|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-1547 |
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: 1726.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 14 GSTFWNATETWYTNDPDFTPCFEQTALVWTPCAFYWAFVIFDFYYLKASLDRNIPWNKLNVSKALVNLGLLVITALDLIM 93
Cdd:TIGR00957 6 SDPLWDWNVTWHTSNPDFTKCFQNTVLAWVPCFYLWVCFPCYFLYLSRHDRGYIQMTHLNKTKTALGFLLWIVCWADLFY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 94 ALVKKG-GDSELPLYdldVWGPIIKFATFLLLFIFIPLNRKYGVQTTGCQFIFWFLLTVLSIPRCRTevrldaerqKILN 172
Cdd:TIGR00957 86 SFWERShGRAPAPVF---LVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALVCALAILRS---------KILL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 173 SQQPSEQDfswEEYQFVSFFIFFTFTSIMLILNCFADGMPRQTKYQRGENEIPELSASFLSRITYQWFDKMALKGYRNPL 252
Cdd:TIGR00957 154 ALKEDAIV---DPFRDTTFYIYFALVLSQLVLSCFSDKSPLFSETNHDPNPCPESSASFLSRITFWWITGMAVYGYRQPL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 253 EEKDLWDLRPQDSCSEVMPIFAHHWNQNVRKNYKNKARV--EPKAQFSNGNVTFENPHGE------KNGRKKGMASIMPP 324
Cdd:TIGR00957 231 EESDLWSLNKEDTSEMVVPVLVENWKKECKKTRKQPVSAvyGKKDPSKPKGSSQLDANEEvealivKSPHKPRKPSLFKV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 325 IYKSFGGVFLFGALMKLFTDTLTFAQPQVLSLIISFVEAQDAePEWKGILYAVLLFVLAAAQTFILGQYFHRMFIVGLRI 404
Cdd:TIGR00957 311 LYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMA-PDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 405 RTALINAIYRKALRISNSTKKESTVGEIVNLMAVDAQRFMELTTYLNMIWSAPLQIGLALYFLWQQLGPSVLAGLAVMII 484
Cdd:TIGR00957 390 KTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 485 LIPVNGVIASRIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPSFEKQVLDIRDKEIATLRSTAYLNAGTSFLWSC 564
Cdd:TIGR00957 470 MVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVC 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 565 APFLVSLVTFATYVLTSEANQLSVEKVLVSIALFDLMKLPLTILPMLSVDIAETQVSVNRINKFLNSEELDPNSVLHDSS 644
Cdd:TIGR00957 550 TPFLVALITFAVYVTVDENNILDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTI 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 645 KP---HPMSIENGEFSW--GDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLAYVPQQAW 719
Cdd:TIGR00957 630 KPgegNSITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAW 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 720 IQNATVRDNILFGQTYDRKRYNKVIDACALRADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLS 799
Cdd:TIGR00957 710 IQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 800 AVDAHVGKHIFEEVIGPKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEISESGTFDQLVKNKGAFADFIIQHLQEgnee 879
Cdd:TIGR00957 790 AVDAHVGKHIFEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPD---- 865
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 880 eeelnqiKRQISSTADVPELLGTVEKAIKLartesLSDSISVTsaDSLmggGGSLRRRTKRQDSHDS-----VASAASLK 954
Cdd:TIGR00957 866 -------EQQGHLEDSWTALVSGEGKEAKL-----IENGMLVT--DVV---GKQLQRQLSASSSDSGdqsrhHGSSAELQ 928
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 955 KK--QEVEGKLIETEKSQTGGVEFAVYKHYIKSVGIFLSVATLVLNFVFQAFQIGSNLWLTQWANDQNVANDTGLRDMYL 1032
Cdd:TIGR00957 929 KAeaKEETWKLMEADKAQTGQVELSVYWDYMKAIGLFITFLSIFLFVCNHVSALASNYWLSLWTDDPMVNGTQNNTSLRL 1008
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1033 GVYGAFGFGQVFSYIGSVVIVYLGALIGTRKIFIQLFGNILHAPQAYFDIKPRARILDRLANDIYKLDVVLPELIRVFNS 1112
Cdd:TIGR00957 1009 SVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMG 1088
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1113 QVFRVLATIVVISLSTPIFLAVIVPIAFLYYFAQRFYVATSRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGDRFIE 1192
Cdd:TIGR00957 1089 SLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIH 1168
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1193 ESDAKVDKNQVCKYPSVIANRWLAIRLEMVGNLIILFASLFAVLGGQT-NPGLVGLSVSYALQVTQTLNWLVRMSSDIET 1271
Cdd:TIGR00957 1169 QSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSlSAGLVGLSVSYSLQVTFYLNWLVRMSSEMET 1248
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1272 NIVSVERIKEYGETKQEAPWELEQDKnKPKNWPQEGRVEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSS 1351
Cdd:TIGR00957 1249 NIVAVERLKEYSETEKEAPWQIQETA-PPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSS 1327
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1352 LTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPVLFSGSLRINLDPFEIKTDDEIWKALELSHLKSFVKSL 1431
Cdd:TIGR00957 1328 LTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSAL 1407
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1432 AAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSD 1511
Cdd:TIGR00957 1408 PDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT 1487
|
1530 1540 1550
....*....|....*....|....*....|....*.
gi 45552357 1512 KVIVLDKGQIIEFASPTELLDNpKSAFYSMAKDANL 1547
Cdd:TIGR00957 1488 RVIVLDKGEVAEFGAPSNLLQQ-RGIFYSMAKDAGL 1522
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
220-1541 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 1046.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 220 GENEIPELSASFLSRITYQWFDKMALKGYRNPLEEKDLWDLRPQDSCSEVMPIFAHHWNQNVRKnyknkarvePKAQfsn 299
Cdd:PLN03130 223 GEQICPERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKK---------PKPW--- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 300 gnvtfenphgekngrkkgmasIMPPIYKSFGGVFLFGALMKLFTDTLTFAQPQVLSLIISfvEAQDAEPEWKGILYAVLL 379
Cdd:PLN03130 291 ---------------------LLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLLNLLLE--SMQNGEPAWIGYIYAFSI 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 380 FVLAAAQTFILGQYFHRMFIVGLRIRTALINAIYRKALRISNSTKKESTVGEIVNLMAVDAQRFMELTTYLNMIWSAPLQ 459
Cdd:PLN03130 348 FVGVVLGVLCEAQYFQNVMRVGFRLRSTLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFR 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 460 IGLALYFLWQQLGPSVLAGLAVMIILIPVNGVIASRIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPSFEKQVLD 539
Cdd:PLN03130 428 IIIAMVLLYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQT 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 540 IRDKEIATLRSTAYLNAGTSFLWSCAPFLVSLVTFATYVLTseANQLSVEKVLVSIALFDLMKLPLTILPMLSVDIAETQ 619
Cdd:PLN03130 508 VRDDELSWFRKAQLLSAFNSFILNSIPVLVTVVSFGVFTLL--GGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNAN 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 620 VSVNRINKFLNSEE--LDPNSVLhDSSKPhPMSIENGEFSW---GDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAF 694
Cdd:PLN03130 586 VSLKRLEELLLAEErvLLPNPPL-EPGLP-AISIKNGYFSWdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 695 LGEMEKLAGVVNTV-GKLAYVPQQAWIQNATVRDNILFGQTYDRKRYNKVIDACALRADIDILSAGDLTEIGEKGINLSG 773
Cdd:PLN03130 664 LGELPPRSDASVVIrGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISG 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 774 GQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEVIgpKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEISESG 853
Cdd:PLN03130 744 GQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCI--KDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEG 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 854 TFDQLVKNKGAFADFIiqhlqegneeeeelnqikrqisstadvpELLGTVEKAIKLARTESLSDSISVTSADslmgGGGS 933
Cdd:PLN03130 822 TYEELSNNGPLFQKLM----------------------------ENAGKMEEYVEENGEEEDDQTSSKPVAN----GNAN 869
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 934 LRRRtkrqdshdsvaSAASLKKKQEVEGKLIETEKSQTGGVEFAVYKHYIKSVGIFLSVATLVLNFVF-QAFQIGSNLWL 1012
Cdd:PLN03130 870 NLKK-----------DSSSKKKSKEGKSVLIKQEERETGVVSWKVLERYKNALGGAWVVMILFLCYVLtEVFRVSSSTWL 938
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1013 TQWAnDQNVANDTGlRDMYLGVYGAFGFGQVFSYIGSVVIVYLGALIGTRKIFIQLFGNILHAPQAYFDIKPRARILDRL 1092
Cdd:PLN03130 939 SEWT-DQGTPKTHG-PLFYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRF 1016
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1093 ANDIYKLDVVLPELIRVFNSQVFRVLATIVVISLSTPIFLAVIVPIAFLYYFAQRFYVATSRQLMRLESVSRSPIYSHFS 1172
Cdd:PLN03130 1017 AKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFG 1096
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1173 ETVTGASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVIANRWLAIRLEMVGNLIILFASLFAVLGGQ--TNP----GLVG 1246
Cdd:PLN03130 1097 EALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQNGraENQaafaSTMG 1176
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1247 LSVSYALQVTQTLNWLVRMSSDIETNIVSVERIKEYGETKQEAPWELEqDKNKPKNWPQEGRVEFQNFQVRYREGLDLVL 1326
Cdd:PLN03130 1177 LLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPSEAPLVIE-NNRPPPGWPSSGSIKFEDVVLRYRPELPPVL 1255
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1327 RGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPVLFSGSLRINLDP 1406
Cdd:PLN03130 1256 HGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDP 1335
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1407 FEIKTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQK 1486
Cdd:PLN03130 1336 FNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQK 1415
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 1487 TIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLDNPKSAFYSM 1541
Cdd:PLN03130 1416 TIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKM 1470
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
220-1541 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 965.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 220 GENEIPELSASFLSRITYQWFDKMALKGYRNPLEEKDLWDLRPQDSCSEVMPIFAHHWNQNVRKnyknkarvePKAqfsn 299
Cdd:PLN03232 223 GENICPERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEESRR---------PKP---- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 300 gnvtfenphgekngrkkgmaSIMPPIYKSFGGVFLFGALMKLFTDTLTFAQPQVLSLIISfvEAQDAEPEWKGILYAVLL 379
Cdd:PLN03232 290 --------------------WLLRALNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLLQ--SMQEGDPAWVGYVYAFLI 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 380 FVLAAAQTFILGQYFHRMFIVGLRIRTALINAIYRKALRISNSTKKESTVGEIVNLMAVDAQRFMELTTYLNMIWSAPLQ 459
Cdd:PLN03232 348 FFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFR 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 460 IGLALYFLWQQLGPSVLAGLAVMIILIPVNGVIASRIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPSFEKQVLD 539
Cdd:PLN03232 428 IIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQG 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 540 IRDKEIATLRSTAYLNAGTSFLWSCAPFLVSLVTFATYVLTseANQLSVEKVLVSIALFDLMKLPLTILPMLSVDIAETQ 619
Cdd:PLN03232 508 IRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFVLL--GGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNAN 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 620 VSVNRINKFLNSEE--LDPNSVLHDSSKPhpMSIENGEFSWGDEI---TLRNINIEVKKGSLVALVGTVGSGKSSVVQAF 694
Cdd:PLN03232 586 VSLQRIEELLLSEEriLAQNPPLQPGAPA--ISIKNGYFSWDSKTskpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 695 LGEMEKL-AGVVNTVGKLAYVPQQAWIQNATVRDNILFGQTYDRKRYNKVIDACALRADIDILSAGDLTEIGEKGINLSG 773
Cdd:PLN03232 664 LGELSHAeTSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISG 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 774 GQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEVIgpKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEISESG 853
Cdd:PLN03232 744 GQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCM--KDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEG 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 854 TFDQLVKNKGAFADFIiqhlqegneeeeelnqikrqisstadvpellgtvEKAIKLARTESLSdsisvTSADSLMGGGGS 933
Cdd:PLN03232 822 TFAELSKSGSLFKKLM----------------------------------ENAGKMDATQEVN-----TNDENILKLGPT 862
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 934 LRRRTKRQdshdsvaSAASLKKKQEVEGKLIETEKSQTGGVEFAVYKHYIKSVGIFLSVATLVLNFVF-QAFQIGSNLWL 1012
Cdd:PLN03232 863 VTIDVSER-------NLGSTKQGKRGRSVLVKQEERETGIISWNVLMRYNKAVGGLWVVMILLVCYLTtEVLRVSSSTWL 935
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1013 TQWANDQNVANDTglRDMYLGVYGAFGFGQVFSYIGSVVIVYLGALIGTRKIFIQLFGNILHAPQAYFDIKPRARILDRL 1092
Cdd:PLN03232 936 SIWTDQSTPKSYS--PGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRF 1013
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1093 ANDIYKLDVVLPELIRVFNSQVFRVLATIVVISLSTPIFLAVIVPIAFLYYFAQRFYVATSRQLMRLESVSRSPIYSHFS 1172
Cdd:PLN03232 1014 SKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFG 1093
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1173 ETVTGASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVIANRWLAIRLEMVGNLIILFASLFAVLG-GQTN-----PGLVG 1246
Cdd:PLN03232 1094 EALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLRnGNAEnqagfASTMG 1173
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1247 LSVSYALQVTQTLNWLVRMSSDIETNIVSVERIKEYGETKQEAPwELEQDKNKPKNWPQEGRVEFQNFQVRYREGLDLVL 1326
Cdd:PLN03232 1174 LLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEAT-AIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVL 1252
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1327 RGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPVLFSGSLRINLDP 1406
Cdd:PLN03232 1253 HGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDP 1332
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1407 FEIKTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQK 1486
Cdd:PLN03232 1333 FSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQR 1412
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 1487 TIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLDNPKSAFYSM 1541
Cdd:PLN03232 1413 TIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRM 1467
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
320-1541 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 804.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 320 SIMPPIYKSFGGVFLFGALMKLFTDTLTFAQPQVLSLIISFVEAQDAEPEWkGILYAVLLFVLAAAQTFILGQYFHRMFI 399
Cdd:PTZ00243 233 SLLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNATWGR-GLGLVLTLFLTQLIQSVCLHRFYYISIR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 400 VGLRIRTALINAIYRKALRISNST--KKESTVGEIVNLMAVDAQRFMELTTYLNMIWSAPLQIGLALYFLWQQLGPSVLA 477
Cdd:PTZ00243 312 CGLQYRSALNALIFEKCFTISSKSlaQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALM 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 478 GLAVMIILIPVNGVIASRIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPSFEKQVLDIRDKEIATLRSTAYLNAG 557
Cdd:PTZ00243 392 AVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVA 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 558 TSFLWSCAPFLVSLVTFATYVLTseANQLSVEKVLVSIALFDLMKLPLTILPMLSVDIAETQVSVNRINKFLNSEE---- 633
Cdd:PTZ00243 472 TSFVNNATPTLMIAVVFTVYYLL--GHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLECDNatcs 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 634 -------------------------------------------------------------------LDPNSVLHDSSKP 646
Cdd:PTZ00243 550 tvqdmeeywreqrehstacqlaavlenvdvtafvpvklprapkvktsllsralrmlcceqcrptkrhPSPSVVVEDTDYG 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 647 HPMS----IENGEFSWGDEIT-------------------------LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGE 697
Cdd:PTZ00243 630 SPSSasrhIVEGGTGGGHEATptsersaktpkmktddffelepkvlLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQ 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 698 MEKLAGVVNTVGKLAYVPQQAWIQNATVRDNILFGQTYDRKRYNKVIDACALRADIDILSAGDLTEIGEKGINLSGGQKQ 777
Cdd:PTZ00243 710 FEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKA 789
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 778 RISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEVIgpKGILARKSRVLVTHGVTFLPQVDsiYVIKMGeisesgtfDQ 857
Cdd:PTZ00243 790 RVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF--LGALAGKTRVLATHQVHVVPRAD--YVVALG--------DG 857
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 858 LVKNKGAFADFIiqhlqegneeeeelnqikrQISSTADvpelLGTVEKAIKLARtESLSDSiSVTSADSLMGGGGSLRRR 937
Cdd:PTZ00243 858 RVEFSGSSADFM-------------------RTSLYAT----LAAELKENKDSK-EGDADA-EVAEVDAAPGGAVDHEPP 912
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 938 TKRQdshDSVASAASLKKKQEVEGKLIETEKSQTGGVEFAVYKHYIKSVGIFLSVATLVLNFVF-QAFQIGSNLWLTQWA 1016
Cdd:PTZ00243 913 VAKQ---EGNAEGGDGAALDAAAGRLMTREEKASGSVPWSTYVAYLRFCGGLHAAGFVLATFAVtELVTVSSGVWLSMWS 989
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1017 NDQNVANDTGLRDMYLGVYGAFGFGQVFSYIGSvvivYLGALIGTRKIFIQLFGNILHAPQAYFDIKPRARILDRLANDI 1096
Cdd:PTZ00243 990 TRSFKLSAATYLYVYLGIVLLGTFSVPLRFFLS----YEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDI 1065
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1097 YKLDVVLPELIRVFNSQVFRVLATIVVISLSTPIFLAVIVPIAFLYYFAQRFYVATSRQLMRLESVSRSPIYSHFSETVT 1176
Cdd:PTZ00243 1066 DILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQ 1145
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1177 GASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVIANRWLAIRLEMVGNLIILFASLFAVLG-----GQTNPGLVGLSVSY 1251
Cdd:PTZ00243 1146 GSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGVIGtmlraTSQEIGLVSLSLTM 1225
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1252 ALQVTQTLNWLVRMSSDIETNIVSVERIKEY-GETKQEAPWELEQDKNK----------------------PKNWP---Q 1305
Cdd:PTZ00243 1226 AMQTTATLNWLVRQVATVEADMNSVERLLYYtDEVPHEDMPELDEEVDAlerrtgmaadvtgtvviepaspTSAAPhpvQ 1305
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1306 EGRVEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSR 1385
Cdd:PTZ00243 1306 AGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQ 1385
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1386 LTIIPQDPVLFSGSLRINLDPFEIKTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTK 1465
Cdd:PTZ00243 1386 FSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGS 1465
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 1466 VLVL-DEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLDNPKSAFYSM 1541
Cdd:PTZ00243 1466 GFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSM 1542
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
225-1538 |
7.55e-162 |
|
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: 529.48 E-value: 7.55e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 225 PELSASFLSRITYQWFDKMALKGYRNPLEEKDLWDLRPQDSCSEVMPIFAHHWNQNVRKNYKNkarvePKaqfsngnvtf 304
Cdd:TIGR01271 5 PVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAKKN-----PK---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 305 enphgekngrkkgmasIMPPIYKSFGGVFLFGALMKLFTDTLTFAQPQVLSLIISFVEAQDAEPEWKGILYAVLLFVLAA 384
Cdd:TIGR01271 70 ----------------LLNALRRCFFWRFVFYGILLYFGEATKAVQPLLLGRIIASYDPFNAPEREIAYYLALGLCLLFI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 385 AQTFILGQYFHRMFIVGLRIRTALINAIYRKALRISNSTKKESTVGEIVNLMAVDAQRFMELTTYLNMIWSAPLQIGLAL 464
Cdd:TIGR01271 134 VRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLM 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 465 YFLWQQLGPSVLAGLAVMIILIPVNGVIASRIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPSFEKQVLDIRDKE 544
Cdd:TIGR01271 214 GLIWELLEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 545 IATLRSTAYLNAGTSFLWSCAPFLVSLVTFATYVLTseaNQLSVEKVLVSIALFDLMKLPLT-ILPMLSVDIAETQVSVN 623
Cdd:TIGR01271 294 LKLTRKIAYLRYFYSSAFFFSGFFVVFLSVVPYALI---KGIILRRIFTTISYCIVLRMTVTrQFPGAIQTWYDSLGAIT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 624 RINKFLNSEEldpNSVLHDSSKPHPMSIENGEFSWGDEI----------------------------------TLRNINI 669
Cdd:TIGR01271 371 KIQDFLCKEE---YKTLEYNLTTTEVEMVNVTASWDEGIgelfekikqnnkarkqpngddglffsnfslyvtpVLKNISF 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 670 EVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLAYVPQQAWIQNATVRDNILFGQTYDRKRYNKVIDACAL 749
Cdd:TIGR01271 448 KLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQL 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 750 RADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEVIGPkgILARKSRVLVT 829
Cdd:TIGR01271 528 EEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCK--LMSNKTRILVT 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 830 HGVTFLPQVDSIYVIKMGEISESGTFDQLVKNKGAFADFIIQHLQEGNEEEEELNQIK----RQISSTADVPELLGT--- 902
Cdd:TIGR01271 606 SKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLEAFDNFSAERRNSILtetlRRVSIDGDSTVFSGPeti 685
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 903 --------------------------------VEKAIKLARTESLSDSISVTS-------ADSLMG-------------- 929
Cdd:TIGR01271 686 kqsfkqpppefaekrkqsiilnpiasarkfsfVQMGPQKAQATTIEDAVREPSerkfslvPEDEQGeeslprgnqyhhgl 765
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 930 -------------------GGGSLRRRT----------------------KRQDSHDSVASAASLKKKQEVEGKLIETEK 968
Cdd:TIGR01271 766 qhqaqrrqsvlqlmthsnrGENRREQLQtsfrkkssitqqnelaseldiySRRLSKDSVYEISEEINEEDLKECFADERE 845
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 969 SQTGGVEFAVYKHYIKSVGIFLSVATLVLnFVFQAFQIGS--NLWL------TQWANDQNVANDTGLRDMY-LGVYGAFG 1039
Cdd:TIGR01271 846 NVFETTTWNTYLRYITTNRNLVFVLIFCL-VIFLAEVAASllGLWLitdnpsAPNYVDQQHANASSPDVQKpVIITPTSA 924
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1040 FGQVFSYIG-SVVIVYLGALIG----------TRKIFIQLFGNILHAPQAYFDIKPRARILDRLANDIYKLDVVLPELIR 1108
Cdd:TIGR01271 925 YYIFYIYVGtADSVLALGFFRGlplvhtlltvSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLF 1004
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1109 VFNSQVFRVLATIVVISLSTPIFLAVIVPIAFLYYFAQRFYVATSRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGD 1188
Cdd:TIGR01271 1005 DFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQS 1084
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1189 RFIEESDAKVDKNQVCKYPSVIANRWLAIRLEMVGNLIILFASLFAVLGGQTNPGLVGLSVSYALQVTQTLNWLVRMSSD 1268
Cdd:TIGR01271 1085 YFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSID 1164
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1269 IETNIVSVERIKEYGETKQEAP--------WELEQD-----KNKPKNWPQEGRVEFQNFQVRYREGLDLVLRGVSFNIQG 1335
Cdd:TIGR01271 1165 VDGLMRSVSRVFKFIDLPQEEPrpsggggkYQLSTVlvienPHAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEG 1244
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1336 GEKVGIVGRTGAGKSSLTLALFRIIeAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPVLFSGSLRINLDPFEIKTDDEI 1415
Cdd:TIGR01271 1245 GQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEI 1323
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1416 WKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKEC 1495
Cdd:TIGR01271 1324 WKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNC 1403
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|...
gi 45552357 1496 TVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLdNPKSAF 1538
Cdd:TIGR01271 1404 TVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL-NETSLF 1445
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
335-625 |
1.34e-161 |
|
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: 489.67 E-value: 1.34e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 335 FGALMKLFTDTLTFAQPQVLSLIISFVEAQDaEPEWKGILYAVLLFVLAAAQTFILGQYFHRMFIVGLRIRTALINAIYR 414
Cdd:cd18595 1 LAALLKLLSDILLFASPQLLKLLINFVEDPD-EPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 415 KALRISNSTKKESTVGEIVNLMAVDAQRFMELTTYLNMIWSAPLQIGLALYFLWQQLGPSVLAGLAVMIILIPVNGVIAS 494
Cdd:cd18595 80 KALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 495 RIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPSFEKQVLDIRDKEIATLRSTAYLNAGTSFLWSCAPFLVSLVTF 574
Cdd:cd18595 160 KIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 45552357 575 ATYVLTSEANQLSVEKVLVSIALFDLMKLPLTILPMLSVDIAETQVSVNRI 625
Cdd:cd18595 240 ATYVLSDPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
991-1282 |
1.45e-148 |
|
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: 455.01 E-value: 1.45e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 991 SVATLVLNFVFQAFQIGSNLWLTQWAND--QNVANDTGLRDMYLGVYGAFGFGQVFSYIGSVVIVYLGALIGTRKIFIQL 1068
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDpaLNGTQDTEQRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1069 FGNILHAPQAYFDIKPRARILDRLANDIYKLDVVLPELIRVFNSQVFRVLATIVVISLSTPIFLAVIVPIAFLYYFAQRF 1148
Cdd:cd18603 81 LHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1149 YVATSRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVIANRWLAIRLEMVGNLIIL 1228
Cdd:cd18603 161 YVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 1229 FASLFAVLGGQT-NPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERIKEY 1282
Cdd:cd18603 241 FAALFAVLSRDSlSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEY 295
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1307-1527 |
8.83e-137 |
|
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: 420.36 E-value: 8.83e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1307 GRVEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRL 1386
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1387 TIIPQDPVLFSGSLRINLDPFEIKTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKV 1466
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45552357 1467 LVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASP 1527
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
335-625 |
1.99e-119 |
|
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: 376.06 E-value: 1.99e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 335 FGALMKLFTDTLTFAQPQVLSLIISFVEAQDAEPEWKGILYAVLLFVLAAAQTFILGQYFHRMFIVGLRIRTALINAIYR 414
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 415 KALRISNSTKKESTVGEIVNLMAVDAQRFMELTTYLNMIWSAPLQIGLALYFLWQQLGPSVLAGLAVMIILIPVNGVIAS 494
Cdd:cd18579 81 KALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 495 RIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPSFEKQVLDIRDKEIATLRSTAYLNAGTSFLWSCAPFLVSLVTF 574
Cdd:cd18579 161 LISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 45552357 575 ATYVLTseANQLSVEKVLVSIALFDLMKLPLTILPMLSVDIAETQVSVNRI 625
Cdd:cd18579 241 ATYVLL--GNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
992-1533 |
5.80e-117 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 380.66 E-value: 5.80e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 992 VATLVLNFVFQAFQIGSnLWLTQWANDQNVAN-DTGLRDMYLGVYGAFGFGQ-VFSYIGSVVIVYLGALIGtRKIFIQLF 1069
Cdd:COG1132 24 ILALLLLLLSALLELLL-PLLLGRIIDALLAGgDLSALLLLLLLLLGLALLRaLLSYLQRYLLARLAQRVV-ADLRRDLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1070 GNILHAPQAYFDIKPRARILDRLANDIYKLDVVLPELIRVFNSQVFRVLATIVV-ISLSTPIFLAVIVPIAfLYYFAQRF 1148
Cdd:COG1132 102 EHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVlFVIDWRLALIVLLVLP-LLLLVLRL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1149 YVATSRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVIANRWLAIRLEMVGNL--- 1225
Cdd:COG1132 181 FGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLgla 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1226 IILFASLFAVLGGQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERIKEYGETKQEAPwELEQDKNKPknwPQ 1305
Cdd:COG1132 261 LVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP-DPPGAVPLP---PV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1306 EGRVEFQNFQVRYREGlDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSR 1385
Cdd:COG1132 337 RGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1386 LTIIPQDPVLFSGSLRINL---DPfEIkTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLR 1462
Cdd:COG1132 416 IGVVPQDTFLFSGTIRENIrygRP-DA-TDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLK 493
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45552357 1463 KTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLDN 1533
Cdd:COG1132 494 DPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR 564
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
649-848 |
4.85e-109 |
|
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: 344.07 E-value: 4.85e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 649 MSIENGEFSWGDE-----ITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLAYVPQQAWIQNA 723
Cdd:cd03250 1 ISVEDASFTWDSGeqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 724 TVRDNILFGQTYDRKRYNKVIDACALRADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDA 803
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 45552357 804 HVGKHIFEEVIGPKGiLARKSRVLVTHGVTFLPQVDSIYVIKMGE 848
Cdd:cd03250 161 HVGRHIFENCILGLL-LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1303-1527 |
6.24e-102 |
|
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: 324.37 E-value: 6.24e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1303 WPQEGRVEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHML 1382
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1383 RSRLTIIPQDPVLFSGSLRINLDPFEIKTDDEIWKALelshlksfvkslaaglnhEIAEGGENLSVGQRQLVCLARALLR 1462
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 1463 KTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASP 1527
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
991-1282 |
7.86e-99 |
|
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: 319.45 E-value: 7.86e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 991 SVATLVLNFVFQAFQIGSNLWLTQWAnDQNVANDTGLRDMYLGVYGAFGF-GQVFSYIGSVVIVYLGALIGTRKIFIQLF 1069
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWS-SDWSSSPNSSSGYYLGVYAALLVlASVLLVLLRWLLFVLAGLRASRRLHDKLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1070 GNILHAPQAYFDIKPRARILDRLANDIYKLDVVLPELIRVFNSQVFRVLATIVVISLSTPIFLAVIVPIAFLYYFAQRFY 1149
Cdd:cd18580 80 RSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1150 VATSRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVIANRWLAIRLEMVGNLIILF 1229
Cdd:cd18580 160 LRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 45552357 1230 ASLFAV-LGGQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERIKEY 1282
Cdd:cd18580 240 VALLAVlLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEY 293
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1032-1543 |
2.58e-92 |
|
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: 315.62 E-value: 2.58e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1032 LGVYGAFGFGQVFSYIGSVVIVYLGALIGTRKIFiQLFGNILHAPQAYFDIKPRARILDRLaNDIYKL-DVVLPELIRVF 1110
Cdd:COG2274 200 IGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSS-RFFRHLLRLPLSFFESRSVGDLASRF-RDVESIrEFLTGSLLTAL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1111 NSQVFRVLATIVVISLSTP---IFLAVIVPIAFLYYFAQRFYVATSRQLMRLESVsrspIYSHFSETVTGASTIRAYNVG 1187
Cdd:COG2274 278 LDLLFVLIFLIVLFFYSPPlalVVLLLIPLYVLLGLLFQPRLRRLSREESEASAK----RQSLLVETLRGIETIKALGAE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1188 DRFIEESDAK----VDKNQVCKYPSVIANRWLAIrLEMVGNLIILFASLFAVLGGQTNPG-LVGlSVSYALQVTQTLNWL 1262
Cdd:COG2274 354 SRFRRRWENLlakyLNARFKLRRLSNLLSTLSGL-LQQLATVALLWLGAYLVIDGQLTLGqLIA-FNILSGRFLAPVAQL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1263 VRMSSDIETNIVSVERIKEYGETKQEAPweleQDKNKPKNWPQEGRVEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIV 1342
Cdd:COG2274 432 IGLLQRFQDAKIALERLDDILDLPPERE----EGRSKLSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIV 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1343 GRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPVLFSGSLRINL---DPfEIkTDDEIWKAL 1419
Cdd:COG2274 508 GRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDP-DA-TDEEIIEAA 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1420 ELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLT 1499
Cdd:COG2274 586 RLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVII 665
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 45552357 1500 IAHRLNTILDSDKVIVLDKGQIIEFASPTELLDNpKSAFYSMAK 1543
Cdd:COG2274 666 IAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR-KGLYAELVQ 708
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
338-625 |
5.08e-90 |
|
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: 294.12 E-value: 5.08e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 338 LMKLFTDTLTFAQPQVLSLIISFVEAQDaEPEWKGILYAVLLFVLAAAQTFILGQYFHRMFIVGLRIRTALINAIYRKAL 417
Cdd:cd18559 4 LIKLVLCNHVFSGPSNLWLLLWFDDPVN-GPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 418 RISNSTKKESTVGEIVNLMAVDAQRFMELTTYLNMIWSAPLQIGLALYFLWQQLGPSVLAGLAVMIILIPVNGVIASRIK 497
Cdd:cd18559 83 RSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 498 TYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPSFEKQVLDIRDKEIATLRSTAYLNAGTSFLWSCAPFLVSLVTFATY 577
Cdd:cd18559 163 QLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAY 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 45552357 578 VLTSEANQLSVEKVLVSIALFDLMKLPLTILPMLSVDIAETQVSVNRI 625
Cdd:cd18559 243 VSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
988-1283 |
9.24e-90 |
|
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: 293.61 E-value: 9.24e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 988 IFLSVATLVLnfvFQAFQIGSNLWLTQWANDQ-NVANDTglrdmYLGVYGAFGFGQ-VFSYIGSVVIVYLGaLIGTRKIF 1065
Cdd:cd18606 1 LPLLLLLLIL---SQFAQVFTNLWLSFWTEDFfGLSQGF-----YIGIYAGLGVLQaIFLFLFGLLLAYLG-IRASKRLH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1066 IQLFGNILHAPQAYFDIKPRARILDRLANDIYKLDVVLPELIRVFNSQVFRVLATIVVISLSTPIFLAVIVPIAFLYYFA 1145
Cdd:cd18606 72 NKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1146 QRFYVATSRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVIANRWLAIRLEMVGNL 1225
Cdd:cd18606 152 ANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSL 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 1226 IILFASLFAVLG-GQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERIKEYG 1283
Cdd:cd18606 232 LVLIVALLCVTRrFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
335-625 |
6.10e-88 |
|
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: 288.30 E-value: 6.10e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 335 FGALMKLFTDTLTFAQPQVLSLIISFVEAQDaEPEWKGILYAVLLFVLAAAQTFILGQYFHRMFIVGLRIRTALINAIYR 414
Cdd:cd18598 1 PLGLLKLLADVLGFAGPLLLNKLVEFLEDSS-EPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 415 KALRISNSTKKESTVGEIVNLMAVDAQRFMELTTYLNMIWSAPLQIGLALYFLWQQLGPSVLAGLAVMIILIPVNGVIAS 494
Cdd:cd18598 80 KALRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 495 RIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPSFEKQVLDIRDKEIATLRSTAYLNAGTSFLWSCAPFLVSLVTF 574
Cdd:cd18598 160 RIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPVLISILTF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 45552357 575 ATYVLTseANQLSVEKVLVSIALFDLMKLPLTILPMLSVDIAETQVSVNRI 625
Cdd:cd18598 240 ATYVLM--GNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
992-1282 |
1.21e-87 |
|
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: 287.83 E-value: 1.21e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 992 VATLVLNFVFQAFQIGSNLWLTQWANDQNVANDTGLRDM----YLGVYGAFGFGQVFSYIGSVVIVYLGALIGTRKIFIQ 1067
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVsvlyYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1068 LFGNILHAPQAYFDIKPRARILDRLANDIYKLDVVLPELIRVFNSQVFRVLATIVVISLSTPIFLAVIVPIAFLYYFAQR 1147
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1148 FYVATSRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVIANRWLAIRLEMVGNLII 1227
Cdd:cd18604 162 LYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFS 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 1228 LFASLFAVLGGQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERIKEY 1282
Cdd:cd18604 242 FATAALLVYGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEY 296
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
337-625 |
6.97e-86 |
|
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: 283.23 E-value: 6.97e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 337 ALMKLFTDTLTFAQPQVLSLIISFVEAQDAEPEWKGILYAVLLFVLAAAQTFILGQYFHRMFIVGLRIRTALINAIYRKA 416
Cdd:cd18596 3 ALLAVLSSVLSFAPPFFLNRLLRYLEDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 417 LRI-------------------SNSTKKESTVGEIVNLMAVDAQRFMELTTYLNMIWSAPLQIGLALYFLWQQLGPSVLA 477
Cdd:cd18596 83 LRRrdksgssksseskkkdkeeDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 478 GLAVMIILIPVNGVIASRIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPSFEKQVLDIRDKEIATLRSTAYLNAG 557
Cdd:cd18596 163 GLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 558 TSFLWSCAPFLVSLVTFATYVLTsEANQLSVEKVLVSIALFDLMKLPLTILPMLSVDIAETQVSVNRI 625
Cdd:cd18596 243 LSLLWFLIPILVTVVTFATYTLV-MGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1307-1543 |
1.67e-85 |
|
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: 280.26 E-value: 1.67e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1307 GRVEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRL 1386
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1387 TIIPQDPVLFSGSLRINLDPFEIKTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKV 1466
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 1467 LVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLDNPKSAFYSMAK 1543
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVR 254
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
335-625 |
6.64e-82 |
|
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: 271.25 E-value: 6.64e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 335 FGALMKLFTDTLTFAQPQVLSLIISFVE---AQDAEPE-WKGILYAVLLFVLAAAQTFILGQYFHRMFIVGLRIRTALIN 410
Cdd:cd18597 1 LAGLLKLLADVLQVLSPLLLKYLINFVEdayLGGPPPSiGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 411 AIYRKALRISNSTKKESTVGEIVNLMAVDAQRFMELTTYLNMIWSAPLQIGLALYFLWQQLGPSVLAGLAVMIILIPVNG 490
Cdd:cd18597 81 AIYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 491 VIASRIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPSFEKQVLDIRDKEIATLRSTAYLNAGTSFLWSCAPFLVS 570
Cdd:cd18597 161 FLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLAS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 571 LVTFATYVLTSeaNQLSVEKVLVSIALFDLMKLPLTILPMLSVDIAETQVSVNRI 625
Cdd:cd18597 241 MLSFITYYATG--HTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
988-1282 |
1.92e-77 |
|
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: 259.07 E-value: 1.92e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 988 IFLSVATLVLNfvfQAFQIGSNLWLTQWAN-------DQNVANDTGLRDM----YLGVYGAFGFGQV-FSYIGSVVIVYL 1055
Cdd:cd18602 1 VALVLALALLK---QGLRVATDFWLADWTEanhdvasVVFNITSSSLEDDevsyYISVYAGLSLGAViLSLVTNLAGELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1056 GaLIGTRKIFIQLFGNILHAPQAYFDIKPRARILDRLANDIYKLDVVLPELIRVFNSQVFRVLATIVVISLSTPIFLAVI 1135
Cdd:cd18602 78 G-LRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1136 VPIAFLYYFAQRFYVATSRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVIANRWL 1215
Cdd:cd18602 157 IPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1216 AIRLEMVGNLIIL---FASLFAVLGGQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERIKEY 1282
Cdd:cd18602 237 GIRLDYLGAVIVFlaaLSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEY 306
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
991-1282 |
1.01e-75 |
|
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: 253.61 E-value: 1.01e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 991 SVATLVLNFVFQAFQIGSNLWLTQWANDQNVANDTGLRD---MYLGVYGAFGFGQ-VFSYIGSVVIVYlGALIGTRKIFI 1066
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWVSHSNNSFFNFINDsfnFFLTVYGFLAGLNsLFTLLRAFLFAY-GGLRAARRLHN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1067 QLFGNILHAPQAYFDIKPRARILDRLANDIYKLDVVLPELIRVFNSQVFRVLATIVVISLSTPIFLAVIVPIAFLYYFAQ 1146
Cdd:cd18605 80 KLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1147 RFYVATSRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVIANRWLAIRLEMVGNLI 1226
Cdd:cd18605 160 RYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVLI 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1227 ILFASLFAVL----GGQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERIKEY 1282
Cdd:cd18605 240 VTFVALTAVVqhffGLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQY 299
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1307-1532 |
6.14e-74 |
|
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: 245.98 E-value: 6.14e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1307 GRVEFQNFQVRYREGlDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRL 1386
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1387 TIIPQDPVLFSGSLRINLDPF-EIKTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTK 1465
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGrPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 1466 VLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLD 1532
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
324-868 |
3.17e-73 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 256.24 E-value: 3.17e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 324 PIYKSFGGVFLFGALMKLFTDTLTFAQPQVLSLII-SFVEAQDAEPEWKGILYAVLLFVLAAAQTFILGQYFHRmfiVGL 402
Cdd:COG1132 14 RYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIdALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLAR---LAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 403 RIRTALINAIYRKALRISNSTKKESTVGEIVNLMAVDAQRFME-LTTYLNMIWSAPLQIGLALYFLWQ---QLGpsvLAG 478
Cdd:COG1132 91 RVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQfLAHGLPQLVRSVVTLIGALVVLFVidwRLA---LIV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 479 LAVMIILIPVNGVIASRIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPS----FEKQVLDIRDKEIATLRSTAYL 554
Cdd:COG1132 168 LLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERelerFREANEELRRANLRAARLSALF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 555 NAGTSFLWSCAPFLVsLVTFATYVLtseANQLSVEKVLVSIALFDLMKLPLTILPMLSVDIAETQVSVNRINKFLNSEEl 634
Cdd:COG1132 248 FPLMELLGNLGLALV-LLVGGLLVL---SGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPP- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 635 dpnsVLHDSSKPHPMSIENGE-------FSW-GDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEME------K 700
Cdd:COG1132 323 ----EIPDPPGAVPLPPVRGEiefenvsFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDptsgriL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 701 LAGV-VNTV------GKLAYVPQQAWIQNATVRDNILFGQ-TYDRKRynkVIDACAL-RAD--IDILSAGDLTEIGEKGI 769
Cdd:COG1132 399 IDGVdIRDLtleslrRQIGVVPQDTFLFSGTIRENIRYGRpDATDEE---VEEAAKAaQAHefIEALPDGYDTVVGERGV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 770 NLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEVigpKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEI 849
Cdd:COG1132 476 NLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL---ERLMKGRTTIVIAHRLSTIRNADRILVLDDGRI 552
|
570
....*....|....*....
gi 45552357 850 SESGTFDQLVKNKGAFADF 868
Cdd:COG1132 553 VEQGTHEELLARGGLYARL 571
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1288-1533 |
1.14e-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: 254.30 E-value: 1.14e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1288 EAPWELEQDKNKPKNWPQEGRVEFQNFQVRYREGlDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRI 1367
Cdd:COG4988 316 DAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGG-RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSI 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1368 SIDGVDIASMGLHMLRSRLTIIPQDPVLFSGSLRINLDPFEIK-TDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENL 1446
Cdd:COG4988 395 LINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDaSDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGL 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1447 SVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFAS 1526
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGT 554
|
....*..
