEITKD 867
Cdd:PRK13651 226 dNVLEWTKRTIFFKDGKIIKDGDTYDILSD 255
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1306-1509 |
1.85e-04 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 44.18 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1306 RPELDLvLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEAS---EGNIVIDNIAINEIGLYDLRHKLSIIPQDSQV 1382
Cdd:cd03233 17 RSKIPI-LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1383 FEGTVRENIDpinqytdeaiwralelshlkeHVLSMSNDgldaQLTEGggnLSVGQRQLLCLARAMLVPSKILVLDQATA 1462
Cdd:cd03233 96 PTLTVRETLD---------------------FALRCKGN----EFVRG---ISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
9AYC_A 1463 AVDVETDKVVQETIRT---AFKDRTILTIAHRLNTIMDS-DRIIVLDNGKV 1509
Cdd:cd03233 148 GLDSSTALEILKCIRTmadVLKTTTFVSLYQASDEIYDLfDKVLVLYEGRQ 198
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1432-1510 |
2.70e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.49 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1432 GNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETD-KVVQETIRTAFKDRTILTIAHRLNTIMD-SDRIIVLDNGKV 1509
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
.
9AYC_A 1510 A 1510
Cdd:PRK10982 470 A 470
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1324-1466 |
3.24e-04 |
|
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: 43.64 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1324 EKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQVFEGTVRENID---PINqyTDE 1400
Cdd:cd03231 27 EALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRfwhADH--SDE 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 1401 AIWRALELSHLK--EHVLSmsndgldaqlteggGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDV 1466
Cdd:cd03231 105 QVEEALARVGLNgfEDRPV--------------AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
311-622 |
4.90e-04 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 43.96 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 311 MLLAAFFKAIHDVLAFTQPQLLRILIkfvtdynserqDDhsslqGFENNHPQKLPIVRGFLIAFAMFLVGFTqtsVLHQY 390
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRII-----------DS-----VIGGGLRELLWLLALLILGVALLRGVFR---YLQGY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 391 FLNVF--NTGMYIKSALtaliYQKSLVLSNEASGLSSTGDIVNLMSVDVQKLQDLTQW-LNLIWSGPFQIIICLYSLYkl 467
Cdd:cd18542 62 LAEKAsqKVAYDLRNDL----YDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFgLVELVRAVLLFIGALIIMF-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 468 lgnSM-WVGVIILVIMMPLNSFLMRIQ-KKLQKSQMKYkDER----TRVISEILNNIKSLKLYAWEKPYREKLEEVrnNK 541
Cdd:cd18542 136 ---SInWKLTLISLAIIPFIALFSYVFfKKVRPAFEEI-REQegelNTVLQENLTGVRVVKAFAREDYEIEKFDKE--NE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 542 ELKNLTK-----LGCYMAVTSFQFNIVPFLVSCCTfAVFVYTEDRALTTDLVFpaLTLFNLLSFPLMIIPMVLNSFIEAS 616
Cdd:cd18542 210 EYRDLNIklaklLAKYWPLMDFLSGLQIVLVLWVG-GYLVINGEITLGELVAF--ISYLWMLIWPVRQLGRLINDMSRAS 286
|
....*.