gi 45552357 1527 PTELLDN 1533
Cdd:COG4988 555 HEELLAK 561
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
331-626 |
1.16e-71 |
|
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: 241.77 E-value: 1.16e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 331 GVFLFgalmklFTDTLTFAQPQVLSLIISFVEAQDAEPEWKGILYAVLLFVLAAAQTFILGQYFHRMFIVGLRIRTALIN 410
Cdd:cd18594 3 GILLF------LEESLKIVQPLLLGRLVAYFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 411 AIYRKALRISNSTKKESTVGEIVNLMAVDAQRFMELTTYLNMIWSAPLQIGLALYFLWQQLGPSVLAGLAVMIILIPVNG 490
Cdd:cd18594 77 LIYKKTLKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 491 VIASRIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPSFEKQVLDIRDKEIATLRSTAYLNA-GTSFLWSCaPFLV 569
Cdd:cd18594 157 YLGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAfNMAFFFFS-PTLV 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 570 SLVTFATYVLTseANQLSVEKVLVSIALFDLMKLPLTI-LPMLSVDIAETQVSVNRIN 626
Cdd:cd18594 236 SFATFVPYVLT--GNTLTARKVFTVISLLNALRMTITRfFPESIQTLSESRVSLKRIQ 291
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1085-1543 |
9.36e-70 |
|
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: 245.83 E-value: 9.36e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1085 RARILDRLANDIYKLDVVLpelIRVfnsqVFRVLATIVVISLSTpIFLAVIVPIA-------------FLYYFAQRFYVA 1151
Cdd:COG4987 111 SGDLLNRLVADVDALDNLY---LRV----LLPLLVALLVILAAV-AFLAFFSPALalvlalglllaglLLPLLAARLGRR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1152 TSRQLMRLesvsRSPIYSHFSETVTGASTIRAYNVGDRFIEESDAkvdknqvckypsvIANRWLAI-----RLEMVGNLI 1226
Cdd:COG4987 183 AGRRLAAA----RAALRARLTDLLQGAAELAAYGALDRALARLDA-------------AEARLAAAqrrlaRLSALAQAL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1227 ILFASLFAVLG-----------GQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERIKEYGETKQEAPweleq 1295
Cdd:COG4987 246 LQLAAGLAVVAvlwlaaplvaaGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPPAVT----- 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1296 DKNKPKNWPQEGRVEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIA 1375
Cdd:COG4987 321 EPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLR 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1376 SMGLHMLRSRLTIIPQDPVLFSGSLRINL---DPfEIkTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQ 1452
Cdd:COG4987 401 DLDEDDLRRRIAVVPQRPHLFDTTLRENLrlaRP-DA-TDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERR 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1453 LVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLD 1532
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLA 558
|
490
....*....|.
gi 45552357 1533 NpKSAFYSMAK 1543
Cdd:COG4987 559 Q-NGRYRQLYQ 568
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
335-625 |
4.68e-68 |
|
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: 232.13 E-value: 4.68e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 335 FGALMKLFTDTLTFAQPQVLSLIISFVE----AQDAEPEWKGILY-------------AVLLFVLAAAQTFILGQYFHRM 397
Cdd:cd18591 1 LGGILKLLGDLLGFVGPLCISGIVDYVEentySSSNSTDKLSVSYvtveeffsngyvlAVILFLALLLQATFSQASYHIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 398 FIVGLRIRTALINAIYRKALRIS--NSTKKESTVGEIVNLMAVDAQRFMELTTYLNMIWSAPLQIGLALYFLWQQLGPSV 475
Cdd:cd18591 81 IREGIRLKTALQAMIYEKALRLSswNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 476 LAGLAVMIILIPVNGVIASRIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPSFEKQVLDIRDKEIATLRSTAYLN 555
Cdd:cd18591 161 LIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYW 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 556 AGTSFLWSCAPFLVSLVTFATYVLtSEANQLSVEKVLVSIALFDLMKLPLTILPMLSVDIAETQVSVNRI 625
Cdd:cd18591 241 SLMTFLTQASPILVTLVTFGLYPY-LEGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
335-625 |
2.36e-65 |
|
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: 223.64 E-value: 2.36e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 335 FGALMKLFTDTLTFAQPQVLSLIIS-FVEAQDAEPEWKGILYAVLLFVLAAAQTFILGQYFHRMFIVGLRIRTALINAIY 413
Cdd:cd18593 1 LLGIFLFLEEAIRVVQPIFLGKLIRyFEGNGSSISLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 414 RKALRISNSTKKESTVGEIVNLMAVDAQRFMELTTYLNMIWSAPLQIGLALYFLWQQLGPSVLAGLAVMIILIPVNGVIA 493
Cdd:cd18593 81 RKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 494 SRIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPSFEKQVLDIRDKEIATLRSTAYL---NAGTSFlwsCAPFLVS 570
Cdd:cd18593 161 KLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLralNMGLFF---VSSKLIL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 45552357 571 LVTFATYVLTseANQLSVEKVLVSIALFDLMKLPLTI-LPMLSVDIAETQVSVNRI 625
Cdd:cd18593 238 FLTFLAYILL--GNILTAERVFVTMALYNAVRLTMTLfFPFAIQFGSELSVSIRRI 291
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
987-1282 |
6.82e-65 |
|
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: 223.21 E-value: 6.82e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 987 GIFLSVATLVLNFVFQAFQIGSNLWLTQWAND------QNVANDTGLR---------DMYLGVYGAFGFGQVFSYIGSVV 1051
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQgsgnttNNVDNSTVDSgnisdnpdlNFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1052 IVYLGALIGTRKIFIQLFGNILHAPQAYFDIKPRARILDRLANDIYKLDVVLPELIRVFNSQVFRVLATIVVISLSTPIF 1131
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1132 LAVIVPIAFLYYFAQRFYVATSRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVIA 1211
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45552357 1212 NRWLAIRLEMVGNLIILFASLFAVLG-GQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERIKEY 1282
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLkGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEY 312
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1062-1532 |
2.47e-64 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 229.99 E-value: 2.47e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1062 RKIFIQLFGNILHAPQAYFDIKPRARILDRLANDIYKLDVVLPELIRVFNSQVFRVLATIVVI---SLSTPIFLAVIVP- 1137
Cdd:TIGR02203 87 RDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLlyySWQLTLIVVVMLPv 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1138 IAFLY-YFAQRFyvatsRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVIANRWLA 1216
Cdd:TIGR02203 167 LSILMrRVSKRL-----RRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISS 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1217 IRLEMVGNL---IILFASLFAVLGGQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERIKEYGETKQEapwel 1293
Cdd:TIGR02203 242 PITQLIASLalaVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPE----- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1294 eQDKNKPKNWPQEGRVEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVD 1373
Cdd:TIGR02203 317 -KDTGTRAIERARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHD 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1374 IASMGLHMLRSRLTIIPQDPVLFSGSLRINL---DPFEIkTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQ 1450
Cdd:TIGR02203 396 LADYTLASLRRQVALVSQDVVLFNDTIANNIaygRTEQA-DRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQ 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1451 RQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTEL 1530
Cdd:TIGR02203 475 RQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNEL 554
|
..
gi 45552357 1531 LD 1532
Cdd:TIGR02203 555 LA 556
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1309-1520 |
3.50e-62 |
|
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: 209.55 E-value: 3.50e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTI 1388
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1389 IPQDPVLFSGSLRINLdpfeiktddeiwkalelshlksfvkslaaglnheiaeggenLSVGQRQLVCLARALLRKTKVLV 1468
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 45552357 1469 LDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQ 1520
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
987-1283 |
3.30e-61 |
|
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: 212.57 E-value: 3.30e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 987 GIFLSVATLVLNFVFQAFQIGSNLWLTQWANDQNVANDTGL----------------RDMYLGVYGAFGFGQVFSYIGSV 1050
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEEKLNDTTDrvqgenstnvdiedldRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1051 VIVYLGALIGTRKIFIQLFGNILHAPQAYFDIKPRARILDRLANDIYKLDVVLPELIRVFNSQVFRVLATIVVISLSTPI 1130
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1131 FLAVIVPIAFLYYFAQRFYVATSRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVI 1210
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45552357 1211 ANRWLAIRLEMVGNLIILFASLFAVLGGQT-NPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERIKEYG 1283
Cdd:cd18601 241 TSRWLAVRLDALCALFVTVVAFGSLFLAESlDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEYS 314
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1309-1532 |
6.42e-61 |
|
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: 208.62 E-value: 6.42e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTI 1388
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1389 IPQDPVLFSGSLRINL---DPFEikTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTK 1465
Cdd:cd03251 81 VSQDVFLFNDTVAENIaygRPGA--TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 1466 VLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLD 1532
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLA 225
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1309-1541 |
1.31e-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: 207.85 E-value: 1.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLDlVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTI 1388
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1389 IPQDPVLFSGSLRINldpfeIK------TDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLR 1462
Cdd:cd03253 80 VPQDTVLFNDTIGYN-----IRygrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 1463 KTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLdNPKSAFYSM 1541
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL-AKGGLYAEM 232
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
651-847 |
2.53e-60 |
|
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: 206.41 E-value: 2.53e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 651 IENGEFSWGDEI-TLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVV-----------------NTVGKLA 712
Cdd:cd03290 3 VTNGYFSWGSGLaTLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRYSVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 713 YVPQQAWIQNATVRDNILFGQTYDRKRYNKVIDACALRADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLY 792
Cdd:cd03290 83 YAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 793 LLDDPLSAVDAHVGKHIFEEvigpkGILA-----RKSRVLVTHGVTFLPQVDSIYVIKMG 847
Cdd:cd03290 163 FLDDPFSALDIHLSDHLMQE-----GILKflqddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1222-1531 |
1.25e-58 |
|
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: 214.30 E-value: 1.25e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1222 VGNLIILFASLFAVLGGQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERIKEYGETKQEApweleQDKNKPK 1301
Cdd:COG5265 275 LGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEV-----ADAPDAP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1302 NWP-QEGRVEFQNFQVRY---REgldlVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASM 1377
Cdd:COG5265 350 PLVvGGGEVRFENVSFGYdpeRP----ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDV 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1378 GLHMLRSRLTIIPQDPVLFSGSLRINldpfeIK------TDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQR 1451
Cdd:COG5265 426 TQASLRAAIGIVPQDTVLFNDTIAYN-----IAygrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEK 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1452 QLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELL 1531
Cdd:COG5265 501 QRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELL 580
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
327-869 |
1.25e-57 |
|
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: 213.54 E-value: 1.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 327 KSFGGVFLFGALMKLFTDTLTFAQPQVLSLIISFVEAQDAEPEWkgILYAVLLFVLAAAQTFIlgQYFhRMFIV---GLR 403
Cdd:COG2274 152 RRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTL--WVLAIGLLLALLFEGLL--RLL-RSYLLlrlGQR 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 404 IRTALINAIYRKALRISNSTKKESTVGEIVN-LMAVDA-QRFmeLTTYLNMIWSAPLQIGLALYFLWQQLGPSVLAGLAV 481
Cdd:COG2274 227 IDLRLSSRFFRHLLRLPLSFFESRSVGDLASrFRDVESiREF--LTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 482 MIILIPVNGVIASRIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPSF----EKQVLDIRDKEIATLRSTAYLNAG 557
Cdd:COG2274 305 IPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFrrrwENLLAKYLNARFKLRRLSNLLSTL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 558 TSFLwscaPFLVSLVTF---ATYVLtseANQLSVEKVLVSIALFDLMKLPLTILPMLSVDIAETQVSVNRINKFLNSE-- 632
Cdd:COG2274 385 SGLL----QQLATVALLwlgAYLVI---DGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPpe 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 633 -ELDPNSVLHDSSKPHpMSIENGEFSWGD--EITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVV---- 705
Cdd:COG2274 458 rEEGRSKLSLPRLKGD-IELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidg 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 706 ---NTVGK------LAYVPQQAWIQNATVRDNILFG-QTYDRKRYNKVIDACALRADIDILSAGDLTEIGEKGINLSGGQ 775
Cdd:COG2274 537 idlRQIDPaslrrqIGVVLQDVFLFSGTIRENITLGdPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQ 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 776 KQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEVigpKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEISESGTF 855
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENL---RRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTH 693
|
570
....*....|....
gi 45552357 856 DQLVKNKGAFADFI 869
Cdd:COG2274 694 EELLARKGLYAELV 707
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1307-1522 |
2.62e-55 |
|
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: 192.03 E-value: 2.62e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1307 GRVEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRL 1386
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1387 TIIPQDPVLFSGSLRINL---DPFeiKTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRK 1463
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAPL--ADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 1464 TKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQII 1522
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1309-1543 |
5.79e-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: 191.60 E-value: 5.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLD-LVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLT 1387
Cdd:cd03249 1 IEFKNVSFRYPSRPDvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1388 IIPQDPVLFSGSLRINldpfeIK------TDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALL 1461
Cdd:cd03249 81 LVSQEPVLFDGTIAEN-----IRygkpdaTDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1462 RKTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLDNpKSAFYSM 1541
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQ-KGVYAKL 234
|
..
gi 45552357 1542 AK 1543
Cdd:cd03249 235 VK 236
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1054-1541 |
1.29e-54 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 204.57 E-value: 1.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1054 YLGALIgTRKIFIQLFGNILHAPQAYFDIKPRARILDRLANDIY--------KLDVVLPELIRVFNSQVFRVLATiVVIS 1125
Cdd:TIGR00958 227 YTMARI-NLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQtmsrslslNVNVLLRNLVMLLGLLGFMLWLS-PRLT 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1126 LSTPIFLAVIVPIAFLYyfaQRFYVATSRQLMrlESVSRSPIYSHfsETVTGASTIRAY----NVGDRFIE--ESDAKVD 1199
Cdd:TIGR00958 305 MVTLINLPLVFLAEKVF---GKRYQLLSEELQ--EAVAKANQVAE--EALSGMRTVRSFaaeeGEASRFKEalEETLQLN 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1200 KNQVCKYpsvIANRWLAIRLEMVGNLIILFASLFAVLGGQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERI 1279
Cdd:TIGR00958 378 KRKALAY---AGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKV 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1280 KEYGETKQEAPWELEQdknKPKNwpQEGRVEFQNFQVRYREGLDL-VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFR 1358
Cdd:TIGR00958 455 FEYLDRKPNIPLTGTL---APLN--LEGLIEFQDVSFSYPNRPDVpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQN 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1359 IIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPVLFSGSLRINLD-PFEIKTDDEIWKALELSHLKSFVKSLAAGLNH 1437
Cdd:TIGR00958 530 LYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDT 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1438 EIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTirTEFKECTVLTIAHRLNTILDSDKVIVLD 1517
Cdd:TIGR00958 610 EVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQILVLK 687
|
490 500
....*....|....*....|....
gi 45552357 1518 KGQIIEFASPTELLDNPkSAFYSM 1541
Cdd:TIGR00958 688 KGSVVEMGTHKQLMEDQ-GCYKHL 710
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
664-870 |
3.60e-54 |
|
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: 191.22 E-value: 3.60e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLAYVPQQAWIQNATVRDNILFGQTYDRKRYNKV 743
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 744 IDACALRADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEVIGPkgILARK 823
Cdd:cd03291 133 VKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCK--LMANK 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 45552357 824 SRVLVTHGVTFLPQVDSIYVIKMGEISESGTFDQLVKNKGAFADFII 870
Cdd:cd03291 211 TRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLM 257
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1307-1538 |
6.89e-54 |
|
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: 190.07 E-value: 6.89e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1307 GRVEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGgRISIDGVDIASMGLHMLRSRL 1386
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEG-DIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1387 TIIPQDPVLFSGSLRINLDPFEIKTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKV 1466
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45552357 1467 LVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLdNPKSAF 1538
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL-NEKSHF 230
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
1004-1282 |
3.48e-53 |
|
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: 188.58 E-value: 3.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1004 FQIGSNLWLTQW-ANDQNVANDTGLrdMYLGVYGAFGFGQVFSYIGSVVIVYLGALIGTRKIFIQLFGNILHAPQAYFDI 1082
Cdd:cd18559 14 FSGPSNLWLLLWfDDPVNGPQEHGQ--VYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1083 KPRARILDRLANDIYKLDVVLPELIRVFNSQVFRVLATIVVISLSTPIFlAVIVPIAFLYYFAQRFYVATSRQLMRLESV 1162
Cdd:cd18559 92 TPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMA-AVGIPLGLLYVPVNRVYAASSRQLKRLESV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1163 SRSPIYSHFSETVTGASTIRAYNVGDRFIEESDAKVDkNQVCKYPSVIANRWLAIRLEMVGNLIILFASLFAVLGGQTNP 1242
Cdd:cd18559 171 SKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHSLA 249
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 45552357 1243 GLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERIKEY 1282
Cdd:cd18559 250 GLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLER 289
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1073-1541 |
7.00e-52 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 193.78 E-value: 7.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1073 LHAPQAYFDIKPRARILDRLANDIyklDVVLPELIRVFNSqVFRVLATIVVI-----SL-------STPIFLAVIVpIAF 1140
Cdd:PRK10790 109 LRQPLSAFDTQPVGQLISRVTNDT---EVIRDLYVTVVAT-VLRSAALIGAMlvamfSLdwrmalvAIMIFPAVLV-VMV 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1141 LYyfaQRFYVATSRQLmrlesvsRS---PIYSHFSETVTGASTIRAYNVGDRFIEesdaKVDKNQVCKYPSvianRWLAI 1217
Cdd:PRK10790 184 IY---QRYSTPIVRRV-------RAylaDINDGFNEVINGMSVIQQFRQQARFGE----RMGEASRSHYMA----RMQTL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1218 RLE--MVGNLIILFASL----FAVLGGQTNPGLVGLSVSYALqvtqtLNWLVRMS----------SDIETNIVSVERIKE 1281
Cdd:PRK10790 246 RLDgfLLRPLLSLFSALilcgLLMLFGFSASGTIEVGVLYAF-----ISYLGRLNeplielttqqSMLQQAVVAGERVFE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1282 YgetkQEAPWELEQDKNKPKnwpQEGRVEFQNFQVRYREGlDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIE 1361
Cdd:PRK10790 321 L----MDGPRQQYGNDDRPL---QSGRIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1362 AAGGRISIDGVDIASMGLHMLRSRLTIIPQDPVLFSGSLRINLDPFEIKTDDEIWKALELSHLKSFVKSLAAGLNHEIAE 1441
Cdd:PRK10790 393 LTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGE 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1442 GGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQI 1521
Cdd:PRK10790 473 QGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQA 552
|
490 500
....*....|....*....|
gi 45552357 1522 IEFASPTELLDNpKSAFYSM 1541
Cdd:PRK10790 553 VEQGTHQQLLAA-QGRYWQM 571
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1309-1532 |
4.15e-51 |
|
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: 180.76 E-value: 4.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTI 1388
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1389 IPQDPVLFSGSLRINLDPFEIKTD-DEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKVL 1467
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSmERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 1468 VLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLD 1532
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA 225
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
335-625 |
5.13e-51 |
|
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: 182.38 E-value: 5.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 335 FGALMKLFTDTLTFAQPQ-VLSLIISFVEAQDaEPEWKGILYAVLLFVLAAAQTFILGQYFHRMFIVGLRIRTALINAIY 413
Cdd:cd18592 1 FSILLLLISLIFGFIGPTiLIRKLLEYLEDSD-SSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 414 RKALRISNStkKESTVGEIVNLMAVDAQRFMELTTYLNMIWSAPLQIGLALYFLWQQLGPSVLAGLAVMIILIPVNGVIA 493
Cdd:cd18592 80 KKILRLRSL--GDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 494 SRIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPSFEKQVLDIRDKEIATLRSTAYLNagtSFLWSCAPFLV---S 570
Cdd:cd18592 158 KLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQ---SISISLAPIVPviaS 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 571 LVTFATYVLTseANQLSVEKVLVSIALFDLMKLPLTILPMLSVDIAETQVSVNRI 625
Cdd:cd18592 235 VVTFLAHVAL--GNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
333-863 |
3.16e-48 |
|
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: 182.27 E-value: 3.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 333 FLFGALMKLFTDTLTFAQPQVLSLIIS--FVEAQDAEPEWKGILYAVLLFVLAAAQTFILGQYFHRMfivGLRIRTALIN 410
Cdd:COG4988 19 LALAVLLGLLSGLLIIAQAWLLASLLAglIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRA---AARVKRRLRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 411 AIYRKALRIS-NSTKKESTvGEIVNLM--AVDAqrfME--LTTYLNMIWSA---PLQIGLALYFLwqqlgpSVLAG--LA 480
Cdd:COG4988 96 RLLEKLLALGpAWLRGKST-GELATLLteGVEA---LDgyFARYLPQLFLAalvPLLILVAVFPL------DWLSGliLL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 481 VMIILIPVnGVIASRIKTyQIRQMKYKDERVKLMN---EVLSGIKVLKLY----AWEPSFEKQVLDIRDKEIATLRSTay 553
Cdd:COG4988 166 VTAPLIPL-FMILVGKGA-AKASRRQWRALARLSGhflDRLRGLTTLKLFgrakAEAERIAEASEDFRKRTMKVLRVA-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 554 lnagtsflwscapFLVSLVT-FATYvltseanqLSVEKVLVSIAlFDLMKLPLTILPMLSV------------------- 613
Cdd:COG4988 242 -------------FLSSAVLeFFAS--------LSIALVAVYIG-FRLLGGSLTLFAALFVlllapefflplrdlgsfyh 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 614 DIAETQVSVNRINKFLNSEELDPNSVLHDSSKPHPMSI--ENGEFSWGDEIT-LRNINIEVKKGSLVALVGTVGSGKSSV 690
Cdd:COG4988 300 ARANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIelEDVSFSYPGGRPaLDGLSLTIPPGERVALVGPSGAGKSTL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 691 VQAFLGEMEKLAGVVnTVG--------------KLAYVPQQAWIQNATVRDNILFGQT-YDRKRYNKVIDACALRADIDI 755
Cdd:COG4988 380 LNLLLGFLPPYSGSI-LINgvdlsdldpaswrrQIAWVPQNPYLFAGTIRENLRLGRPdASDEELEAALEAAGLDEFVAA 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 756 LSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEVigpKGILARKSRVLVTHGVTFL 835
Cdd:COG4988 459 LPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQAL---RRLAKGRTVILITHRLALL 535
|
570 580
....*....|....*....|....*...
gi 45552357 836 PQVDSIYVIKMGEISESGTFDQLVKNKG 863
Cdd:COG4988 536 AQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1299-1516 |
2.10e-47 |
|
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: 179.02 E-value: 2.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1299 KPKNWPQEGRVEFQNFQVRYrEGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMG 1378
Cdd:TIGR02857 312 APVTAAPASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1379 LHMLRSRLTIIPQDPVLFSGSLRINL---DPFeiKTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVC 1455
Cdd:TIGR02857 391 ADSWRDQIAWVPQHPFLFAGTIAENIrlaRPD--ASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45552357 1456 LARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVL 1516
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1306-1521 |
4.50e-47 |
|
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: 168.80 E-value: 4.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1306 EGRVEFQNFQVRYREGLD-LVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRS 1384
Cdd:cd03248 9 KGIVKFQNVTFAYPTRPDtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1385 RLTIIPQDPVLFSGSLRINLD-PFEIKTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRK 1463
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 1464 TKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQI 1521
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
460-868 |
1.53e-46 |
|
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: 177.27 E-value: 1.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 460 IGLALYFLWQQLGPSVLAGLAVMIILIPVNGVIASRIKTYQIRQMKYkDERVKLMnEVLSGIKVLKLYAWEPSFEKQVLD 539
Cdd:COG4987 146 AVAFLAFFSPALALVLALGLLLAGLLLPLLAARLGRRAGRRLAAARA-ALRARLT-DLLQGAAELAAYGALDRALARLDA 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 540 IRDKEIATLRSTAYLNAGTSFLWSCAPFLVSLVTFATYVLTSEANQLSVEK----VLVSIALFDlmklPLTILPMLSVDI 615
Cdd:COG4987 224 AEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLlallVLAALALFE----ALAPLPAAAQHL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 616 AETQVSVNRINKFLNSEeldPNSVLHDSSKPHP----MSIENGEFSW--GDEITLRNINIEVKKGSLVALVGTVGSGKSS 689
Cdd:COG4987 300 GRVRAAARRLNELLDAP---PAVTEPAEPAPAPggpsLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKST 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 690 VVQAFLGEMEKLAGVVnTVG--------------KLAYVPQQAWIQNATVRDNILFG-QTYDRKRYNKVIDACALRADID 754
Cdd:COG4987 377 LLALLLRFLDPQSGSI-TLGgvdlrdldeddlrrRIAVVPQRPHLFDTTLRENLRLArPDATDEELWAALERVGLGDWLA 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 755 ILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEVigpKGILARKSRVLVTHGVTF 834
Cdd:COG4987 456 ALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADL---LEALAGRTVLLITHRLAG 532
|
410 420 430
....*....|....*....|....*....|....
gi 45552357 835 LPQVDSIYVIKMGEISESGTFDQLVKNKGAFADF 868
Cdd:COG4987 533 LERMDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1126-1543 |
3.94e-46 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 176.69 E-value: 3.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1126 LSTPIFLAVIVPIAFlyYFAQR----------FYVATSRQLMR-----LESVSR--SPIYSHFSETVTGASTIRAYNvgd 1188
Cdd:PRK13657 138 LATLVALVVLLPLAL--FMNWRlslvlvvlgiVYTLITTLVMRktkdgQAAVEEhyHDLFAHVSDAIGNVSVVQSYN--- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1189 RFIEESDA---KVDKNQVCKYPSV-------IANRwLAIRLEMvgnLIILFASLFAVLGGQTNPGLVGLSVSYALQVTQT 1258
Cdd:PRK13657 213 RIEAETQAlrdIADNLLAAQMPVLswwalasVLNR-AASTITM---LAILVLGAALVQKGQLRVGEVVAFVGFATLLIGR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1259 LNwlvRMSSDIETNIVSVERIKEYGETKQEAPweleqDKNKPKNWPQ----EGRVEFQNFQVRY---REGLDlvlrGVSF 1331
Cdd:PRK13657 289 LD---QVVAFINQVFMAAPKLEEFFEVEDAVP-----DVRDPPGAIDlgrvKGAVEFDDVSFSYdnsRQGVE----DVSF 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1332 NIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPVLFSGSLRINLD-PFEIK 1410
Cdd:PRK13657 357 EAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRvGRPDA 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1411 TDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRT 1490
Cdd:PRK13657 437 TDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDE 516
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 45552357 1491 EFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLDNpKSAFYSMAK 1543
Cdd:PRK13657 517 LMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVAR-GGRFAALLR 568
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1292-1531 |
1.50e-45 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 174.82 E-value: 1.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1292 ELEQDKNKPKNWPQEGRVEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDG 1371
Cdd:PRK11176 325 EQEKDEGKRVIERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1372 VDIASMGLHMLRSRLTIIPQDPVLFSGSLRINL--DPFEIKTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVG 1449
Cdd:PRK11176 405 HDLRDYTLASLRNQVALVSQNVHLFNDTIANNIayARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGG 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1450 QRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTE 1529
Cdd:PRK11176 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAE 564
|
..
gi 45552357 1530 LL 1531
Cdd:PRK11176 565 LL 566
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
983-1532 |
5.04e-45 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 175.31 E-value: 5.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 983 IKSVGIFLSVATLVLNFVFQAF-----QIGSNLWLTQWAN---DQNVANDTGLrdMYLGVYGAFGFGQVFSYIGSVVIVY 1054
Cdd:TIGR01193 145 LKFIPLITRQKKLIVNIVIAAIivtliSIAGSYYLQKIIDtyiPHKMMGTLGI--ISIGLIIAYIIQQILSYIQIFLLNV 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1055 LGALIgTRKIFIQLFGNILHAPQAYFDIKPRARILDRLANDIYKLDVVLPELIRVFNSQVFRVLATIVVISLSTPIFLAV 1134
Cdd:TIGR01193 223 LGQRL-SIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLS 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1135 IVPI---AFLYYFAQRFYVATSRQLMRLESVSRSPIYshfsETVTGASTIRAYNVGDrfieESDAKVDK------NQVCK 1205
Cdd:TIGR01193 302 LLSIpvyAVIIILFKRTFNKLNHDAMQANAVLNSSII----EDLNGIETIKSLTSEA----ERYSKIDSefgdylNKSFK 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1206 YPSVIANRwLAIR--LEMVGNLIILFASLFAVLGGQTNpglVGLSVSYALQVTQTLNWL---VRMSSDIETNIVSVERIK 1280
Cdd:TIGR01193 374 YQKADQGQ-QAIKavTKLILNVVILWTGAYLVMRGKLT---LGQLITFNALLSYFLTPLeniINLQPKLQAARVANNRLN 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1281 EYgetkQEAPWELEQDKNKPKNWPQEGRVEFQNFQVRYREGlDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRII 1360
Cdd:TIGR01193 450 EV----YLVDSEFINKKKRTELNNLNGDIVINDVSYSYGYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFF 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1361 EAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPVLFSGSLRINL--DPFEIKTDDEIWKALELSHLKSFVKSLAAGLNHE 1438
Cdd:TIGR01193 525 QARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLllGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTE 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1439 IAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIrTEFKECTVLTIAHRLNTILDSDKVIVLDK 1518
Cdd:TIGR01193 605 LSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNL-LNLQDKTIIFVAHRLSVAKQSDKIIVLDH 683
|
570
....*....|....
gi 45552357 1519 GQIIEFASPTELLD 1532
Cdd:TIGR01193 684 GKIIEQGSHDELLD 697
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1085-1504 |
4.02e-44 |
|
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: 169.46 E-value: 4.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1085 RARILDRLANDIYKLDVVLPELIRVFNSQVFRVLATIVVISLSTPIFLAVIVPIAFLYYF-AQRFYVATSRQLMRLESVS 1163
Cdd:TIGR02868 109 RGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLAGFvAPLVSLRAARAAEQALARL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1164 RSPIYSHFSETVTGASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVIANRW------LAIRLEMVGNLIilfASLFAVLG 1237
Cdd:TIGR02868 189 RGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALgaaltlLAAGLAVLGALW---AGGPAVAD 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1238 GQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERIKEYGETKQEAPW-ELEQDKNKPknwPQEGRVEFQNFQV 1316
Cdd:TIGR02868 266 GRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVAEgSAPAAGAVG---LGKPTLELRDLSA 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1317 RYrEGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPVLF 1396
Cdd:TIGR02868 343 GY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLF 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1397 SGSLRINL-----DpfeiKTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDE 1471
Cdd:TIGR02868 422 DTTVRENLrlarpD----ATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDE 497
|
410 420 430
....*....|....*....|....*....|...
gi 45552357 1472 ATAAVDLETDDLIQKTIRTEFKECTVLTIAHRL 1504
Cdd:TIGR02868 498 PTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1213-1531 |
4.49e-44 |
|
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: 172.06 E-value: 4.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1213 RWLAIRLEMVGNLIILF---------ASLFAVLGGQ-TNPGL-VGLSVSYALQVTQTLNWLVRMSSDIeTNIVSV----E 1277
Cdd:TIGR03797 348 RKLELSAQRIENLLTVFnavlpvltsAALFAAAISLlGGAGLsLGSFLAFNTAFGSFSGAVTQLSNTL-ISILAViplwE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1278 RIKEYGETKQEApweleqDKNKPKNWPQEGRVEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLtlalF 1357
Cdd:TIGR03797 427 RAKPILEALPEV------DEAKTDPGKLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTL----L 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1358 RII---EAAG-GRISIDGVDIASMGLHMLRSRLTIIPQDPVLFSGSLRINLDPFEIKTDDEIWKALELSHLKSFVKSLAA 1433
Cdd:TIGR03797 497 RLLlgfETPEsGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPM 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1434 GLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIrtEFKECTVLTIAHRLNTILDSDKV 1513
Cdd:TIGR03797 577 GMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESL--ERLKVTRIVIAHRLSTIRNADRI 654
|
330
....*....|....*...
gi 45552357 1514 IVLDKGQIIEFASPTELL 1531
Cdd:TIGR03797 655 YVLDAGRVVQQGTYDELM 672
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1329-1541 |
1.82e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 159.63 E-value: 1.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1329 VSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIeAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPVLFSGSLRINLDPFE 1408
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1409 IK-TDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKT 1487
Cdd:PRK11174 448 PDaSDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 45552357 1488 IRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLDNPkSAFYSM 1541
Cdd:PRK11174 528 LNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG-GLFATL 580
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
333-601 |
1.70e-39 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 148.56 E-value: 1.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 333 FLFGALMKLFTDTLTFAQPQVLSLIISFVEAQDAEPEWKGILYAVLLFVLAAAQTFILGQYFHRMFIVGLRIRTALINAI 412
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 413 YRKALRISNSTKKESTVGEIVNLMAVDAQRFMELTTYLNMIWSAPLQIGLALYFLWQQLGPSV-LAGLAVMIILIPVNGV 491
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLtLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 492 IASRIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPSFEKQVLDIRDKEI-ATLRSTAYLNAGTSFLWSCAPFLVS 570
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALkAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|.
gi 45552357 571 LVTFATYVLtSEANQLSVEKVLVSIALFDLM 601
Cdd:pfam00664 241 LALWFGAYL-VISGELSVGDLVAFLSLFAQL 270
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1309-1535 |
5.73e-39 |
|
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: 145.55 E-value: 5.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGlDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTI 1388
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1389 IPQDP------------VLFsGSLRINLDPFEIKtdDEIWKALELSHLKSFvkslaagLNHEIAEggenLSVGQRQLVCL 1456
Cdd:COG1122 80 VFQNPddqlfaptveedVAF-GPENLGLPREEIR--ERVEEALELVGLEHL-------ADRPPHE----LSGGQKQRVAI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1457 ARALLRKTKVLVLDEATAAVDLETDDLIQKTIRtEFKE--CTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDN 1533
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLK-RLNKegKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSD 224
|
..
gi 45552357 1534 PK 1535
Cdd:COG1122 225 YE 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1309-1525 |
3.52e-38 |
|
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: 143.03 E-value: 3.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLDLV--LRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHML---R 1383
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1384 SRLTIIPQDPvlfSGSL-------RINLDPFEIKTDDEIWKALELSHLKSFVK-SLAAG-LN---HEiaeggenLSVGQR 1451
Cdd:cd03257 82 KEIQMVFQDP---MSSLnprmtigEQIAEPLRIHGKLSKKEARKEAVLLLLVGvGLPEEvLNrypHE-------LSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 1452 QLVCLARALLRKTKVLVLDEATAAVDLETDDLIQ---KTIRTEFKeCTVLTIAHRLNTILD-SDKVIVLDKGQIIEFA 1525
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILdllKKLQEELG-LTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
331-844 |
5.59e-37 |
|
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: 147.82 E-value: 5.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 331 GVFLFGALMKLFTDTLTFAQPQVLSLIISFVEAQdAEPeWKGILYAVLLFVLAAAQTFILGQYFHRM-FIVGLRIRTALI 409
Cdd:TIGR02857 3 RALALLALLGVLGALLIIAQAWLLARVVDGLISA-GEP-LAELLPALGALALVLLLRALLGWLQERAaARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 410 NAIYRKALRISNSTKKESTVGEIVNLM--AVDAqrfME--LTTYLNMIWSA---PLQIGLALyfLWQqlgpSVLAGLAVM 482
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGELATLAleGVEA---LDgyFARYLPQLVLAvivPLAILAAV--FPQ----DWISGLILL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 483 II--LIPV-NGVIASRIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPSFEKQVLDI----RDKEIATLRstayln 555
Cdd:TIGR02857 152 LTapLIPIfMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSseeyRERTMRVLR------ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 556 agTSFLWSCApflvsLVTFATyvltseanqLSVEKVLVSI-------------ALFDLMKLPLTILPMLSV-----DIAE 617
Cdd:TIGR02857 226 --IAFLSSAV-----LELFAT---------LSVALVAVYIgfrllagdldlatGLFVLLLAPEFYLPLRQLgaqyhARAD 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 618 TQVSVNRINKFLNSEELdPNSVLHDSSKPHPMSIE--NGEFSWGDE-ITLRNINIEVKKGSLVALVGTVGSGKSSVVQAF 694
Cdd:TIGR02857 290 GVAAAEALFAVLDAAPR-PLAGKAPVTAAPASSLEfsGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 695 LGEMEKLAGVVNTVG-------------KLAYVPQQAWIQNATVRDNILFGQTY-DRKRYNKVIDACALRADIDILSAGD 760
Cdd:TIGR02857 369 LGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIAENIRLARPDaSDAEIREALERAGLDEFVAALPQGL 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 761 LTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEVigpKGILARKSRVLVTHGVTFLPQVDS 840
Cdd:TIGR02857 449 DTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEAL---RALAQGRTVLLVTHRLALAALADR 525
|
....
gi 45552357 841 IYVI 844
Cdd:TIGR02857 526 IVVL 529
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
986-1259 |
7.83e-37 |
|
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: 140.86 E-value: 7.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 986 VGIFLSVATLVLNFVFqafqigsNLWLTQWANDQNVANDTGLRDM--YLGVYGAFGFGQ-VFSYIGSVVIVYLGALIgTR 1062
Cdd:pfam00664 3 LAILLAILSGAISPAF-------PLVLGRILDVLLPDGDPETQALnvYSLALLLLGLAQfILSFLQSYLLNHTGERL-SR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1063 KIFIQLFGNILHAPQAYFDIKPRARILDRLANDIYKLDVVLPELIRVFNSQVFRVLATIVVISLSTPIFLAVIVPIAFLY 1142
Cdd:pfam00664 75 RLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1143 YFAQRFYVATSRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVIANRWLAIRLEMV 1222
Cdd:pfam00664 155 ILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFI 234
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 45552357 1223 GNLIILFASLFA---VLGGQTNPGLVGLSVSYALQVTQTL 1259
Cdd:pfam00664 235 GYLSYALALWFGaylVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1309-1536 |
8.13e-37 |
|
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: 146.97 E-value: 8.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAG---GRISIDGVDIASMGLHMLRSR 1385
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1386 LTIIPQDPvlfsgslRINLDPFEIktDDEIWKALELSHL-----KSFVKSLAA--GLNHEIAEGGENLSVGQRQLVCLAR 1458
Cdd:COG1123 85 IGMVFQDP-------MTQLNPVTV--GDQIAEALENLGLsraeaRARVLELLEavGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1459 ALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKE--CTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNPK 1535
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
.
gi 45552357 1536 S 1536
Cdd:COG1123 236 A 236
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1273-1531 |
1.04e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 147.66 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1273 IVSVERIKEYgeTKQEAPWELEQDKNKPknwPQEGRVEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSL 1352
Cdd:PRK11160 308 IASARRINEI--TEQKPEVTFPTTSTAA---ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1353 TLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPVLFSGSLRINL---DPfeIKTDDEIWKALELSHLKSFVK 1429
Cdd:PRK11160 383 LQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKLLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1430 SlAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILD 1509
Cdd:PRK11160 461 D-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQ 539
|
250 260
....*....|....*....|..
gi 45552357 1510 SDKVIVLDKGQIIEFASPTELL 1531
Cdd:PRK11160 540 FDRICVMDNGQIIEQGTHQELL 561
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1310-1521 |
1.11e-36 |
|
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: 136.58 E-value: 1.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1310 EFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTII 1389
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1390 PQDPVLFSGSLRINLdpfeiktddeiwkalelshlksfvkslaaglnheiaeggenLSVGQRQLVCLARALLRKTKVLVL 1469
Cdd:cd03246 82 PQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 45552357 1470 DEATAAVDLETDDLIQKTI-RTEFKECTVLTIAHRLNTILDSDKVIVLDKGQI 1521
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIaALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1278-1537 |
1.45e-36 |
|
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: 146.20 E-value: 1.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1278 RIKEYGETKQ--------EAPWELEQDKNKPKNWPQEGR--VEFQNFQVRYREGLD---LVLRGVSFNIQGGEKVGIVGR 1344
Cdd:COG1123 220 RIVEDGPPEEilaapqalAAVPRLGAARGRAAPAAAAAEplLEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1345 TGAGKSSLTLALFRIIEAAGGRISIDGVDIASMG---LHMLRSRLTIIPQDPvlfSGSlrinLDPFEiKTDDEIWKALEL 1421
Cdd:COG1123 300 SGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDP---YSS----LNPRM-TVGDIIAEPLRL 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1422 SHLKSF------VKSLAA--GLNHEIAE--GGEnLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLetddLIQKTIRTE 1491
Cdd:COG1123 372 HGLLSRaerrerVAELLErvGLPPDLADryPHE-LSGGQRQRVAIARALALEPKLLILDEPTSALDV----SVQAQILNL 446
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 45552357 1492 FKE------CTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNPKSA 1537
Cdd:COG1123 447 LRDlqrelgLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFANPQHP 499
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1310-1520 |
1.06e-35 |
|
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: 135.29 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1310 EFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTII 1389
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1390 PQDP------------VLFsGSLRINLDPFEI-KTDDEIWKALELSHLksfvkslaagLNHEIAEggenLSVGQRQLVCL 1456
Cdd:cd03225 81 FQNPddqffgptveeeVAF-GLENLGLPEEEIeERVEEALELVGLEGL----------RDRSPFT----LSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 1457 ARALLRKTKVLVLDEATAAVDLETDDLIQKTIRtEFKEC--TVLTIAHRLNTILD-SDKVIVLDKGQ 1520
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLK-KLKAEgkTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1306-1531 |
3.69e-35 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 142.96 E-value: 3.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1306 EGRVEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSR 1385
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1386 LTIIPQDPVLFSGSLRINLDPFEIKTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTK 1465
Cdd:COG4618 408 IGYLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPR 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 1466 VLVLDEATAAVDLETDDLIQKTIRtEFKE--CTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELL 1531
Cdd:COG4618 488 LVVLDEPNSNLDDEGEAALAAAIR-ALKArgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1310-1520 |
7.24e-34 |
|
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: 128.13 E-value: 7.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1310 EFQNFQVRYREGLdlVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTII 1389
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1390 PQdpvlfsgslrinldpfeiktddeiwkalelshlksfvkslaaglnheiaeggenLSVGQRQLVCLARALLRKTKVLVL 1469
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 45552357 1470 DEATAAVDLETDDLIQKTIRTEFKE-CTVLTIAHRLNTILD-SDKVIVLDKGQ 1520
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
660-871 |
9.68e-34 |
|
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: 130.74 E-value: 9.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 660 DEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFL-------GEMEkLAGV-VNTV------GKLAYVPQQAWIQNATV 725
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLErfydptsGEIL-LDGVdIRDLnlrwlrSQIGLVSQEPVLFDGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 726 RDNILFGqtyDRKRYNKVIDACALRADID--ILSAGDL--TEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAV 801
Cdd:cd03249 94 AENIRYG---KPDATDEEVEEAAKKANIHdfIMSLPDGydTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45552357 802 DAHVgkhifEEVIGPKGILARKSR--VLVTHGVTFLPQVDSIYVIKMGEISESGTFDQLVKNKGAFADFIIQ 871
Cdd:cd03249 171 DAES-----EKLVQEALDRAMKGRttIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1309-1538 |
2.07e-33 |
|
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: 129.92 E-value: 2.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLDL--VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRL 1386
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1387 TIIPQDPvlfSGSL-------RINLDPFEI----KTDDEIWKALELSHLKSfvkSLAAGLNHEiaeggenLSVGQRQLVC 1455
Cdd:COG1124 82 QMVFQDP---YASLhprhtvdRILAEPLRIhglpDREERIAELLEQVGLPP---SFLDRYPHQ-------LSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1456 LARALLRKTKVLVLDEATAAVDL----ETDDLIQKtIRTEFKeCTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTEL 1530
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVsvqaEILNLLKD-LREERG-LTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADL 226
|
....*...