9AYC_A 617 VSIGRL 622
Cdd:cd18542 287 ASAERI 292
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
668-870 |
5.57e-04 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 43.94 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 668 VALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLG-------DLFrVKGFATVHGS-----VAYVSQ----VPWIMNGtv 731
Cdd:PRK11432 20 TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGlekptegQIF-IDGEDVTHRSiqqrdICMVFQsyalFPHMSLG-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 732 kENILFGHRY----DAEFYEKTIKACALtIDLAILMDgdkTLVGEkgisLSGGQKARLSLARAVYARADTYLLDDPLAAV 807
Cdd:PRK11432 97 -ENVGYGLKMlgvpKEERKQRVKEALEL-VDLAGFED---RYVDQ----ISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
9AYC_A 808 DEHVARHLIEHVLGPNGLLHTKTKVLATNKVSALSIADSIALLDNGEITQQGTYDEITKDADS 870
Cdd:PRK11432 168 DANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPAS 230
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
655-812 |
5.77e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.71 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 655 DATFLWQRKPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDL--------FRVKGF----ATVHGSVAYVSQ 722
Cdd:TIGR00956 764 NLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVttgvitggDRLVNGrpldSSFQRSIGYVQQ 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 723 VPW-IMNGTVKENILFGHRY----------DAEFYEKTIKACALTiDLAilmdgdKTLVGEKGISLSGGQKARLSLARAV 791
Cdd:TIGR00956 844 QDLhLPTSTVRESLRFSAYLrqpksvskseKMEYVEEVIKLLEME-SYA------DAVVGVPGEGLNVEQRKRLTIGVEL 916
|
170 180
....*....|....*....|..
9AYC_A 792 YARADTYL-LDDPLAAVDEHVA 812
Cdd:TIGR00956 917 VAKPKLLLfLDEPTSGLDSQTA 938
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
669-860 |
6.89e-04 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 42.94 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 669 ALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGSVAYVSQVPWIMNG---------------TVKE 733
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREavaivpegrrvfsrmTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 734 NILFGHRY-DAEFYEKTIKAcalTIDLAILMDGDKTlvgEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVA 812
Cdd:PRK11614 100 NLAMGGFFaERDQFQERIKW---VYELFPRLHERRI---QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
9AYC_A 813 RHLIEHV--LGPNGLlhtKTKVLATNKVSALSIADSIALLDNGEITQQGT 860
Cdd:PRK11614 174 QQIFDTIeqLREQGM---TIFLVEQNANQALKLADRGYVLENGHVVLEDT 220
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1016-1231 |
7.92e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 43.29 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1016 LAIYFALGIGSALATLIQTIVLWvfctihasKYLHNLMT---NSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTF 1092
Cdd:cd18778 47 LGAYLLRALLNFLRIYLNHVAEQ--------KVVADLRSdlyDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1093 SQFFVNAVKVtFTITVICATT-WQFIFI-IIPLsVFYIYYQQYYLRTSRELRRLDSITRSPIYSHFQETLGGLATVRGYS 1170
Cdd:cd18778 119 PQGITNVLTL-VGVAIILFSInPKLALLtLIPI-PFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFG 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
9AYC_A 1171 QQ----KRFSHIN------QCRIDNNMSAFYPSINanrWLAYrlelIGSIIILGAATLSVFrlkQGTLTAG 1231
Cdd:cd18778 197 REeeeaKRFEALSrryrkaQLRAMKLWAIFHPLME---FLTS----LGTVLVLGFGGRLVL---AGELTIG 257
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1434-1512 |
9.97e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.79 E-value: 9.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1434 LSVGQRQLLCLARAMLVPSKILVLDQATAAVDVETDKVVQETIrTAFKDrTILTIAH-RL---NTIMDSdrIIVLDNGKV 1509
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELL-DSYQG-TVLLVSHdRQfvdNTVTEC--WIFEGNGKI 516
|
...
9AYC_A 1510 AEF 1512
Cdd:PRK11147 517 GRY 519
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
370-622 |
1.31e-03 |
|
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: 42.78 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 370 FLIAFAMFLVGFTQtsvlhQYFLnvFNTGMYIKSALTALIYQKSLVLSNEASGLSSTGDIVNLMSVDVQKLQDLTQW-LN 448
Cdd:cd18541 47 LLLALLIGIFRFLW-----RYLI--FGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPgIL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 449 LIWSGPFQIIICLYSLY----KLlgnsMWVGVIILVIMMPLNSFLMR-IQKKLQKSQMKYKD--ERTRvisEILNNIKSL 521
Cdd:cd18541 120 YLVDALFLGVLVLVMMFtispKL----TLIALLPLPLLALLVYRLGKkIHKRFRKVQEAFSDlsDRVQ---ESFSGIRVI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 522 KLYAWEKPYREKLEEV-RNNKElKNLTklgcYMAVTSFQFNIVPFLVSCCTFAVFVY----TEDRALTT-DLVfpALTL- 594
Cdd:cd18541 193 KAFVQEEAEIERFDKLnEEYVE-KNLR----LARVDALFFPLIGLLIGLSFLIVLWYggrlVIRGTITLgDLV--AFNSy 265
|
250 260
....*....|....*....|....*...