gi 45552357 1531 LDNPKSAF 1538
Cdd:COG1124 227 LAGPKHPY 234
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
649-848 |
4.26e-33 |
|
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: 126.34 E-value: 4.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 649 MSIENGEFSWGDEIT--LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVnTVG--------------KLA 712
Cdd:cd03228 1 IEFKNVSFSYPGRPKpvLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI-LIDgvdlrdldleslrkNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 713 YVPQQAWIQNATVRDNILfgqtydrkrynkvidacalradidilsagdlteigekginlSGGQKQRISLARAVYSDADLY 792
Cdd:cd03228 80 YVPQDPFLFSGTIRENIL-----------------------------------------SGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 45552357 793 LLDDPLSAVDAHVGKHIFEEVigpKGILARKSRVLVTHGVTFLPQVDSIYVIKMGE 848
Cdd:cd03228 119 ILDEATSALDPETEALILEAL---RALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1309-1523 |
6.45e-33 |
|
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: 126.27 E-value: 6.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGlHMLRSRLTI 1388
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1389 IPQDPVLFSGSLRINLdpfeiktddeiwkalelshlksfvkslaaglnheiaegGENLSVGQRQLVCLARALLRKTKVLV 1468
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 1469 LDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIE 1523
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1326-1474 |
1.92e-32 |
|
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: 123.91 E-value: 1.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1326 LRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPVLFSGS-----L 1400
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLtvrenL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1401 RINLDPFEIKT---DDEIWKALE---LSHLksfvkslaagLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATA 1474
Cdd:pfam00005 81 RLGLLLKGLSKrekDARAEEALEklgLGDL----------ADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
625-868 |
2.26e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 134.97 E-value: 2.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 625 INKFLNSEELDPNSVLHDSSKPHPMSIENGE---FSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEME-- 699
Cdd:PRK11174 324 LVTFLETPLAHPQQGEKELASNDPVTIEAEDleiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPyq 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 700 ---KLAGV-VNTVGKLAYVPQQAWI-QN-----ATVRDNILFGQ-TYDRKRYNKVIDACALRADIDILSAGDLTEIGEKG 768
Cdd:PRK11174 404 gslKINGIeLRELDPESWRKHLSWVgQNpqlphGTLRDNVLLGNpDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 769 INLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEVigpKGILARKSRVLVTHGVTFLPQVDSIYVIKMGE 848
Cdd:PRK11174 484 AGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQAL---NAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQ 560
|
250 260
....*....|....*....|
gi 45552357 849 ISESGTFDQLVKNKGAFADF 868
Cdd:PRK11174 561 IVQQGDYAELSQAGGLFATL 580
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1309-1520 |
3.01e-32 |
|
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: 125.27 E-value: 3.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRY---REGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGvdiasmglhmlrsR 1385
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1386 LTIIPQDPVLFSGSLRINL---DPFEiktDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLR 1462
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENIlfgKPFD---EERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1463 KTKVLVLDEATAAVDLET-DDLIQKTIRTEFKEC-TVLTIAHRLNTILDSDKVIVLDKGQ 1520
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1306-1531 |
3.86e-32 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 133.63 E-value: 3.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1306 EGRVEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSR 1385
Cdd:TIGR01842 314 EGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKH 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1386 LTIIPQDPVLFSGSLRINLDPF-EIKTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKT 1464
Cdd:TIGR01842 394 IGYLPQDVELFPGTVAENIARFgENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDP 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 1465 KVLVLDEATAAVDLETDD-LIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELL 1531
Cdd:TIGR01842 474 KLVVLDEPNSNLDEEGEQaLANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
651-863 |
4.46e-32 |
|
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: 125.42 E-value: 4.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 651 IENGEFSW-GDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG-------------KLAYVPQ 716
Cdd:cd03254 5 FENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 717 QAWIQNATVRDNILFGQTYDRKryNKVIDAC-ALRAD--IDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYL 793
Cdd:cd03254 85 DTFLFSGTIMENIRLGRPNATD--EEVIEAAkEAGAHdfIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 794 LDDPLSAVDAHVGKHIFEEVigpKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEISESGTFDQLVKNKG 863
Cdd:cd03254 163 LDEATSNIDTETEKLIQEAL---EKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
652-867 |
9.91e-32 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 124.65 E-value: 9.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 652 ENGEFSWGDE-ITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG-------------KLAYVPQQ 717
Cdd:cd03253 4 ENVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVVPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 718 AWIQNATVRDNILFGqtydrkRYN----KVIDACaLRADID--ILSAGD--LTEIGEKGINLSGGQKQRISLARAVYSDA 789
Cdd:cd03253 84 TVLFNDTIGYNIRYG------RPDatdeEVIEAA-KAAQIHdkIMRFPDgyDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 790 DLYLLDDPLSAVDAHVGKHIFEEVigpKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEISESGTFDQLVKNKGAFAD 867
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAAL---RDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAE 231
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
650-830 |
1.62e-31 |
|
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: 123.41 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 650 SIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK--------LAYVPQQA--- 718
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerkrIGYVPQRRsid 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 719 WIQNATVRDNILFGQTYDR---KRYNKVIDACALRAdidiLSAGDLTEIGEKGI-NLSGGQKQRISLARAVYSDADLYLL 794
Cdd:cd03235 81 RDFPISVRDVVLMGLYGHKglfRRLSKADKAKVDEA----LERVGLSELADRQIgELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 45552357 795 DDPLSAVDAHVGKHIFEEVIGpkgiLARKSR--VLVTH 830
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRE----LRREGMtiLVVTH 190
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1308-1532 |
2.00e-31 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 124.39 E-value: 2.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1308 RVEFQNFQVRYREGLdlVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLT 1387
Cdd:COG1120 1 MLEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1388 IIPQDPVL-FSGSLR----------INLDPFEIKTDDEI-WKALE---LSHLKsfvkslaaglNHEIAEggenLSVGQRQ 1452
Cdd:COG1120 79 YVPQEPPApFGLTVRelvalgryphLGLFGRPSAEDREAvEEALErtgLEHLA----------DRPVDE----LSGGERQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1453 LVCLARALLRKTKVLVLDEATAAVDL----ETDDLIQKTIRTEfkECTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASP 1527
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARER--GRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPP 222
|
....*
gi 45552357 1528 TELLD 1532
Cdd:COG1120 223 EEVLT 227
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
762-1517 |
2.08e-31 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 134.77 E-value: 2.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 762 TEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDaHVGKHIFEEVIGP-KGILARKSrVLVTHGVTFLPQVDS 840
Cdd:PTZ00265 571 TLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNlKGNENRIT-IIIAHRLSTIRYANT 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 841 IYVIKMGEISESGTFDQLV----------KNKGAFADFIIQHLQEGNEEEEELNQIKRQISSTADVPELLGTVEKAIKLA 910
Cdd:PTZ00265 649 IFVLSNRERGSTVDVDIIGedptkdnkenNNKNNKDDNNNNNNNNNNKINNAGSYIIEQGTHDALMKNKNGIYYTMINNQ 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 911 RTESLSDSISVTSADSLMGGggSLRRRTKRQDSHDSVASAASLK------KKQEVEGKLIETEKSQTGGVEF-------- 976
Cdd:PTZ00265 729 KVSSKKSSNNDNDKDSDMKS--SAYKDSERGYDPDEMNGNSKHEnesasnKKSCKMSDENASENNAGGKLPFlrnlfkrk 806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 977 --------AVYKH---YIKSVGI-FLSVatLVLNFVFQAFQIGSNLWLTQWANDQNVANDTGLRDMYLGVYGafgfgqVF 1044
Cdd:PTZ00265 807 pkapnnlrIVYREifsYKKDVTIiALSI--LVAGGLYPVFALLYAKYVSTLFDFANLEANSNKYSLYILVIA------IA 878
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1045 SYIGSVVIVYLGALIGTR---KIFIQLFGNILHAPQAYFDIKPRARIL--DRLANDIYKLDVVLPELIRVFNSQVFRVLA 1119
Cdd:PTZ00265 879 MFISETLKNYYNNVIGEKvekTMKRRLFENILYQEISFFDQDKHAPGLlsAHINRDVHLLKTGLVNNIVIFTHFIVLFLV 958
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1120 TIVVISLSTPIFLAVIVPIAFLYY--FAQRFYVATSRQLMRLESVSRSPIYSHFS-------------ETVTGASTIRAY 1184
Cdd:PTZ00265 959 SMVMSFYFCPIVAAVLTGTYFIFMrvFAIRARLTANKDVEKKEINQPGTVFAYNSddeifkdpsfliqEAFYNMNTVIIY 1038
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1185 NVGDRFIEESDAKVDKNQVCKYPSVIANR------------------WLAIRLEMVGNLII--LFASLFAVLggqtnpgl 1244
Cdd:PTZ00265 1039 GLEDYFCNLIEKAIDYSNKGQKRKTLVNSmlwgfsqsaqlfinsfayWFGSFLIRRGTILVddFMKSLFTFL-------- 1110
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1245 vgLSVSYALQvtqtlnwLVRMSSDIETNIVSVERIkeYGETKQEAPWELEQD---KNKPKNwPQEGRVEFQNFQVRYREG 1321
Cdd:PTZ00265 1111 --FTGSYAGK-------LMSLKGDSENAKLSFEKY--YPLIIRKSNIDVRDNggiRIKNKN-DIKGKIEIMDVNFRYISR 1178
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1322 LDL-VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAA------------------------------------- 1363
Cdd:PTZ00265 1179 PNVpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtndmtneqdyqgdeeqnvgmknvnef 1258
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1364 -----------------GGRISIDGVDIASMGLHMLRSRLTIIPQDPVLFSGSLRINLDpF--EIKTDDEIWKALELSHL 1424
Cdd:PTZ00265 1259 sltkeggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FgkEDATREDVKRACKFAAI 1337
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1425 KSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIrTEFKEC---TVLTIA 1501
Cdd:PTZ00265 1338 DEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI-VDIKDKadkTIITIA 1416
|
890
....*....|....*.
gi 45552357 1502 HRLNTILDSDKVIVLD 1517
Cdd:PTZ00265 1417 HRIASIKRSDKIVVFN 1432
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1310-1522 |
2.42e-31 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 121.77 E-value: 2.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1310 EFQNFQVRYREGLdlVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTII 1389
Cdd:cd03214 1 EVENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1390 PQdpVLfsgslrinldpfeiktddeiwKALELSHLKsfvkslaaglNHEIAEggenLSVGQRQLVCLARALLRKTKVLVL 1469
Cdd:cd03214 79 PQ--AL---------------------ELLGLAHLA----------DRPFNE----LSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 1470 DEATAAVDL----ETDDLIQKTIRTefKECTVLTIAHRLNTILD-SDKVIVLDKGQII 1522
Cdd:cd03214 122 DEPTSHLDIahqiELLELLRRLARE--RGKTVVMVLHDLNLAARyADRVILLKDGRIV 177
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
644-830 |
2.72e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 117.88 E-value: 2.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 644 SKPHPMSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK--------LAYVP 715
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKpprrarrrIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 716 QQA---WIQNATVRDNILFGQTYDR---KRYNKVIDACALRAdidiLSAGDLTEIGEKGIN-LSGGQKQRISLARAVYSD 788
Cdd:COG1121 82 QRAevdWDFPITVRDVVLMGRYGRRglfRRPSRADREAVDEA----LERVGLEDLADRPIGeLSGGQQQRVLLARALAQD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 45552357 789 ADLYLLDDPLSAVDAHvGKHIFEEVIgpkGILARKSR--VLVTH 830
Cdd:COG1121 158 PDLLLLDEPFAGVDAA-TEEALYELL---RELRREGKtiLVVTH 197
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
650-867 |
2.92e-29 |
|
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: 117.72 E-value: 2.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 650 SIENGEFSWGDEIT--LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG-------------KLAYV 714
Cdd:cd03251 2 EFKNVTFRYPGDGPpvLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 715 PQQAWIQNATVRDNILFGQT-YDRKRYNKVIDACALRADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYL 793
Cdd:cd03251 82 SQDVFLFNDTVAENIAYGRPgATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45552357 794 LDDPLSAVDAHVGKHIFEEVigpKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEISESGTFDQLVKNKGAFAD 867
Cdd:cd03251 162 LDEATSALDTESERLVQAAL---ERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
568-869 |
4.06e-29 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 125.62 E-value: 4.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 568 LVSLVTFATYVLTseaNQLSVEKVLVSIALFDLMKLPLTILPMLSVDIAETQVSVNRINK--FLNSEELDPNSVLHDSSK 645
Cdd:TIGR01193 394 VVILWTGAYLVMR---GKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEvyLVDSEFINKKKRTELNNL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 646 PHPMSIENGEFSWG--DEItLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKL------------ 711
Cdd:TIGR01193 471 NGDIVINDVSYSYGygSNI-LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlkdidrhtlrqf 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 712 -AYVPQQAWIQNATVRDNILFGQTyDRKRYNKVIDACAL---RADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYS 787
Cdd:TIGR01193 550 iNYLPQEPYIFSGSILENLLLGAK-ENVSQDEIWAACEIaeiKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLT 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 788 DADLYLLDDPLSAVDAHVGKHIFEEVIGpkgiLARKSRVLVTHGVTFLPQVDSIYVIKMGEISESGTFDQLVKNKGAFAD 867
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITEKKIVNNLLN----LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYAS 704
|
..
gi 45552357 868 FI 869
Cdd:TIGR01193 705 LI 706
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1325-1534 |
1.27e-28 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 122.90 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPVLFSGSLRINL 1404
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1405 ---DPfeIKTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETD 1481
Cdd:PRK10789 410 algRP--DATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTE 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 45552357 1482 DLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLDNP 1534
Cdd:PRK10789 488 HQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
374-830 |
1.60e-28 |
|
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: 122.08 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 374 LYAVLLFVLAAAQTFILGQYFHRMfiVG----LRIRTALINAIYRKALRISNSTKKESTVGEIVNLMA--VDAQRFMELT 447
Cdd:TIGR02868 52 LSVAAVAVRAFGIGRAVFRYLERL--VGhdaaLRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGadVDALQDLYVR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 448 TYLNMIWSAPLQIG--LALYFLWQQLGPSVLAGLAVMIILIPVNGVIASRIKTYQIRQMKykDERVKLMNEVLSGIKVLK 525
Cdd:TIGR02868 130 VIVPAGVALVVGAAavAAIAVLSVPAALILAAGLLLAGFVAPLVSLRAARAAEQALARLR--GELAAQLTDALDGAAELV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 526 LYAWEPSFEKQVLDIRDKEIATLRSTAYLNAGTSFLWSCAPFLVSLVTFATYVLTSEANQLSVekvlVSIALFDLMKLPL 605
Cdd:TIGR02868 208 ASGALPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAP----VTLAVLVLLPLAA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 606 T----ILPMLSVDIAETQVSVNRINKFLNSEELDPNSVLH---DSSKPHP-MSIENGEFSW-GDEITLRNINIEVKKGSL 676
Cdd:TIGR02868 284 FeafaALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPaagAVGLGKPtLELRDLSAGYpGAPPVLDGVSLDLPPGER 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 677 VALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG-------------KLAYVPQQAWIQNATVRDNILFGQ-TYDRKRYNK 742
Cdd:TIGR02868 364 VAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssldqdevrrRVSVCAQDAHLFDTTVRENLRLARpDATDEELWA 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 743 VIDACALRADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEVIGPkgiLAR 822
Cdd:TIGR02868 444 ALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA---LSG 520
|
....*...
gi 45552357 823 KSRVLVTH 830
Cdd:TIGR02868 521 RTVVLITH 528
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1325-1535 |
3.00e-28 |
|
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: 117.08 E-value: 3.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEA---AGGRISIDGVDIASMGLHMLR----SRLTIIPQDPvlfS 1397
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRkirgREIQMIFQDP---M 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1398 GSL-------RINLDPFEI---KTDDEIW-KALEL----------SHLKSFvkslaaglNHEiaeggenLSVGQRQLVCL 1456
Cdd:COG0444 97 TSLnpvmtvgDQIAEPLRIhggLSKAEAReRAIELlervglpdpeRRLDRY--------PHE-------LSGGMRQRVMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1457 ARALLRKTKVLVLDEATAAVD-------LetdDLIQKtIRTEFKeCTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPT 1528
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDvtiqaqiL---NLLKD-LQRELG-LAILFITHDLGVVAEiADRVAVMYAGRIVEEGPVE 236
|
....*..
gi 45552357 1529 ELLDNPK 1535
Cdd:COG0444 237 ELFENPR 243
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1309-1530 |
6.40e-28 |
|
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: 113.43 E-value: 6.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREglDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEA-----AGGRISIDGVDIASMGLHM-- 1381
Cdd:cd03260 1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1382 LRSRLTIIPQDPVLFSGS--------LRINLDPFEIKTDDEIWKALELSHLKSFVKSLAAGLNheiaeggenLSVGQRQL 1453
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSiydnvaygLRLHGIKLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 1454 VCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTEL 1530
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1309-1535 |
7.18e-28 |
|
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: 113.44 E-value: 7.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLDLV--LRGVSFNIQGGEKVGIVGRTGAGKSSLtLALFRIIEA-AGGRISIDGVDIASM---GLHML 1382
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTL-IRCINGLERpTSGSVLVDGTDLTLLsgkELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1383 RSRLTIIPQDPVLFSGslRINLD----PFEI---KTDDEIWKALELSHLksfvkslaAGLNHEIAEGGENLSVGQRQLVC 1455
Cdd:cd03258 81 RRRIGMIFQHFNLLSS--RTVFEnvalPLEIagvPKAEIEERVLELLEL--------VGLEDKADAYPAQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1456 LARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKE--CTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLD 1532
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRElgLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFA 230
|
...
gi 45552357 1533 NPK 1535
Cdd:cd03258 231 NPQ 233
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1309-1532 |
1.31e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 113.26 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREglDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIAsmglhmlRSRLTI 1388
Cdd:COG1121 7 IELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR-------RARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1389 --IPQ----DP--------VLFSGSL-RINLDPFEIKTDDE-IWKALE---LSHLKsfvkslaaglNHEIAEggenLSVG 1449
Cdd:COG1121 78 gyVPQraevDWdfpitvrdVVLMGRYgRRGLFRRPSRADREaVDEALErvgLEDLA----------DRPIGE----LSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1450 QRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRtEFKE--CTVLTIAHRLNTILD-SDKVIVLDKGqIIEFAS 1526
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLR-ELRRegKTILVVTHDLGAVREyFDRVLLLNRG-LVAHGP 221
|
....*.
gi 45552357 1527 PTELLD 1532
Cdd:COG1121 222 PEEVLT 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1309-1521 |
1.54e-27 |
|
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: 110.57 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLdlVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHmLRSRLTI 1388
Cdd:cd03230 1 IEVRNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1389 IPQDPVLFSgslriNLDPFEiktddeiwkalelsHLKsfvkslaaglnheiaeggenLSVGQRQLVCLARALLRKTKVLV 1468
Cdd:cd03230 78 LPEEPSLYE-----NLTVRE--------------NLK--------------------LSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 1469 LDEATAAVDLETDDLIQKTIRTEFKE-CTVLTIAHRLNTILD-SDKVIVLDKGQI 1521
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEgKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1309-1525 |
1.71e-27 |
|
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: 111.84 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREglDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHmlRSRLTI 1388
Cdd:cd03259 1 LELKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1389 IPQDPVLF----------SGsLRINLDPFEIKTD--DEIWKALELSHLksfvkslaagLNHEIAEggenLSVGQRQLVCL 1456
Cdd:cd03259 77 VFQDYALFphltvaeniaFG-LKLRGVPKAEIRArvRELLELVGLEGL----------LNRYPHE----LSGGQQQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45552357 1457 ARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKE--CTVLTIAHRLNTILD-SDKVIVLDKGQIIEFA 1525
Cdd:cd03259 142 ARALAREPSLLLLDEPLSALDAKLREELREELKELQRElgITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1325-1546 |
2.22e-27 |
|
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: 112.26 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLhMLRSRLTIIPQDPVLFSG-SLRIN 1403
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIGVLPDERGLYDRlTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1404 LDPF---------EIKTD-DEIWKALELShlkSFVKSLAAGLnheiaeggenlSVGQRQLVCLARALLRKTKVLVLDEAT 1473
Cdd:COG4555 95 IRYFaelyglfdeELKKRiEELIELLGLE---EFLDRRVGEL-----------STGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1474 AAVDLETDDLIQKTIRtEFKE--CTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELL-----DNPKSAFYSMAKDA 1545
Cdd:COG4555 161 NGLDVMARRLLREILR-ALKKegKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELReeigeENLEDAFVALIGSE 239
|
.
gi 45552357 1546 N 1546
Cdd:COG4555 240 E 240
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1208-1503 |
2.94e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 118.76 E-value: 2.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1208 SVIANRWLAIRLEM--------VGNLIILFASLFA---VLGGQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSV 1276
Cdd:COG4178 253 AVIANWRRLIRRQRnltffttgYGQLAVIFPILVAaprYFAGEITLGGLMQAASAFGQVQGALSWFVDNYQSLAEWRATV 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1277 ERIKEYGETKQEAPwELEQDKNKPKNwPQEGRVEFQNFQVRYREGlDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLtlal 1356
Cdd:COG4178 333 DRLAGFEEALEAAD-ALPEAASRIET-SEDGALALEDLTLRTPDG-RPLLEDLSLSLKPGERLLITGPSGSGKSTL---- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1357 FRIIeaAG------GRISIDGvdiasmGLHMLrsrltIIPQDPVLFSGSLRINL---DPFEIKTDDEIWKALELSHLKSF 1427
Cdd:COG4178 406 LRAI--AGlwpygsGRIARPA------GARVL-----FLPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGLGHL 472
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552357 1428 VKSLaaglnHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHR 1503
Cdd:COG4178 473 AERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
374-866 |
3.34e-27 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 119.83 E-value: 3.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 374 LYAVLLFVLAAAQTfilGQYFHRMFIVGLRIRTALINAIYRKALRISNSTKkestVGEIVNLMAVDAQRFME-LTTYLN- 451
Cdd:TIGR00958 209 LLSIASSVSAGLRG---GSFNYTMARINLRIREDLFRSLLRQDLGFFDENK----TGELTSRLSSDTQTMSRsLSLNVNv 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 452 MIWSapLQIGLALYFLWQQLGPSvlagLA-VMIILIPVNGVIASRIKTY------QIRQMKYKDERVKLmnEVLSGIKVL 524
Cdd:TIGR00958 282 LLRN--LVMLLGLLGFMLWLSPR----LTmVTLINLPLVFLAEKVFGKRyqllseELQEAVAKANQVAE--EALSGMRTV 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 525 KLYAWEPS----FEKQVLDIRDkeIATLRSTAYLnagtSFLWS---CAPFLVSLVTF--ATYVLTSEanqlsVEK-VLVS 594
Cdd:TIGR00958 354 RSFAAEEGeasrFKEALEETLQ--LNKRKALAYA----GYLWTtsvLGMLIQVLVLYygGQLVLTGK-----VSSgNLVS 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 595 IALFDlMKLPLTILPMLSV--DIAETQVSVNRINKFLNSEELDPNSVLHdssKPHPMS--IE--NGEFSW---GDEITLR 665
Cdd:TIGR00958 423 FLLYQ-EQLGEAVRVLSYVysGMMQAVGASEKVFEYLDRKPNIPLTGTL---APLNLEglIEfqDVSFSYpnrPDVPVLK 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 666 NINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG-------------KLAYVPQQAWIQNATVRDNILFG 732
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVALVGQEPVLFSGSVRENIAYG 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 733 QTY--DRKRYNKVIDACAlRADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVgkhif 810
Cdd:TIGR00958 579 LTDtpDEEIMAAAKAANA-HDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC----- 652
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 45552357 811 EEVIGPKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEISESGTFDQLVKNKGAFA 866
Cdd:TIGR00958 653 EQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYK 708
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1309-1520 |
4.55e-27 |
|
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: 109.20 E-value: 4.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYreGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHM--LRSRL 1386
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1387 TIIPQDPVLFSgslriNLDPFEIktddeiwkalelshlksfvkslaaglnheIAEGgenLSVGQRQLVCLARALLRKTKV 1466
Cdd:cd03229 79 GMVFQDFALFP-----HLTVLEN-----------------------------IALG---LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 1467 LVLDEATAAVDLETDDLIQKTIRTEFKE--CTVLTIAHRLNTILD-SDKVIVLDKGQ 1520
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1328-1535 |
9.03e-27 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 112.90 E-value: 9.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1328 GVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMG---LHMLRSRLTIIPQDPvlfSGSL---- 1400
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP---YASLnprm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1401 ---RINLDPFEIKT-------DDEIWKALELshlksfVkslaaGLN--------HEiaeggenLSVGQRQLVCLARALLR 1462
Cdd:COG4608 113 tvgDIIAEPLRIHGlaskaerRERVAELLEL------V-----GLRpehadrypHE-------FSGGQRQRIGIARALAL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1463 KTKVLVLDEATAAVDLEtddlIQKTI-------RTEFKeCTVLTIAHRLNT---IldSDKVIVLDKGQIIEFASPTELLD 1532
Cdd:COG4608 175 NPKLIVCDEPVSALDVS----IQAQVlnlledlQDELG-LTYLFISHDLSVvrhI--SDRVAVMYLGKIVEIAPRDELYA 247
|
...
gi 45552357 1533 NPK 1535
Cdd:COG4608 248 RPL 250
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
652-849 |
1.33e-26 |
|
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: 109.60 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 652 ENGEFSW-GDEI-TLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG-------------KLAYVPQ 716
Cdd:cd03245 6 RNVSFSYpNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 717 QAWIQNATVRDNILFGQTY-DRKRYNKVIDACALRADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLD 795
Cdd:cd03245 86 DVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 45552357 796 DPLSAVDAHVGKHIFEEVigpKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEI 849
Cdd:cd03245 166 EPTSAMDMNSEERLKERL---RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
618-860 |
1.68e-26 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 116.29 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 618 TQVSVNRINKFLNSEeldpnsvlhdSSKPHPMSIENGEFSW-----------GDEITLRNINIEVKKGSLVALVGTVGSG 686
Cdd:TIGR01842 287 ARQAYKRLNELLANY----------PSRDPAMPLPEPEGHLsvenvtivppgGKKPTLRGISFSLQAGEALAIIGPSGSG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 687 KSSVVQAFLGEMEKLAGVV------------NTVGK-LAYVPQQAWIQNATVRDNIL-FGQTYDRKrynKVIDACALrAD 752
Cdd:TIGR01842 357 KSTLARLIVGIWPPTSGSVrldgadlkqwdrETFGKhIGYLPQDVELFPGTVAENIArFGENADPE---KIIEAAKL-AG 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 753 ----IDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAhVGkhifeEVIGPKGILARKSR--- 825
Cdd:TIGR01842 433 vhelILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDE-EG-----EQALANAIKALKARgit 506
|
250 260 270
....*....|....*....|....*....|....*.
gi 45552357 826 -VLVTHGVTFLPQVDSIYVIKMGEISESGTFDQLVK 860
Cdd:TIGR01842 507 vVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1326-1537 |
1.69e-26 |
|
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: 115.94 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1326 LRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEaAGGRISIDGVDIASMG---LHMLRSRLTIIPQDPvlFsGSL-- 1400
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--F-GSLsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1401 ---------------RINLDPFEIktDDEIWKALELSHLKsfvkslAAGLN---HEiaeggenLSVGQRQLVCLARALLR 1462
Cdd:COG4172 378 rmtvgqiiaeglrvhGPGLSAAER--RARVAEALEEVGLD------PAARHrypHE-------FSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1463 KTKVLVLDEATAAVDLetddLIQKTIRTEFKE------CTVLTIAHRLNTI--LdSDKVIVLDKGQIIEFASPTELLDNP 1534
Cdd:COG4172 443 EPKLLVLDEPTSALDV----SVQAQILDLLRDlqrehgLAYLFISHDLAVVraL-AHRVMVMKDGKVVEQGPTEQVFDAP 517
|
...
gi 45552357 1535 KSA 1537
Cdd:COG4172 518 QHP 520
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1309-1533 |
2.20e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 110.47 E-value: 2.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTI 1388
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1389 IPQDP-VLFSGslrinldpfeIKTDDEIWKALE-----LSHLKSFVKSLA--AGLNHEIAEGGENLSVGQRQLVCLARAL 1460
Cdd:PRK13632 88 IFQNPdNQFIG----------ATVEDDIAFGLEnkkvpPKKMKDIIDDLAkkVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 1461 LRKTKVLVLDEATAAVDLETDDLIQKTIRT--EFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLDN 1533
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1310-1533 |
6.60e-26 |
|
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: 107.52 E-value: 6.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1310 EFQNFQVRYreGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMlRSRLTI- 1388
Cdd:cd03224 2 EVENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARAGIg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1389 -IPQDPVLFSG-SLRINLD-----PFEIKTDDEIWKALEL-SHLKSFVKSLAAglnheiaeggeNLSVGQRQLVCLARAL 1460
Cdd:cd03224 79 yVPEGRRIFPElTVEENLLlgayaRRRAKRKARLERVYELfPRLKERRKQLAG-----------TLSGGEQQMLAIARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 1461 LRKTKVLVLDEATAA-----VDlETDDLIQKtIRTEfkECTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDN 1533
Cdd:cd03224 148 MSRPKLLLLDEPSEGlapkiVE-EIFEAIRE-LRDE--GVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1310-1519 |
7.03e-26 |
|
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: 107.23 E-value: 7.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1310 EFQNFQVRYREGLdlVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIAsmglhMLRSRLTII 1389
Cdd:cd03235 1 EVEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-----KERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1390 PQ-------------DPVLFSGSLRINLDPFEIKTD----DEIWKALELSHLKsfvkslaaglNHEIAEggenLSVGQRQ 1452
Cdd:cd03235 74 PQrrsidrdfpisvrDVVLMGLYGHKGLFRRLSKADkakvDEALERVGLSELA----------DRQIGE----LSGGQQQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 1453 LVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRT-EFKECTVLTIAHRLNTILDS-DKVIVLDKG 1519
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYfDRVLLLNRT 208
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1323-1538 |
1.54e-25 |
|
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: 107.04 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1323 DLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIAsmGLHMLRSRLTIIPQDPVLF------ 1396
Cdd:cd03299 12 EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFphmtvy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1397 ---SGSLRINLDP-FEIKTD-DEIWKALELSHLksfvkslaagLNHEIaeggENLSVGQRQLVCLARALLRKTKVLVLDE 1471
Cdd:cd03299 90 kniAYGLKKRKVDkKEIERKvLEIAEMLGIDHL----------LNRKP----ETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45552357 1472 ATAAVDLETDDLIQ---KTIRTEFkECTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNPKSAF 1538
Cdd:cd03299 156 PFSALDVRTKEKLReelKKIRKEF-GVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKPKNEF 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1309-1534 |
1.81e-25 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 106.82 E-value: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREglDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMG---LHMLRSR 1385
Cdd:cd03261 1 IELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1386 LTIIPQDPVLFSgSLRI------NLDPFEIKTDDEIwKALELSHLKsfvkslAAGLnheiaEGGEN-----LSVGQRQLV 1454
Cdd:cd03261 79 MGMLFQSGALFD-SLTVfenvafPLREHTRLSEEEI-REIVLEKLE------AVGL-----RGAEDlypaeLSGGMKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1455 CLARALLRKTKVLVLDEATAAVD----LETDDLIQKTIRTefKECTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTE 1529
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDpiasGVIDDLIRSLKKE--LGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEE 223
|
....*..
gi 45552357 1530 LL--DNP 1534
Cdd:cd03261 224 LRasDDP 230
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
624-868 |
2.57e-25 |
|
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: 112.87 E-value: 2.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 624 RINKFLNsEELDPNSVLHDSSKPHP----MSIENGEFSWG---DEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLG 696
Cdd:TIGR02204 310 RLIELLQ-AEPDIKAPAHPKTLPVPlrgeIEFEQVNFAYParpDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLR 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 697 EMEKLAGVVNTVG-------------KLAYVPQQAWIQNATVRDNILFGQTyDRKRyNKVIDAC-ALRAD--IDILSAGD 760
Cdd:TIGR02204 389 FYDPQSGRILLDGvdlrqldpaelraRMALVPQDPVLFAASVMENIRYGRP-DATD-EEVEAAArAAHAHefISALPEGY 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 761 LTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEVigpKGILARKSRVLVTHGVTFLPQVDS 840
Cdd:TIGR02204 467 DTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQAL---ETLMKGRTTLIIAHRLATVLKADR 543
|
250 260
....*....|....*....|....*...
gi 45552357 841 IYVIKMGEISESGTFDQLVKNKGAFADF 868
Cdd:TIGR02204 544 IVVMDQGRIVAQGTHAELIAKGGLYARL 571
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
333-625 |
3.36e-25 |
|
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: 107.64 E-value: 3.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 333 FLFGALMKLFTDTLTFAQPQVLSLIISFVEAQDAEPEWkgILYAVLLFVLAAAQTFILGQYFHRMFIVGLRIRTALINAI 412
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLL--LWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 413 YRKALRISNSTKKESTVGEIVNLMAVDAQRFMEL-TTYLNMIWSAPLQIGLALYFL----WQqlgpSVLAGLAVMIILIP 487
Cdd:cd07346 79 FRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLvSSGLLQLLSDVLTLIGALVILfylnWK----LTLVALLLLPLYVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 488 VNGVIASRIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPS----FEKQVLDIRDKEIATLRSTAYLNAGTSFLWS 563
Cdd:cd07346 155 ILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEReierFREANRDLRDANLRAARLSALFSPLIGLLTA 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45552357 564 CAPFLVsLVTFATYVLtseANQLSVEKVLVSIALFDLMKLPLTILPMLSVDIAETQVSVNRI 625
Cdd:cd07346 235 LGTALV-LLYGGYLVL---QGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1309-1523 |
8.21e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 104.36 E-value: 8.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLDlVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASM---GLHMLRSR 1385
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1386 LTIIPQDP-----------VLFsgSLRIN-LDPFEIKTDdeIWKALELSHLKSFVKSLAaglnHEiaeggenLSVGQRQL 1453
Cdd:COG2884 81 IGVVFQDFrllpdrtvyenVAL--PLRVTgKSRKEIRRR--VREVLDLVGLSDKAKALP----HE-------LSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552357 1454 VCLARALLRKTKVLVLDEATAAVDLET-DDLIQktIRTEFKE--CTVLtIA-HRLNtILDS--DKVIVLDKGQIIE 1523
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETsWEIME--LLEEINRrgTTVL-IAtHDLE-LVDRmpKRVLELEDGRLVR 217
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
1072-1279 |
9.71e-25 |
|
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: 106.81 E-value: 9.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1072 ILHAPQAYFDIKPRARILDRLANDIYKLDVVLPELIRVFNSQVFRVLATIVVISLSTPIFLAVIVPIAFLYYFAQRFYVA 1151
Cdd:cd18600 113 VLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLR 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1152 TSRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVIANRWLAIRLEMVGNLIILFAS 1231
Cdd:cd18600 193 TSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFTAVT 272
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 45552357 1232 LFAVLGGQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERI 1279
Cdd:cd18600 273 FISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRI 320
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1309-1522 |
1.70e-24 |
|
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: 101.35 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYreGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDG--VDIASMGlHMLRSRL 1386
Cdd:cd03216 1 LELRGITKRF--GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGkeVSFASPR-DARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1387 TIIPQdpvlfsgslrinldpfeiktddeiwkalelshlksfvkslaaglnheiaeggenLSVGQRQLVCLARALLRKTKV 1466
Cdd:cd03216 78 AMVYQ------------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1467 LVLDEATAAVDL-ETDDLIqKTIRtEFKE--CTVLTIAHRLNTILD-SDKVIVLDKGQII 1522
Cdd:cd03216 104 LILDEPTAALTPaEVERLF-KVIR-RLRAqgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1309-1537 |
3.34e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 105.55 E-value: 3.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLDLV--LRGVSFNIQGGEKVGIVGRTGAGKSslTLAlfRII----EAAGGRISIDGVDIASM---GL 1379
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKS--TLI--RCInlleRPTSGSVLVDGVDLTALserEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1380 HMLRSRLTIIPQDPVLFSG---------SLRI-NLDPFEIKTddeiwKALELshLKsFVkslaaGLNHEIAEGGENLSVG 1449
Cdd:COG1135 78 RAARRKIGMIFQHFNLLSSrtvaenvalPLEIaGVPKAEIRK-----RVAEL--LE-LV-----GLSDKADAYPSQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1450 QRQLVCLARALLRKTKVLVLDEATAAVDLETD----DLIQKtIRTEFKeCTVLTIAHRLNTILD-SDKVIVLDKGQIIEF 1524
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETTrsilDLLKD-INRELG-LTIVLITHEMDVVRRiCDRVAVLENGRIVEQ 222
|
250
....*....|...
gi 45552357 1525 ASPTELLDNPKSA 1537
Cdd:COG1135 223 GPVLDVFANPQSE 235
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
664-866 |
3.94e-24 |
|
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: 102.95 E-value: 3.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG-------------KLAYVPQQAWIQNATVRDNIL 730
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 731 FGQT-YDRKRynkVIDACAL---RADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVG 806
Cdd:cd03252 98 LADPgMSMER---VIEAAKLagaHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 807 KHIFEEVigpKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEISESGTFDQLVKNKGAFA 866
Cdd:cd03252 175 HAIMRNM---HDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1325-1535 |
9.95e-24 |
|
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: 101.74 E-value: 9.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHmLRSRLTIIP--QDPVLFSG---- 1398
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFPEltvl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1399 -----------SLRINLDPF---EIKTDDEIWKALELSHLksfvkslaAGLNHEIAEggeNLSVGQRQLVCLARALLRKT 1464
Cdd:cd03219 94 envmvaaqartGSGLLLARArreEREARERAEELLERVGL--------ADLADRPAG---ELSYGQQRRLEIARALATDP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45552357 1465 KVLVLDEATAAVDL-ETDDLIQKTIRTEFKECTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNPK 1535
Cdd:cd03219 163 KLLLLDEPAAGLNPeETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
600-867 |
1.00e-23 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 107.88 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 600 LMKLPLTILPMLSV----DIAET-QVSVNRINKFLNSEeldpnSVLHDSSKPHP-----MSIENGEFSW--GDEITLRNI 667
Cdd:PRK10789 260 VMYLGLMIWPMLALawmfNIVERgSAAYSRIRAMLAEA-----PVVKDGSEPVPegrgeLDVNIRQFTYpqTDHPALENV 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 668 NIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVV-------------NTVGKLAYVPQQAWIQNATVRDNILFGQ- 733
Cdd:PRK10789 335 NFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdipltklqldSWRSRLAVVSQTPFLFSDTVANNIALGRp 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 734 TYDRKRYNKVIDACALRADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEV 813
Cdd:PRK10789 415 DATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNL 494
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 45552357 814 igpkgILARKSRVLV--THGVTFLPQVDSIYVIKMGEISESGTFDQLVKNKGAFAD 867
Cdd:PRK10789 495 -----RQWGEGRTVIisAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRD 545
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
513-867 |
1.29e-23 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 108.29 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 513 LMNEVLSGIKVLKLYAWEPsfekQVLDIRDKEIA--TLRSTAYLNAGTsfLWSCAPFLVSLVTFA-------TYVLTSEa 583
Cdd:TIGR01846 319 FLVESVTGIETIKATATEP----QFQNRWDRQLAayVAASFRVTNLGN--IAGQAIELIQKLTFAillwfgaHLVIGGA- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 584 nqLSVEKvLVSIALF-DLMKLPLTILPMLSVDIAETQVSVNRINKFLNSeeldPNSVLHDSSKPHP-----MSIENGEFS 657
Cdd:TIGR01846 392 --LSPGQ-LVAFNMLaGRVTQPVLRLAQLWQDFQQTGIALERLGDILNS----PTEPRSAGLAALPelrgaITFENIRFR 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 658 WGDE--ITLRNINIEVKKGSLVALVGTVGSGKSSVV------------QAFLGEME-KLAGVVNTVGKLAYVPQQAWIQN 722
Cdd:TIGR01846 465 YAPDspEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTkllqrlytpqhgQVLVDGVDlAIADPAWLRRQMGVVLQENVLFS 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 723 ATVRDNILFGQTydRKRYNKVIDACALRADIDILSA---GDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLS 799
Cdd:TIGR01846 545 RSIRDNIALCNP--GAPFEHVIHAAKLAGAHDFISElpqGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATS 622
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 800 AVDAHVGKHIFEEVigpKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEISESGTFDQLVKNKGAFAD 867
Cdd:TIGR01846 623 ALDYESEALIMRNM---REICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYAR 687
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
649-854 |
2.08e-23 |
|
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: 100.26 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 649 MSIENGEFSWGDEI--TLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVV-------NTVG------KLAY 713
Cdd:cd03244 3 IEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIlidgvdiSKIGlhdlrsRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 714 VPQQAWIQNATVRDNI-LFGQTYDRKRYNkVIDACALRADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLY 792
Cdd:cd03244 83 IPQDPVLFSGTIRSNLdPFGEYSDEELWQ-ALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45552357 793 LLDDPLSAVDAHVGKHIfEEVIGpkgiLARKSRVLVT--HGVTFLPQVDSIYVIKMGEISESGT 854
Cdd:cd03244 162 VLDEATASVDPETDALI-QKTIR----EAFKDCTVLTiaHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1310-1535 |
2.35e-23 |
|
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: 100.72 E-value: 2.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1310 EFQNFQVRYREGlDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMG---LHMLRSRL 1386
Cdd:cd03256 2 EVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1387 TIIPQDP-----------VLfSGSL------RINLDPFeikTDDEIWKALELshLKSFvkslaaGLNHEIAEGGENLSVG 1449
Cdd:cd03256 81 GMIFQQFnlierlsvlenVL-SGRLgrrstwRSLFGLF---PKEEKQRALAA--LERV------GLLDKAYQRADQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1450 QRQLVCLARALLRKTKVLVLDEATAAVDLET-----DDLiqKTIRTEfKECTVLTIAHRLNTILD-SDKVIVLDKGQIIe 1523
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASsrqvmDLL--KRINRE-EGITVIVSLHQVDLAREyADRIVGLKDGRIV- 224
|
250
....*....|..