9AYC_A 595 FNLLSFPLMIIPMVLNSFIEASVSIGRL 622
Cdd:cd18541 266 LGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1380-1518 |
1.46e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.19 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1380 SQVF----EGTVRENID--------P---INQYTDEAIWRAlelsHLKEHVLSMSNDgldaqltegggnLSVGQRQLLCL 1444
Cdd:NF033858 345 SQAFslygELTVRQNLElharlfhlPaaeIAARVAEMLERF----DLADVADALPDS------------LPLGIRQRLSL 408
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
9AYC_A 1445 ARAMLVPSKILVLDQATAAVD-VETDKVVQETIRTAFKDR-TILTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQL 1518
Cdd:NF033858 409 AVAVIHKPELLILDEPTSGVDpVARDMFWRLLIELSREDGvTIFISTHFMNEAERCDRISLMHAGRVLASDTPAAL 484
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1312-1505 |
1.57e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.40 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIG---LYDLRHKLSIipqdsqVFEGTVR 1388
Cdd:PRK13541 15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkpyCTYIGHNLGL------KLEMTVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1389 ENIDPINQYTDEAIWRALELSHLKEHVLsmsndgldaqLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDQATAAVDVET 1468
Cdd:PRK13541 89 ENLKFWSEIYNSAETLYAAIHYFKLHDL----------LDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN 158
|
170 180 190
....*....|....*....|....*....|....*..
9AYC_A 1469 DKVVQETIRTAFKDRTILTIAHRLNTIMDSDRIIVLD 1505
Cdd:PRK13541 159 RDLLNNLIVMKANSGGIVLLSSHLESSIKSAQILQLD 195
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
659-863 |
1.58e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 43.11 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 659 LWQRKPeYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMlgdLFRVKGFATVHGSV----------------AYVSQ 722
Cdd:TIGR00955 31 FCRERP-RKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNAL---AFRSPKGVKGSGSVllngmpidakemraisAYVQQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 723 VP-WIMNGTVKENILF-GH-RYDAEFYEKTIKACALTIDLAI-LMDGDKTLVGEKGI--SLSGGQKARLSLARAVYARAD 796
Cdd:TIGR00955 107 DDlFIPTLTVREHLMFqAHlRMPRRVTKKEKRERVDEVLQALgLRKCANTRIGVPGRvkGLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
9AYC_A 797 TYLLDDPLAAVDEHVARHLIEHV--LGPNGllhtKTKVLATNKVSA--LSIADSIALLDNGEITQQGTYDE 863
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLkgLAQKG----KTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
658-809 |
1.68e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.96 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 658 FLWQRKPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGSVAYVSqVPWIMNGTVK--ENI 735
Cdd:PRK13545 28 FFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIA-ISSGLNGQLTgiENI 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
9AYC_A 736 LFGHRYDAEFYEKTIKACALTIDLAilmDGDKtLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDE 809
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFA---DIGK-FIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQ 176
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1312-1508 |
1.80e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.17 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEAS----EGNIVIDNIAINEIglydLRHK----LSIIPQDSQVF 1383
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFhigvEGVITYDGITPEEI----KKHYrgdvVYNAETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1384 EGTVRENID-------PINQYtdEAIWRALELSHLKEhvLSMSNDGLDAQLTEGGGN-----LSVGQRQLLCLARAMLVP 1451
Cdd:TIGR00956 152 HLTVGETLDfaarcktPQNRP--DGVSREEYAKHIAD--VYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGG 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
9AYC_A 1452 SKILVLDQATAAVDVETD----KVVQETIRTAfKDRTILTIAHRLNTIMDS-DRIIVLDNGK 1508
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATAlefiRALKTSANIL-DTTPLVAIYQCSQDAYELfDKVIVLYEGY 288
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1312-1448 |
2.15e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 42.14 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1312 VLKHINIHIKPNEKVGIVGRTGAGKSSltlaLFRMI----EASEGNIVIDNIAINEIGlydlrhklsiiPQD---SQVFE 1384
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKST----LLRMVagleRITSGEIWIGGRVVNELE-----------PADrdiAMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1385 G-------TVRENI-----------DPINQYTDEAIwRALELSHLkehvlsmsndgLDAQLTEgggnLSVGQRQLLCLAR 1446
Cdd:PRK11650 84 NyalyphmSVRENMayglkirgmpkAEIEERVAEAA-RILELEPL-----------LDRKPRE----LSGGQRQRVAMGR 147
|
..