gi 45552357 1524 FASPTELLDNPK 1535
Cdd:cd03256 225 FDGPPAELTDEV 236
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1309-1538 |
3.78e-23 |
|
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: 100.07 E-value: 3.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLDLVlRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTI 1388
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1389 IPQDPVLF---SGSLRINLDP-----FEIKTDDEIWKALELSHLKSfvKSLAAGLNHEiaeggenLSVGQRQLVCLARAL 1460
Cdd:cd03295 80 VIQQIGLFphmTVEENIALVPkllkwPKEKIRERADELLALVGLDP--AEFADRYPHE-------LSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1461 LRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKEC--TVLTIAHRLN-TILDSDKVIVLDKGQIIEFASPTELLDNPKSA 1537
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILRSPAND 230
|
.
gi 45552357 1538 F 1538
Cdd:cd03295 231 F 231
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
649-869 |
4.99e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 105.68 E-value: 4.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 649 MSIENGEFSWGDEIT--LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK-------------LAY 713
Cdd:PRK11160 339 LTLNNVSFTYPDQPQpvLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiadyseaalrqaISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 714 VPQQAWIQNATVRDNILFgqtydrkrynkvidACAlRADIDILSA-------GDLTE--------IGEKGINLSGGQKQR 778
Cdd:PRK11160 419 VSQRVHLFSATLRDNLLL--------------AAP-NASDEALIEvlqqvglEKLLEddkglnawLGEGGRQLSGGEQRR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 779 ISLARAVYSDADLYLLDDPLSAVDAHVGKHIFE---EVIgpkgilARKSRVLVTHGVTFLPQVDSIYVIKMGEISESGTF 855
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILEllaEHA------QNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTH 557
|
250
....*....|....
gi 45552357 856 DQLVKNKGAFADFI 869
Cdd:PRK11160 558 QELLAQQGRYYQLK 571
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1325-1535 |
5.71e-23 |
|
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: 100.11 E-value: 5.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLtlalFRII----EAAGGRISIDGVDIASMGLH------MLRS--------RL 1386
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTL----FNLItgfyRPTSGRILFDGRDITGLPPHriarlgIARTfqnprlfpEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1387 T-----IIPQDPVLFSGSLRINLDPF-----EIKTDDEIWKALELSHLKSFVKSLAAglnheiaeggeNLSVGQRQLVCL 1456
Cdd:COG0411 95 TvlenvLVAAHARLGRGLLAALLRLPrarreEREARERAEELLERVGLADRADEPAG-----------NLSYGQQRRLEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1457 ARALLRKTKVLVLDEATAAVDL-ETDDLIQ--KTIRTEFKeCTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLD 1532
Cdd:COG0411 164 ARALATEPKLLLLDEPAAGLNPeETEELAEliRRLRDERG-ITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEVRA 242
|
...
gi 45552357 1533 NPK 1535
Cdd:COG0411 243 DPR 245
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1309-1521 |
8.88e-23 |
|
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: 98.33 E-value: 8.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLD--LVLRGVSFNIQGGEKVGIVGRTGAGKSSLtLALFRIIEAA-GGRISIDGVDIASMGLHML--- 1382
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTL-LNILGGLDRPtSGEVRVDGTDISKLSEKELaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1383 -RSRLTIIPQD---------------PVLFSGSLRinldpFEIKTddeiwKALELshLKSFvkSLAAGLNHEIAEggenL 1446
Cdd:cd03255 80 rRRHIGFVFQSfnllpdltalenvelPLLLAGVPK-----KERRE-----RAEEL--LERV--GLGDRLNHYPSE----L 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 1447 SVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIR--TEFKECTVLTIAHRLNTILDSDKVIVLDKGQI 1521
Cdd:cd03255 142 SGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
659-857 |
2.03e-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: 103.67 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 659 GDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVV------------NTVGK-LAYVPQQAWIQNATV 725
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsqwdrEELGRhIGYLPQDVELFDGTI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 726 RDNI-LFGQTYDRKrynkVIDAcALRADID--ILSagdL-----TEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDP 797
Cdd:COG4618 423 AENIaRFGDADPEK----VVAA-AKLAGVHemILR---LpdgydTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 798 LSAVDAhvgkhifeevIGPKG----ILARKSR----VLVTHGVTFLPQVDSIYVIKMGEISESGTFDQ 857
Cdd:COG4618 495 NSNLDD----------EGEAAlaaaIRALKARgatvVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDE 552
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1309-1538 |
2.08e-22 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 100.56 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYreGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLtlaLfRII----EAAGGRISIDGVDIASMGLHmlRS 1384
Cdd:COG3842 6 LELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTL---L-RMIagfeTPDSGRILLDGRDVTGLPPE--KR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1385 RLTIIPQDPVLFS----------GsLRI-NLDPFEIKtdDEIWKALELSHLKSFVKSLAaglnHEiaeggenLSVGQRQL 1453
Cdd:COG3842 78 NVGMVFQDYALFPhltvaenvafG-LRMrGVPKAEIR--ARVAELLELVGLEGLADRYP----HQ-------LSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1454 VCLARALLRKTKVLVLDEATAAVDLETddliQKTIRTEFKEctvltIAHRLN--TIL---D-------SDKVIVLDKGQI 1521
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALDAKL----REEMREELRR-----LQRELGitFIYvthDqeealalADRIAVMNDGRI 214
|
250
....*....|....*..
gi 45552357 1522 IEFASPTELLDNPKSAF 1538
Cdd:COG3842 215 EQVGTPEEIYERPATRF 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1308-1489 |
2.08e-22 |
|
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: 96.78 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1308 RVEFQNFQVRYREglDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLtlalFRII----EAAGGRISIDGVDIASMGLHmLR 1383
Cdd:COG4133 2 MLEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTL----LRILagllPPSAGEVLWNGEPIRDARED-YR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1384 SRLTIIPQDPVLFSG-SLRINLDpF------EIKTDDEIWKALElshlksfvkslAAGLNHEIAEGGENLSVGQRQLVCL 1456
Cdd:COG4133 75 RRLAYLGHADGLKPElTVRENLR-FwaalygLRADREAIDEALE-----------AVGLAGLADLPVRQLSAGQKRRVAL 142
|
170 180 190
....*....|....*....|....*....|...
gi 45552357 1457 ARALLRKTKVLVLDEATAAVDLETDDLIQKTIR 1489
Cdd:COG4133 143 ARLLLSPAPLWLLDEPFTALDAAGVALLAELIA 175
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
660-866 |
2.16e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 103.56 E-value: 2.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 660 DEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFL-------GEME---------KLAGVVNTVgklAYVPQQAWIQNA 723
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTrfydideGEILldghdlrdyTLASLRNQV---ALVSQNVHLFND 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 724 TVRDNILF--GQTYDRKRYNKVID-ACALRAdIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSA 800
Cdd:PRK11176 432 TIANNIAYarTEQYSREQIEEAARmAYAMDF-INKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSA 510
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45552357 801 VDAHVGKHI---FEEVigpkgilaRKSR-VLV-THGVTFLPQVDSIYVIKMGEISESGTFDQLVKNKGAFA 866
Cdd:PRK11176 511 LDTESERAIqaaLDEL--------QKNRtSLViAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYA 573
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1305-1530 |
2.37e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 98.93 E-value: 2.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1305 QEGRVEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRS 1384
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1385 RLTIIPQDP------------VLFSgslrinLDPFEIKTDDEIWK---ALELSHLKSFvkslaagLNHEIAeggeNLSVG 1449
Cdd:PRK13635 82 QVGMVFQNPdnqfvgatvqddVAFG------LENIGVPREEMVERvdqALRQVGMEDF-------LNREPH----RLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1450 QRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRT--EFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASP 1527
Cdd:PRK13635 145 QKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTP 224
|
...
gi 45552357 1528 TEL 1530
Cdd:PRK13635 225 EEI 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
664-799 |
2.85e-22 |
|
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: 94.64 E-value: 2.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG-------------KLAYVPQQAWIQNA-TVRDNI 729
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45552357 730 LFGQtYDRKRYNKVIDAcalRADIDI--LSAGDL--TEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLS 799
Cdd:pfam00005 81 RLGL-LLKGLSKREKDA---RAEEALekLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1309-1523 |
5.20e-22 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 96.27 E-value: 5.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLDLV--LRGVSFNIQGGEKVGIVGRTGAGKSSL--TLALfrIIEAAGGRISIDGVDIASMG---LHM 1381
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLlnILGG--LDRPTSGEVLIDGQDISSLSereLAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1382 LRSR-LTIIPQD---------------PVLFSGslrinLDPFEIKTD-DEIWKALELSHLksfvkslaagLNHEIAEgge 1444
Cdd:COG1136 83 LRRRhIGFVFQFfnllpeltalenvalPLLLAG-----VSRKERRERaRELLERVGLGDR----------LDHRPSQ--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1445 nLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKE--CTVLTIAHRLNTILDSDKVIVLDKGQII 1522
Cdd:COG1136 145 -LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRIV 223
|
.
gi 45552357 1523 E 1523
Cdd:COG1136 224 S 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1309-1538 |
5.30e-22 |
|
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: 96.64 E-value: 5.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYreGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLtlalFRII----EAAGGRISIDGVDIASMGL----- 1379
Cdd:cd03296 3 IEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTL----LRLIagleRPDSGTILFGGEDATDVPVqernv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1380 ------HMLRSRLTIIpqDPVLFSgsLRI---NLDPFEIKTDDEIWKALELSHLKSFVKSLAAglnheiaeggeNLSVGQ 1450
Cdd:cd03296 77 gfvfqhYALFRHMTVF--DNVAFG--LRVkprSERPPEAEIRAKVHELLKLVQLDWLADRYPA-----------QLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1451 RQLVCLARALLRKTKVLVLDEATAAVDLEtddlIQKTIRTEFKE------CTVLTIAHRLNTILD-SDKVIVLDKGQIIE 1523
Cdd:cd03296 142 RQRVALARALAVEPKVLLLDEPFGALDAK----VRKELRRWLRRlhdelhVTTVFVTHDQEEALEvADRVVVMNKGRIEQ 217
|
250
....*....|....*
gi 45552357 1524 FASPTELLDNPKSAF 1538
Cdd:cd03296 218 VGTPDEVYDHPASPF 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1310-1535 |
5.63e-22 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 96.59 E-value: 5.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1310 EFQNFQVRYreGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMlRSRLTI- 1388
Cdd:COG0410 5 EVENLHAGY--GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHR-IARLGIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1389 -IPQDPVLFSG-SLRINL--------DPFEIKTDDEiwKALEL-SHLKSFVKSLAAglnheiaeggeNLSVGQRQLVCLA 1457
Cdd:COG0410 82 yVPEGRRIFPSlTVEENLllgayarrDRAEVRADLE--RVYELfPRLKERRRQRAG-----------TLSGGEQQMLAIG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1458 RALLRKTKVLVLDEATAA-----VDlETDDLIqKTIRTEfkECTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELL 1531
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGlapliVE-EIFEII-RRLNRE--GVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELL 224
|
....
gi 45552357 1532 DNPK 1535
Cdd:COG0410 225 ADPE 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
650-848 |
1.90e-21 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 94.07 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 650 SIENGEFSWGD--EITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKL-------------AYV 714
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDltklslkelrrkvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 715 PQQAWIQ--NATVRDNILFG---QTYDRKRYNKVIDACalradidiLSAGDLTEIGEKGI-NLSGGQKQRISLARAVYSD 788
Cdd:cd03225 81 FQNPDDQffGPTVEEEVAFGlenLGLPEEEIEERVEEA--------LELVGLEGLRDRSPfTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45552357 789 ADLYLLDDPLSAVDAHVGKHIFEEVIGpkgiLARKSR--VLVTHGVTFLPQV-DSIYVIKMGE 848
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKK----LKAEGKtiIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
664-830 |
3.45e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.07 E-value: 3.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG--KLAYVPQQ---AWIQNATVRDNILFGqTYDRK 738
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRsevPDSLPLTVRDLVAMG-RWARR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 739 RYNKVIDACALRADIDILSAGDLTEIGEKGIN-LSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEevigpk 817
Cdd:NF040873 87 GLWRRLTRDDRAAVDDALERVGLADLAGRQLGeLSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA------ 160
|
170
....*....|....*...
gi 45552357 818 gILARKSR-----VLVTH 830
Cdd:NF040873 161 -LLAEEHArgatvVVVTH 177
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1309-1537 |
4.28e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 96.41 E-value: 4.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLDLV--LRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASM---GLHMLR 1383
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1384 SRLTIIPQDPVLFSG---------SLRI-NLDPFEIKTD-DEIWKALELSHLKSFVKSlaaglnheiaeggeNLSVGQRQ 1452
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrtvfdnvalPLELaGTPKAEIKARvTELLELVGLSDKADRYPA--------------QLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1453 LVCLARALLRKTKVLVLDEATAAVDLETDDLIQ---KTIRTEFKeCTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPT 1528
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILellKDINRELG-LTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGTVS 226
|
....*....
gi 45552357 1529 ELLDNPKSA 1537
Cdd:PRK11153 227 EVFSHPKHP 235
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1309-1503 |
7.87e-21 |
|
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: 91.06 E-value: 7.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGlDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLtlalFRII----EAAGGRISIDGvdiasmglhmlRS 1384
Cdd:cd03223 1 IELENLSLATPDG-RVLLKDLSFEIKPGDRLLITGPSGTGKSSL----FRALaglwPWGSGRIGMPE-----------GE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1385 RLTIIPQDPVLFSGSLRinldpfeiktdDEI---WkalelshlksfvkslaaglnheiaegGENLSVGQRQLVCLARALL 1461
Cdd:cd03223 65 DLLFLPQRPYLPLGTLR-----------EQLiypW--------------------------DDVLSGGEQQRLAFARLLL 107
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 45552357 1462 RKTKVLVLDEATAAVDLETDDLIQKTIRTEFkeCTVLTIAHR 1503
Cdd:cd03223 108 HKPKFVFLDEATSALDEESEDRLYQLLKELG--ITVISVGHR 147
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1316-1537 |
1.16e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 92.51 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1316 VRYREGlDLVLRgVSFNIQGGEKVGIVGRTGAGKSSLtLAL---FriIEAAGGRISIDGVDIASMGLHmlrSR-LTIIPQ 1391
Cdd:COG3840 7 LTYRYG-DFPLR-FDLTIAAGERVAILGPSGAGKSTL-LNLiagF--LPPDSGRILWNGQDLTALPPA---ERpVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1392 DPVLFSG-SLRIN----LDPfeiktddeiwkALELSHL-KSFVKSLAA--GLNHEIAEGGENLSVGQRQLVCLARALLRK 1463
Cdd:COG3840 79 ENNLFPHlTVAQNiglgLRP-----------GLKLTAEqRAQVEQALErvGLAGLLDRLPGQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 1464 TKVLVLDEATAAVD----LETDDLIqKTIRTEFKeCTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNPKSA 1537
Cdd:COG3840 148 RPILLLDEPFSALDpalrQEMLDLV-DELCRERG-LTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGEPPP 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1309-1523 |
1.16e-20 |
|
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: 92.15 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLD--LVLRGVSFNIQGGEKVGIVGRTGAGKSSLtlalFRII----EAAGGRISIDGVDIASmglhmL 1382
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTL----LRIIagleRPTSGEVLVDGEPVTG-----P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1383 RSRLTIIPQDPVLF---------SGSLRINLDPFEiKTDDEIWKALELSHLKSFvkslaagLNHEIAEggenLSVGQRQL 1453
Cdd:cd03293 72 GPDRGYVFQQDALLpwltvldnvALGLELQGVPKA-EARERAEELLELVGLSGF-------ENAYPHQ----LSGGMRQR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 1454 VCLARALLRKTKVLVLDEATAAVDLET----DDLIQKTIRTEFKecTVLTIAHRLN-TILDSDKVIVLDK--GQIIE 1523
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTreqlQEELLDIWRETGK--TVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
649-853 |
1.45e-20 |
|
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: 91.81 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 649 MSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK-----------LAYVPQQ 717
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvpperrnIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 718 -AWIQNATVRDNILFGqTYDRKRYNKVIDACALRadidILSAGDLTEIGEKGIN-LSGGQKQRISLARAVYSDADLYLLD 795
Cdd:cd03259 81 yALFPHLTVAENIAFG-LKLRGVPKAEIRARVRE----LLELVGLEGLLNRYPHeLSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45552357 796 DPLSAVDAHVGKHIFEEVigpKGILAR--KSRVLVTHGVT-FLPQVDSIYVIKMGEISESG 853
Cdd:cd03259 156 EPLSALDAKLREELREEL---KELQRElgITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1304-1523 |
2.02e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 92.46 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1304 PQEGRVEFQNFQVRYREGLD--LVLRGVSFNIQGGEKVGIVGRTGAGKSSLtlalFRII----EAAGGRISIDGVDIASM 1377
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLIagleKPTSGEVLVDGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1378 GlhmlrSRLTIIPQDPVLF----------SGsLRI-NLDPFEIKtdDEIWKALELSHLKSFVKSLAaglnHEiaeggenL 1446
Cdd:COG1116 79 G-----PDRGVVFQEPALLpwltvldnvaLG-LELrGVPKAERR--ERARELLELVGLAGFEDAYP----HQ-------L 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1447 SVGQRQLVCLARALLRKTKVLVLDEATAAVDLET-----DDLIQktIRTEFKeCTVLTIAH------RLntildSDKVIV 1515
Cdd:COG1116 140 SGGMRQRVAIARALANDPEVLLMDEPFGALDALTrerlqDELLR--LWQETG-KTVLFVTHdvdeavFL-----ADRVVV 211
|
250
....*....|
gi 45552357 1516 LDK--GQIIE 1523
Cdd:COG1116 212 LSArpGRIVE 221
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
649-858 |
2.04e-20 |
|
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: 91.86 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 649 MSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAF-----LGEMEKLAGVVNTVGKLAYVP-------- 715
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLdvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 716 -------QQAWIQNATVRDNILFGQTYDRKRYNKVIDACALRAdidiLSAGDLTEIGE---KGINLSGGQKQRISLARAV 785
Cdd:cd03260 81 rrvgmvfQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERVEEA----LRKAALWDEVKdrlHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 786 YSDADLYLLDDPLSAVDAhVGKHIFEEVIGPkgiLARKSR-VLVTHGvtfLPQV----DSIYVIKMGEISESGTFDQL 858
Cdd:cd03260 157 ANEPEVLLLDEPTSALDP-ISTAKIEELIAE---LKKEYTiVIVTHN---MQQAarvaDRTAFLLNGRLVEFGPTEQI 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1307-1538 |
2.51e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 94.37 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1307 GRVEFQNFQVRYreGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLtlaLfRII----EAAGGRISIDGVDIASM----- 1377
Cdd:COG3839 2 ASLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTL---L-RMIagleDPTSGEILIGGRDVTDLppkdr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1378 GLHMlrsrltiIPQDPVLF----------SGsLRI-NLDPFEIKTD-DEIWKALELSHLksfvkslaagLNHEIAEggen 1445
Cdd:COG3839 76 NIAM-------VFQSYALYphmtvyeniaFP-LKLrKVPKAEIDRRvREAAELLGLEDL----------LDRKPKQ---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1446 LSVGQRQLVCLARALLRKTKVLVLDEATAAVD----LETddliqktiRTEFKEctvltIAHRLNTIL-----D------- 1509
Cdd:COG3839 134 LSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEM--------RAEIKR-----LHRRLGTTTiyvthDqveamtl 200
|
250 260
....*....|....*....|....*....
gi 45552357 1510 SDKVIVLDKGQIIEFASPTELLDNPKSAF 1538
Cdd:COG3839 201 ADRIAVMNDGRIQQVGTPEELYDRPANLF 229
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1309-1538 |
2.52e-20 |
|
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: 91.53 E-value: 2.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYreGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLtlalFRII----EAAGGRISIDGVDIASMGLHmlRS 1384
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLIagfeTPTSGEILLDGKDITNLPPH--KR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1385 RLTIIPQDPVLF---------SGSLRI-NLDPFEIKtdDEIWKALELSHLKSFvkslaagLNHEIAEggenLSVGQRQLV 1454
Cdd:cd03300 73 PVNTVFQNYALFphltvfeniAFGLRLkKLPKAEIK--ERVAEALDLVQLEGY-------ANRKPSQ----LSGGQQQRV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1455 CLARALLRKTKVLVLDEATAAVDLEtddlIQKTIRTEFKE------CTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASP 1527
Cdd:cd03300 140 AIARALVNEPKVLLLDEPLGALDLK----LRKDMQLELKRlqkelgITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTP 215
|
250
....*....|.
gi 45552357 1528 TELLDNPKSAF 1538
Cdd:cd03300 216 EEIYEEPANRF 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
660-849 |
3.22e-20 |
|
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: 90.99 E-value: 3.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 660 DEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK-------------LAYVPQQAWIQNATVR 726
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVSLVGQEPVLFARSLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 727 DNILFG-QTYDRKRYNKVIDACALRADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHv 805
Cdd:cd03248 106 DNIAYGlQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE- 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 45552357 806 GKHIFEEVIgpKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEI 849
Cdd:cd03248 185 SEQQVQQAL--YDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
650-848 |
3.73e-20 |
|
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: 88.84 E-value: 3.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 650 SIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGvvntvgklayvpqQAWIQNATVRDNI 729
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSG-------------EILIDGKDIAKLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 730 LFgqtydrkrynkvidacALRADIDILSAgdlteigekginLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHvGKHI 809
Cdd:cd00267 68 LE----------------ELRRRIGYVPQ------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA-SRER 118
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 45552357 810 FEEVIgpKGILARKSRVL-VTHGVTFLPQV-DSIYVIKMGE 848
Cdd:cd00267 119 LLELL--RELAEEGRTVIiVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1325-1535 |
7.58e-20 |
|
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: 90.29 E-value: 7.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMlRSRLTII--PQDPVLFSG-SLR 1401
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIGylPQEASIFRKlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1402 INLDPF--EIKTDDEIWKA-----LELSHLKSFVKSLAAGlnheiaeggenLSVGQRQLVCLARALLRKTKVLVLDEATA 1474
Cdd:cd03218 94 ENILAVleIRGLSKKEREEkleelLEEFHITHLRKSKASS-----------LSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45552357 1475 AVDLETDDLIQKTIRtEFKE--CTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNPK 1535
Cdd:cd03218 163 GVDPIAVQDIQKIIK-ILKDrgIGVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1309-1547 |
1.58e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 90.68 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLDlVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDG--VDIASMGLHMLRSRL 1386
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1387 TIIPQDP--VLFSGSL--RINLDPFEIK-TDDEIWKALELSHLKSFVKSLAAGLNHEiaeggenLSVGQRQLVCLARALL 1461
Cdd:PRK13636 85 GMVFQDPdnQLFSASVyqDVSFGAVNLKlPEDEVRKRVDNALKRTGIEHLKDKPTHC-------LSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1462 RKTKVLVLDEATAAVDLETDDLIQKTIRTEFKE--CTVLTIAHRLNTI-LDSDKVIVLDKGQIIEFASPTELLdnpksAF 1538
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElgLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVF-----AE 232
|
....*....
gi 45552357 1539 YSMAKDANL 1547
Cdd:PRK13636 233 KEMLRKVNL 241
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1239-1516 |
1.64e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 95.87 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1239 QTNPGLVGLSV-SYALQVTQTLNWLVRMSSDIETNIVSVERIKEYGETKQEAPweLEQDKNKPKNWPQEGRVEFQNFQVR 1317
Cdd:PTZ00265 314 QPNNDFHGGSViSILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKP--LVENNDDGKKLKDIKKIQFKNVRFH 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1318 YREGLDL-VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISI-DGVDIASMGLHMLRSRLTIIPQDPVL 1395
Cdd:PTZ00265 392 YDTRKDVeIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLL 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1396 FSGSLRINLD----------------------------------------------------------PFEIKTDDEIWK 1417
Cdd:PTZ00265 472 FSNSIKNNIKyslyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrkNYQTIKDSEVVD 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1418 ALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTI---RTEFKE 1494
Cdd:PTZ00265 552 VSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnlKGNENR 631
|
330 340
....*....|....*....|..
gi 45552357 1495 CTVLtIAHRLNTILDSDKVIVL 1516
Cdd:PTZ00265 632 ITII-IAHRLSTIRYANTIFVL 652
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1309-1547 |
1.99e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 90.24 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRII---EAAGGRISIDGVDIASMGLHMLRSR 1385
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1386 LTIIPQDP-VLFSGSlrinldpfeiKTDDEIWKALE-----LSHLKSFVKSLAA--GLNHEIAEGGENLSVGQRQLVCLA 1457
Cdd:PRK13640 86 VGIVFQNPdNQFVGA----------TVGDDVAFGLEnravpRPEMIKIVRDVLAdvGMLDYIDSEPANLSGGQKQRVAIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1458 RALLRKTKVLVLDEATAAVDLETDDLIQKTIR--TEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLDNPk 1535
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRklKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV- 234
|
250
....*....|..
gi 45552357 1536 safySMAKDANL 1547
Cdd:PRK13640 235 ----EMLKEIGL 242
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
664-858 |
2.04e-19 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 88.97 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVnTVG-------------KLAYVPQQAWI-QNATVRDNI 729
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEV-RVLgedvardpaevrrRIGYVPQEPALyPDLTVRENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 730 -LFGQTYDrkrynkvIDACALRADID-ILSAGDLTEIGEKGI-NLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAhVG 806
Cdd:COG1131 95 rFFARLYG-------LPRKEARERIDeLLELFGLTDAADRKVgTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP-EA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 807 KHIFEEVIgpKGILARKSRVLV-THgvtFLPQV----DSIYVIKMGEISESGTFDQL 858
Cdd:COG1131 167 RRELWELL--RELAAEGKTVLLsTH---YLEEAerlcDRVAIIDKGRIVADGTPDEL 218
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
649-853 |
2.07e-19 |
|
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: 87.37 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 649 MSIENGEFSWGDEIT--LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK------------LAYV 714
Cdd:cd03247 1 LSINNVSFSYPEQEQqvLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 715 PQQAWIQNATVRDNIlfgqtydrkrynkvidacalradidilsagdlteigekGINLSGGQKQRISLARAVYSDADLYLL 794
Cdd:cd03247 81 NQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 795 DDPLSAVDAHVGKHIFEEVIgpkGILARKSRVLVTHGVTFLPQVDSIYVIKMGEISESG 853
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIF---EVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1325-1523 |
2.08e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.54 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMG-LHMLRSRLTIIPQDPVLFSG-SLRI 1402
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPNlSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1403 NLdpF---EIKTDDEI-WKALElshlkSFVKSLAAGLNHEI---AEGGEnLSVGQRQLVCLARALLRKTKVLVLDEATAA 1475
Cdd:COG1129 99 NI--FlgrEPRRGGLIdWRAMR-----RRARELLARLGLDIdpdTPVGD-LSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 45552357 1476 VDL-ETDDLIqKTIRtEFKE--CTVLTIAHRLNTILD-SDKVIVLDKGQIIE 1523
Cdd:COG1129 171 LTErEVERLF-RIIR-RLKAqgVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1309-1536 |
2.65e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 89.81 E-value: 2.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTI 1388
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1389 IPQDPV-LFSGSL-----RINLDPFEIKTDD---EIWKALELshlksfVKSLAAGlNHEiaegGENLSVGQRQLVCLARA 1459
Cdd:PRK13648 88 VFQNPDnQFVGSIvkydvAFGLENHAVPYDEmhrRVSEALKQ------VDMLERA-DYE----PNALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1460 LLRKTKVLVLDEATAAVDLETD----DLIQKTirTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLDNPK 1535
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARqnllDLVRKV--KSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
.
gi 45552357 1536 S 1536
Cdd:PRK13648 235 E 235
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
650-804 |
3.02e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 91.29 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 650 SIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSvvqafLGEMekLAG--------------VVNTVG----KL 711
Cdd:COG3839 5 ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKST-----LLRM--IAGledptsgeiliggrDVTDLPpkdrNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 712 AYVPQQ-AWIQNATVRDNILFGQtydrkRYNKVidacaLRADID--ILSAGDLTEIGE----KGINLSGGQKQRISLARA 784
Cdd:COG3839 78 AMVFQSyALYPHMTVYENIAFPL-----KLRKV-----PKAEIDrrVREAAELLGLEDlldrKPKQLSGGQRQRVALGRA 147
|
170 180
....*....|....*....|
gi 45552357 785 VYSDADLYLLDDPLSAVDAH 804
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDAK 167
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1309-1521 |
5.11e-19 |
|
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: 87.20 E-value: 5.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYreGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDI--ASMGLHMLRSRL 1386
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1387 TIIPQDPVLFSgslriNLDPFEIKTDDEIW---------KALELSHLKSfvkslaAGLNHEIAEGGENLSVGQRQLVCLA 1457
Cdd:cd03262 79 GMVFQQFNLFP-----HLTVLENITLAPIKvkgmskaeaEERALELLEK------VGLADKADAYPAQLSGGQQQRVAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552357 1458 RALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKE-CTVLTIAHRLNTILD-SDKVIVLDKGQI 1521
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEgMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1315-1531 |
6.20e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 88.29 E-value: 6.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1315 QVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPV 1394
Cdd:PRK13548 7 NLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1395 L-FSGS----LRINLDPF---EIKTDDEIWKALE---LSHLKSfvKSLAAglnheiaeggenLSVGQRQLVCLARALLR- 1462
Cdd:PRK13548 87 LsFPFTveevVAMGRAPHglsRAEDDALVAAALAqvdLAHLAG--RDYPQ------------LSGGEQQRVQLARVLAQl 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1463 -----KTKVLVLDEATAAVDLetddLIQKTIRTEFKECT------VLTIAHRLN-TILDSDKVIVLDKGQIIEFASPTEL 1530
Cdd:PRK13548 153 wepdgPPRWLLLDEPTSALDL----AHQHHVLRLARQLAherglaVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEV 228
|
.
gi 45552357 1531 L 1531
Cdd:PRK13548 229 L 229
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1309-1534 |
6.23e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.89 E-value: 6.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLDlVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMG-LHMLRSRLT 1387
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1388 IIPQDPV-----------LFSGSLRINLDPFEIKtddeiwkalelshlKSFVKSLA-AGLNHEIAEGGENLSVGQRQLVC 1455
Cdd:PRK13644 81 IVFQNPEtqfvgrtveedLAFGPENLCLPPIEIR--------------KRVDRALAeIGLEKYRHRSPKTLSGGQGQCVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1456 LARALLRKTKVLVLDEATAAVDLETDDLIQKTI-RTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLDNP 1534
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIkKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1326-1533 |
6.42e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 88.95 E-value: 6.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1326 LRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHM--LRSRLTIIPQDP--VLFS---- 1397
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLsdIRKKVGLVFQYPeyQLFEetie 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1398 -----GSLRINLDPFEIKtdDEIWKALELshlksfvkslaAGLNHEIAEGGE--NLSVGQRQLVCLARALLRKTKVLVLD 1470
Cdd:PRK13637 103 kdiafGPINLGLSEEEIE--NRVKRAMNI-----------VGLDYEDYKDKSpfELSGGQKRRVAIAGVVAMEPKILILD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552357 1471 EATAAVDLETDDLIQKTIRTEFKE--CTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDN 1533
Cdd:PRK13637 170 EPTAGLDPKGRDEILNKIKELHKEynMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
664-832 |
6.54e-19 |
|
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: 87.14 E-value: 6.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK--------LAYVPQQA----WiqnATVRDNILF 731
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgpdRGYVFQQDallpW---LTVLDNVAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 732 GQtydrkRYNKVIDACALRADIDILSAGDLTEIGEKGIN-LSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIF 810
Cdd:cd03293 97 GL-----ELQGVPKAEARERAEELLELVGLSGFENAYPHqLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQ 171
|
170 180
....*....|....*....|....*
gi 45552357 811 EEVIGpkgiLARKSR---VLVTHGV 832
Cdd:cd03293 172 EELLD----IWRETGktvLLVTHDI 192
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1325-1522 |
7.40e-19 |
|
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: 87.39 E-value: 7.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVD--------IASMGLhMLRSRLTIIPQDPVLF 1396
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrrkkfLRRIGV-VFGQKTQLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1397 SGSL--RI-NLDPFEIKTD-DEIWKALELSH-LKSFVKslaaglnheiaeggeNLSVGQRQLVCLARALLRKTKVLVLDE 1471
Cdd:cd03267 115 SFYLlaAIyDLPPARFKKRlDELSELLDLEElLDTPVR---------------QLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 45552357 1472 ATAAVDLETDDLIQKTIRTEFKE--CTVLTIAHRLNTILD-SDKVIVLDKGQII 1522
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRErgTTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1325-1522 |
7.76e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 88.22 E-value: 7.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLtlalFRIIeaAG------GRISIDGVDIASMGLHMlRSRLtI--IPQDPVL- 1395
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTL----LNAI--AGslppdsGSILIDGKDVTKLPEYK-RAKY-IgrVFQDPMMg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1396 ------------------FSGSLRINLDpfeiKTDDEIWKALelshlksfVKSLAAGLNHEIAEGGENLSVGQRQLVCLA 1457
Cdd:COG1101 93 tapsmtieenlalayrrgKRRGLRRGLT----KKRRELFREL--------LATLGLGLENRLDTKVGLLSGGQRQALSLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45552357 1458 RALLRKTKVLVLDEATAAVD-------LE-TDDLIQKtirtefKECTVLTIAHRLNTILD-SDKVIVLDKGQII 1522
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDpktaalvLElTEKIVEE------NNLTTLMVTHNMEQALDyGNRLIMMHEGRII 228
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1325-1538 |
8.06e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 89.82 E-value: 8.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLtlaLfRIIeaAG------GRISIDGVDIASmGLHMLRSRLTIIPQDPVLFS- 1397
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTL---L-RII--AGletpdsGRIVLNGRDLFT-NLPPRERRVGFVFQHYALFPh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1398 ---------GsLRI-NLDPFEIKTDDEIWkaLELSHLKSFVKSLAAglnheiaeggeNLSVGQRQLVCLARALLRKTKVL 1467
Cdd:COG1118 90 mtvaeniafG-LRVrPPSKAEIRARVEEL--LELVQLEGLADRYPS-----------QLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 1468 VLDEATAAVdletDDLIQKTIRTEFKE------CTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNPKSAF 1538
Cdd:COG1118 156 LLDEPFGAL----DAKVRKELRRWLRRlhdelgGTTVFVTHDQEEALElADRVVVMNQGRIEQVGTPDEVYDRPATPF 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
664-868 |
8.09e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 92.33 E-value: 8.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVV----QAF---LGEMeKLAGV-VNTVGK------LAYVPQQAWIQNATVRDNI 729
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLInllqRVFdpqSGRI-LIDGTdIRTVTRaslrrnIAVVFQDAGLFNRSIEDNI 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 730 LFGQTydrKRYNKVIDACALRAD----IDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHV 805
Cdd:PRK13657 430 RVGRP---DATDEEMRAAAERAQahdfIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVET 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 806 G---KHIFEEVigpkgilaRKSRV--LVTHGVTFLPQVDSIYVIKMGEISESGTFDQLVKNKGAFADF 868
Cdd:PRK13657 507 EakvKAALDEL--------MKGRTtfIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAAL 566
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
649-804 |
8.71e-19 |
|
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: 87.79 E-value: 8.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 649 MSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVnTVG--------------KLAYV 714
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEV-LLDgrdlaslsrrelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 715 PQQ---AWiqNATVRDNILFG--------QTYDRKRYNKVIDAcalradidiLSAGDLTEIGEKGIN-LSGGQKQRISLA 782
Cdd:COG1120 81 PQEppaPF--GLTVRELVALGryphlglfGRPSAEDREAVEEA---------LERTGLEHLADRPVDeLSGGERQRVLIA 149
|
170 180
....*....|....*....|...
gi 45552357 783 RAVYSDADLYLLDDPLSAVD-AH 804
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDlAH 172
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
664-832 |
9.24e-19 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 87.84 E-value: 9.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSV-------VQAFLGEMEkLAG--VVNTVGKLAYVPQQA----WiqnATVRDNIL 730
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLlrliaglEKPTSGEVL-VDGkpVTGPGPDRGVVFQEPallpW---LTVLDNVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 731 FG-------QTYDRKRYNKVIDACALRADIDILSAgdlteigekgiNLSGGQKQRISLARAVYSDADLYLLDDPLSAVDA 803
Cdd:COG1116 103 LGlelrgvpKAERRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIARALANDPEVLLMDEPFGALDA 171
|
170 180 190
....*....|....*....|....*....|..
gi 45552357 804 HVGKHIFEEVIGpkgiLARKSR---VLVTHGV 832
Cdd:COG1116 172 LTRERLQDELLR----LWQETGktvLFVTHDV 199
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1304-1535 |
1.36e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 87.40 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1304 PQEGRVEFQNFQVRYreGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIE-----AAGGRISIDGVDI--AS 1376
Cdd:COG1117 7 TLEPKIEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlipgaRVEGEILLDGEDIydPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1377 MGLHMLRSRLTIIPQDPVLFSGS--------LRINldpfEIKTDDEIWKALElshlksfvKSL-AAGLNHEIA----EGG 1443
Cdd:COG1117 85 VDVVELRRRVGMVFQKPNPFPKSiydnvaygLRLH----GIKSKSELDEIVE--------ESLrKAALWDEVKdrlkKSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1444 ENLSVGQRQLVCLARALLRKTKVLVLDEATAAVD-LETD---DLIQktirtEFKE-CTVLTIAH------RLntildSDK 1512
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTAkieELIL-----ELKKdYTIVIVTHnmqqaaRV-----SDY 222
|
250 260
....*....|....*....|...
gi 45552357 1513 VIVLDKGQIIEFASPTELLDNPK 1535
Cdd:COG1117 223 TAFFYLGELVEFGPTEQIFTNPK 245
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1309-1541 |
1.71e-18 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 86.68 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLdlVLRGVSFNIQGGEKVGIVGRTGAGKSSL-TLALFRIIEAAGGRISI-----DGVDI-------- 1374
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLlSLITGDLPPTYGNDVRLfgerrGGEDVwelrkrig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1375 -ASMGLHM-LRSRLTIIpqDPVL--FSGSLRI--NLDPFEIKTDDEIWKALELSHLKsfvkslaaglNHEIAEggenLSV 1448
Cdd:COG1119 82 lVSPALQLrFPRDETVL--DVVLsgFFDSIGLyrEPTDEQRERARELLELLGLAHLA----------DRPFGT----LSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1449 GQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRT--EFKECTVLTIAHRLNTILDS-DKVIVLDKGQIIEFA 1525
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAG 225
|
250
....*....|....*..
gi 45552357 1526 SPTELL-DNPKSAFYSM 1541
Cdd:COG1119 226 PKEEVLtSENLSEAFGL 242
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1325-1535 |
1.77e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.89 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIE-----AAGGRISIDGVDIASMGLHMLRSRLTIIPQDPVLFSgs 1399
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIP-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1400 lriNLDPFE-----------IKTDDEIWK----ALELSHLKSFVKslaaglNHEIAEGGEnLSVGQRQLVCLARALLRKT 1464
Cdd:PRK14247 96 ---NLSIFEnvalglklnrlVKSKKELQErvrwALEKAQLWDEVK------DRLDAPAGK-LSGGQQQRLCIARALAFQP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 1465 KVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAH------RLntildSDKVIVLDKGQIIEFASPTELLDNPK 1535
Cdd:PRK14247 166 EVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVEWGPTREVFTNPR 237
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1309-1522 |
1.94e-18 |
|
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: 85.88 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYR--EGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIAS--------MG 1378
Cdd:cd03266 2 ITADALTKRFRdvKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKepaearrrLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1379 LHM----LRSRLTIIPQdpVLFSGSLRinldpfeiktddeiwkALELSHLKSFVKSLAA--GLNHEIAEGGENLSVGQRQ 1452
Cdd:cd03266 82 FVSdstgLYDRLTAREN--LEYFAGLY----------------GLKGDELTARLEELADrlGMEELLDRRVGGFSTGMRQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45552357 1453 LVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRtEFKE--CTVLTIAHRLNTILD-SDKVIVLDKGQII 1522
Cdd:cd03266 144 KVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIR-QLRAlgKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
657-805 |
2.47e-18 |
|
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: 85.38 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 657 SWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAG-------VVNTVG----KLAYVPQQ-AWIQNAT 724
Cdd:cd03301 9 RFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGriyiggrDVTDLPpkdrDIAMVFQNyALYPHMT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 725 VRDNILFGQTYdRKRYNKVIDAcalradiDILSAGDLTEIGE----KGINLSGGQKQRISLARAVYSDADLYLLDDPLSA 800
Cdd:cd03301 89 VYDNIAFGLKL-RKVPKDEIDE-------RVREVAELLQIEHlldrKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
....*
gi 45552357 801 VDAHV 805
Cdd:cd03301 161 LDAKL 165
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
650-853 |
2.76e-18 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 84.02 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 650 SIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVnTVG--------------KLAYVP 715
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI-LLDgkdlaslspkelarKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 716 QqawiqnatvrdnilfgqtydrkrynkvidacalradidILSAGDLTEIGEKGIN-LSGGQKQRISLARAVYSDADLYLL 794
Cdd:cd03214 80 Q--------------------------------------ALELLGLAHLADRPFNeLSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45552357 795 DDPLSAVDAHVGKHIFEEVIGpkgiLARKSR---VLVTHGVTFLPQV-DSIYVIKMGEISESG 853
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRR----LARERGktvVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1326-1519 |
2.97e-18 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 85.46 E-value: 2.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1326 LRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSR----LTIIPQDPVLFSGSLR 1401
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1402 INLdPFEIKTDDEIWKAL-ELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLE- 1479
Cdd:cd03290 97 ENI-TFGSPFNKQRYKAVtDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHl 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 45552357 1480 TDDLIQKTIRTEFKE--CTVLTIAHRLNTILDSDKVIVLDKG 1519
Cdd:cd03290 176 SDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
649-861 |
3.07e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 88.28 E-value: 3.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 649 MSIE--NGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAflgemekLAG--------------VVNT----- 707
Cdd:COG1118 1 MSIEvrNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRI-------IAGletpdsgrivlngrDLFTnlppr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 708 ---VGklaYVPQQ-AWIQNATVRDNILFGQTyDRKRYNKVIDAcalRADiDILSAGDLTEIGEKGIN-LSGGQKQRISLA 782
Cdd:COG1118 74 errVG---FVFQHyALFPHMTVAENIAFGLR-VRPPSKAEIRA---RVE-ELLELVQLEGLADRYPSqLSGGQRQRVALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 783 RAVYSDADLYLLDDPLSAVDAHVGK-------HIFEEVigpkGIlarkSRVLVTH------GVTflpqvDSIYVIKMGEI 849
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKelrrwlrRLHDEL----GG----TTVFVTHdqeealELA-----DRVVVMNQGRI 212
|
250
....*....|..