9AYC_A 1447 AM 1448
Cdd:PRK11650 148 AI 149
|
|
| ABC_6TM_PglK_like |
cd18553 |
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group ... |
370-540 |
2.35e-03 |
|
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group represents the transmembrane (TM) domain of an active lipid-linked oligosaccharides flippase PglK (protein glycosylation K), which is a homodimeric ABC transporter that flips a lipid-linked oligosaccharide that serves as a glycan donor in N-linked protein glycosylation. Pglk mediates the ATP-dependent translocation of the undecaprenylpyrophosphate-linked heptasaccharide intermediate across the cell membrane; this is an essential step during the N-linked protein glycosylation pathway. This TM subunit exhibits 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. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 349997 Cd Length: 300 Bit Score: 41.76 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 370 FLIAFAMFLVGF----TQTSVLHQYFLNVFNTGMYikSALTALIYQKSLVLSNEASGLSSTGDIVNLMSVDVQKLQDLTQ 445
Cdd:cd18553 52 FVIFFGIILIGFyifrSLYNIFYTYLLNRFSFGRY--HSIAYRLFKNYLKLNYQDFTNKNSSDLSKSIINEASNLSQVIQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 446 WLNLIWSGPFqIIICLYSLYkLLGNsmWVGVIILVIMMPLNSFLM------RIQKKLQKSqMKYKDERTRVISEILNNIK 519
Cdd:cd18553 130 SFLFILSEIF-VILFIYSLL-LYVN--WKITLVLTLFLGLNVFFItkivskKIKKQGKKR-EESQKKFYKILSETFGNFK 204
|
170 180
....*....|....*....|.
9AYC_A 520 SLKLYAWEKPYREKLEEVRNN 540
Cdd:cd18553 205 IIKLKSNEKEILKNFSQASLK 225
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
370-577 |
2.61e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 41.69 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 370 FLIAFAMFLVGFTQTSVLHQyflnvfnTGMYIKSALTALIYQKslVLSNEAS--GLSSTGDIVNLMSVDVQKLQD----- 442
Cdd:cd18577 54 VYLGIGSFVLSYIQTACWTI-------TGERQARRIRKRYLKA--LLRQDIAwfDKNGAGELTSRLTSDTNLIQDgigek 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 443 ---LTQWLNLIWSGpfqIIICLYSLYKLLGNSMWVGVIILVIMMplnsFLMRIQKKLQKSQMKYKDERTRVISEILNNIK 519
Cdd:cd18577 125 lglLIQSLSTFIAG---FIIAFIYSWKLTLVLLATLPLIAIVGG----IMGKLLSKYTKKEQEAYAKAGSIAEEALSSIR 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 520 SLKLYAwekpyREKLEEVRNNKELKNLTKLGCYMA-VTSFQFNIVpFLVSCCTFAV-FVY 577
Cdd:cd18577 198 TVKAFG-----GEEKEIKRYSKALEKARKAGIKKGlVSGLGLGLL-FFIIFAMYALaFWY 251
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1320-1509 |
2.93e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 41.07 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1320 IKPNEKVGIVGRTGAGKSSLtlaLFRM--IEASEGNIVIDNIAINEIGLYDL-RHKLSIIPQDSQVFegtvrenIDPINQ 1396
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTL---LARMagLLPGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPF-------AMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1397 YtdeaiwraLELS-------HLKEHVLSMSND--GLDAQLTEGGGNLSVGQRQLLCLARAMLV------P-SKILVLDQA 1460
Cdd:PRK03695 89 Y--------LTLHqpdktrtEAVASALNEVAEalGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinPaGQLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
9AYC_A 1461 TAAVDVETDKVVQETIRT-AFKDRTILTIAHRLN-TIMDSDRIIVLDNGKV 1509
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSElCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKL 211
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1313-1509 |
3.09e-03 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 41.01 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1313 LKHINIHIKPNEKVGIVGRTGAGKSSLtLALFRMIE-ASEGNIV-----IDNIAINEIGLydLRHKLSIIPQDSQVF-EG 1385
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTL-LKLICGIErPSAGKIWfsghdITRLKNREVPF--LRRQIGMIFQDHHLLmDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1386 TVRENID-P--INQYTDEAIWRALELSHLKEHVLSMSNDgLDAQltegggnLSVGQRQLLCLARAMLVPSKILVLDQATA 1462
Cdd:PRK10908 95 TVYDNVAiPliIAGASGDDIRRRVSAALDKVGLLDKAKN-FPIQ-------LSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
9AYC_A 1463 AVdvetDKVVQETIRTAFKD-----RTILTIAHRLNTIMDSD-RIIVLDNGKV 1509
Cdd:PRK10908 167 NL----DDALSEGILRLFEEfnrvgVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
667-872 |
3.50e-03 |
|
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: 41.05 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 667 KVALKNINFQAKKGNLTCIVGKVGSGKTALLSCM--LGDLFRVK-----------GFATVHGSVAYVSQVPWIMNGTVKE 733
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFfrMVDIFDGKividgidisklPLHTLRSRLSIILQDPILFSGSIRF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 734 NILFGHRYDAEFYEKTIKACALTIDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVAR 813
Cdd:cd03288 114 NLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEN 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 814 HLIEHVLGPnglLHTKTKVLATNKVSALSIADSIALLDNGEITQQGTYDEITKDADSPL 872
Cdd:cd03288 194 ILQKVVMTA---FADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
764-818 |
3.86e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 39.86 E-value: 3.86e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
9AYC_A 764 DGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDE----HVA---RHLIEH 818
Cdd:cd03222 59 DGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAAraiRRLSEE 120
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
662-863 |
4.37e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.02 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 662 RKPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDL--FRVKGFATVH--------------GSVAYVSQ--- 722
Cdd:TIGR00956 69 RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdgFHIGVEGVITydgitpeeikkhyrGDVVYNAEtdv 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 723 -VPWImngTVKENILF-------GHRYDA---EFYEKTIKACALTI-DLAILMDgdkTLVGE---KGIslSGGQKARLSL 787
Cdd:TIGR00956 149 hFPHL---TVGETLDFaarcktpQNRPDGvsrEEYAKHIADVYMATyGLSHTRN---TKVGNdfvRGV--SGGERKRVSI 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
9AYC_A 788 ARAVYARADTYLLDDPLAAVDEHVARHLIEHVLGPNGLLHTkTKVLATNKVS--ALSIADSIALLDNGEITQQGTYDE 863
Cdd:TIGR00956 221 AEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDT-TPLVAIYQCSqdAYELFDKVIVLYEGYQIYFGPADK 297
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
1018-1233 |
4.56e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. 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 I 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). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 40.96 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1018 IYFALGIGSALATLIQTIVLWV--FCTIHASKYL-HNLMT---NSVLRAPMTFFETTPIGRILNRFsNDIYKVDALLGRT 1091