gi 45552357 850 SESGTFDQLVKN 861
Cdd:COG1118 213 EQVGTPDEVYDR 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
650-830 |
3.69e-18 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 84.48 E-value: 3.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 650 SIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK-------------LAYVPQ 716
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKplsampppewrrqVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 717 Q-AWIQNaTVRDNILFGQTYDRKRYNKViDACALRADIDiLSAGDLteigEKGI-NLSGGQKQRISLARAVYSDADLYLL 794
Cdd:COG4619 82 EpALWGG-TVRDNLPFPFQLRERKFDRE-RALELLERLG-LPPDIL----DKPVeRLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 45552357 795 DDPLSAVDAHvGKHIFEEVIgpKGILARKSR--VLVTH 830
Cdd:COG4619 155 DEPTSALDPE-NTRRVEELL--REYLAEEGRavLWVSH 189
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1309-1530 |
4.15e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 86.32 E-value: 4.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLD-LVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLT 1387
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1388 IIPQDP------------VLFsGSLRINLDPFEIKtdDEIWKALELSHLKSFVKSLAAglnheiaeggeNLSVGQRQLVC 1455
Cdd:PRK13650 85 MVFQNPdnqfvgatveddVAF-GLENKGIPHEEMK--ERVNEALELVGMQDFKEREPA-----------RLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 1456 LARALLRKTKVLVLDEATAAVDLETD-DLIQ--KTIRTEFkECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTEL 1530
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRlELIKtiKGIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
988-1279 |
4.35e-18 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 86.45 E-value: 4.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 988 IFLSVATLVLNFVFQAFQIgsnlWLTQWANDQNVAND--TGLRDMYLGVYGAFGFGQVFSYIGSVVIVYLGALIgTRKIF 1065
Cdd:cd07346 1 LLLALLLLLLATALGLALP----LLTKLLIDDVIPAGdlSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRV-VFDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1066 IQLFGNILHAPQAYFDIKPRARILDRLANDIYKLDVVLPELIRVFNSQVFRVLATIVV-ISLSTPIFLAVIVPIAFLYYF 1144
Cdd:cd07346 76 RDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVIlFYLNWKLTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1145 AQRFYV---ATSRQLMrlESVSRspIYSHFSETVTGASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVIANRWLAIRLEM 1221
Cdd:cd07346 156 LRYFRRrirKASREVR--ESLAE--LSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45552357 1222 VGNLIILFASLFA---VLGGQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERI 1279
Cdd:cd07346 232 LTALGTALVLLYGgylVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1309-1521 |
4.65e-18 |
|
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: 84.38 E-value: 4.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLdLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIAsmGLH-----MLR 1383
Cdd:cd03292 1 IEFINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS--DLRgraipYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1384 SRLTIIPQDPVLFSgslriNLDPFEiktddEIWKALELSHL--KSFVKSLAA-----GLNHEIAEGGENLSVGQRQLVCL 1456
Cdd:cd03292 78 RKIGVVFQDFRLLP-----DRNVYE-----NVAFALEVTGVppREIRKRVPAalelvGLSHKHRALPAELSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 1457 ARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILD--SDKVIVLDKGQI 1521
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDttRHRVIALERGKL 214
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1315-1516 |
4.86e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 84.77 E-value: 4.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1315 QVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPV 1394
Cdd:PRK10247 12 NVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1395 LFSGSLRINLD-PFEI--KTDDEiwkalelshlKSFVKSLAA-GLNHEIAEGGEN-LSVGQRQLVCLARALLRKTKVLVL 1469
Cdd:PRK10247 92 LFGDTVYDNLIfPWQIrnQQPDP----------AIFLDDLERfALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 45552357 1470 DEATAAVD----LETDDLIQKTIRTefKECTVLTIAHRLNTILDSDKVIVL 1516
Cdd:PRK10247 162 DEITSALDesnkHNVNEIIHRYVRE--QNIAVLWVTHDKDEINHADKVITL 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
650-849 |
6.12e-18 |
|
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: 83.03 E-value: 6.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 650 SIENGEFSWGD--EITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVV-------NTVGK------LAYV 714
Cdd:cd03246 2 EVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldgadiSQWDPnelgdhVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 715 PQQAWIQNATVRDNILfgqtydrkrynkvidacalradidilsagdlteigekginlSGGQKQRISLARAVYSDADLYLL 794
Cdd:cd03246 82 PQDDELFSGSIAENIL-----------------------------------------SGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 795 DDPLSAVDAHVGKHIFEEVIGPKgiLARKSRVLVTHGVTFLPQVDSIYVIKMGEI 849
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALK--AAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
655-861 |
7.70e-18 |
|
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: 88.81 E-value: 7.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 655 EFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTV----------------GKLAYVPQQA 718
Cdd:COG1123 13 RYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVlldgrdllelsealrgRRIGMVFQDP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 719 WIQ--NATVRDNILFGQtydrkRYNKVIDACALRADIDILSAGDLTEIGEKGIN-LSGGQKQRISLARAVYSDADLYLLD 795
Cdd:COG1123 93 MTQlnPVTVGDQIAEAL-----ENLGLSRAEARARVLELLEAVGLERRLDRYPHqLSGGQRQRVAIAMALALDPDLLIAD 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 796 DPLSAVDAHVGKHIFEEVigpkGILAR---KSRVLVTHGVTFLPQV-DSIYVIKMGEISESGTFDQLVKN 861
Cdd:COG1123 168 EPTTALDVTTQAEILDLL----RELQRergTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1280-1538 |
7.71e-18 |
|
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: 85.39 E-value: 7.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1280 KEYGETKQEAPWELEQDKNKPknwpqegrvefqnfQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRI 1359
Cdd:cd03294 8 KIFGKNPQKAFKLLAKGKSKE--------------EILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1360 IEAAGGRISIDGVDIASMG---LHMLRS-RLTIIPQDPVLFSGslRINLD----PFEIKTDDE------IWKALELSHLK 1425
Cdd:cd03294 74 IEPTSGKVLIDGQDIAAMSrkeLRELRRkKISMVFQSFALLPH--RTVLEnvafGLEVQGVPRaereerAAEALELVGLE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1426 SFvkslaagLNHEIAEggenLSVGQRQLVCLARALLRKTKVLVLDEATAAVdletDDLIQKTIRTEFKEC------TVLT 1499
Cdd:cd03294 152 GW-------EHKYPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSAL----DPLIRREMQDELLRLqaelqkTIVF 216
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 45552357 1500 IAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNPKSAF 1538
Cdd:cd03294 217 ITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
664-849 |
8.68e-18 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 83.69 E-value: 8.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVqAFLGEMEKL-AGVVNTVGK-----------------LAYVPQQ-AWIQNAT 724
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLL-NILGGLDRPtSGEVRVDGTdisklsekelaafrrrhIGFVFQSfNLLPDLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 725 VRDNILFGQTYDRKRYNKvidaCALRAdIDILSAGDLTEIGEKGIN-LSGGQKQRISLARAVYSDADLYLLDDPLSAVDA 803
Cdd:cd03255 99 ALENVELPLLLAGVPKKE----RRERA-EELLERVGLGDRLNHYPSeLSGGQQQRVAIARALANDPKIILADEPTGNLDS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 45552357 804 HVGKHIFEevigpkgILARKSR------VLVTHGVTFLPQVDSIYVIKMGEI 849
Cdd:cd03255 174 ETGKEVME-------LLRELNKeagttiVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1309-1522 |
9.32e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 83.48 E-value: 9.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREglDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDG--VDIASmglhmlRSRL 1386
Cdd:cd03269 1 LEVENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpLDIAA------RNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1387 TIIP-----------QDPVLFSGSLRiNLDPFEIKTDDEIW-KALELSHLKSfvKSLaaglnheiaeggENLSVGQRQLV 1454
Cdd:cd03269 73 GYLPeerglypkmkvIDQLVYLAQLK-GLKKEEARRRIDEWlERLELSEYAN--KRV------------EELSKGNQQKV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45552357 1455 CLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRtEFKE--CTVLTIAHRLNTILD-SDKVIVLDKGQII 1522
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIR-ELARagKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
651-872 |
1.13e-17 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 84.14 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 651 IENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG------------KLAYVPQQA 718
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 719 WI-QNATVRDNI-LFGQTYDRKRynkviDACALRADiDILSAGDLTEIGEKGI-NLSGGQKQRISLARAVYSDADLYLLD 795
Cdd:COG4555 84 GLyDRLTVRENIrYFAELYGLFD-----EELKKRIE-ELIELLGLEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 796 DPLSAVDAhVGKHIFEEVIgpKGILARKSRVLV-THGVTFLPQV-DSIYVIKMGEISESGTFDQLVKNKG------AFAD 867
Cdd:COG4555 158 EPTNGLDV-MARRLLREIL--RALKKEGKTVLFsSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIGeenledAFVA 234
|
....*
gi 45552357 868 FIIQH 872
Cdd:COG4555 235 LIGSE 239
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
651-869 |
1.15e-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: 83.92 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 651 IENGEFSWGdEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK-----------LAYVPQQ-A 718
Cdd:cd03299 3 VENLSKDWK-EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 719 WIQNATVRDNILFG---QTYDRKRYNKVIDACALRADIDILsagdlteIGEKGINLSGGQKQRISLARAVYSDADLYLLD 795
Cdd:cd03299 82 LFPHMTVYKNIAYGlkkRKVDKKEIERKVLEIAEMLGIDHL-------LNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 796 DPLSAVDAHVGKHIFEEVigpkGILARKSRVLVTHgVTF-----LPQVDSIYVIKMGEISESGTFDQLVKN--KGAFADF 868
Cdd:cd03299 155 EPFSALDVRTKEKLREEL----KKIRKEFGVTVLH-VTHdfeeaWALADKVAIMLNGKLIQVGKPEEVFKKpkNEFVAEF 229
|
.
gi 45552357 869 I 869
Cdd:cd03299 230 L 230
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
659-814 |
1.22e-17 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 82.91 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 659 GDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK------------LAYVPQQ-AWIQNATV 725
Cdd:COG4133 13 GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpirdaredyrrrLAYLGHAdGLKPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 726 RDNILF-----GQTYDRKRYNKVIDACALRADIDILSAgdlteigekgiNLSGGQKQRISLARAVYSDADLYLLDDPLSA 800
Cdd:COG4133 93 RENLRFwaalyGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170
....*....|....
gi 45552357 801 VDAHvGKHIFEEVI 814
Cdd:COG4133 162 LDAA-GVALLAELI 174
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
650-860 |
1.95e-17 |
|
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: 83.32 E-value: 1.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 650 SIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG----------------KLAY 713
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglseaelyrlrrRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 714 VPQQawiqNA-----TVRDNILF--------GQTYDRKRYNKVIDACALRADIDILSAgdlteigekgiNLSGGQKQRIS 780
Cdd:cd03261 82 LFQS----GAlfdslTVFENVAFplrehtrlSEEEIREIVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 781 LARAVYSDADLYLLDDPLSAVDAhVGKHIFEEVIgpkgilaRKSR-------VLVTHGVTFLPQV-DSIYVIKMGEISES 852
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDP-IASGVIDDLI-------RSLKkelgltsIMVTHDLDTAFAIaDRIAVLYDGKIVAE 218
|
....*...
gi 45552357 853 GTFDQLVK 860
Cdd:cd03261 219 GTPEELRA 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1324-1533 |
2.01e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 84.37 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1324 LVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMG-LHMLRSRLTIIPQDP--------- 1393
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQNPdnqivativ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1394 ---VLFsGSLRINLDPFEIKTD-DEIWKALELSHLKSFVKSLaaglnheiaeggenLSVGQRQLVCLARALLRKTKVLVL 1469
Cdd:PRK13633 104 eedVAF-GPENLGIPPEEIRERvDESLKKVGMYEYRRHAPHL--------------LSGGQKQRVAIAGILAMRPECIIF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552357 1470 DEATAAVDLETDDLIQKTIRTEFKE--CTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLDN 1533
Cdd:PRK13633 169 DEPTAMLDPSGRREVVNTIKELNKKygITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1311-1524 |
2.43e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.43 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1311 FQNFQVRYreGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSltlaLFRII----EAAGGRISID-GVDIASMglhmlrsr 1385
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKST----LLKILagelEPDSGEVSIPkGLRIGYL-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1386 ltiiPQDPVLFSG---------------SLRINLDPFEIKTDDEIWKALELSHL------------KSFVKSLAAGLNHE 1438
Cdd:COG0488 67 ----PQEPPLDDDltvldtvldgdaelrALEAELEELEAKLAEPDEDLERLAELqeefealggweaEARAEEILSGLGFP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1439 IAEGG---ENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEfkECTVLTIAH-R--LNTIldSDK 1512
Cdd:COG0488 143 EEDLDrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNY--PGTVLVVSHdRyfLDRV--ATR 218
|
250
....*....|..
gi 45552357 1513 VIVLDKGQIIEF 1524
Cdd:COG0488 219 ILELDRGKLTLY 230
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
650-862 |
3.92e-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: 82.38 E-value: 3.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 650 SIENGEFSWGDEIT-LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG-------------KLAYVP 715
Cdd:COG1122 2 ELENLSFSYPGGTPaLDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknlrelrrKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 716 QQAWIQ--NATVRDNILFG---QTYDRKRynkvIDAcalRADiDILSAGDLTEIGEKGI-NLSGGQKQRISLARAVYSDA 789
Cdd:COG1122 82 QNPDDQlfAPTVEEDVAFGpenLGLPREE----IRE---RVE-EALELVGLEHLADRPPhELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 790 DLYLLDDPLSAVDAHVGKHIFEevigpkgILAR-----KSRVLVTHGVTFLPQV-DSIYVIKMGEISESGTFDQLVKNK 862
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLE-------LLKRlnkegKTVIIVTHDLDLVAELaDRVIVLDDGRIVADGTPREVFSDY 225
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1325-1536 |
3.93e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.17 E-value: 3.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGV------DIASMGLHMLRSRLTIIPQDPVLFS- 1397
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPh 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1398 ----GSLRINLDPFEIKTDDEIWKALELSHLK-SFVKSLAAGLNHEIAEggenLSVGQRQLVCLARALLRKTKVLVLDEA 1472
Cdd:PRK14246 105 lsiyDNIAYPLKSHGIKEKREIKKIVEECLRKvGLWKEVYDRLNSPASQ----LSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 1473 TAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNPKS 1536
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
650-861 |
4.03e-17 |
|
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: 82.73 E-value: 4.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 650 SIENGEFSWGD-EITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG-------------KLAYVP 715
Cdd:cd03295 2 EFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 716 QQAWI-QNATVRDNI-----LFGqtYDRKRYNKvidacalRADiDILSAGDLTEIGEKG---INLSGGQKQRISLARAVY 786
Cdd:cd03295 82 QQIGLfPHMTVEENIalvpkLLK--WPKEKIRE-------RAD-ELLALVGLDPAEFADrypHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552357 787 SDADLYLLDDPLSAVDAHVGKHIFEEVIGPKGILaRKSRVLVTHGV-TFLPQVDSIYVIKMGEISESGTFDQLVKN 861
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQEL-GKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
650-849 |
4.06e-17 |
|
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: 80.52 E-value: 4.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 650 SIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVV------------NTVGKLAYVPQQ 717
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIkvlgkdikkepeEVKRRIGYLPEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 718 A-WIQNATVRDNIlfgqtydrkrynkvidacalradidilsagdlteigekgiNLSGGQKQRISLARAVYSDADLYLLDD 796
Cdd:cd03230 82 PsLYENLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 797 PLSAVDAhVGKHIFEEVIgpKGILAR-KSRVLVTHGVTFLPQV-DSIYVIKMGEI 849
Cdd:cd03230 122 PTSGLDP-ESRREFWELL--RELKKEgKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1309-1536 |
5.23e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 82.06 E-value: 5.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYreGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDI--ASMGLHMLR--- 1383
Cdd:PRK09493 2 IEFKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRqea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1384 ----SRLTIIPQ----DPVLFsGSLRINldpfEIKTDDEIWKALELshLKSFvkSLAAGLNHEIAEggenLSVGQRQLVC 1455
Cdd:PRK09493 80 gmvfQQFYLFPHltalENVMF-GPLRVR----GASKEEAEKQAREL--LAKV--GLAERAHHYPSE----LSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1456 LARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKE-CTVLTIAHRLNTildSDKV----IVLDKGQIIEFASPTEL 1530
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGF---AEKVasrlIFIDKGRIAEDGDPQVL 223
|
....*.
gi 45552357 1531 LDNPKS 1536
Cdd:PRK09493 224 IKNPPS 229
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1309-1531 |
6.27e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.83 E-value: 6.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLDL-VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLT 1387
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1388 IIPQDP------VLFSGSLRINLD----PFE--IKTDDEIWKALELSHLKSfvkslaaglnHEIAEggenLSVGQRQLVC 1455
Cdd:PRK13642 85 MVFQNPdnqfvgATVEDDVAFGMEnqgiPREemIKRVDEALLAVNMLDFKT----------REPAR----LSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 1456 LARALLRKTKVLVLDEATAAVDLETDDLIQKTIRtEFKE---CTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELL 1531
Cdd:PRK13642 151 VAGIIALRPEIIILDESTSMLDPTGRQEIMRVIH-EIKEkyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
649-858 |
6.44e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 84.37 E-value: 6.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 649 MSIE--NGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK-----------LAYVP 715
Cdd:PRK10851 1 MSIEiaNIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 716 QQ-AWIQNATVRDNILFGQTY--DRKRYNK-VIDACALRadidILSAGDLTEIGEK-GINLSGGQKQRISLARAVYSDAD 790
Cdd:PRK10851 81 QHyALFRHMTVFDNIAFGLTVlpRRERPNAaAIKAKVTQ----LLEMVQLAHLADRyPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552357 791 LYLLDDPLSAVDAHVGK-------HIFEEVigpkgilaRKSRVLVTHGVTFLPQV-DSIYVIKMGEISESGTFDQL 858
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKelrrwlrQLHEEL--------KFTSVFVTHDQEEAMEVaDRVVVMSQGNIEQAGTPDQV 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1325-1538 |
7.55e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.89 E-value: 7.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPvlfsgSLRINl 1404
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDT-----SLSFE- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1405 dpFEIKTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGG---------ENLSVGQRQLVCLARALLRKTKVLVLDEATAA 1475
Cdd:PRK09536 92 --FDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGvaqfadrpvTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1476 VDL----ETDDLIQKTIRTEFkecTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNP--KSAF 1538
Cdd:PRK09536 170 LDInhqvRTLELVRRLVDDGK---TAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLTADtlRAAF 236
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
649-858 |
9.27e-17 |
|
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: 81.62 E-value: 9.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 649 MSIE--NGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLA-----------YVP 715
Cdd:cd03296 1 MSIEvrNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAtdvpvqernvgFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 716 QQ-AWIQNATVRDNILFGQTYDRKRYNKVIDACALRADiDILSAGDLTEIGEKGIN-LSGGQKQRISLARAVYSDADLYL 793
Cdd:cd03296 81 QHyALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVH-ELLKLVQLDWLADRYPAqLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45552357 794 LDDPLSAVDAHVGKHIfeevigpKGILAR------KSRVLVTHGVTFLPQV-DSIYVIKMGEISESGTFDQL 858
Cdd:cd03296 160 LDEPFGALDAKVRKEL-------RRWLRRlhdelhVTTVFVTHDQEEALEVaDRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1322-1521 |
1.11e-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: 79.40 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1322 LDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLH-MLRSRLTIIPQDP----VLF 1396
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdAIRAGIAYVPEDRkregLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1397 SGSLRINldpfeiktddeiwkaLELSHLksfvkslaaglnheiaeggenLSVGQRQLVCLARALLRKTKVLVLDEATAAV 1476
Cdd:cd03215 92 DLSVAEN---------------IALSSL---------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 45552357 1477 DLETDDLIQKTIRtEFKE--CTVLTIAHRLNTILD-SDKVIVLDKGQI 1521
Cdd:cd03215 136 DVGAKAEIYRLIR-ELADagKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
649-863 |
1.21e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 85.54 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 649 MSIENGEFSW-GDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK-------------LAYV 714
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplsslshsvlrqgVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 715 PQQAWIQNATVRDNILFGQTYDRKRYNKVIDACALRADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLL 794
Cdd:PRK10790 421 QQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILIL 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45552357 795 DDPLSAVDAHVgkhifEEVIGPKGILARKSRVLV--THGVTFLPQVDSIYVIKMGEISESGTFDQLVKNKG 863
Cdd:PRK10790 501 DEATANIDSGT-----EQAIQQALAAVREHTTLVviAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQG 566
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1310-1529 |
1.26e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.14 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1310 EFQNFQVRY--REGL-------DLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIeAAGGRISIDGvdiasMGLH 1380
Cdd:PRK15134 277 DVEQLQVAFpiRKGIlkrtvdhNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDG-----QPLH 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1381 ------ML--RSRLTIIPQDPvlfSGSLRINLDPFEIktddeIWKALELSHlksfvKSLAAGLNHE-----IAEGG---- 1443
Cdd:PRK15134 351 nlnrrqLLpvRHRIQVVFQDP---NSSLNPRLNVLQI-----IEEGLRVHQ-----PTLSAAQREQqviavMEEVGldpe 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1444 ------ENLSVGQRQLVCLARALLRKTKVLVLDEATAAVdletDDLIQKTIRTEFKEctvLTIAHRLNTILDS------- 1510
Cdd:PRK15134 418 trhrypAEFSGGQRQRIAIARALILKPSLIILDEPTSSL----DKTVQAQILALLKS---LQQKHQLAYLFIShdlhvvr 490
|
250 260
....*....|....*....|....*....
gi 45552357 1511 ---DKVIVLDKGQIIE-------FASPTE 1529
Cdd:PRK15134 491 alcHQVIVLRQGEVVEqgdcervFAAPQQ 519
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1326-1529 |
1.34e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 84.69 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1326 LRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDG--VDIAS------MGLHMlrsrltiIPQDPVLFs 1397
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSprdaiaLGIGM-------VHQHFMLV- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1398 gslrinlDPFeikTddeiwkALE-----LSHLKSFVKSLAAgLNHEIAEGGE-------------NLSVGQRQLVCLARA 1459
Cdd:COG3845 93 -------PNL---T------VAEnivlgLEPTKGGRLDRKA-ARARIRELSErygldvdpdakveDLSVGEQQRVEILKA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 1460 LLRKTKVLVLDEATaAV--DLETDDLIqKTIRtEFKE--CTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTE 1529
Cdd:COG3845 156 LYRGARILILDEPT-AVltPQEADELF-EILR-RLAAegKSIIFITHKLREVMAiADRVTVLRRGKVVGTVDTAE 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1315-1538 |
1.70e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.54 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1315 QVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMG-----------LHMLR 1383
Cdd:PRK10070 33 QILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelrevrrkkIAMVF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1384 SRLTIIPQDPVLFSGSLRINLDPFEIKTDDEiwKALELSHlksfvkslAAGLNHEIAEGGENLSVGQRQLVCLARALLRK 1463
Cdd:PRK10070 113 QSFALMPHMTVLDNTAFGMELAGINAEERRE--KALDALR--------QVGLENYAHSYPDELSGGMRQRVGLARALAIN 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 1464 TKVLVLDEATAAVD-LETDDLIQKTIRTEFK-ECTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNPKSAF 1538
Cdd:PRK10070 183 PDILLMDEAFSALDpLIRTEMQDELVKLQAKhQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
664-851 |
2.43e-16 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 79.70 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAfLGEMEK-------LAGV-VNTVG----------KLAYVPQQA-WIQNAT 724
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNI-LGGLDRptsgevlIDGQdISSLSerelarlrrrHIGFVFQFFnLLPELT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 725 VRDNILFGQTYDRKRYNKVIDacalRADiDILSAGDLTEIGEKGIN-LSGGQKQRISLARAVYSDADLYLLDDPLSAVDA 803
Cdd:COG1136 103 ALENVALPLLLAGVSRKERRE----RAR-ELLERVGLGDRLDHRPSqLSGGQQQRVAIARALVNRPKLILADEPTGNLDS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 45552357 804 HVGKHIFEevigpkgILARKSR------VLVTHGVTFLPQVDSIYVIKMGEISE 851
Cdd:COG1136 178 KTGEEVLE-------LLRELNRelgttiVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1325-1533 |
2.51e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 80.32 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMlRSRLTI--IPQDPVLFSG-SLR 1401
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA-RARRGIgyLPQEASIFRRlSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1402 INLDP-FEIKTD----------DEIWKALELSHLKSFVkslaaglnheiaegGENLSVGQRQLVCLARALLRKTKVLVLD 1470
Cdd:PRK10895 97 DNLMAvLQIRDDlsaeqredraNELMEEFHIEHLRDSM--------------GQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 1471 EATAAVDLETDDLIQKTIR-TEFKECTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDN 1533
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEhLRDSGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
664-867 |
3.25e-16 |
|
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: 84.10 E-value: 3.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSsvvqaflgemeklagvvnTVGKLAY------------------------------ 713
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKS------------------TLARLLFrfydvtsgrilidgqdirdvtqaslraaig 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 714 -VPQQAWIQNATVRDNILFGQT-YDRKRYNKVIDACALRADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADL 791
Cdd:COG5265 436 iVPQDTVLFNDTIAYNIAYGRPdASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPI 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 792 YLLDDPLSAVDAHVGKHIFEEvigpkgiLARKSR---VLV-THGVTFLPQVDSIYVIKMGEISESGTFDQLVKNKGAFAD 867
Cdd:COG5265 516 LIFDEATSALDSRTERAIQAA-------LREVARgrtTLViAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQ 588
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1325-1524 |
4.11e-16 |
|
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: 79.11 E-value: 4.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHM-LRSRLTIIpqDPVLFSGSLRiN 1403
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGGgFNPELTGR--ENIYLNGRLL-G 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1404 LDPFEIKT-DDEIWkalELSHLKSF----VKslaaglnheiaeggeNLSVGQRQLVCLARALLRKTKVLVLDEATAAVDL 1478
Cdd:cd03220 114 LSRKEIDEkIDEII---EFSELGDFidlpVK---------------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 45552357 1479 ETDDLIQKTIRTEFKEC-TVLTIAHRLNTILD-SDKVIVLDKGQIIEF 1524
Cdd:cd03220 176 AFQEKCQRRLRELLKQGkTVILVSHDPSSIKRlCDRALVLEKGKIRFD 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1312-1531 |
4.68e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 79.67 E-value: 4.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1312 QNFQVRYreGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQ 1391
Cdd:PRK11231 6 ENLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1392 DPVLFSG-SLR----INLDPF-----EIKTDDE--IWKALELSHLKSFVKSLAaglnheiaeggENLSVGQRQLVCLARA 1459
Cdd:PRK11231 84 HHLTPEGiTVRelvaYGRSPWlslwgRLSAEDNarVNQAMEQTRINHLADRRL-----------TDLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 1460 LLRKTKVLVLDEATAAVDL----ETDDLIQKtIRTEFKecTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELL 1531
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDInhqvELMRLMRE-LNTQGK--TVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVM 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1325-1535 |
4.93e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 79.30 E-value: 4.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLtlalFRII----EAAGGRISIDGVDIASMGLHMlRSRLTI--IPQDPVLFSG 1398
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTT----FYMIvglvKPDSGRIFLDGEDITHLPMHK-RARLGIgyLPQEASIFRK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1399 -----SLRI-----NLDPFEIKTD-DEIWKALELSHLKsfvKSLAAGLNheiaeGGEnlsvgqRQLVCLARALLRKTKVL 1467
Cdd:COG1137 93 ltvedNILAvlelrKLSKKEREERlEELLEEFGITHLR---KSKAYSLS-----GGE------RRRVEIARALATNPKFI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45552357 1468 VLDEATAAVD-LETDDlIQKTIRtEFKE--CTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNPK 1535
Cdd:COG1137 159 LLDEPFAGVDpIAVAD-IQKIIR-HLKErgIGVLITDHNVRETLGiCDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1310-1535 |
5.00e-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: 5.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1310 EFQNFQVRYR--EGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRI----IEAAGGRISIDGVDIASMGLHMLR 1383
Cdd:COG4172 8 SVEDLSVAFGqgGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLLGLSERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1384 ----SRLTIIPQDPV-----LFS-G-----SLRI--NLDPFEIKTddeiwKALEL----------SHLKSFvkslaaglN 1436
Cdd:COG4172 88 rirgNRIAMIFQEPMtslnpLHTiGkqiaeVLRLhrGLSGAAARA-----RALELlervgipdpeRRLDAY--------P 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1437 HEiaeggenLSVGQRQLVCLARALLRKTKVLVLDEATAAVD-------LetdDLIqKTIRTEFKeCTVLTIAHRLNTILD 1509
Cdd:COG4172 155 HQ-------LSGGQRQRVMIAMALANEPDLLIADEPTTALDvtvqaqiL---DLL-KDLQRELG-MALLLITHDLGVVRR 222
|
250 260
....*....|....*....|....*..
gi 45552357 1510 -SDKVIVLDKGQIIEFASPTELLDNPK 1535
Cdd:COG4172 223 fADRVAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1328-1535 |
6.15e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 80.91 E-value: 6.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1328 GVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMG---LHMLRSRLTIIPQDPvLFSGSLRINL 1404
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddeWRAVRSDIQMIFQDP-LASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1405 dpfeiktDDEIWKALELSH-------LKSFVKSLAA--GL-----N---HEiaeggenLSVGQRQLVCLARALLRKTKVL 1467
Cdd:PRK15079 118 -------GEIIAEPLRTYHpklsrqeVKDRVKAMMLkvGLlpnliNrypHE-------FSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 1468 VLDEATAAVDLEtddlIQKTIRTEFKEC------TVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNPK 1535
Cdd:PRK15079 184 ICDEPVSALDVS----IQAQVVNLLQQLqremglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1309-1524 |
8.63e-16 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 78.00 E-value: 8.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLdlVLRGVSFNIQGGeKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHmLRSRLTI 1388
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1389 IPQDPVLFSG-SLRINLDPFEI-------KTDDEIWKALELSHLKSFVKSLAAGLnheiaeggenlSVGQRQLVCLARAL 1460
Cdd:cd03264 77 LPQEFGVYPNfTVREFLDYIAWlkgipskEVKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45552357 1461 LRKTKVLVLDEATAAVDLETddliqktiRTEF--------KECTVLTIAHRLNTILDS-DKVIVLDKGQIIEF 1524
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEE--------RIRFrnllselgEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFE 210
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1309-1535 |
1.12e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 79.01 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLDlVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTI 1388
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1389 IPQDP--VLFS---------GSLRINLDPFEIKTDDEiwKALELSHLKSFVKslaaglnheiaEGGENLSVGQRQLVCLA 1457
Cdd:PRK13647 84 VFQDPddQVFSstvwddvafGPVNMGLDKDEVERRVE--EALKAVRMWDFRD-----------KPPYHLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1458 RALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIA-HRLNTILD-SDKVIVLDKGQIIEFASPtELLDNPK 1535
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDK-SLLTDED 229
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
664-853 |
1.22e-15 |
|
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: 77.93 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK----------------LAYVPQQAwiQNA---- 723
Cdd:cd03257 21 LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllklsrrlrkirrkeIQMVFQDP--MSSlnpr 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 724 -TVRDNILFGQtydRKRYNKVIDACALRADIDILSAGDLTE--IGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSA 800
Cdd:cd03257 99 mTIGEQIAEPL---RIHGKLSKKEARKEAVLLLLVGVGLPEevLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 801 VDAHVGKHIFEevigpkgILAR------KSRVLVTHGVTFLPQV-DSIYVIKMGEISESG 853
Cdd:cd03257 176 LDVSVQAQILD-------LLKKlqeelgLTLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1321-1490 |
2.26e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.45 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1321 GLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIasmGLHMLRSRLTII-PQD---PVLf 1396
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHYLgHRNamkPAL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1397 sgSLRINLdpfeiktddEIWKALELSHLKSFVKSLAA-GLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAA 1475
Cdd:PRK13539 89 --TVAENL---------EFWAAFLGGEELDIAAALEAvGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170
....*....|....*
gi 45552357 1476 VDLETDDLIQKTIRT 1490
Cdd:PRK13539 158 LDAAAVALFAELIRA 172
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1328-1531 |
2.37e-15 |
|
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: 81.00 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1328 GVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGG----RISIDGVDIASMG----------LHMLRSRLTIIPQDP 1393
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevnvRVGDEWVDMTKPGpdgrgrakryIGILHQEYDLYPHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1394 VLFSGSLRINLD-PFeiktddeiwkalELSHLKSFVKSLAAGLNHEIAEG-----GENLSVGQRQLVCLARALLRKTKVL 1467
Cdd:TIGR03269 382 VLDNLTEAIGLElPD------------ELARMKAVITLKMVGFDEEKAEEildkyPDELSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 1468 VLDEATAAVDLETDDLIQKTI---RTEFKEcTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELL 1531
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSIlkaREEMEQ-TFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
651-848 |
2.96e-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: 75.30 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 651 IENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAG-------VVNTVG--------KLAYVP 715
Cdd:cd03229 3 LKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGsilidgeDLTDLEdelpplrrRIGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 716 QQ-AWIQNATVRDNILFGqtydrkrynkvidacalradidilsagdlteigekginLSGGQKQRISLARAVYSDADLYLL 794
Cdd:cd03229 83 QDfALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 795 DDPLSAVDAHVGKHIFEEVigpKGILAR--KSRVLVTHGVTFLPQV-DSIYVIKMGE 848
Cdd:cd03229 125 DEPTSALDPITRREVRALL---KSLQAQlgITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1325-1534 |
3.47e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 77.38 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAG-----GRISIDGVDIAS--MGLHMLRSRLTIIPQDPVLFS 1397
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYErrVNLNRLRRQVSMVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1398 GSLRINL---------DPfEIKTDDEIWKALELSHLKSFVKslaaglnHEIAEGGENLSVGQRQLVCLARALLRKTKVLV 1468
Cdd:PRK14258 102 MSVYDNVaygvkivgwRP-KLEIDDIVESALKDADLWDEIK-------HKIHKSALDLSGGQQQRLCIARALAVKPKVLL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 1469 LDEATAAVD----LETDDLIQK-TIRTEFkecTVLTIAHRLNTILDSDKVIVLDKG------QIIEFASPTELLDNP 1534
Cdd:PRK14258 174 MDEPCFGLDpiasMKVESLIQSlRLRSEL---TMVIVSHNLHQVSRLSDFTAFFKGnenrigQLVEFGLTKKIFNSP 247
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
650-869 |
5.13e-15 |
|
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: 76.12 E-value: 5.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 650 SIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK-LAYVP----------QQ- 717
Cdd:cd03300 2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKdITNLPphkrpvntvfQNy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 718 AWIQNATVRDNILFGQTYdRKRYNKVIDACALRAdidiLSAGDLTEIGEKGIN-LSGGQKQRISLARAVYSDADLYLLDD 796
Cdd:cd03300 82 ALFPHLTVFENIAFGLRL-KKLPKAEIKERVAEA----LDLVQLEGYANRKPSqLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 797 PLSAVDAHVGKHIFEEvigpkgiLARKSRVLvthGVTF----------LPQVDSIYVIKMGEISESGTFDQLVKN-KGAF 865
Cdd:cd03300 157 PLGALDLKLRKDMQLE-------LKRLQKEL---GITFvfvthdqeeaLTMSDRIAVMNKGKIQQIGTPEEIYEEpANRF 226
|
....*
gi 45552357 866 -ADFI 869
Cdd:cd03300 227 vADFI 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
664-858 |
5.49e-15 |
|
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: 75.93 E-value: 5.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK--------------LAYVPQ-QAWIQNATVRDN 728
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEgRRIFPELTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 729 ILFGqTYDRKRynkvidaCALRADIDILSA--GDLTEI-GEKGINLSGGQKQRISLARAVYSDADLYLLDDP---LSAVd 802
Cdd:cd03224 96 LLLG-AYARRR-------AKRKARLERVYElfPRLKERrKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPsegLAPK- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 803 ahVGKHIFEEVIGpkgiLARK--SRVLVTHGVTFLPQV-DSIYVIKMGEISESGTFDQL 858
Cdd:cd03224 167 --IVEEIFEAIRE----LRDEgvTILLVEQNARFALEIaDRAYVLERGRVVLEGTAAEL 219
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1309-1535 |
5.73e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 77.18 E-value: 5.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLDLVLRG---VSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDI----ASMGLHM 1381
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGldnISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1382 LRSRLTIIPQDP--VLFSGSL--RINLDPFEIKTDDEIWKALELSHLKSfvkslaAGLNHEIAEGGE-NLSVGQRQLVCL 1456
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTVlkDVEFGPKNFGFSEDEAKEKALKWLKK------VGLSEDLISKSPfELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1457 ARALLRKTKVLVLDEATAAVDLETddliQKTIRTEFKEC-----TVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTEL 1530
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEG----RKEMMQLFKDYqkaghTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEI 232
|
....*
gi 45552357 1531 LDNPK 1535
Cdd:PRK13641 233 FSDKE 237
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
664-862 |
6.61e-15 |
|
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: 75.66 E-value: 6.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSS-------VVQAFLGE------------MEKLAGVvntvgKLAYVPQQAWI-QNA 723
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTtfymivgLVKPDSGKilldgqditklpMHKRARL-----GIGYLPQEASIfRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 724 TVRDNI---LFGQTYDRKRYNKVIDAcalradidILSAGDLTEI-GEKGINLSGGQKQRISLARAVYSDADLYLLDDPLS 799
Cdd:cd03218 91 TVEENIlavLEIRGLSKKEREEKLEE--------LLEEFHITHLrKSKASSLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 800 AVDAHVGKHIfeevigpKGILAR-KSR---VLVT-HGV--TfLPQVDSIYVIKMGEISESGTFDQLVKNK 862
Cdd:cd03218 163 GVDPIAVQDI-------QKIIKIlKDRgigVLITdHNVreT-LSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
650-830 |
7.22e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 77.83 E-value: 7.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 650 SIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQA---FL----GEMEkLAG-VVNTV--GK--LAYVPQQ 717
Cdd:COG3842 7 ELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMiagFEtpdsGRIL-LDGrDVTGLppEKrnVGMVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 718 AwiqnA-----TVRDNILFGQTYdRKRYNKVIDAcalRADiDILSAGDLTEIGEKGIN-LSGGQKQRISLARAVYSDADL 791
Cdd:COG3842 86 Y----AlfphlTVAENVAFGLRM-RGVPKAEIRA---RVA-ELLELVGLEGLADRYPHqLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 45552357 792 YLLDDPLSAVDAHVGKHIFEEVigpKGILAR--KSRVLVTH 830
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREEL---RRLQRElgITFIYVTH 194
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
673-805 |
7.22e-15 |
|
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: 75.41 E-value: 7.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 673 KGSLVALVGTVGSGKSSVVQAFLGeMEKLAG---VVNTV---------------GKLAYVPQQ-AWIQNATVRDNILFGq 733
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAG-LEKPDGgtiVLNGTvlfdsrkkinlppqqRKIGLVFQQyALFPHLNVRENLAFG- 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45552357 734 tYDRKRYNKVIDacalRADiDILSAGDLTEIGEKGI-NLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHV 805
Cdd:cd03297 100 -LKRKRNREDRI----SVD-ELLDLLGLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1315-1537 |
7.33e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 76.16 E-value: 7.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1315 QVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASM-------------GLHM 1381
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1382 LRSRLTIIPQDPVLFSgslriNLDPFEIKTDDEIwKALELSHLKS---FVKSLAAGLNHEIAEGG--ENLSVGQRQLVCL 1456
Cdd:PRK10619 90 LRTRLTMVFQHFNLWS-----HMTVLENVMEAPI-QVLGLSKQEArerAVKYLAKVGIDERAQGKypVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1457 ARALLRKTKVLVLDEATAAVDLEtddLIQKTIRTEFKEC----TVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELL 1531
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPE---LVGEVLRIMQQLAeegkTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
....*.
gi 45552357 1532 DNPKSA 1537
Cdd:PRK10619 241 GNPQSP 246
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1333-1522 |
8.41e-15 |
|
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: 74.84 E-value: 8.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1333 IQGGEKVGIVGRTGAGKSSL--TLALFRIieAAGGRISIDGVDIASMglHMLRSRLTIIPQDPVLFS-----GSLRINLD 1405
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLlnLIAGFET--PQSGRVLINGVDVTAA--PPADRPVSMLFQENNLFAhltveQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1406 PfEIKTDDEIWKAlelshlksfVKSLAA--GLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVD----LE 1479
Cdd:cd03298 97 P-GLKLTAEDRQA---------IEVALArvGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 45552357 1480 TDDLIQKTIRTefKECTVLTIAHRLNTILD-SDKVIVLDKGQII 1522
Cdd:cd03298 167 MLDLVLDLHAE--TKMTVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
648-804 |
8.81e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 78.34 E-value: 8.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 648 PMSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG-------------KLAYV 714
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 715 PQQAWIQ-NATVRDNILFGQTYDRKRYN-------KVIDACALRADIDILSAGDLTEigekginLSGGQKQRISLARAVY 786
Cdd:PRK09536 83 PQDTSLSfEFDVRQVVEMGRTPHRSRFDtwtetdrAAVERAMERTGVAQFADRPVTS-------LSGGERQRVLLARALA 155
|
170
....*....|....*...
gi 45552357 787 SDADLYLLDDPLSAVDAH 804
Cdd:PRK09536 156 QATPVLLLDEPTASLDIN 173
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1315-1489 |
9.15e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 74.70 E-value: 9.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1315 QVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPV 1394
Cdd:TIGR01189 5 NLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1395 LFSGSLRINLD---PFEIKTDDEIWKALELSHLKSFVKSLAAglnheiaeggeNLSVGQRQLVCLARALLRKTKVLVLDE 1471
Cdd:TIGR01189 85 KPELSALENLHfwaAIHGGAQRTIEDALAAVGLTGFEDLPAA-----------QLSAGQQRRLALARLWLSRRPLWILDE 153
|
170
....*....|....*...
gi 45552357 1472 ATAAVDLETDDLIQKTIR 1489
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLR 171
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
664-854 |
1.20e-14 |
|
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: 74.37 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG-------------KLAYVPQQAWIQNATVRDNIl 730
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTIRSNL- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 731 fgqtydrKRYNKVidacalrADIDILSAgdlTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVgKHIF 810
Cdd:cd03369 103 -------DPFDEY-------SDEEIYGA---LRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT-DALI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 45552357 811 EEVIgpKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEISESGT 854
Cdd:cd03369 165 QKTI--REEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
664-802 |
1.35e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.69 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK----------LAYVPQQA---WIQNATVRDNIL 730
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVPQSEevdWSFPVLVEDVVM 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 731 FGQ-------TYDRKRYNKVIDACALRADidiLSAGDLTEIGEkginLSGGQKQRISLARAVYSDADLYLLDDPLSAVD 802
Cdd:PRK15056 103 MGRyghmgwlRRAKKRDRQIVTAALARVD---MVEFRHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1317-1534 |
1.94e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 75.21 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1317 RYREGL------DLVlRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIaSMGLHMLRS-RLTII 1389
Cdd:PRK15112 15 RYRTGWfrrqtvEAV-KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSYRSqRIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1390 PQDPV-----------LFSGSLRINLDPFEIKTDDEIWKALELSHLksfVKSLAAGLNHEIAEggenlsvGQRQLVCLAR 1458
Cdd:PRK15112 93 FQDPStslnprqrisqILDFPLRLNTDLEPEQREKQIIETLRQVGL---LPDHASYYPHMLAP-------GQKQRLGLAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 1459 ALLRKTKVLVLDEATAAVDLET-DDLIQKTIRTEFKE-CTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNP 1534
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMrSQLINLMLELQEKQgISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLASP 241
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1325-1530 |
2.30e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 77.92 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALF----------RII------EAAG--GRISIDGVDIASMGLHM----- 1381
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRgmdqyeptsgRIIyhvalcEKCGyvERPSKVGEPCPVCGGTLepeev 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1382 ------------LRSRLTIIPQDPVLFSGSLRI------NLDPFEIKTDDEIWKALELSHLksfvkslaAGLNHEIAEGG 1443
Cdd:TIGR03269 95 dfwnlsdklrrrIRKRIAIMLQRTFALYGDDTVldnvleALEEIGYEGKEAVGRAVDLIEM--------VQLSHRITHIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1444 ENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKE--CTVLTIAHRLNTILD-SDKVIVLDKGQ 1520
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsgISMVLTSHWPEVIEDlSDKAIWLENGE 246
|
250
....*....|
gi 45552357 1521 IIEFASPTEL 1530
Cdd:TIGR03269 247 IKEEGTPDEV 256
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1309-1535 |
2.39e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 75.11 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGlDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIA--SMGLHMLRSRL 1386
Cdd:PRK13639 2 LETRDLKYSYPDG-TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1387 TIIPQDP--VLFSGSLR--INLDPFEIKTD-DEIWKALELShLKsfvkslAAGLnheiaEGGEN-----LSVGQRQLVCL 1456
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEedVAFGPLNLGLSkEEVEKRVKEA-LK------AVGM-----EGFENkpphhLSGGQKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1457 ARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKE-CTVLTIAHRLNTI-LDSDKVIVLDKGQIIEFASPTELLDNP 1534
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEgITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
.
gi 45552357 1535 K 1535
Cdd:PRK13639 229 E 229
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1325-1532 |
2.42e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 74.35 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGvDIASM-----GLHMlrsRLTIIpqDPVLFSGS 1399
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-RVSALlelgaGFHP---ELTGR--ENIYLNGR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1400 LrINLDPFEIKT-DDEIwkaLELSHLKSF----VK------------SLAAGLNHEIaeggenlsvgqrqlvclarallr 1462
Cdd:COG1134 115 L-LGLSRKEIDEkFDEI---VEFAELGDFidqpVKtyssgmrarlafAVATAVDPDI----------------------- 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 1463 ktkvLVLDEATAAVDLEtddLIQKTIR--TEFKE--CTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLD 1532
Cdd:COG1134 168 ----LLVDEVLAVGDAA---FQKKCLAriRELREsgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1325-1531 |
2.55e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 74.72 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASM---GLHMLRSRLTIIPQDPV------- 1394
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSIsavnprk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1395 ----LFSGSLR--INLDPFEiktddEIWKALELshLKsfvkslAAGLNHEIAEG-GENLSVGQRQLVCLARALLRKTKVL 1467
Cdd:PRK10419 107 tvreIIREPLRhlLSLDKAE-----RLARASEM--LR------AVDLDDSVLDKrPPQLSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 1468 VLDEATAAVDL----ETDDLIQKtIRTEFKECTVLtIAHRLNTILD-SDKVIVLDKGQIIEFASPTELL 1531
Cdd:PRK10419 174 ILDEAVSNLDLvlqaGVIRLLKK-LQQQFGTACLF-ITHDLRLVERfCQRVMVMDNGQIVETQPVGDKL 240
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1329-1535 |
3.72e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 77.59 E-value: 3.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1329 VSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMG---LHMLRSRLTIIPQDPVlfsgslrINLD 1405
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY-------ASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1406 PFEiKTDDEIWKALELSHL---KSFVKSLA-----AGLNHEIA-EGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAV 1476
Cdd:PRK10261 416 PRQ-TVGDSIMEPLRVHGLlpgKAAAARVAwllerVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45552357 1477 DLETDDLIQKTIRTEFKECTV--LTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNPK 1535
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFENPQ 556
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1313-1545 |
4.65e-14 |
|
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: 75.52 E-value: 4.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1313 NFQVRyREGLDLVlrgVSFNIQGGEKVGIVGRTGAGKSSLtlalFRIIeaAG------GRISIDG---VDIASmGLHML- 1382
Cdd:COG4148 6 DFRLR-RGGFTLD---VDFTLPGRGVTALFGPSGSGKTTL----LRAI--AGlerpdsGRIRLGGevlQDSAR-GIFLPp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1383 -RSRLTIIPQDPVLFSG-SLRINLD-------PFEIKTD-DEIWKALELSHLksfvkslaagLNHEIAeggeNLSVGQRQ 1452
Cdd:COG4148 75 hRRRIGYVFQEARLFPHlSVRGNLLygrkrapRAERRISfDEVVELLGIGHL----------LDRRPA----TLSGGERQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1453 LVCLARALLRKTKVLVLDEATAAVDLETDDLIQ---KTIRTEFkECTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPT 1528
Cdd:COG4148 141 RVAIGRALLSSPRLLLMDEPLAALDLARKAEILpylERLRDEL-DIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLA 219
|
250
....*....|....*..
gi 45552357 1529 ELLDNPKSAFYSMAKDA 1545
Cdd:COG4148 220 EVLSRPDLLPLAGGEEA 236
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1309-1521 |
7.32e-14 |
|
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: 72.29 E-value: 7.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYreGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASM-----GLHMLR 1383
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLppkdrDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1384 SRLTIIPQ----DPVLFSGSLRiNLDPFEIKTD-DEIWKALELSHLksfvkslaagLNHEIAEggenLSVGQRQLVCLAR 1458
Cdd:cd03301 79 QNYALYPHmtvyDNIAFGLKLR-KVPKDEIDERvREVAELLQIEHL----------LDRKPKQ----LSGGQRQRVALGR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1459 ALLRKTKVLVLDEATAAVDLetddLIQKTIRTEFK------ECTVLTIAH-RLNTILDSDKVIVLDKGQI 1521
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDA----KLRVQMRAELKrlqqrlGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1325-1532 |
7.63e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.24 E-value: 7.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIA--------SMGLHMlrsrltiIPQDPVLF 1396
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCArltpakahQLGIYL-------VPQEPLLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1397 SG-SLRINLdPFEIKTddeiwKALELSHLKSFVKSLAAGLNHEIAEGgeNLSVGQRQLVCLARALLRKTKVLVLDEATAA 1475
Cdd:PRK15439 99 PNlSVKENI-LFGLPK-----RQASMQKMKQLLAALGCQLDLDSSAG--SLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 1476 VD-LETDDLIQKTIRTEFKECTVLTIAHRLNTILD-SDKVIVLDKGQIIeFASPTELLD 1532
Cdd:PRK15439 171 LTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIA-LSGKTADLS 228
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1325-1523 |
7.92e-14 |
|
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: 71.79 E-value: 7.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSL--TLALFRIIEAAGGRISIDGVDIASMGLHmLRSR--LTIIPQDPVLFSGsl 1400
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLakTIMGHPKYEVTEGEILFKGEDITDLPPE-ERARlgIFLAFQYPPEIPG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1401 rinldpfeIKTDDeiwkalelshlksFVKSLaaglnheiaegGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLET 1480
Cdd:cd03217 92 --------VKNAD-------------FLRYV-----------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 45552357 1481 DDLIQKTIRtEFKE--CTVLTIAHRLNtILD---SDKVIVLDKGQIIE 1523
Cdd:cd03217 140 LRLVAEVIN-KLREegKSVLIITHYQR-LLDyikPDRVHVLYDGRIVK 185
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1287-1530 |
8.24e-14 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 73.74 E-value: 8.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1287 QEAPWEL----EQDKNKPKNWPQEGRVEFQNFQVRYREgldlVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEA 1362
Cdd:cd03291 14 DEGFGELlekaKQENNDRKHSSDDNNLFFSNLCLVGAP----VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1363 AGGRISIDGvdiasmglhmlrsRLTIIPQDPVLFSGSLRINLdPFEIKTDDEIWKA-LELSHLKSFVKSLAAGLNHEIAE 1441
Cdd:cd03291 90 SEGKIKHSG-------------RISFSSQFSWIMPGTIKENI-IFGVSYDEYRYKSvVKACQLEEDITKFPEKDNTVLGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1442 GGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIqktirteFKEC--------TVLTIAHRLNTILDSDKV 1513
Cdd:cd03291 156 GGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI-------FESCvcklmankTRILVTSKMEHLKKADKI 228
|
250
....*....|....*..
gi 45552357 1514 IVLDKGQIIEFASPTEL 1530
Cdd:cd03291 229 LILHEGSSYFYGTFSEL 245
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1326-1535 |
8.54e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 74.23 E-value: 8.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1326 LRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIAS---MGLHMLRSRLTIIPQDPVlfsGSL-- 1400
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQKIQIVFQNPY---GSLnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1401 -----RINLDPFEIKTDdeiwkaleLSHLKSFVKSLA----AGLNHEIAEGGENL-SVGQRQLVCLARALLRKTKVLVLD 1470
Cdd:PRK11308 108 rkkvgQILEEPLLINTS--------LSAAERREKALAmmakVGLRPEHYDRYPHMfSGGQRQRIAIARALMLDPDVVVAD 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45552357 1471 EATAAVDLETD--------DLiQKTIRTEFkectvLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNPK 1535
Cdd:PRK11308 180 EPVSALDVSVQaqvlnlmmDL-QQELGLSY-----VFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNNPR 247
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1325-1535 |
1.01e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 72.86 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDI-------ASMGL-HMLRSRLTIIPQDPVLF 1396
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsQQKGLiRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1397 SGslRINLD-----PFEIK---TDDEIWKALELshlksfvksLA-AGLNheiaeGGEN-----LSVGQRQLVCLARALLR 1462
Cdd:PRK11264 98 PH--RTVLEniiegPVIVKgepKEEATARAREL---------LAkVGLA-----GKETsyprrLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 1463 KTKVLVLDEATAAVDLETDDLIQKTIRTEFKEC-TVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNPK 1535
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFADPQ 236
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1318-1530 |
1.65e-13 |
|
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: 71.63 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1318 YREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHmLRSRLTIIPQDPVLfs 1397
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIGIVFQDLSV-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1398 gslrinldpfeiktDDEI--WKALEL---------SHLKSFVKSLAAGLnhEIAEGGENL----SVGQRQLVCLARALLR 1462
Cdd:cd03265 85 --------------DDELtgWENLYIharlygvpgAERRERIDELLDFV--GLLEAADRLvktySGGMRRRLEIARSLVH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45552357 1463 KTKVLVLDEATAAVDLETDDLIQKTIRTEFKE--CTVLTIAHRLNTI-LDSDKVIVLDKGQIIEFASPTEL 1530
Cdd:cd03265 149 RPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEfgMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
662-861 |
1.92e-13 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 72.29 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 662 ITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG-----------------KLAYVPQQ-AWIQNA 723
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrelrrkKISMVFQSfALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 724 TVRDNILFG---QTYDRK-RYNKVIDAcalradidiLSAGDLTEIGEKGIN-LSGGQKQRISLARAVYSDADLYLLDDPL 798
Cdd:cd03294 118 TVLENVAFGlevQGVPRAeREERAAEA---------LELVGLEGWEHKYPDeLSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45552357 799 SAVDAHVGKHIFEEVIGpkgiLARKSR---VLVTH--------GvtflpqvDSIYVIKMGEISESGTFDQLVKN 861
Cdd:cd03294 189 SALDPLIRREMQDELLR----LQAELQktiVFITHdldealrlG-------DRIAIMKDGRLVQVGTPEEILTN 251
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
664-803 |
1.98e-13 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 72.20 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKL--------AYVPQQ----AWIqnaTVRDNILF 731
Cdd:COG4525 23 LQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVFQKdallPWL---NVLDNVAF 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45552357 732 GQtydrkRYNKVIDA-CALRADiDILSAGDLTEIGEKGI-NLSGGQKQRISLARAVYSDADLYLLDDPLSAVDA 803
Cdd:COG4525 100 GL-----RLRGVPKAeRRARAE-ELLALVGLADFARRRIwQLSGGMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1325-1522 |
2.01e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 72.83 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSltlaLFRII----EAAGGRISIDG-----VDIASMGlHM-----LRSRLTIIP 1390
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTT----TIRIIlgilAPDSGEVLWDGepldpEDRRRIG-YLpeergLYPKMKVGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1391 QdpVLFSGSLRiNLDPFEIKTDDEIW-KALELSHLKsfvkslaaglNHEIaeggENLSVGQRQLVCLARALLRKTKVLVL 1469
Cdd:COG4152 91 Q--LVYLARLK-GLSKAEAKRRADEWlERLGLGDRA----------NKKV----EELSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 1470 DEATAAVDLETDDLIQKTIRtEFKE--CTVLTIAHRLNTI--LdSDKVIVLDKGQII 1522
Cdd:COG4152 154 DEPFSGLDPVNVELLKDVIR-ELAAkgTTVIFSSHQMELVeeL-CDRIVIINKGRKV 208
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1325-1522 |
2.17e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.67 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDG--VDIAS------MGLHML---RSRLTIIPQDP 1393
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSprdairAGIAYVpedRKGEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1394 VL----------FSGSLRINldpfeiktddeiwKALELSHLKSFVKSL---AAGLNHEIAeggeNLSVGQRQLVCLARAL 1460
Cdd:COG1129 347 IRenitlasldrLSRGGLLD-------------RRRERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWL 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 1461 LRKTKVLVLDEATAAVDLETDDLIQKTIR-------------TEFKEctVLTIAHRlntildsdkVIVLDKGQII 1522
Cdd:COG1129 410 ATDPKVLILDEPTRGIDVGAKAEIYRLIRelaaegkavivisSELPE--LLGLSDR---------ILVMREGRIV 473
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1325-1522 |
2.26e-13 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 70.27 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSL--TLALFRIIEAAGGRISIDGVDIasmGLHMLRSRLTIIPQDPVLFSgslri 1402
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLlnALAGRRTGLGVSGEVLINGRPL---DKRSFRKIIGYVPQDDILHP----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1403 NLDPFEiktddeiwkALELS-HLKSfvkslaaglnheiaeggenLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETD 1481
Cdd:cd03213 96 TLTVRE---------TLMFAaKLRG-------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 45552357 1482 DLIQKTIRTEFKE-CTVLTIAHRLNTILDS--DKVIVLDKGQII 1522
Cdd:cd03213 148 LQVMSLLRRLADTgRTIICSIHQPSSEIFElfDKLLLLSQGRVI 191
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
664-860 |
2.35e-13 |
|
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: 71.76 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLAYVPQQAWI--------QNA--------TVRD 727
Cdd:COG1124 21 LKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFrrrvqmvfQDPyaslhprhTVDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 728 NI-----LFGQTYDRKRYNKVIDACALRADIdilsagdLTEIGEKginLSGGQKQRISLARAVYSDADLYLLDDPLSAVD 802
Cdd:COG1124 101 ILaeplrIHGLPDREERIAELLEQVGLPPSF-------LDRYPHQ---LSGGQRQRVAIARALILEPELLLLDEPTSALD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45552357 803 AHVGKHI---FEEVIGPKGIlarkSRVLVTHG---VTFLpqVDSIYVIKMGEISESGTFDQLVK 860
Cdd:COG1124 171 VSVQAEIlnlLKDLREERGL----TYLFVSHDlavVAHL--CDRVAVMQNGRIVEELTVADLLA 228
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1309-1532 |
2.39e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.53 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYreGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMlRSRLTI 1388
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1389 IPQdpvlFSgslriNLDP-FEIKTDDEIWK---ALELSHLKSFVKSL---AAGLNHEIAEGGEnLSVGQRQLVCLARALL 1461
Cdd:PRK13537 85 VPQ----FD-----NLDPdFTVRENLLVFGryfGLSAAAARALVPPLlefAKLENKADAKVGE-LSGGMKRRLTLARALV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 1462 RKTKVLVLDEATAAVDLETDDLIQKTIRTEFKEC-TVLTIAH------RLntildSDKVIVLDKGQIIEFASPTELLD 1532
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGkTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHALIE 227
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1310-1529 |
3.23e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 70.20 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1310 EFQNFQVRYREGLdlVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLAL-------FRiieaAGGRISIDGVDIAsmGLHML 1382
Cdd:COG4136 3 SLENLTITLGGRP--LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagtlspaFS----ASGEVLLNGRRLT--ALPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1383 RSRLTIIPQDPVLFS-----GSLRINLdPFEIKT---DDEIWKALElshlksfvkslAAGL----NHEIAEggenLSVGQ 1450
Cdd:COG4136 75 QRRIGILFQDDLLFPhlsvgENLAFAL-PPTIGRaqrRARVEQALE-----------EAGLagfaDRDPAT----LSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1451 RQLVCLARALLRKTKVLVLDEATAAVDletddliqKTIRTEFKEcTVLTIAHRLN--TIL---DSDKviVLDKGQIIEFA 1525
Cdd:COG4136 139 RARVALLRALLAEPRALLLDEPFSKLD--------AALRAQFRE-FVFEQIRQRGipALLvthDEED--APAAGRVLDLG 207
|
....
gi 45552357 1526 SPTE 1529
Cdd:COG4136 208 NWQH 211
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
992-1279 |
3.37e-13 |
|
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: 72.07 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 992 VATLVLNFVFQAFQIGSnLWLTQWANDQ-NVANDTGLRDMY-LGVYGAFGFGQVFSYIGSVVIVYLGALIgTRKIFIQLF 1069
Cdd:cd18552 2 ALAILGMILVAATTAAL-AWLLKPLLDDiFVEKDLEALLLVpLAIIGLFLLRGLASYLQTYLMAYVGQRV-VRDLRNDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1070 GNILHAPQAYFDIKPRARILDRLANDIYKLDVVLPELIRVFNSQVFRVLATIVV-ISLS---TPIFLaVIVPIAFL--YY 1143
Cdd:cd18552 80 DKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVlFYLDwklTLIAL-VVLPLAALpiRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1144 FAQRFYVATSRQLMRLESVSrspiySHFSETVTGASTIRAYNVGDRFIEESDAKVDKNQvckypsVIANRWLAIR----- 1218
Cdd:cd18552 159 IGKRLRKISRRSQESMGDLT-----SVLQETLSGIRVVKAFGAEDYEIKRFRKANERLR------RLSMKIARARalssp 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 1219 -LEMVGNL---IILFASLFAVLGGQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERI 1279
Cdd:cd18552 228 lMELLGAIaiaLVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1325-1529 |
3.49e-13 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 70.93 E-value: 3.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLtLALfriieAAG------GRISIDGVDIASM---GLHMLRSRL--------T 1387
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTL-LGL-----LAGldrptsGTVRLAGQDLFALdedARARLRARHvgfvfqsfQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1388 IIPQ----DPVLFSGSLRINLDPFEIKTDdeiwkALE---LSHLksfvkslaagLNHEIAEggenLSVGQRQLVCLARAL 1460
Cdd:COG4181 101 LLPTltalENVMLPLELAGRRDARARARA-----LLErvgLGHR----------LDHYPAQ----LSGGEQQRVALARAF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45552357 1461 LRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKE--CTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTE 1529
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNRErgTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1308-1534 |
3.59e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 72.45 E-value: 3.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1308 RVEFQNfqvryREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIeAAGGRIS----IDGVDIASM---GLH 1380
Cdd:PRK09473 19 RVTFST-----PDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIGgsatFNGREILNLpekELN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1381 MLRS-RLTIIPQDPVlfsgslrINLDPFeIKTDDEIWKALEL----SHLKSF---VKSLAA-----------GLNHEiae 1441
Cdd:PRK09473 93 KLRAeQISMIFQDPM-------TSLNPY-MRVGEQLMEVLMLhkgmSKAEAFeesVRMLDAvkmpearkrmkMYPHE--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1442 ggenLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLEtddlIQKTIRT---EFKE---CTVLTIAHRLNTILDS-DKVI 1514
Cdd:PRK09473 162 ----FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVT----VQAQIMTllnELKRefnTAIIMITHDLGVVAGIcDKVL 233
|
250 260
....*....|....*....|
gi 45552357 1515 VLDKGQIIEFASPTELLDNP 1534
Cdd:PRK09473 234 VMYAGRTMEYGNARDVFYQP 253
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
657-861 |
4.71e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 70.51 E-value: 4.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 657 SWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAfLGEMEKLAGVVNTVGKLA----------------YVPQQAWI 720
Cdd:PRK09493 10 HFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRC-INKLEEITSGDLIVDGLKvndpkvderlirqeagMVFQQFYL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 721 -QNATVRDNILFGQTYDRKrynkvidacALRADIDILSAGDLTEIG-EKGIN-----LSGGQKQRISLARAVYSDADLYL 793
Cdd:PRK09493 89 fPHLTALENVMFGPLRVRG---------ASKEEAEKQARELLAKVGlAERAHhypseLSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45552357 794 LDDPLSAVDAHVgKHifeEVIGPKGILARK--SRVLVTHGVTFLPQVDS-IYVIKMGEISESGTFDQLVKN 861
Cdd:PRK09493 160 FDEPTSALDPEL-RH---EVLKVMQDLAEEgmTMVIVTHEIGFAEKVASrLIFIDKGRIAEDGDPQVLIKN 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
650-862 |
5.46e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 71.18 E-value: 5.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 650 SIENGEFSWGDEIT--LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK------LAYVPQQAWI- 720
Cdd:PRK13632 9 KVENVSFSYPNSENnaLKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGItiskenLKEIRKKIGIi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 721 -QN-------ATVRDNILFG---QTYDRKRYNKVIDACALRADIDILsagdlteIGEKGINLSGGQKQRISLARAVYSDA 789
Cdd:PRK13632 89 fQNpdnqfigATVEDDIAFGlenKKVPPKKMKDIIDDLAKKVGMEDY-------LDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45552357 790 DLYLLDDPLSAVDAHvGKHIFEEVIGPKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEISESGTFDQLVKNK 862
Cdd:PRK13632 162 EIIIFDESTSMLDPK-GKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1329-1538 |
5.73e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 72.56 E-value: 5.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1329 VSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMG-----LHMLRSRLTIIPQDPV---LFSGSL 1400
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPpyqrpINMMFQSYALFPHMTVeqnIAFGLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1401 RINLDPFEIKtdDEIWKALELSHLKSFVKSLAaglnHEiaeggenLSVGQRQLVCLARALLRKTKVLVLDEATAAVD--- 1477
Cdd:PRK11607 118 QDKLPKAEIA--SRVNEMLGLVHMQEFAKRKP----HQ-------LSGGQRQRVALARSLAKRPKLLLLDEPMGALDkkl 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 1478 -----LETDDLIQKTIRTefkeCTVLTiaHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNPKSAF 1538
Cdd:PRK11607 185 rdrmqLEVVDILERVGVT----CVMVT--HDQEEAMTmAGRIAIMNRGKFVQIGEPEEIYEHPTTRY 245
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
650-834 |
7.07e-13 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 69.48 E-value: 7.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 650 SIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLAYVPQQAWIQ-------- 721
Cdd:cd03262 2 EIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElrqkvgmv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 722 --------NATVRDNILFGQTYDRKRYNKVIDACALRAdidilsagdLTEIG--EKG----INLSGGQKQRISLARAVYS 787
Cdd:cd03262 82 fqqfnlfpHLTVLENITLAPIKVKGMSKAEAEERALEL---------LEKVGlaDKAdaypAQLSGGQQQRVAIARALAM 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 45552357 788 DADLYLLDDPLSAVDAHVGKhifeEVIGPKGILARKSR--VLVTHGVTF 834
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVG----EVLDVMKDLAEEGMtmVVVTHEMGF 197
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
664-858 |
9.08e-13 |
|
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: 72.63 E-value: 9.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVV----NTVGKLA------------YVPQQAWIQ-NA--T 724
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIlfdgKDLTKLSrrslrelrrrvqMVFQDPYSSlNPrmT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 725 VRDNILFGQtydrkRYNKVIDACALRADI-DILSAGDLTE------IGEkginLSGGQKQRISLARAVYSDADLYLLDDP 797
Cdd:COG1123 361 VGDIIAEPL-----RLHGLLSRAERRERVaELLERVGLPPdladryPHE----LSGGQRQRVAIARALALEPKLLILDEP 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 798 LSAVDAHVGKHI---FEEvigpkgiLARKSR---VLVTHGVTFLPQV-DSIYVIKMGEISESGTFDQL 858
Cdd:COG1123 432 TSALDVSVQAQIlnlLRD-------LQRELGltyLFISHDLAVVRYIaDRVAVMYDGRIVEDGPTEEV 492
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1326-1535 |
9.38e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.97 E-value: 9.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1326 LRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDG----------VDIASMGLHMLR----SRLTIIPQ 1391
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRhvrgADMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1392 DPVlfsgslrINLDPFeIKTDDEIWKALELSHLKSFVKSLAAGLNH----EIAEGGE-------NLSVGQRQLVCLARAL 1460
Cdd:PRK10261 112 EPM-------TSLNPV-FTVGEQIAESIRLHQGASREEAMVEAKRMldqvRIPEAQTilsryphQLSGGMRQRVMIAMAL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 1461 LRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKECT--VLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNPK 1535
Cdd:PRK10261 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQIFHAPQ 261
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1316-1532 |
1.09e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 71.02 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1316 VRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGlHMLRSRLTIIPQ-DPV 1394
Cdd:PRK13536 47 VSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA-RLARARIGVVPQfDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1395 LFSGSLRINL----DPFEIKTDD---EIWKALELSHLKSFVKSLAAglnheiaeggeNLSVGQRQLVCLARALLRKTKVL 1467
Cdd:PRK13536 126 DLEFTVRENLlvfgRYFGMSTREieaVIPSLLEFARLESKADARVS-----------DLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45552357 1468 VLDEATAAVDLETDDLIQKTIRTEF-KECTVLTIAH------RLntildSDKVIVLDKGQIIEFASPTELLD 1532
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHfmeeaeRL-----CDRLCVLEAGRKIAEGRPHALID 261
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
650-849 |
1.24e-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: 68.44 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 650 SIENGEFSWGDEIT-LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLA----------YVPQQA 718
Cdd:cd03226 1 RIENISFSYKKGTEiLDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkakerrksigYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 719 WIQ--NATVRDNILFGqtydrkryNKVIDACALRADiDILSAGDLTEIGEKG-INLSGGQKQRISLARAVYSDADLYLLD 795
Cdd:cd03226 81 DYQlfTDSVREELLLG--------LKELDAGNEQAE-TVLKDLDLYALKERHpLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45552357 796 DPLSAVDAH----VGKHIfeevigpkGILAR--KSRVLVTHGVTFLPQV-DSIYVIKMGEI 849
Cdd:cd03226 152 EPTSGLDYKnmerVGELI--------RELAAqgKAVIVITHDYEFLAKVcDRVLLLANGAI 204
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
664-853 |
1.44e-12 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 68.71 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLAYVPQ-QAWIQ-NATVRDNILFGQTY---DRK 738
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGlGGGFNpELTGRENIYLNGRLlglSRK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 739 RYNKVIDACAlradidilsagDLTEIGE------KgiNLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAH----VGKH 808
Cdd:cd03220 118 EIDEKIDEII-----------EFSELGDfidlpvK--TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfqekCQRR 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 45552357 809 IFEEVIGPKGIlarksrVLVTHGVTFLPQV-DSIYVIKMGEISESG 853
Cdd:cd03220 185 LRELLKQGKTV------ILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
650-845 |
1.66e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 66.32 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 650 SIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNT--VGKLAYVPQqawiqnatvrd 727
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWgsTVKIGYFEQ----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 728 nilfgqtydrkrynkvidacalradidilsagdlteigekginLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGK 807
Cdd:cd03221 71 -------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIE 107
|
170 180 190
....*....|....*....|....*....|....*....
gi 45552357 808 HIFEEVIGPKGILarksrVLVTHGVTFLPQV-DSIYVIK 845
Cdd:cd03221 108 ALEEALKEYPGTV-----ILVSHDRYFLDQVaTKIIELE 141
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1316-1521 |
1.86e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 69.32 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1316 VRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLtLALFRIIEAAGGRISIDGvdiaSMGLHMLRSRLTIIPQDPVL 1395
Cdd:PRK11247 18 VSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTL-LRLLAGLETPSAGELLAG----TAPLAEAREDTRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1396 FSGSLRINLDPFEIKTDdeiWKALELSHLKsfvkslAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAA 1475
Cdd:PRK11247 93 LPWKKVIDNVGLGLKGQ---WRDAALQALA------AVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 45552357 1476 VD----LETDDLIQKTIRTE-FkecTVLTIAHRLN-TILDSDKVIVLDKGQI 1521
Cdd:PRK11247 164 LDaltrIEMQDLIESLWQQHgF---TVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
649-841 |
1.87e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 69.30 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 649 MSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAfLGEMEKLAGVVNTVGKLAYVPQQAWIQNATV--- 725
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNIYERRVNLnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 726 ---------RDNILFGQTYDRKRYNKVIDACALRADID-----ILSAGDL-----TEIGEKGINLSGGQKQRISLARAVY 786
Cdd:PRK14258 87 rrqvsmvhpKPNLFPMSVYDNVAYGVKIVGWRPKLEIDdivesALKDADLwdeikHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 787 SDADLYLLDDPLSAVDAHVGKHIfEEVIGPKGILARKSRVLVTHGvtfLPQVDSI 841
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKV-ESLIQSLRLRSELTMVIVSHN---LHQVSRL 217
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1309-1520 |
2.15e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 65.93 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYreGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLtlalfriieaaggrisidgvdiasmgLHMLRSRLTI 1388
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTL--------------------------LKLIAGELEP 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1389 IpqdpvlfSGSLRINldpfeiktddeiwKALELSHLksfvkslaaglnheiaeggENLSVGQRQLVCLARALLRKTKVLV 1468
Cdd:cd03221 53 D-------EGIVTWG-------------STVKIGYF-------------------EQLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 1469 LDEATAAVDLETDDLIQKTIRtEFKeCTVLTIAH-R--LNTIldSDKVIVLDKGQ 1520
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALK-EYP-GTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1309-1547 |
2.94e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.13 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYreGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLtLALFRIIEA-AGGRISIDGVDIASMGLHmlRSRLT 1387
Cdd:PRK11432 7 VVLKNITKRF--GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTV-LRLVAGLEKpTEGQIFIDGEDVTHRSIQ--QRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1388 IIPQDPVLFS----------GSLRINLDPFEIKTddEIWKALELSHLKSFVKSLAaglnheiaeggENLSVGQRQLVCLA 1457
Cdd:PRK11432 82 MVFQSYALFPhmslgenvgyGLKMLGVPKEERKQ--RVKEALELVDLAGFEDRYV-----------DQISGGQQQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1458 RALLRKTKVLVLDEATAAVDLETDDLIQKTIRtEFKE---CTVLTIAH-RLNTILDSDKVIVLDKGQIIEFASPTELLDN 1533
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIR-ELQQqfnITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
250
....*....|....*..
gi 45552357 1534 PKSAFysMAK---DANL 1547
Cdd:PRK11432 228 PASRF--MASfmgDANI 242
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1309-1535 |
3.41e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 68.33 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYreGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIE-----AAGGRISIDGVDIASMGLHML- 1382
Cdd:PRK14267 5 IETVNLRVYY--GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1383 -RSRLTIIPQDPVLF-------SGSLRINLDPFeIKTDDEIWKALELSHLKSfvkSLAAGLNHEIAEGGENLSVGQRQLV 1454
Cdd:PRK14267 83 vRREVGMVFQYPNPFphltiydNVAIGVKLNGL-VKSKKELDERVEWALKKA---ALWDEVKDRLNDYPSNLSGGQRQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1455 CLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHR-LNTILDSDKVIVLDKGQIIEFASPTELLDN 1533
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
..
gi 45552357 1534 PK 1535
Cdd:PRK14267 239 PE 240
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1326-1522 |
4.12e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 69.35 E-value: 4.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1326 LRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDI--------ASMGLHM-LRSRL--TIIPQDpv 1394
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPfkrrkefaRRIGVVFgQRSQLwwDLPAID-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1395 lfsgSLRINLDPFEIktDDEIWKA--------LELSH-LKSFVKslaaglnheiaeggeNLSVGQRQLVCLARALLRKTK 1465
Cdd:COG4586 116 ----SFRLLKAIYRI--PDAEYKKrldelvelLDLGElLDTPVR---------------QLSLGQRMRCELAAALLHRPK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1466 VLVLDEATAAVDLETDDLIQKTIRTEFKE--CTVLTIAHRLNTILD-SDKVIVLDKGQII 1522
Cdd:COG4586 175 ILFLDEPTIGLDVVSKEAIREFLKEYNRErgTTILLTSHDMDDIEAlCDRVIVIDHGRII 234
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1325-1517 |
4.19e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.83 E-value: 4.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGvdiasmglhmlRSRLTIIPQ----DPVL-FSGS 1399
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----------KLRIGYVPQklylDTTLpLTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1400 LRINLDPFEIKTDdeIWKALelshlksfvKSLAAGlnHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVD-- 1477
Cdd:PRK09544 88 RFLRLRPGTKKED--ILPAL---------KRVQAG--HLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDvn 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 45552357 1478 --LETDDLIQKtIRTEFkECTVLTIAHRLNTIL-DSDKVIVLD 1517
Cdd:PRK09544 155 gqVALYDLIDQ-LRREL-DCAVLMVSHDLHLVMaKTDEVLCLN 195
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
648-830 |
4.87e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 68.68 E-value: 4.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 648 PMSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG------------KLAYVP 715
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpsrarharqRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 716 QQAWIQ-NATVRDNIL-FGQTYD------RKRYNKVIDACALRADIDilsagdlTEIGEkginLSGGQKQRISLARAVYS 787
Cdd:PRK13537 87 QFDNLDpDFTVRENLLvFGRYFGlsaaaaRALVPPLLEFAKLENKAD-------AKVGE----LSGGMKRRLTLARALVN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 45552357 788 DADLYLLDDPLSAVDAHVGKHIFEEVigpKGILAR-KSRVLVTH 830
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERL---RSLLARgKTILLTTH 196
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
657-830 |
6.38e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 68.70 E-value: 6.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 657 SWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGklAYVPQQAWIQNA------------- 723
Cdd:PRK13536 50 SYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG--VPVPARARLARArigvvpqfdnldl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 724 --TVRDNILFGQTYDRKRYNKVIDACALRADIDILSAGDLTEIGEkginLSGGQKQRISLARAVYSDADLYLLDDPLSAV 801
Cdd:PRK13536 128 efTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190
....*....|....*....|....*....|
gi 45552357 802 DAHVGKHIFEEVigpKGILAR-KSRVLVTH 830
Cdd:PRK13536 204 DPHARHLIWERL---RSLLARgKTILLTTH 230
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
649-854 |
6.72e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 67.73 E-value: 6.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 649 MSIENGEFSWGD--EITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVnTVGKLAYVPQQAW------- 719
Cdd:PRK13635 6 IRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI-TVGGMVLSEETVWdvrrqvg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 720 --IQN-------ATVRDNILFG---QTYDRKRYNKVIDAcALRaDIDILSAGDlteigEKGINLSGGQKQRISLARAVYS 787
Cdd:PRK13635 85 mvFQNpdnqfvgATVQDDVAFGlenIGVPREEMVERVDQ-ALR-QVGMEDFLN-----REPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 788 DADLYLLDDPLSAVDAhVGKhifEEVIGPKGILARKSRVLV---THGVTFLPQVDSIYVIKMGEISESGT 854
Cdd:PRK13635 158 QPDIIILDEATSMLDP-RGR---REVLETVRQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEEGT 223
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1325-1520 |
7.23e-12 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 66.36 E-value: 7.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPVLFSGSLRINL 1404
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1405 DPF-EIKTDDEIWKALELSHLksfvkslaAGLNHEIAEggeNLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDL 1483
Cdd:cd03231 95 RFWhADHSDEQVEEALARVGL--------NGFEDRPVA---QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 45552357 1484 IQKTIR--TEFKECTVLTIAHRLNtiLDSDKVIVLDKGQ 1520
Cdd:cd03231 164 FAEAMAghCARGGMVVLTTHQDLG--LSEAGARELDLGF 200
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1336-1522 |
7.39e-12 |
|
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: 66.55 E-value: 7.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1336 GEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGV--DIASMGLHM--LRSRLTIIPQDPVLFSG-SLRINL------ 1404
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlFDSRKKINLppQQRKIGLVFQQYALFPHlNVRENLafglkr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1405 -DPFEIK-TDDEIWKALELSHLksfvkslaagLNHEIAEggenLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDD 1482
Cdd:cd03297 103 kRNREDRiSVDELLDLLGLDHL----------LNRYPAQ----LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 45552357 1483 LIQKTIRTEFKE--CTVLTIAHRLNTI-LDSDKVIVLDKGQII 1522
Cdd:cd03297 169 QLLPELKQIKKNlnIPVIFVTHDLSEAeYLADRIVVMEDGRLQ 211
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1329-1521 |
7.42e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.57 E-value: 7.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1329 VSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAA-GGRISIDG--VDIAS------MGLHML---RSRLTIIPQDPV-- 1394
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGkpVKIRNpqqaiaQGIAMVpedRKRDGIVPVMGVgk 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1395 --------LFSGSLRINlDPFEIKTDDEiwkalELSHLKsfVKSLAAGLnhEIAeggeNLSVGQRQLVCLARALLRKTKV 1466
Cdd:PRK13549 361 nitlaaldRFTGGSRID-DAAELKTILE-----SIQRLK--VKTASPEL--AIA----RLSGGNQQKAVLAKCLLLNPKI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 1467 LVLDEATAAVDLETDDLIQKTIRTEFKE-CTVLTIAHRLNTILD-SDKVIVLDKGQI 1521
Cdd:PRK13549 427 LILDEPTRGIDVGAKYEIYKLINQLVQQgVAIIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
651-797 |
7.69e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 69.71 E-value: 7.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 651 IENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVnTVG---KLAYVPQQawiQ-----N 722
Cdd:COG0488 318 LEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-KLGetvKIGYFDQH---QeeldpD 393
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 723 ATVRDNIlfGQTYDRKRYNKVIDACAlradiDILSAGD--LTEIGekgiNLSGGQKQRISLARAVYSDADLYLLDDP 797
Cdd:COG0488 394 KTVLDEL--RDGAPGGTEQEVRGYLG-----RFLFSGDdaFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
988-1279 |
7.88e-12 |
|
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: 67.80 E-value: 7.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 988 IFLSVATLVLNFVFQAFQIgsnlWLTQWANDQNVANDTGLRDM---YLGVY-GAFGFGQVFSYIGSVVIVYLGALIgTRK 1063
Cdd:cd18544 1 FILALLLLLLATALELLGP----LLIKRAIDDYIVPGQGDLQGlllLALLYlGLLLLSFLLQYLQTYLLQKLGQRI-IYD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1064 IFIQLFGNILHAPQAYFDIKPRARILDRLANDIYKLDvvlpELIRVFNSQVFRVLATIVVI-----SLS---TPIFLAVI 1135
Cdd:cd18544 76 LRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALN----ELFTSGLVTLIGDLLLLIGIliamfLLNwrlALISLLVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1136 VPIAFLYYFAQRFyvatSRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVIANRWL 1215
Cdd:cd18544 152 PLLLLATYLFRKK----SRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALF 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 1216 AIRLEMVGNLIIlfASLFAVLGGQTNPGLVGLSVSYA-LQVTQTLNWLVRMSSD----IETNIVSVERI 1279
Cdd:cd18544 228 RPLVELLSSLAL--ALVLWYGGGQVLSGAVTLGVLYAfIQYIQRFFRPIRDLAEkfniLQSAMASAERI 294
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
649-830 |
9.65e-12 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 66.15 E-value: 9.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 649 MSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK---------LAYVPQQAW 719
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarnrIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 720 I-QNATVRDNIL-FGQTYDRKRYnkviDAcalRADID-ILSAGDLTEIGEKGIN-LSGGQKQRISLARAVYSDADLYLLD 795
Cdd:cd03269 81 LyPKMKVIDQLVyLAQLKGLKKE----EA---RRRIDeWLERLELSEYANKRVEeLSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 45552357 796 DPLSAVDAhVGKHIFEEVIGPkgiLARKSR--VLVTH 830
Cdd:cd03269 154 EPFSGLDP-VNVELLKDVIRE---LARAGKtvILSTH 186
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1330-1537 |
9.79e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.53 E-value: 9.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1330 SFNIQGGEKVGIVGRTGAGKSSLtLALFR-IIEAAGGRISIDGVDiasmglHmlrsRLTIIPQDPV--------LFSG-S 1399
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTL-LNLIAgFLTPASGSLTLNGQD------H----TTTPPSRRPVsmlfqennLFSHlT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1400 LRIN----LDPfeiktddeiwkALELSHL-KSFVKSLAA--GLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEA 1472
Cdd:PRK10771 88 VAQNiglgLNP-----------GLKLNAAqREKLHAIARqmGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45552357 1473 TAAVD----LETDDLIQKTIRTefKECTVLTIAHRLNtilDSDKV----IVLDKGQIIEFASPTELLDNPKSA 1537
Cdd:PRK10771 157 FSALDpalrQEMLTLVSQVCQE--RQLTLLMVSHSLE---DAARIaprsLVVADGRIAWDGPTDELLSGKASA 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1325-1516 |
9.81e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 65.72 E-value: 9.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDG---------------------VDIASMGLHMLR 1383
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgarvayvpqrsevpdslpltvRDLVAMGRWARR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1384 srltiipqdpvlfsGSLRinldpfEIKTDD--EIWKALELSHLKSFVK-SLAAglnheiaeggenLSVGQRQLVCLARAL 1460
Cdd:NF040873 87 --------------GLWR------RLTRDDraAVDDALERVGLADLAGrQLGE------------LSGGQRQRALLAQGL 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 1461 LRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKE-CTVLTIAHRLNTILDSDKVIVL 1516
Cdd:NF040873 135 AQEADLLLLDEPTTGLDAESRERIIALLAEEHARgATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1326-1535 |
1.17e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 66.72 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1326 LRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIE-----AAGGRISIDGVDIASMGLHM--LRSRLTIIPQDPVLFSG 1398
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1399 S--------LRINLDPFEIKTDDEIWKALELSHLKSFVKSLAaglnHEIAEGgenLSVGQRQLVCLARALLRKTKVLVLD 1470
Cdd:PRK14239 101 SiyenvvygLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRL----HDSALG---LSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552357 1471 EATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNPK 1535
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
659-814 |
1.25e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.67 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 659 GDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK----LAYVPQQAWI--QNA-----TVRD 727
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiddPDVAEACHYLghRNAmkpalTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 728 NILFGQTYdRKRYNKVIDACalradIDILSAGDLTEIgeKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHvGK 807
Cdd:PRK13539 93 NLEFWAAF-LGGEELDIAAA-----LEAVGLAPLAHL--PFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AV 163
|
....*..