Cdd:cd18555 40 LLNVLGIGILILFLLYGLFSFLrgYIIIKLQTKLdKSLMSdffEHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQILSNQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1092 FSQFFVNAVKVTFTITVICATTWQFIFIIIPLSVFYIYYQQYYLRTSRELRRLDSITRSPIYSHFQETLGGLATVRGY-S 1170
Cdd:cd18555 119 VISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLgS 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
9AYC_A 1171 QQKRFSHINQcRIDNNMSAFYpsiNANRWLAY------RLELIGSIIILGAATLSVFrlkQGTLTAGMV 1233
Cdd:cd18555 199 EKNIYKKWEN-LFKKQLKAFK---KKERLSNIlnsissSIQFIAPLLILWIGAYLVI---NGELTLGEL 260
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
370-628 |
4.70e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 40.90 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 370 FLIAFAMFLVGFTQTsvlhqYFLNvfntgmYIKSALTALIYQKSL--VLSNEAS----GLSSTGDIVNLMSVDVQKLQDL 443
Cdd:cd18578 59 LVLAIVAGIAYFLQG-----YLFG------IAGERLTRRLRKLAFraILRQDIAwfddPENSTGALTSRLSTDASDVRGL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 444 T-QWLNLIwsgpFQ--------IIICLYSLYKL-LgnsmwVGVIILVIMMPLNSFLMRIQKKLQKSQMKYKDERTRVISE 513
Cdd:cd18578 128 VgDRLGLI----LQaivtlvagLIIAFVYGWKLaL-----VGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 514 ILNNIK---SLKL--YAWEKpYREKLEEVRnNKELKNLTKLGCYMAVTSFqfniVPFLVSCCTF---AVFVYTEDraltt 585
Cdd:cd18578 199 AVSNIRtvaSLTLedYFLEK-YEEALEEPL-KKGLRRALISGLGFGLSQS----LTFFAYALAFwygGRLVANGE----- 267
|
250 260 270 280
....*....|....*....|....*....|....*....|...
9AYC_A 586 dlvfpaLTLFNLLsfplmiipMVLNSFIEASVSIGRLFTFFTN 628
Cdd:cd18578 268 ------YTFEQFF--------IVFMALIFGAQSAGQAFSFAPD 296
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
668-719 |
5.05e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 40.68 E-value: 5.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
9AYC_A 668 VALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLfrvkgfATVHGSVAY 719
Cdd:PRK11701 20 KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARL------APDAGEVHY 65
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
1021-1167 |
6.24e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of 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: 350055 [Multi-domain] Cd Length: 294 Bit Score: 40.65 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1021 ALGIGSALATLIQTIVlwvfcTIhASKYLHNLMTNSV------------LRAPMTFFETTPIGRILNRFSnDIYKVDALL 1088
Cdd:cd18782 43 VIGVVMLVAALLEAVL-----TA-LRTYLFTDTANRIdlelggtiidhlLRLPLGFFDKRPVGELSTRIS-ELDTIRGFL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9AYC_A 1089 GRTFSQFFVNAVKVTFTITVICATTWQFIFII---IPLSVFYIYYQQYYLRtsRELRRLdSITRSPIYSHFQETLGGLAT 1165
Cdd:cd18782 116 TGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVlatVPLQLLLTFLFGPILR--RQIRRR-AEASAKTQSYLVESLTGIQT 192
|
..
9AYC_A 1166 VR 1167
Cdd:cd18782 193 VK 194
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
1306-1345 |
9.65e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 40.13 E-value: 9.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|
9AYC_A 1306 RPELDLVLKHINIhikpnekvGIVGRTGAGKSSLTLALFR 1345
Cdd:COG3596 30 LERLLVELPPPVI--------ALVGKTGAGKSSLINALFG 61
|
|
| |