gi 45552357 808 HIFEEVI 814
Cdd:PRK13539 164 ALFAELI 170
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
664-832 |
1.26e-11 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 66.34 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLAYVP---QQAWIQN------ATVRDNILFGQT 734
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpdRMVVFQNysllpwLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 735 YDRKRYNKVIDACALRADIDILSagdLTEIGEKGIN-LSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEV 813
Cdd:TIGR01184 81 RVLPDLSKSERRAIVEEHIALVG---LTEAADKRPGqLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180
....*....|....*....|.
gi 45552357 814 IgpkGIL--ARKSRVLVTHGV 832
Cdd:TIGR01184 158 M---QIWeeHRVTVLMVTHDV 175
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
648-803 |
1.29e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 66.62 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 648 PMSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLG-----EMEKLAGvvntvgklayvpqQAWIQN 722
Cdd:PRK11247 12 PLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGletpsAGELLAG-------------TAPLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 723 AtvRDNI-LFGQTYDRKRYNKVID-----------ACALRAdidiLSAGDLTE-IGEKGINLSGGQKQRISLARAVYSDA 789
Cdd:PRK11247 79 A--REDTrLMFQDARLLPWKKVIDnvglglkgqwrDAALQA----LAAVGLADrANEWPAALSGGQKQRVALARALIHRP 152
|
170
....*....|....
gi 45552357 790 DLYLLDDPLSAVDA 803
Cdd:PRK11247 153 GLLLLDEPLGALDA 166
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
1036-1279 |
1.41e-11 |
|
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: 67.04 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1036 GAFGFGQVFSYIGSVVIVYLGALIgTRKIFIQLFGNILHAPQAYFDIKPRARILDRLANDIYKL-DVVLPELIRVFNSqV 1114
Cdd:cd18547 53 GLYLLSALFSYLQNRLMARVSQRT-VYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNIsQALSQSLTQLISS-I 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1115 FRVLATIVV-ISLSTPIFLAVIVPIAFLYYFA-------QRFYVATSRQLMRLEsvsrspiySHFSETVTGASTIRAYNV 1186
Cdd:cd18547 131 LTIVGTLIMmLYISPLLTLIVLVTVPLSLLVTkfiakrsQKYFRKQQKALGELN--------GYIEEMISGQKVVKAFNR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1187 GDRFIEESDAKVDKNQVCkypSVIANRWLAIR---LEMVGNL----IILFASLFaVLGGQTNPGLVGLSVSYALQVTQTL 1259
Cdd:cd18547 203 EEEAIEEFDEINEELYKA---SFKAQFYSGLLmpiMNFINNLgyvlVAVVGGLL-VINGALTVGVIQAFLQYSRQFSQPI 278
|
250 260
....*....|....*....|
gi 45552357 1260 NWLVRMSSDIETNIVSVERI 1279
Cdd:cd18547 279 NQISQQINSLQSALAGAERV 298
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
649-830 |
1.42e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 67.94 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 649 MSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK-LAYVP-----------Q 716
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdLSHVPpyqrpinmmfqS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 717 QAWIQNATVRDNILFGQTYDRKRYNKVIDACAlradiDILSAGDLTEI-GEKGINLSGGQKQRISLARAVYSDADLYLLD 795
Cdd:PRK11607 100 YALFPHMTVEQNIAFGLKQDKLPKAEIASRVN-----EMLGLVHMQEFaKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 45552357 796 DPLSAVDAHVGKHIFEEVIgpkGILAR--KSRVLVTH 830
Cdd:PRK11607 175 EPMGALDKKLRDRMQLEVV---DILERvgVTCVMVTH 208
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
651-797 |
1.45e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.94 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 651 IENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG--KLAYVPQQAWI-QNATVRD 727
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLdDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 728 NILFG--------QTYDR------------KRYNKV------IDACALRADID-ILSAGDLTEI-GEKGI-NLSGGQKQR 778
Cdd:COG0488 81 TVLDGdaelraleAELEEleaklaepdedlERLAELqeefeaLGGWEAEARAEeILSGLGFPEEdLDRPVsELSGGWRRR 160
|
170
....*....|....*....
gi 45552357 779 ISLARAVYSDADLYLLDDP 797
Cdd:COG0488 161 VALARALLSEPDLLLLDEP 179
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1317-1531 |
1.58e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.57 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1317 RYREglDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDG--VDIASMGLHMLRSRLTIIPQDP- 1393
Cdd:PRK13638 10 RYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDPe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1394 --VLFSG-------SLRiNLDPFEIKTDDEIWKALELSHLKSFVKSLAAGLNHeiaeggenlsvGQRQLVCLARALLRKT 1464
Cdd:PRK13638 88 qqIFYTDidsdiafSLR-NLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSH-----------GQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 1465 KVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTI-AHRLNTILD-SDKVIVLDKGQIIEFASPTELL 1531
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVF 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1324-1524 |
1.59e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.55 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1324 LVLRGVSFNIQGGEKVGIVGRTGAGKSSltlaLFRII----EAAGGRISI-DGVDIA--SMGLHMLRSRLTII------- 1389
Cdd:COG0488 329 TLLDDLSLRIDRGDRIGLIGPNGAGKST----LLKLLagelEPDSGTVKLgETVKIGyfDQHQEELDPDKTVLdelrdga 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1390 PQDPV----------LFSGslrinldpfeiktdDEIWKalelshlksFVKSlaaglnheiaeggenLSVGQRQLVCLARA 1459
Cdd:COG0488 405 PGGTEqevrgylgrfLFSG--------------DDAFK---------PVGV---------------LSGGEKARLALAKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 1460 LLRKTKVLVLDEATAAVDLETDDLIQKTIRtEFkECTVLTIAH-R--LNTIldSDKVIVLDKGQIIEF 1524
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIETLEALEEALD-DF-PGTVLLVSHdRyfLDRV--ATRILEFEDGGVREY 510
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1329-1521 |
1.61e-11 |
|
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: 68.70 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1329 VSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAA-GGRISIDG--VDIASMgLHMLRSRLTIIPQD-------PVL--- 1395
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNP-AQAIRAGIAMVPEDrkrhgivPILgvg 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1396 ----------FSGSLRINldpfEIKTDDEIWKALELSHLKSFVKSLAAGlnheiaeggeNLSVGQRQLVCLARALLRKTK 1465
Cdd:TIGR02633 358 knitlsvlksFCFKMRID----AAAELQIIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNPR 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 1466 VLVLDEATAAVDLETDDLIQKTIRTEFKE-CTVLTIAHRLNTILD-SDKVIVLDKGQI 1521
Cdd:TIGR02633 424 VLILDEPTRGVDVGAKYEIYKLINQLAQEgVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
666-804 |
1.66e-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: 67.82 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 666 NINIEVKKGSLVALVGTVGSGKSSVVQAflgemekLAGVVN------TVG------------------KLAYVPQQAwiq 721
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRA-------IAGLERpdsgriRLGgevlqdsargiflpphrrRIGYVFQEA--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 722 nA-----TVRDNILFGqtydRKRynkvidACALRADIDILSAGDLTEIG---EKGI-NLSGGQKQRISLARAVYSDADLY 792
Cdd:COG4148 87 -RlfphlSVRGNLLYG----RKR------APRAERRISFDEVVELLGIGhllDRRPaTLSGGERQRVAIGRALLSSPRLL 155
|
170
....*....|..
gi 45552357 793 LLDDPLSAVDAH 804
Cdd:COG4148 156 LMDEPLAALDLA 167
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
657-854 |
1.68e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 68.05 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 657 SWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVV-------QAFLGEM----EKLAGV------VNTVGKlayvpQQAW 719
Cdd:PRK09452 23 SFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLrliagfeTPDSGRImldgQDITHVpaenrhVNTVFQ-----SYAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 720 IQNATVRDNILFGQtydrkRYNKVIDACALRADIDILSAGDLTEIGE-KGINLSGGQKQRISLARAVYSDADLYLLDDPL 798
Cdd:PRK09452 98 FPHMTVFENVAFGL-----RMQKTPAAEITPRVMEALRMVQLEEFAQrKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552357 799 SAVDAHVGKHIFEEvigpkgiLARKSRVLvthGVTF----------LPQVDSIYVIKMGEISESGT 854
Cdd:PRK09452 173 SALDYKLRKQMQNE-------LKALQRKL---GITFvfvthdqeeaLTMSDRIVVMRDGRIEQDGT 228
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1317-1484 |
1.81e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 65.61 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1317 RYREG--LDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASM---GLHMLRSR-LTIIP 1390
Cdd:PRK11629 14 RYQEGsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRNQkLGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1391 Q------D---------PVLFSGSlrinlDPFEIKTddeiwKALELshlksfvksLAA-GLNHEIAEGGENLSVGQRQLV 1454
Cdd:PRK11629 94 QfhhllpDftalenvamPLLIGKK-----KPAEINS-----RALEM---------LAAvGLEHRANHRPSELSGGERQRV 154
|
170 180 190
....*....|....*....|....*....|
gi 45552357 1455 CLARALLRKTKVLVLDEATAAVDLETDDLI 1484
Cdd:PRK11629 155 AIARALVNNPRLVLADEPTGNLDARNADSI 184
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
664-861 |
1.84e-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: 65.68 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGeMEK-------LAGV-VNTVGKLAYVPQQAWI----------QNATV 725
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING-LERptsgsvlVDGTdLTLLSGKELRKARRRIgmifqhfnllSSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 726 RDNILF-------GQTYDRKRYNKVIDACALRADIDILSAgdlteigekgiNLSGGQKQRISLARAVYSDADLYLLDDPL 798
Cdd:cd03258 100 FENVALpleiagvPKAEIEERVLELLELVGLEDKADAYPA-----------QLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45552357 799 SAVDAHVGKHIFEevigpkgiLARKSR-------VLVTHGVTFLPQV-DSIYVIKMGEISESGTFDQLVKN 861
Cdd:cd03258 169 SALDPETTQSILA--------LLRDINrelgltiVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1325-1534 |
1.86e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 67.18 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHM----------------LRSRLTI 1388
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHelitnpyskkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1389 IPQDP--VLFSGSLR--INLDPFEIKTDDEIWKALELSHLKSFvkslaaGLNHEIAEGGE-NLSVGQRQLVCLARALLRK 1463
Cdd:PRK13631 121 VFQFPeyQLFKDTIEkdIMFGPVALGVKKSEAKKLAKFYLNKM------GLDDSYLERSPfGLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45552357 1464 TKVLVLDEATAAVDLETDDLIQKTIRTEFKEC-TVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNP 1534
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILDAKANNkTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1309-1534 |
1.89e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 66.36 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLDlVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTI 1388
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1389 IPQDP--VLFSGSLR--INLDPFEIKTDDEIWKalelSHLKSFVKSLaaGLNHEIAEGGENLSVGQRQLVCLARALLRKT 1464
Cdd:PRK13652 83 VFQNPddQIFSPTVEqdIAFGPINLGLDEETVA----HRVSSALHML--GLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45552357 1465 KVLVLDEATAAVDLETDDLIQKTIRTEFKE--CTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNP 1534
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
651-802 |
1.93e-11 |
|
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: 65.67 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 651 IENGEFSWGDEIT-LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVV-------NTVGK---------LAY 713
Cdd:cd03256 3 VENLSKTYPNGKKaLKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgtdiNKLKGkalrqlrrqIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 714 VPQQ-AWIQNATVRDNILFG------------QTYDRKRYNKvidACALRADIDILS-----AGdlteigekgiNLSGGQ 775
Cdd:cd03256 83 IFQQfNLIERLSVLENVLSGrlgrrstwrslfGLFPKEEKQR---ALAALERVGLLDkayqrAD----------QLSGGQ 149
|
170 180
....*....|....*....|....*..
gi 45552357 776 KQRISLARAVYSDADLYLLDDPLSAVD 802
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLD 176
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
651-854 |
1.97e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 66.55 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 651 IENGEFSWGDEI-TLRNINIEVKKGSLVALVGTVGSGKSSVVQAF-----------------LGEMEKLAGVVNTVGKLA 712
Cdd:PRK13644 4 LENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLngllrpqkgkvlvsgidTGDFSKLQGIRKLVGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 713 YVPQQAWIqNATVRDNILFGQTydrkryNKVIDACALRADIDILsagdLTEIG-EK-----GINLSGGQKQRISLARAVY 786
Cdd:PRK13644 84 QNPETQFV-GRTVEEDLAFGPE------NLCLPPIEIRKRVDRA----LAEIGlEKyrhrsPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 787 SDADLYLLDDPLSAVDAHVGKHIFEEV--IGPKGilarKSRVLVTHGVTFLPQVDSIYVIKMGEISESGT 854
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIkkLHEKG----KTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
664-830 |
2.11e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 65.20 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEmekLAGVVNTVGKL-----------------AYVPQQAWI-QNATV 725
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGT---LSPAFSASGEVllngrrltalpaeqrriGILFQDDLLfPHLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 726 RDNILFGQTYDRKRYNKviDACALRAdidiLSAGDLTEIGEKGIN-LSGGQKQRISLARAVYSDADLYLLDDPLSAVDAH 804
Cdd:COG4136 94 GENLAFALPPTIGRAQR--RARVEQA----LEEAGLAGFADRDPAtLSGGQRARVALLRALLAEPRALLLDEPFSKLDAA 167
|
170 180 190
....*....|....*....|....*....|
gi 45552357 805 ----VGKHIFEEvIGPKGILArksrVLVTH 830
Cdd:COG4136 168 lraqFREFVFEQ-IRQRGIPA----LLVTH 192
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1325-1502 |
2.22e-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: 65.53 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISID----GVDIASMGLH-MLRSR----------LTII 1389
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASPReILALRrrtigyvsqfLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1390 PqdpvlfsgslRInldpfeiktddeiwKALELshlksfVKS--LAAGLNHEIAEG-----------GENL--------SV 1448
Cdd:COG4778 106 P----------RV--------------SALDV------VAEplLERGVDREEARArarellarlnlPERLwdlppatfSG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1449 GQRQLVCLARALLRKTKVLVLDEATAAVDLETD----DLIQktirtEFKE--CTVLTIAH 1502
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRavvvELIE-----EAKArgTAIIGIFH 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
659-830 |
2.33e-11 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 65.12 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 659 GDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK-LAYVPQQA----------------WIQ 721
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdVSDLRGRAipylrrkigvvfqdfrLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 722 NATVRDNILF-------GQTYDRKRYNKVIDACALRADIDILSAGdlteigekginLSGGQKQRISLARAVYSDADLYLL 794
Cdd:cd03292 92 DRNVYENVAFalevtgvPPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 45552357 795 DDPLSAVDAHVGKHIFEEVigpKGILARKSRVLV-TH 830
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLL---KKINKAGTTVVVaTH 194
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
667-802 |
2.38e-11 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 67.06 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 667 INIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG-----------------KLAYVPQQAWI-QNATVRDN 728
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrkgiflppekrRIGYVFQEARLfPHLSVRGN 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45552357 729 ILFGQTYDRKRYNKVIDAcalrADIDILSAGDLTEIGEKgiNLSGGQKQRISLARAVYSDADLYLLDDPLSAVD 802
Cdd:TIGR02142 96 LRYGMKRARPSERRISFE----RVIELLGIGHLLGRLPG--RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
664-797 |
2.43e-11 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 65.07 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEmEKL-AGVVNTVG----------------KLAYVPQQAW-IQNATV 725
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGE-ERPtSGQVLVNGqdlsrlkrreipylrrRIGVVFQDFRlLPDRTV 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 726 RDNILFG---QTYDRKRYNKVIDAcALradidilsagDLTEIGEKG----INLSGGQKQRISLARAVYSDADLYLLDDP 797
Cdd:COG2884 97 YENVALPlrvTGKSRKEIRRRVRE-VL----------DLVGLSDKAkalpHELSGGEQQRVAIARALVNRPELLLADEP 164
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
648-811 |
2.63e-11 |
|
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: 68.24 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 648 PMSIENGEfswgdeITLRNINIEVKKGSLVALVGTVGSGKSSVvQAFLGEMEKLAGVVNTV---GKLAYVPQQAWIQNAT 724
Cdd:TIGR00954 458 PLVTPNGD------VLIESLSFEVPSGNNLLICGPNGCGKSSL-FRILGELWPVYGGRLTKpakGKLFYVPQRPYMTLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 725 VRDNILFGQTYDRKRYNKVIDACAlradIDILSAGDLTEIGEKGIN----------LSGGQKQRISLARAVYSDADLYLL 794
Cdd:TIGR00954 531 LRDQIIYPDSSEDMKRRGLSDKDL----EQILDNVQLTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAIL 606
|
170
....*....|....*..
gi 45552357 795 DDPLSAVDAHVGKHIFE 811
Cdd:TIGR00954 607 DECTSAVSVDVEGYMYR 623
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
649-869 |
2.89e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 65.42 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 649 MSIE--NGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAF-LGEMEKlAGVVNTVG---------------- 709
Cdd:PRK11124 1 MSIQlnGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPR-SGTLNIAGnhfdfsktpsdkaire 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 710 ---KLAYVPQQ--AWiQNATVRDNILFGQTydrkRYNKVIDACALRADIDILSAGDLTEIGEK-GINLSGGQKQRISLAR 783
Cdd:PRK11124 80 lrrNVGMVFQQynLW-PHLTVQQNLIEAPC----RVLGLSKDQALARAEKLLERLRLKPYADRfPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 784 AVYSDADLYLLDDPLSAVD----AHVGKHIFEevIGPKGIlarkSRVLVTHGVTFLPQVDSiYVIKM--GEISESGTFDQ 857
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDpeitAQIVSIIRE--LAETGI----TQVIVTHEVEVARKTAS-RVVYMenGHIVEQGDASC 227
|
250
....*....|...
gi 45552357 858 LVKNK-GAFADFI 869
Cdd:PRK11124 228 FTQPQtEAFKNYL 240
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1326-1522 |
3.76e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.34 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1326 LRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIA--------SMGLHMLRSRLTIIPQdpvlfs 1397
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssqEAGIGIIHQELNLIPQ------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1398 gsLRINLDPF---EIKTddeIWKALELSHLKSFVKSLAAGLN-----HEIAegGEnLSVGQRQLVCLARALLRKTKVLVL 1469
Cdd:PRK10762 94 --LTIAENIFlgrEFVN---RFGRIDWKKMYAEADKLLARLNlrfssDKLV--GE-LSIGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 1470 DEATAAV-DLETDDLIqKTIRtEFKE--CTVLTIAHRLNTILD-SDKVIVLDKGQII 1522
Cdd:PRK10762 166 DEPTDALtDTETESLF-RVIR-ELKSqgRGIVYISHRLKEIFEiCDDVTVFRDGQFI 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
648-862 |
3.77e-11 |
|
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: 65.00 E-value: 3.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 648 PM-SIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK-LAYVPQQAWI----- 720
Cdd:COG1127 4 PMiEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQdITGLSEKELYelrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 721 -----QNA------TVRDNILFGQtydrkRYNKVIDAcALRADI--DILSAGDLTEIGEKGIN-LSGGQKQRISLARAVY 786
Cdd:COG1127 84 igmlfQGGalfdslTVFENVAFPL-----REHTDLSE-AEIRELvlEKLELVGLPGAADKMPSeLSGGMRKRVALARALA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 787 SDADLYLLDDPLSAVDAhVGKHIFEEVIgpkgilaRKSR-------VLVTHGVTFLPQV-DSIYVIKMGEISESGTFDQL 858
Cdd:COG1127 158 LDPEILLYDEPTAGLDP-ITSAVIDELI-------RELRdelgltsVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEEL 229
|
....
gi 45552357 859 VKNK 862
Cdd:COG1127 230 LASD 233
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1325-1538 |
4.21e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 66.51 E-value: 4.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLtlalFRII----EAAGGRISIDGVDIA--------------SMGL--HMlrs 1384
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTV----LRLIagfeTPDSGRIMLDGQDIThvpaenrhvntvfqSYALfpHM--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1385 rlTIIpqDPVLFsgSLRINLDPF-EIKTddEIWKALELSHLKSFVkslaaglNHEIAeggeNLSVGQRQLVCLARALLRK 1463
Cdd:PRK09452 102 --TVF--ENVAF--GLRMQKTPAaEITP--RVMEALRMVQLEEFA-------QRKPH----QLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1464 TKVLVLDEATAAVDLEtddlIQKTIRTEFKE------CTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNPKS 1536
Cdd:PRK09452 163 PKVLLLDESLSALDYK----LRKQMQNELKAlqrklgITFVFVTHDQEEALTmSDRIVVMRDGRIEQDGTPREIYEEPKN 238
|
..
gi 45552357 1537 AF 1538
Cdd:PRK09452 239 LF 240
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1312-1523 |
5.99e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.82 E-value: 5.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1312 QNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIasmglhmlrsrltIIPQ 1391
Cdd:COG2401 32 EAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDN-------------QFGR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1392 DPVLfsgslrinLDPFEIKTDdeIWKALELSHlksfvkslAAGLN---------HEiaeggenLSVGQRQLVCLARALLR 1462
Cdd:COG2401 99 EASL--------IDAIGRKGD--FKDAVELLN--------AVGLSdavlwlrrfKE-------LSTGQKFRFRLALLLAE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 1463 KTKVLVLDEATAAVDLETDDLIQKTIRTEFKEC--TVLTIAHRLNTI--LDSDKVIVLDKGQIIE 1523
Cdd:COG2401 154 RPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAgiTLVVATHHYDVIddLQPDLLIFVGYGGVPE 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
664-797 |
6.81e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.58 E-value: 6.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK--------------LAYVP----QQAWIQNATV 725
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVPedrkGEGLVLDLSI 347
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 726 RDNILFGqTYDRKRYNKVID-------ACALRADIDILSAGDLTEIGekgiNLSGGQKQRISLARAVYSDADLYLLDDP 797
Cdd:COG1129 348 RENITLA-SLDRLSRGGLLDrrreralAEEYIKRLRIKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
658-861 |
7.46e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.22 E-value: 7.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 658 WGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQA--FLGEMEKLAGVVN---------TVGKLAyVPQQAWIQNATVR 726
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCinFLEKPSEGSIVVNgqtinlvrdKDGQLK-VADKNQLRLLRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 727 DNILFgQTYDRKRYNKVIDAcALRADIDIL--SAGDLTEIGEK-----GIN----------LSGGQKQRISLARAVYSDA 789
Cdd:PRK10619 94 LTMVF-QHFNLWSHMTVLEN-VMEAPIQVLglSKQEARERAVKylakvGIDeraqgkypvhLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552357 790 DLYLLDDPLSAVDAH-VGkhifeEVIGPKGILAR--KSRVLVTHGVTFLPQVDS-IYVIKMGEISESGTFDQLVKN 861
Cdd:PRK10619 172 EVLLFDEPTSALDPElVG-----EVLRIMQQLAEegKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQLFGN 242
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1325-1537 |
7.79e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 64.73 E-value: 7.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPVLFSgslRINl 1404
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVLEFRRRVGMLFQ---RPN- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1405 dPFEIKTDDEIW---KALELSHLKSFVKSLAAGLNH---------EIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEA 1472
Cdd:PRK14271 112 -PFPMSIMDNVLagvRAHKLVPRKEFRGVAQARLTEvglwdavkdRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552357 1473 TAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNPKSA 1537
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1312-1538 |
8.23e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.65 E-value: 8.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1312 QNFQVRYREG--LDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAA-----GGRISIDGVDIASMGLHMLR- 1383
Cdd:PRK15134 9 ENLSVAFRQQqtVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1384 ---SRLTIIPQDPVlfsgslrINLDPFEiktddEIWKALelshlkSFVKSLAAGLNHEIAEG------------------ 1442
Cdd:PRK15134 89 vrgNKIAMIFQEPM-------VSLNPLH-----TLEKQL------YEVLSLHRGMRREAARGeilncldrvgirqaakrl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1443 ---GENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLEtddlIQKTIRTEFKEC------TVLTIAHRLNTILD-SDK 1512
Cdd:PRK15134 151 tdyPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVS----VQAQILQLLRELqqelnmGLLFITHNLSIVRKlADR 226
|
250 260
....*....|....*....|....*.
gi 45552357 1513 VIVLDKGQIIEFASPTELLDNPKSAF 1538
Cdd:PRK15134 227 VAVMQNGRCVEQNRAATLFSAPTHPY 252
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1292-1522 |
8.63e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.20 E-value: 8.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1292 ELEQDKNKPKNWPQEGRVEFQNFQVRYREGLDlVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDG 1371
Cdd:COG3845 241 EVLLRVEKAPAEPGEVVLEVENLSVRDDRGVP-ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1372 VDIASMG-LHMLRSRLTIIPQDP-----VLfSGSLRINLdpfeiktddeiwkALELSHLKSFVKSL-------------- 1431
Cdd:COG3845 320 EDITGLSpRERRRLGVAYIPEDRlgrglVP-DMSVAENL-------------ILGRYRRPPFSRGGfldrkairafaeel 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1432 -------AAGLNHEIAeggeNLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKE-CTVLTIAHR 1503
Cdd:COG3845 386 ieefdvrTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAgAAVLLISED 461
|
250 260
....*....|....*....|
gi 45552357 1504 LNTILD-SDKVIVLDKGQII 1522
Cdd:COG3845 462 LDEILAlSDRIAVMYEGRIV 481
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1305-1503 |
9.23e-11 |
|
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: 66.70 E-value: 9.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1305 QEGRVEFQNFQVRYREGlDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLtlalFRII----EAAGGRISIDGvdiasmglh 1380
Cdd:TIGR00954 448 QDNGIKFENIPLVTPNG-DVLIESLSFEVPSGNNLLICGPNGCGKSSL----FRILgelwPVYGGRLTKPA--------- 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1381 mlRSRLTIIPQDPVLFSGSLR---INLD-PFEIK----TDDEIWKALELSHLKSFVK---SLAAglnheIAEGGENLSVG 1449
Cdd:TIGR00954 514 --KGKLFYVPQRPYMTLGTLRdqiIYPDsSEDMKrrglSDKDLEQILDNVQLTHILEregGWSA-----VQDWMDVLSGG 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 45552357 1450 QRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTefKECTVLTIAHR 1503
Cdd:TIGR00954 587 EKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHR 638
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1309-1534 |
1.03e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 64.66 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGL---DLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIdGVDIASMG-----LH 1380
Cdd:PRK13634 3 ITFQKVEHRYQYKTpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGkknkkLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1381 MLRSRLTIIPQDP--VLFSGSLR--INLDP--FEIKTDDEIWKALELSHLksfvkslaAGLNHEIAEGGE-NLSVGQRQL 1453
Cdd:PRK13634 82 PLRKKVGIVFQFPehQLFEETVEkdICFGPmnFGVSEEDAKQKAREMIEL--------VGLPEELLARSPfELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1454 VCLARALLRKTKVLVLDEATAAVD----LETDDLIQKTIRTefKECTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPT 1528
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDpkgrKEMMEMFYKLHKE--KGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR 231
|
....*.
gi 45552357 1529 ELLDNP 1534
Cdd:PRK13634 232 EIFADP 237
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
664-862 |
1.18e-10 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 63.22 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK--------------LAYVPQQAWI-QNATVRDN 728
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglppheiarlgIGRTFQIPRLfPELTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 729 ILFGQTYDRK------RYNKVIDACALRADiDILsagDLTEIGEKG----INLSGGQKQRISLARAVYSDADLYLLDDP- 797
Cdd:cd03219 96 VMVAAQARTGsglllaRARREEREARERAE-ELL---ERVGLADLAdrpaGELSYGQQRRLEIARALATDPKLLLLDEPa 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 798 --LSAVDAHVGKHIFEEvigpkgiLARKSR--VLVTHGVTFLPQV-DSIYVIKMGEISESGTFDQLVKNK 862
Cdd:cd03219 172 agLNPEETEELAELIRE-------LRERGItvLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDEVRNNP 234
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1325-1531 |
1.25e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.08 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAG--------GRISIDGVDIASMGLHMLRSRLTIIPQ--DPV 1394
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaaQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1395 L-FSGSLRINLDPF---------EIKTDDEIWKALELshlksfvkslaAGLNHEIAEGGENLSVGQRQLVCLARAL---- 1460
Cdd:PRK13547 96 FaFSAREIVLLGRYpharragalTHRDGEIAWQALAL-----------AGATALVGRDVTTLSGGELARVQFARVLaqlw 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 1461 -----LRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKE--CTVLTIAHRLN-TILDSDKVIVLDKGQIIEFASPTELL 1531
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwnLGVLAIVHDPNlAARHADRIAMLADGAIVAHGAPADVL 243
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
664-869 |
1.48e-10 |
|
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: 63.72 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFL------GEMEkLAGVV-NTVG------KLAYVPQQAWIQNATVRDNI- 729
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLrllnteGDIQ-IDGVSwNSVPlqkwrkAFGVIPQKVFIFSGTFRKNLd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 730 LFGQTYDRKRYnKVIDACALRADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAhVGKHI 809
Cdd:cd03289 99 PYGKWSDEEIW-KVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-ITYQV 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 810 FEEVIgpKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEISESGTFDQLVKNKGAFADFI 869
Cdd:cd03289 177 IRKTL--KQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAI 234
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1032-1471 |
1.51e-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: 65.59 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1032 LGVYGAFGFGQVFSYIGSVVIVYLGALI--------GTRKIF---IQLFGNILHAPQAYFDIKPRARILDRLANDIYKLD 1100
Cdd:COG4615 40 LNATGAALARLLLLFAGLLVLLLLSRLAsqllltrlGQHAVArlrLRLSRRILAAPLERLERIGAARLLAALTEDVRTIS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1101 ---VVLPELIRvfnsQVFRVLATIVVIS-LSTPIFLAVIVPIAFLYYFAQRFyVATSRQLMRLESVSRSPIYSHFSETVT 1176
Cdd:COG4615 120 qafVRLPELLQ----SVALVLGCLAYLAwLSPPLFLLTLVLLGLGVAGYRLL-VRRARRHLRRAREAEDRLFKHFRALLE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1177 GA-----STIRAYNVGDRFIEESDAKVDKNqvckypSVIANRWLAIrLEMVGNLIILF--ASLFAVLggqtnPGLVGLS- 1248
Cdd:COG4615 195 GFkelklNRRRRRAFFDEDLQPTAERYRDL------RIRADTIFAL-ANNWGNLLFFAliGLILFLL-----PALGWADp 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1249 ---VSYAL-------QVTQTLNWLVRMSSdieTNiVSVERIKEYG--ETKQEAPWELEQDKNKPKNWpqeGRVEFQNfqV 1316
Cdd:COG4615 263 avlSGFVLvllflrgPLSQLVGALPTLSR---AN-VALRKIEELElaLAAAEPAAADAAAPPAPADF---QTLELRG--V 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1317 RYR-------EGLDLvlrG-VSFNIQGGEKVGIVGRTGAGKSslTLA-----LFRiieAAGGRISIDGVDIASMGLHMLR 1383
Cdd:COG4615 334 TYRypgedgdEGFTL---GpIDLTIRRGELVFIVGGNGSGKS--TLAklltgLYR---PESGEILLDGQPVTADNREAYR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1384 SRLTIIPQDPVLFSGslriNLDPFEIKTDDEI--W-KALELSHLKSFvkslaaglnheiaEGGE----NLSVGQRQLVCL 1456
Cdd:COG4615 406 QLFSAVFSDFHLFDR----LLGLDGEADPARAreLlERLELDHKVSV-------------EDGRfsttDLSQGQRKRLAL 468
|
490
....*....|....*
gi 45552357 1457 ARALLRKTKVLVLDE 1471
Cdd:COG4615 469 LVALLEDRPILVFDE 483
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1327-1521 |
1.60e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.46 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1327 RGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMG-LHMLRSRLTIIPQD----------PVL 1395
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLARGLVYLPEDrqssglyldaPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1396 FS-GSLRINLDPFEIKTddeiwkALELSHLKSFVKSLAAGLNHEIAEGGeNLSVGQRQLVCLARALLRKTKVLVLDEATA 1474
Cdd:PRK15439 360 WNvCALTHNRRGFWIKP------ARENAVLERYRRALNIKFNHAEQAAR-TLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 45552357 1475 AVDLETDDLIQKTIRTEFKECT-VLTIAHRLNTILD-SDKVIVLDKGQI 1521
Cdd:PRK15439 433 GVDVSARNDIYQLIRSIAAQNVaVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
650-861 |
1.61e-10 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 63.09 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 650 SIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSvvqaFL-----------GEMEkLAGV--------VNTV-G 709
Cdd:COG1126 3 EIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKST----LLrcinlleepdsGTIT-VDGEdltdskkdINKLrR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 710 KLAYVPQQ-AWIQNATVRDNILFGQTYDRKRYNKVIDACALRAdidilsagdLTEIG--EKG----INLSGGQKQRISLA 782
Cdd:COG1126 78 KVGMVFQQfNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMEL---------LERVGlaDKAdaypAQLSGGQQQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 783 RAVYSDADLYLLDDPLSAVD----AHVgkhifEEVIgpKGiLARKSR--VLVTHGVTFLPQV-DSIYVIKMGEISESGTF 855
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDpelvGEV-----LDVM--RD-LAKEGMtmVVVTHEMGFAREVaDRVVFMDGGRIVEEGPP 220
|
....*.
gi 45552357 856 DQLVKN 861
Cdd:COG1126 221 EEFFEN 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
658-861 |
1.86e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 63.32 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 658 WGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAF-----LGEMEKLAGVVNTVGKLAYVPQQAWIQ----------- 721
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIEvrrevgmvfqy 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 722 -----NATVRDNILFGQtydrkRYNKVIDAcalRADID-----ILSAGDLTE-----IGEKGINLSGGQKQRISLARAVY 786
Cdd:PRK14267 94 pnpfpHLTIYDNVAIGV-----KLNGLVKS---KKELDervewALKKAALWDevkdrLNDYPSNLSGGQRQRLVIARALA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 787 SDADLYLLDDPLSAVDAhVGKHIFEEVigpkgILARKSR---VLVTHGVTFLPQV-DSIYVIKMGEISESGTFDQLVKN 861
Cdd:PRK14267 166 MKPKILLMDEPTANIDP-VGTAKIEEL-----LFELKKEytiVLVTHSPAQAARVsDYVAFLYLGKLIEVGPTRKVFEN 238
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1316-1529 |
2.04e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 63.36 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1316 VRYREGlDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIAsmglHMLRSRL-TIIPQ-DP 1393
Cdd:PRK15056 14 VTWRNG-HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNLvAYVPQsEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1394 VLFSgslrinldpFEIKTDDEI---------WKALELSHLKSFVKSLAAG---LNHEIAEGGEnLSVGQRQLVCLARALL 1461
Cdd:PRK15056 89 VDWS---------FPVLVEDVVmmgryghmgWLRRAKKRDRQIVTAALARvdmVEFRHRQIGE-LSGGQKKRVFLARAIA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 1462 RKTKVLVLDEATAAVDLETDDLIQKTIRTEFKE-CTVLTIAHRLNTILDSDKVIVLDKGQIIEfASPTE 1529
Cdd:PRK15056 159 QQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLA-SGPTE 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1326-1519 |
2.09e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.19 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1326 LRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDI--------ASMGLHMLRSRLTIIPQDPV--- 1394
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnkldhklaAQLGIGIIYQELSVIDELTVlen 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1395 LFSGSLRINlDPFEIKTDDeiWKALElshLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATA 1474
Cdd:PRK09700 101 LYIGRHLTK-KVCGVNIID--WREMR---VRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 45552357 1475 AV-DLETDDL--IQKTIRTEFKecTVLTIAHRLNTILD-SDKVIVLDKG 1519
Cdd:PRK09700 175 SLtNKEVDYLflIMNQLRKEGT--AIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
657-803 |
2.11e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 64.28 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 657 SWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGeMEKLagvvnTVGKLaYVPQQ------------------- 717
Cdd:PRK11000 12 AYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAG-LEDI-----TSGDL-FIGEKrmndvppaergvgmvfqsy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 718 AWIQNATVRDNILFG-------QTYDRKRYNKVIDacalradidILSAGDLTEIGEKGinLSGGQKQRISLARAVYSDAD 790
Cdd:PRK11000 85 ALYPHLSVAENMSFGlklagakKEEINQRVNQVAE---------VLQLAHLLDRKPKA--LSGGQRQRVAIGRTLVAEPS 153
|
170
....*....|...
gi 45552357 791 LYLLDDPLSAVDA 803
Cdd:PRK11000 154 VFLLDEPLSNLDA 166
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
650-830 |
2.88e-10 |
|
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: 62.41 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 650 SIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGvvNTVG----------------KLAY 713
Cdd:COG1119 5 ELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG--NDVRlfgerrggedvwelrkRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 714 V-P--QQAWIQNATVRDNIL---FGQTYdrkRYNKVIDACALRADiDILSAGDLTEIGEKGIN-LSGGQKQRISLARAVY 786
Cdd:COG1119 83 VsPalQLRFPRDETVLDVVLsgfFDSIG---LYREPTDEQRERAR-ELLELLGLAHLADRPFGtLSQGEQRRVLIARALV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 45552357 787 SDADLYLLDDPLSAVDAHvGKHIFEEVIgpkGILARKSR---VLVTH 830
Cdd:COG1119 159 KDPELLILDEPTAGLDLG-ARELLLALL---DKLAAEGAptlVLVTH 201
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
664-864 |
2.96e-10 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 62.35 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKS----SVV--------QAFLGE-------MEKLA--GvvntvgkLAYVPQQAWI-Q 721
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTttfyMIVglvkpdsgRIFLDGedithlpMHKRArlG-------IGYLPQEASIfR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 722 NATVRDNI---LFGQTYDRKRYNKVIDacalradiDILSAGDLTEIGE-KGINLSGGQKQRISLARAVYSDADLYLLDDP 797
Cdd:COG1137 92 KLTVEDNIlavLELRKLSKKEREERLE--------ELLEEFGITHLRKsKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552357 798 LSAVD--AhvgkhifeeVIGPKGILAR-KSR---VLVT-HGV--TfLPQVDSIYVIKMGEISESGTFDQLVKNKGA 864
Cdd:COG1137 164 FAGVDpiA---------VADIQKIIRHlKERgigVLITdHNVreT-LGICDRAYIISEGKVLAEGTPEEILNNPLV 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
664-803 |
3.23e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 62.41 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLAYVP---------QQAWIQNATVRDNILFG-Q 733
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPgaergvvfqNEGLLPWRNVQDNVAFGlQ 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45552357 734 TYDRKRYNKVIDACALRADIDilsagdLTEIGEKGI-NLSGGQKQRISLARAVYSDADLYLLDDPLSAVDA 803
Cdd:PRK11248 97 LAGVEKMQRLEIAHQMLKKVG------LEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
657-849 |
4.29e-10 |
|
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: 60.13 E-value: 4.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 657 SWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAflgemekLAGVvntvgklaYVPQQAwiqnatvrdNILF-GQTY 735
Cdd:cd03216 9 RFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKI-------LSGL--------YKPDSG---------EILVdGKEV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 736 DRKRYNKvidacALRAdidilsagdlteigekGIN----LSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFE 811
Cdd:cd03216 65 SFASPRD-----ARRA----------------GIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK 123
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 45552357 812 EVigpKGILAR-KSRVLVTHgvtFLPQV----DSIYVIKMGEI 849
Cdd:cd03216 124 VI---RRLRAQgVAVIFISH---RLDEVfeiaDRVTVLRDGRV 160
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1324-1520 |
4.36e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.97 E-value: 4.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1324 LVLRGVSFNIQGGEKVGIVGRTGAGKSSLtlalFRII----EAAGGRISIDGVDIASMGLHMLR------------SRLT 1387
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSL----LRILaglaRPDAGEVLWQGEPIRRQRDEYHQdllylghqpgikTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1388 iiPQDPVLFSGSLRINLDpfeiktDDEIWKALElshlksfvkslAAGLnheiaEGGEN-----LSVGQRQLVCLARALLR 1462
Cdd:PRK13538 91 --ALENLRFYQRLHGPGD------DEALWEALA-----------QVGL-----AGFEDvpvrqLSAGQQRRVALARLWLT 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1463 KTKVLVLDEATAAVDLETDDLIQKTIR--TEFKECTVLTIAHRLNtiLDSDKVIVLDKGQ 1520
Cdd:PRK13538 147 RAPLWILDEPFTAIDKQGVARLEALLAqhAEQGGMVILTTHQDLP--VASDKVRKLRLGQ 204
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
656-830 |
5.02e-10 |
|
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: 61.37 E-value: 5.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 656 FSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVnTVGK-------------LAYVPQQawiqN 722
Cdd:cd03263 10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTA-YINGysirtdrkaarqsLGYCPQF----D 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 723 A-----TVRDNILF-------GQTYDRKRYNKVIDACALRADIDilsagdlTEIGekgiNLSGGQKQRISLARAVYSDAD 790
Cdd:cd03263 85 AlfdelTVREHLRFyarlkglPKSEIKEEVELLLRVLGLTDKAN-------KRAR----TLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 45552357 791 LYLLDDPLSAVDaHVGKHIFEEVIgpKGILARKSRVLVTH 830
Cdd:cd03263 154 VLLLDEPTSGLD-PASRRAIWDLI--LEVRKGRSIILTTH 190
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
650-854 |
5.56e-10 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 62.06 E-value: 5.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 650 SIENGEFSW--GDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLAYVPQQAW-------- 719
Cdd:TIGR04520 2 EVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeirkkvgm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 720 -IQN-------ATVRDNILFG---QTYDRKRYNKVIDacalradiDILSAGDLTEIGEKG-INLSGGQKQRISLARAVYS 787
Cdd:TIGR04520 82 vFQNpdnqfvgATVEDDVAFGlenLGVPREEMRKRVD--------EALKLVGMEDFRDREpHLLSGGQKQRVAIAGVLAM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45552357 788 DADLYLLDDPLSAVDAhVGKhifEEVIgpKGILA-RKSR----VLVTHGVTFLPQVDSIYVIKMGEISESGT 854
Cdd:TIGR04520 154 RPDIIILDEATSMLDP-KGR---KEVL--ETIRKlNKEEgitvISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
664-861 |
6.19e-10 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 61.15 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK--------------LAYVPQQAWI-QNATVRDN 728
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarlgIGYVPEGRRIfPSLTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 729 ILFGqTYDRKrynkviDACALRADIDilsagdltEIGE-----------KGINLSGGQKQRISLARAVYSDADLYLLDDP 797
Cdd:COG0410 99 LLLG-AYARR------DRAEVRADLE--------RVYElfprlkerrrqRAGTLSGGEQQMLAIGRALMSRPKLLLLDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45552357 798 ---LSAVdahVGKHIFEevigpkgILAR-KSR----VLVTHGVTFLPQV-DSIYVIKMGEISESGTFDQLVKN 861
Cdd:COG0410 164 slgLAPL---IVEEIFE-------IIRRlNREgvtiLLVEQNARFALEIaDRAYVLERGRIVLEGTAAELLAD 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
614-803 |
6.79e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 63.67 E-value: 6.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 614 DIAETQVSVNRINKFLNS-EELDPnsvlHDSSKPHPMSIENGEFSWGD--------EITLRNINIEVKKGSLVALVGTVG 684
Cdd:COG4178 324 SLAEWRATVDRLAGFEEAlEAADA----LPEAASRIETSEDGALALEDltlrtpdgRPLLEDLSLSLKPGERLLITGPSG 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 685 SGKSSVVQAflgemekLAG---------VVNTVGKLAYVPQQAWIQNATVRDNILFGQT---YDRKRYNKVIDACALrAD 752
Cdd:COG4178 400 SGKSTLLRA-------IAGlwpygsgriARPAGARVLFLPQRPYLPLGTLREALLYPATaeaFSDAELREALEAVGL-GH 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 45552357 753 IdilsAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDA 803
Cdd:COG4178 472 L----AERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1326-1522 |
7.70e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.41 E-value: 7.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1326 LRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAA--GGRISIDGVDIAS--------MGLHMLRSRLTIIPQDPVL 1395
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQAsnirdterAGIAIIHQELALVKELSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1396 ---FSGSlriNLDPFEIKTDDEIwkalelsHLKSfvKSLAAGLNHEI--AEGGENLSVGQRQLVCLARALLRKTKVLVLD 1470
Cdd:PRK13549 101 eniFLGN---EITPGGIMDYDAM-------YLRA--QKLLAQLKLDInpATPVGNLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 45552357 1471 EATAAV-DLETDDLIqkTIRTEFKE--CTVLTIAHRLNTILD-SDKVIVLDKGQII 1522
Cdd:PRK13549 169 EPTASLtESETAVLL--DIIRDLKAhgIACIYISHKLNEVKAiSDTICVIRDGRHI 222
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1325-1538 |
7.93e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 62.41 E-value: 7.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLtlalFRIIeaAG------GRISIDGVDIAsmGLHMLRSRLTIIPQDPVLF-- 1396
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTL----LRII--AGlehqtsGHIRFHGTDVS--RLHARDRKVGFVFQHYALFrh 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1397 -------SGSLRI-----NLDPFEIKTddEIWKALE---LSHLKSFVKSlaaglnheiaeggeNLSVGQRQLVCLARALL 1461
Cdd:PRK10851 89 mtvfdniAFGLTVlprreRPNAAAIKA--KVTQLLEmvqLAHLADRYPA--------------QLSGGQKQRVALARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1462 RKTKVLVLDEATAAVDLETDDLIQKTIR---TEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLDNPKSAF 1538
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRqlhEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRF 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
664-861 |
8.09e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 61.30 E-value: 8.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAfLGEMEKLAGVVNTVGKL------AYVPQQAWI-----------QN---- 722
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRC-INLLEQPEAGTIRVGDItidtarSLSQQKGLIrqlrqhvgfvfQNfnlf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 723 --ATVRDNILFGQTYDRK--RYNKVIDACALRADIDIlsAGDLTEIGEKginLSGGQKQRISLARAVYSDADLYLLDDPL 798
Cdd:PRK11264 98 phRTVLENIIEGPVIVKGepKEEATARARELLAKVGL--AGKETSYPRR---LSGGQQQRVAIARALAMRPEVILFDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 799 SAVDAH-VGkhifeEVIGPKGILARKSR--VLVTHGVTFLPQV-DSIYVIKMGEISESGTFDQLVKN 861
Cdd:PRK11264 173 SALDPElVG-----EVLNTIRQLAQEKRtmVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKALFAD 234
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
658-829 |
8.25e-10 |
|
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: 60.75 E-value: 8.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 658 WGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEK---LAGVVNTVGK----------LAYVPQQ-AWIQNA 723
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQprkpdqfqkcVAYVRQDdILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 724 TVRDNILFGQTY--DRKRYNKVIDAcalRADIDILSAGDLTEIGEKGI-NLSGGQKQRISLARAVYSDADLYLLDDPLSA 800
Cdd:cd03234 97 TVRETLTYTAILrlPRKSSDAIRKK---RVEDVLLRDLALTRIGGNLVkGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190
....*....|....*....|....*....|
gi 45552357 801 VDAHVGKHIFEEVIGpkgiLARKSR-VLVT 829
Cdd:cd03234 174 LDSFTALNLVSTLSQ----LARRNRiVILT 199
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
670-802 |
8.38e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 60.88 E-value: 8.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 670 EVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNT-VGKLAYVPQQAWI-QNATVRDnILFGQT---YDRKRYNkvi 744
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIeLDTVSYKPQYIKAdYEGTVRD-LLSSITkdfYTHPYFK--- 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 745 dacalradIDILSAGDLTEIGEKGIN-LSGGQKQRISLARAVYSDADLYLLDDPLSAVD 802
Cdd:cd03237 97 --------TEIAKPLQIEQILDREVPeLSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1309-1530 |
8.76e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 61.72 E-value: 8.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLDL---VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMG----LHM 1381
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1382 LRSRLTIIPQDP--VLFSGSL--RINLDPFEIKTDDEIWKAlelshlKSFVKSLAAGLNHEIAEGGE-NLSVGQRQLVCL 1456
Cdd:PRK13646 83 VRKRIGMVFQFPesQLFEDTVerEIIFGPKNFKMNLDEVKN------YAHRLLMDLGFSRDVMSQSPfQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 1457 ARALLRKTKVLVLDEATAAVDLETDDLIQ---KTIRTEfKECTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTEL 1530
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMrllKSLQTD-ENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
652-830 |
9.35e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 61.34 E-value: 9.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 652 ENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAF-----LGEMEKLAGVVNTVGKLAYVPQqawIQNATVR 726
Cdd:PRK14243 14 ENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYAPD---VDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 727 DNIlfGQTYDRKR-YNKVI-DACALRADIDILSaGDLTEIGEK------------------GINLSGGQKQRISLARAVY 786
Cdd:PRK14243 91 RRI--GMVFQKPNpFPKSIyDNIAYGARINGYK-GDMDELVERslrqaalwdevkdklkqsGLSLSGGQQQRLCIARAIA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 45552357 787 SDADLYLLDDPLSAVDAHVGKHIfEEVIgpKGILARKSRVLVTH 830
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRI-EELM--HELKEQYTIIIVTH 208
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
670-800 |
1.06e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.90 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 670 EVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLAYVPQqaWI---QNATVRDnILFGQT--YDRKRYNkvi 744
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQ--YIkpdYDGTVED-LLRSITddLGSSYYK--- 434
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 745 dacalradIDILSAGDLTEIGEKGIN-LSGGQKQRISLARAVYSDADLYLLDDPlSA 800
Cdd:PRK13409 435 --------SEIIKPLQLERLLDKNVKdLSGGELQRVAIAACLSRDADLYLLDEP-SA 482
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
664-811 |
1.17e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.80 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLG----------EMEKLAGVVNTVGKLA-----------YVPQQAWIQN 722
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksagsHIELLGRTVQREGRLArdirksrantgYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 723 A-TVRDNILFGQTYDRKRYNKVIDACALRADIDILSAgdLTEIG------EKGINLSGGQKQRISLARAVYSDADLYLLD 795
Cdd:PRK09984 100 RlSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQA--LTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170
....*....|....*.
gi 45552357 796 DPLSAVDAHVGKHIFE 811
Cdd:PRK09984 178 EPIASLDPESARIVMD 193
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
664-804 |
1.19e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 60.94 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK-------------LAYVPQQAWIQNA-TVRDNI 729
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRpladwspaelarrRAVLPQHSSLSFPfTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 730 LFGQ---TYDRKRYNKVIDACALRADIDILSAGDLTEigekginLSGGQKQRISLARA---VYSDAD---LYLLDDPLSA 800
Cdd:PRK13548 98 AMGRaphGLSRAEDDALVAAALAQVDLAHLAGRDYPQ-------LSGGEQQRVQLARVlaqLWEPDGpprWLLLDEPTSA 170
|
....*
gi 45552357 801 VD-AH 804
Cdd:PRK13548 171 LDlAH 175
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
664-849 |
1.19e-09 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 59.37 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK--------------LAYVP----QQAWIQNATV 725
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairagIAYVPedrkREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 726 RDNILFGQTydrkrynkvidacalradidilsagdlteigekginLSGGQKQRISLARAVYSDADLYLLDDPLSAVDahV 805
Cdd:cd03215 96 AENIALSSL------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVD--V 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 45552357 806 G--KHIFEEVIgpkgILARKSR--VLVThgvTFLPQV----DSIYVIKMGEI 849
Cdd:cd03215 138 GakAEIYRLIR----ELADAGKavLLIS---SELDELlglcDRILVMYEGRI 182
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
656-814 |
1.30e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 60.11 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 656 FSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK-LAYVPQQAWIQNA----------- 723
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdISTLKPEIYRQQVsycaqtptlfg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 724 -TVRDNILF-----GQTYDRKrynkvidacALRADIDILSAGDltEIGEKGIN-LSGGQKQRISLARAVYSDADLYLLDD 796
Cdd:PRK10247 95 dTVYDNLIFpwqirNQQPDPA---------IFLDDLERFALPD--TILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170
....*....|....*...
gi 45552357 797 PLSAVDAHvGKHIFEEVI 814
Cdd:PRK10247 164 ITSALDES-NKHNVNEII 180
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
649-804 |
1.42e-09 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 60.51 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 649 MSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK-------------LAYVP 715
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRplaawspwelarrRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 716 QQAWIQNA-TVRDNILFG---QTYDRKRYNKVIDACALRADIDILSAGDLTEigekginLSGGQKQRISLARA------- 784
Cdd:COG4559 82 QHSSLAFPfTVEEVVALGrapHGSSAAQDRQIVREALALVGLAHLAGRSYQT-------LSGGEQQRVQLARVlaqlwep 154
|
170 180
....*....|....*....|.
gi 45552357 785 VYSDADLYLLDDPLSAVD-AH 804
Cdd:COG4559 155 VDGGPRWLFLDEPTSALDlAH 175
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1326-1523 |
1.46e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 62.24 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1326 LRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIA-SMGLHMLRSRLTIIPQDpvlfsgslrINL 1404
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAIIYQE---------LHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1405 DPfEIKTDDEIWkaleLSHLKS---FV--KSLAAGLNHEIAEGGEN---------LSVGQRQLVCLARALLRKTKVLVLD 1470
Cdd:PRK11288 91 VP-EMTVAENLY----LGQLPHkggIVnrRLLNYEAREQLEHLGVDidpdtplkyLSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 1471 EATAAVDL-ETDDL--IQKTIRTEFKecTVLTIAHRLNTILD-SDKVIVLDKGQIIE 1523
Cdd:PRK11288 166 EPTSSLSArEIEQLfrVIRELRAEGR--VILYVSHRMEEIFAlCDAITVFKDGRYVA 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
649-830 |
1.48e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.56 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 649 MSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAfLGEMEKLAGVVNTVGKLAY--------------- 713
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRS-INRMNDLNPEVTITGSIVYnghniysprtdtvdl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 714 ------VPQQAWIQNATVRDNILFG----QTYDRKRYNKVIDACALRADI-----DILSagdlteigEKGINLSGGQKQR 778
Cdd:PRK14239 85 rkeigmVFQQPNPFPMSIYENVVYGlrlkGIKDKQVLDEAVEKSLKGASIwdevkDRLH--------DSALGLSGGQQQR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 45552357 779 ISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEVIGPKgilARKSRVLVTH 830
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLK---DDYTMLLVTR 205
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
664-830 |
1.66e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.59 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKL--AGVVNtvgklayVPQQAWIQNATVRDNILFGQTYDRKRYn 741
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTpvAGCVD-------VPDNQFGREASLIDAIGRKGDFKDAVE- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 742 kVIDACALrADIDILSAgdlteigeKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVD---AHVGKHIFEEvigpkg 818
Cdd:COG2401 118 -LLNAVGL-SDAVLWLR--------RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQK------ 181
|
170
....*....|....*
gi 45552357 819 iLARKSR---VLVTH 830
Cdd:COG2401 182 -LARRAGitlVVATH 195
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
333-561 |
1.70e-09 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 60.89 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 333 FLFGALMKLFTDTLTFAQPQVLSLIISFVEAQDAEpeWKGILYAVLLFVLAAAQTFILgQYFHRMFIVGL--RIRTALIN 410
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLT--ASQLLRYALLILLLALLIGIF-RFLWRYLIFGAsrRIEYDLRN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 411 AIYRKALRISNSTKKESTVGEIVNLMAVDAQRFMELTTY-LNMIWSAPLQIGLALYFLWQQLGPSVLAGLAVMIILIPVN 489
Cdd:cd18541 78 DLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPgILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 490 GVIASRI-KTYQIRQMKYKD--ERVKlmnEVLSGIKVLKLYAWEPS----FEKQVLDIRDKEIATLRSTAYLNAGTSFL 561
Cdd:cd18541 158 YRLGKKIhKRFRKVQEAFSDlsDRVQ---ESFSGIRVIKAFVQEEAeierFDKLNEEYVEKNLRLARVDALFFPLIGLL 233
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
648-802 |
1.93e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.03 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 648 PMSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK-------------LAYV 714
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpismlssrqlarrLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 715 PQQAWI-QNATVRDNILFGQ-----------TYDRKRYNKVIDacalRADIDILSAGDLTEigekginLSGGQKQRISLA 782
Cdd:PRK11231 82 PQHHLTpEGITVRELVAYGRspwlslwgrlsAEDNARVNQAME----QTRINHLADRRLTD-------LSGGQRQRAFLA 150
|
170 180
....*....|....*....|
gi 45552357 783 RAVYSDADLYLLDDPLSAVD 802
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLD 170
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
664-870 |
2.24e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.56 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVN--------------------TVGKLAYVPQQAWIQNa 723
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTvdditithktkdkyirpvrkRIGMVFQFPESQLFED- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 724 TVRDNILFGQtydrKRYNKVIDACALRADIDILSAGDLTEIGEKG-INLSGGQKQRISLARAVYSDADLYLLDDPLSAVD 802
Cdd:PRK13646 102 TVEREIIFGP----KNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSpFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 803 AHvGKHIFEEVIGPKGILARKSRVLVTHGVTFLPQ-VDSIYVIKMGEISESGTFDQLVKNKGAFADFII 870
Cdd:PRK13646 178 PQ-SKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKDKKKLADWHI 245
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1327-1537 |
2.70e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.72 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1327 RGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASmglhmlRSRLTIIPQDPVLFSGSLRIN--L 1404
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP------RSPLDAVKKGMAYITESRRDNgfF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1405 DPFEIKTDDEIWKALELSHLKSFV----------------KSLA---AGLNHEIAEggenLSVGQRQLVCLARALLRKTK 1465
Cdd:PRK09700 354 PNFSIAQNMAISRSLKDGGYKGAMglfhevdeqrtaenqrELLAlkcHSVNQNITE----LSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45552357 1466 VLVLDEATAAVDLETDDLIQKTIRTEFKEC-TVLTIAHRLNTILD-SDKVIVLDKGQIiefaspTELLDNPKSA 1537
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKAEIYKVMRQLADDGkVILMVSSELPEIITvCDRIAVFCEGRL------TQILTNRDDM 497
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
664-872 |
2.87e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.13 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNT--------------------VGKLAYVPQQAWIQNA 723
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstskqkeikpvrkkVGVVFQFPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 724 TVRDnILFG-QTYD-RKRYNKVIDACALRAdidilsAGDLTEIGEKG-INLSGGQKQRISLARAVYSDADLYLLDDPLSA 800
Cdd:PRK13643 102 VLKD-VAFGpQNFGiPKEKAEKIAAEKLEM------VGLADEFWEKSpFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 801 VD--AHVGKHIFEEVIGPKGilarKSRVLVTHGVTFLPQ-VDSIYVIKMGEISESGTFDQLVKNkgafADFIIQH 872
Cdd:PRK13643 175 LDpkARIEMMQLFESIHQSG----QTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE----VDFLKAH 241
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
670-800 |
2.87e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 61.72 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 670 EVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLAYVPQqaWI---QNATVRDNIlfgqtydRKRYNKVIDA 746
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQ--YIspdYDGTVEEFL-------RSANTDDFGS 432
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 747 CALRADIdiLSAGDLTEIGEKGI-NLSGGQKQRISLARAVYSDADLYLLDDPlSA 800
Cdd:COG1245 433 SYYKTEI--IKPLGLEKLLDKNVkDLSGGELQRVAIAACLSRDADLYLLDEP-SA 484
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
714-859 |
3.42e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.97 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 714 VPQQAWIQNATVRDNILFG-QTYDRKRYNKVIDACALRADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLY 792
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGkEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKIL 1380
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45552357 793 LLDDPLSAVDAHVGKHIFEEVIGPKGiLARKSRVLVTHGVTFLPQVDSIYVI----KMGEISES-GTFDQLV 859
Cdd:PTZ00265 1381 LLDEATSSLDSNSEKLIEKTIVDIKD-KADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQAhGTHEELL 1451
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
664-831 |
5.78e-09 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 57.75 E-value: 5.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVV----NTVGKLAYVPQQ--AWIQNA-------TVRDNIL 730
Cdd:TIGR01189 16 FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVrwngTPLAEQRDEPHEniLYLGHLpglkpelSALENLH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 731 FgqtydrkrYNKVIDAcalrADIDILSAgdLTEIGEKGIN------LSGGQKQRISLARAVYSDADLYLLDDPLSAVDAH 804
Cdd:TIGR01189 96 F--------WAAIHGG----AQRTIEDA--LAAVGLTGFEdlpaaqLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180 190
....*....|....*....|....*....|
gi 45552357 805 -VGK--HIFEEVIGPKGILarksrVLVTHG 831
Cdd:TIGR01189 162 gVALlaGLLRAHLARGGIV-----LLTTHQ 186
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
649-858 |
5.85e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 58.95 E-value: 5.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 649 MSIENGEFSWGDEITLRNIN---IEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKlAYVPQQAW------ 719
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVWnlrrki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 720 ---IQN-------ATVRDNILFGQTYDRKRYNKVIDacalRADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDA 789
Cdd:PRK13642 84 gmvFQNpdnqfvgATVEDDVAFGMENQGIPREEMIK----RVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 790 DLYLLDDPLSAVDAhVGKHIFEEVIGPKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEISESGTFDQL 858
Cdd:PRK13642 160 EIIILDESTSMLDP-TGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1326-1535 |
5.89e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.87 E-value: 5.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1326 LRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRII---EAAGGRISIDG----------VDIASMGLHM--------LRS 1384
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGrtvqregrlaRDIRKSRANTgyifqqfnLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1385 RLTIIPQDPVLFSGSL---RINLDPFEIKTDDEIWKALElshlksfvkslAAGLNHEIAEGGENLSVGQRQLVCLARALL 1461
Cdd:PRK09984 100 RLSVLENVLIGALGSTpfwRTCFSWFTREQKQRALQALT-----------RVGMVHFAHQRVSTLSGGQQQRVAIARALM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 1462 RKTKVLVLDEATAAVDLETDDLIQKTIR--TEFKECTVLTIAHRLNTILD-SDKVIVLDKGQIIeFASPTELLDNPK 1535
Cdd:PRK09984 169 QQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDYALRyCERIVALRQGHVF-YDGSSQQFDNER 244
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
651-858 |
6.46e-09 |
|
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: 57.76 E-value: 6.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 651 IENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG------------KLAYVPQQA 718
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 719 WIQNA-TVRDNI-LFGQTYDRKRynkviDACALRADiDILSAGDLTEIGEKGI-NLSGGQKQRISLARAVYSDADLYLLD 795
Cdd:cd03265 83 SVDDElTGWENLyIHARLYGVPG-----AERRERID-ELLDFVGLLEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552357 796 DPLSAVDAHVGKHIFEEVigpKGILARK--SRVLVTHGVTFLPQV-DSIYVIKMGEISESGTFDQL 858
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYI---EKLKEEFgmTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
659-861 |
6.95e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 59.66 E-value: 6.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 659 GDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG-----------------KLAYVPQQ-AWI 720
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSfALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 721 QNATVRDNILFGQTYD----RKRYNKVIDACAlRADIDILSAGDLTEigekginLSGGQKQRISLARAVYSDADLYLLDD 796
Cdd:PRK10070 119 PHMTVLDNTAFGMELAginaEERREKALDALR-QVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552357 797 PLSAVDAHVGKHIFEEVIGPKGILARkSRVLVTHGVTFLPQV-DSIYVIKMGEISESGTFDQLVKN 861
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVKLQAKHQR-TIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1321-1534 |
7.07e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 58.46 E-value: 7.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1321 GLdLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHM--------------LRSRL 1386
Cdd:PRK11300 17 GL-LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiarmgvvrtfqhvrLFREM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1387 TIIPQDPV---------LFSGSLriNLDPFEIKTDDEIWKA---LELSHLKSFVKSlAAGlnheiaeggeNLSVGQRQLV 1454
Cdd:PRK11300 96 TVIENLLVaqhqqlktgLFSGLL--KTPAFRRAESEALDRAatwLERVGLLEHANR-QAG----------NLAYGQQRRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1455 CLARALLRKTKVLVLDEATAAVD-LETDDLIQ--KTIRTEFKeCTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTEL 1530
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNpKETKELDEliAELRNEHN-VTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
....
gi 45552357 1531 LDNP 1534
Cdd:PRK11300 242 RNNP 245
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
664-854 |
8.22e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 58.55 E-value: 8.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK--------LAYVPQQAWI--QNA-------TVR 726
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydkksLLEVRKTVGIvfQNPddqlfapTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 727 DNILFGQTY----DRKRYNKVIDAcalradidilsagdLTEIGEKGI------NLSGGQKQRISLARAVYSDADLYLLDD 796
Cdd:PRK13639 98 EDVAFGPLNlglsKEEVEKRVKEA--------------LKAVGMEGFenkpphHLSGGQKKRVAIAGILAMKPEIIVLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45552357 797 PLSAVDAHVGKHIFEEV--IGPKGIlarkSRVLVTHGVTFLP-QVDSIYVIKMGEISESGT 854
Cdd:PRK13639 164 PTSGLDPMGASQIMKLLydLNKEGI----TIIISTHDVDLVPvYADKVYVMSDGKIIKEGT 220
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
664-872 |
8.47e-09 |
|
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: 58.38 E-value: 8.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG-------------KLAYVPQQAWIQNATVRDNIL 730
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSGSIRFNLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 731 FGQTYDRKRYNKVIDACALRADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVgKHIF 810
Cdd:cd03288 117 PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT-ENIL 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45552357 811 EEVIgpKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEISESGTFDQLVKNK-GAFADFIIQH 872
Cdd:cd03288 196 QKVV--MTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLVRTD 256
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
641-830 |
9.61e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 58.12 E-value: 9.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 641 HDSSKPHPMSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAF-----L-------GEMEkLAGV---- 704
Cdd:COG1117 4 PASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndLipgarveGEIL-LDGEdiyd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 705 --VNTVG---KLAYVPQQAwiqN---ATVRDNILFGQtydrkRYNKVIDacalRADIDilsagdltEIGEK--------- 767
Cdd:COG1117 83 pdVDVVElrrRVGMVFQKP---NpfpKSIYDNVAYGL-----RLHGIKS----KSELD--------EIVEEslrkaalwd 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 768 ---------GINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIfEEVigpkgILARKSR---VLVTH 830
Cdd:COG1117 143 evkdrlkksALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKI-EEL-----ILELKKDytiVIVTH 211
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1324-1522 |
9.62e-09 |
|
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: 57.67 E-value: 9.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1324 LVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAG---GRISIDGVDiasMGLHMLRSRLTIIPQDPVLFSG-- 1398
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQP---RKPDQFQKCVAYVRQDDILLPGlt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1399 -----------SLRINLDPFEIKTDDEIWKALELSHLKsfvkslaagLNHEIAEGgenLSVGQRQLVCLARALLRKTKVL 1467
Cdd:cd03234 98 vretltytailRLPRKSSDAIRKKRVEDVLLRDLALTR---------IGGNLVKG---ISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 1468 VLDEATAAVDLETDDLIQKTIR-TEFKECTVLTIAHRLNTILDS--DKVIVLDKGQII 1522
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSqLARRNRIVILTIHQPRSDLFRlfDRILLLSSGEIV 223
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1321-1531 |
1.05e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 58.07 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1321 GLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPVlfsgsl 1400
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNAT------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1401 rinlDPFEIKTDDEI-------------WKALELSHLKSFVKslAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKVL 1467
Cdd:PRK10253 92 ----TPGDITVQELVargryphqplftrWRKEDEEAVTKAMQ--ATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 1468 VLDEATAAVDLETD----DLIQKTIRTefKECTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELL 1531
Cdd:PRK10253 166 LLDEPTTWLDISHQidllELLSELNRE--KGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1309-1535 |
1.17e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 57.87 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYreGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFR---IIEA--AGGRISIDGVDIASMGLH--M 1381
Cdd:PRK14243 11 LRTENLNVYY--GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGfrVEGKVTFHGKNLYAPDVDpvE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1382 LRSRLTIIPQDPVLFSGSL--------RINldPFEIKTDDEIWKALELSHLKSFVKSlaaglnhEIAEGGENLSVGQRQL 1453
Cdd:PRK14243 89 VRRRIGMVFQKPNPFPKSIydniaygaRIN--GYKGDMDELVERSLRQAALWDEVKD-------KLKQSGLSLSGGQQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1454 VCLARALLRKTKVLVLDEATAAVD----LETDDLIQktirtEFKE-CTVLTIAHRL-------------NTILDSDKVIV 1515
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALDpistLRIEELMH-----ELKEqYTIIIVTHNMqqaarvsdmtaffNVELTEGGGRY 234
|
250 260
....*....|....*....|
gi 45552357 1516 ldkGQIIEFASPTELLDNPK 1535
Cdd:PRK14243 235 ---GYLVEFDRTEKIFNSPQ 251
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1309-1533 |
1.32e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 57.20 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYreGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIAS-MGLHMLRSRLT 1387
Cdd:PRK11614 6 LSFDKVSAHY--GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1388 IIPQDPVLFSG-SLRINLDPFEIKTDDEIWKalelsHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKV 1466
Cdd:PRK11614 84 IVPEGRRVFSRmTVEENLAMGGFFAERDQFQ-----ERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45552357 1467 LVLDEATAA----VDLETDDLIQKtIRTEfkECTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDN 1533
Cdd:PRK11614 159 LLLDEPSLGlapiIIQQIFDTIEQ-LREQ--GMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALLAN 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
664-861 |
1.34e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 58.14 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEME------------------KLAGVVNTVGKLAYVPQQAWIQNaTV 725
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKptsgkiiidgvditdkkvKLSDIRKKVGLVFQYPEYQLFEE-TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 726 RDNILFGQT----YDRKRYNKVIDAcalradIDILSAgDLTEIGEKG-INLSGGQKQRISLARAVYSDADLYLLDDPLSA 800
Cdd:PRK13637 102 EKDIAFGPInlglSEEEIENRVKRA------MNIVGL-DYEDYKDKSpFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45552357 801 VDAHVGKHIFEEVigpKGILARKSR--VLVTHGVTFLPQ-VDSIYVIKMGEISESGTFDQLVKN 861
Cdd:PRK13637 175 LDPKGRDEILNKI---KELHKEYNMtiILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVFKE 235
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
644-854 |
1.65e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 57.50 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 644 SKPHPMSIENGEFSWGD--EITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEM--EKLAGVVNTVGKLAYVPQQAW 719
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpDDNPNSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 720 ---------IQN-------ATVRDNILFG---QTYDRKRYNKVIDacalradiDILSAGDLTE-IGEKGINLSGGQKQRI 779
Cdd:PRK13640 81 direkvgivFQNpdnqfvgATVGDDVAFGlenRAVPRPEMIKIVR--------DVLADVGMLDyIDSEPANLSGGQKQRV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 780 SLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEVIGpkgiLARKSRVLV---THGVTFLPQVDSIYVIKMGEISESGT 854
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRK----LKKKNNLTVisiTHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1309-1531 |
1.95e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.44 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLDLVLRG---VSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMG----LHM 1381
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRAlfdIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1382 LRSRLTIIPQDP--VLFSGSL--RINLDPFEIKTDDEIWKALELSHLKsfvkslAAGLNHEIAEGGE-NLSVGQRQLVCL 1456
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVlkDVAFGPQNFGIPKEKAEKIAAEKLE------MVGLADEFWEKSPfELSGGQMRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 1457 ARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKEC-TVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELL 1531
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGqTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVF 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
664-811 |
2.61e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 57.15 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK-------------------LAYVPQQAWIQNAT 724
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpetgnknlkklrkkvsLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 725 VRDNILFGQtydrKRYNKVIDACALRADIDILSAGDLTEIGEKG-INLSGGQKQRISLARAVYSDADLYLLDDPLSAVDA 803
Cdd:PRK13641 103 VLKDVEFGP----KNFGFSEDEAKEKALKWLKKVGLSEDLISKSpFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
....*...
gi 45552357 804 HVGKHIFE 811
Cdd:PRK13641 179 EGRKEMMQ 186
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
649-802 |
2.62e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 56.63 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 649 MSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVvqafLGEMEKL----AGVVNTVG-------------KL 711
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTL----LSMISRLlppdSGEVLVDGldvattpsrelakRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 712 AYVPQQawiqNA-----TVRDNILFGQ-TYDRKRYNK----VIDacalRAdIDILsagDLTEIGEKGIN-LSGGQKQRIS 780
Cdd:COG4604 78 AILRQE----NHinsrlTVRELVAFGRfPYSKGRLTAedreIID----EA-IAYL---DLEDLADRYLDeLSGGQRQRAF 145
|
170 180
....*....|....*....|..
gi 45552357 781 LARAVYSDADLYLLDDPLSAVD 802
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLD 167
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
659-803 |
3.44e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 55.58 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 659 GDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK------------LAYVPQQAWIQNA-TV 725
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldfqrdsiargLLYLGHAPGIKTTlSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 726 RDNILFgqtydrkrynkvidACALRADIDILSAgdLTEIGEKGI------NLSGGQKQRISLARAVYSDADLYLLDDPLS 799
Cdd:cd03231 91 LENLRF--------------WHADHSDEQVEEA--LARVGLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
....
gi 45552357 800 AVDA 803
Cdd:cd03231 155 ALDK 158
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
659-849 |
3.57e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 58.20 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 659 GDEIT--LRNINIEVKKGSLVALVGTVGSGKSSVVQaFLGEMEK-LAGVVNTVGklayvpqqawiQN-ATVRDNIL---- 730
Cdd:PRK10535 17 GEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKpTSGTYRVAG-----------QDvATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 731 ---FGQTYDRKRYNKVIDAcALRADIDILSAGD------------LTEIG-EKGIN-----LSGGQKQRISLARAVYSDA 789
Cdd:PRK10535 85 rehFGFIFQRYHLLSHLTA-AQNVEVPAVYAGLerkqrllraqelLQRLGlEDRVEyqpsqLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45552357 790 DLYLLDDPLSAVDAHVGkhifEEVIGPKGILARKSR--VLVTHGVTFLPQVDSIYVIKMGEI 849
Cdd:PRK10535 164 QVILADEPTGALDSHSG----EEVMAILHQLRDRGHtvIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
656-853 |
3.93e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 56.55 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 656 FSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLAYVPQQAWI----QNATVRdnilf 731
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLalrqQVATVF----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 732 gQTYDRKRYNKVID---ACALR------ADI-----DILSAGDLTEIGEKGIN-LSGGQKQRISLARAVYSDADLYLLDD 796
Cdd:PRK13638 84 -QDPEQQIFYTDIDsdiAFSLRnlgvpeAEItrrvdEALTLVDAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 797 PLSAVDAhVGKHIFEEVIgpKGILARKSRVLV-THGVTFLPQV-DSIYVIKMGEISESG 853
Cdd:PRK13638 163 PTAGLDP-AGRTQMIAII--RRIVAQGNHVIIsSHDIDLIYEIsDAVYVLRQGQILTHG 218
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1329-1535 |
5.21e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 56.67 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1329 VSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAG----GRISIDGVDIASMGLHMLR----SRLTIIPQDPVlfsgsl 1400
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGrvmaEKLEFNGQDLQRISEKERRnlvgAEVAMIFQDPM------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1401 rINLDP-----FEI------------KTDDEiwKALELSHLKSfVKSLAAGLN---HEiaeggenLSVGQRQLVCLARAL 1460
Cdd:PRK11022 100 -TSLNPcytvgFQImeaikvhqggnkKTRRQ--RAIDLLNQVG-IPDPASRLDvypHQ-------LSGGMSQRVMIAMAI 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 1461 LRKTKVLVLDEATAAVDLETD-DLIQKTIRTEFKECTVLT-IAHRLNTILDS-DKVIVLDKGQIIEFASPTELLDNPK 1535
Cdd:PRK11022 169 ACRPKLLIADEPTTALDVTIQaQIIELLLELQQKENMALVlITHDLALVAEAaHKIIVMYAGQVVETGKAHDIFRAPR 246
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
664-861 |
6.47e-08 |
|
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: 56.21 E-value: 6.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLG-------------------------EMEKLAGvvntvGKLAYVPQQA 718
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpppgitsgeilfdgedllklsekELRKIRG-----REIQMIFQDP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 719 wiQNA-----TVRDNI-----LFGQTYDRKRYNKVIDAcalradidilsagdLTEIG----EKGIN-----LSGGQKQRI 779
Cdd:COG0444 96 --MTSlnpvmTVGDQIaeplrIHGGLSKAEARERAIEL--------------LERVGlpdpERRLDrypheLSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 780 SLARAVYSDADLYLLDDPLSAVDAHVGKHI---FEEvigpkgiLARKSR---VLVTH--GVtflpqV----DSIYVIKMG 847
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQIlnlLKD-------LQRELGlaiLFITHdlGV-----VaeiaDRVAVMYAG 227
|
250
....*....|....
gi 45552357 848 EISESGTFDQLVKN 861
Cdd:COG0444 228 RIVEEGPVEELFEN 241
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1332-1517 |
6.64e-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: 6.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1332 NIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASmglhmlrSRLTIIPQDPV----LFSGSLRINLDPF 1407
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY-------KPQYIKADYEGtvrdLLSSITKDFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1408 EIKTddEIWKALELSHLksfvkslaagLNHEIAEggenLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKT 1487
Cdd:cd03237 94 YFKT--EIAKPLQIEQI----------LDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKV 157
|
170 180 190
....*....|....*....|....*....|...
gi 45552357 1488 IR--TEFKECTVLTIAHRLNTI-LDSDKVIVLD 1517
Cdd:cd03237 158 IRrfAENNEKTAFVVEHDIIMIdYLADRLIVFE 190
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
660-858 |
6.74e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.89 E-value: 6.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 660 DEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLaYVPQQAW---------IQN-------A 723
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL-LTEENVWdirhkigmvFQNpdnqfvgA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 724 TVRDNILFGQTydrkryNKVIDACALRADID-ILSAGDLTEIGEKG-INLSGGQKQRISLARAVYSDADLYLLDDPLSAV 801
Cdd:PRK13650 98 TVEDDVAFGLE------NKGIPHEEMKERVNeALELVGMQDFKEREpARLSGGQKQRVAIAGAVAMRPKIIILDEATSML 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 802 DahvgkhifeevigPKGIL-----ARKSR-------VLVTHGVTFLPQVDSIYVIKMGEISESGTFDQL 858
Cdd:PRK13650 172 D-------------PEGRLeliktIKGIRddyqmtvISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1326-1521 |
6.85e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.94 E-value: 6.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1326 LRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASmglhmlRSrltiiPQDPvLFSGSLRINLD 1405
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVT------RS-----PQDG-LANGIVYISED 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1406 PfeiKTDDEIwkaLELShlksfVK---SLAA---------GLNH--EIAEGGE-----------------NLSVGQRQLV 1454
Cdd:PRK10762 336 R---KRDGLV---LGMS-----VKenmSLTAlryfsraggSLKHadEQQAVSDfirlfniktpsmeqaigLLSGGNQQKV 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45552357 1455 CLARALLRKTKVLVLDEATAAVDL----ETDDLIQKtirteFKE--CTVLTIAHRLNTILD-SDKVIVLDKGQI 1521
Cdd:PRK10762 405 AIARGLMTRPKVLILDEPTRGVDVgakkEIYQLINQ-----FKAegLSIILVSSEMPEVLGmSDRILVMHEGRI 473
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1321-1523 |
6.86e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 55.41 E-value: 6.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1321 GLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSL--TLALFRIieAAGGRISIDG------VDIASMGLHMLRSRLTIIPQd 1392
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLlrVLNLLEM--PRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQ- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1393 pvlfsgslRINLDPFEIKTDDEI---WKALELShlKSFVKSLAAGL--NHEIAEGGE----NLSVGQRQLVCLARALLRK 1463
Cdd:PRK11124 90 --------QYNLWPHLTVQQNLIeapCRVLGLS--KDQALARAEKLleRLRLKPYADrfplHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45552357 1464 TKVLVLDEATAAVDLETDDLIQKTIRtEFKEC--TVLTIAHRLNTILD-SDKVIVLDKGQIIE 1523
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIR-ELAETgiTQVIVTHEVEVARKtASRVVYMENGHIVE 221
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1309-1538 |
7.52e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 56.39 E-value: 7.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYrEGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSltlaLFRIIeaAG------GRISIDG--V-------- 1372
Cdd:PRK11650 4 LKLQAVRKSY-DGKTQVIKGIDLDVADGEFIVLVGPSGCGKST----LLRMV--AGleritsGEIWIGGrvVnelepadr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1373 DIAsM-----GL--HM---------LRSRltiipqdpvlfsgslriNLDPFEIKTD-DEIWKALELSHLksfvkslaagL 1435
Cdd:PRK11650 77 DIA-MvfqnyALypHMsvrenmaygLKIR-----------------GMPKAEIEERvAEAARILELEPL----------L 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1436 NHEIAEggenLSVGQRQLVCLARALLRKTKVLVLDEATAAVD--------LETDDLiQKTIRTefkecTVLTIAHrlnti 1507
Cdd:PRK11650 129 DRKPRE----LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDaklrvqmrLEIQRL-HRRLKT-----TSLYVTH----- 193
|
250 260 270
....*....|....*....|....*....|....*...
gi 45552357 1508 lD-------SDKVIVLDKGQIIEFASPTELLDNPKSAF 1538
Cdd:PRK11650 194 -DqveamtlADRVVVMNGGVAEQIGTPVEVYEKPASTF 230
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1325-1545 |
7.62e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 57.04 E-value: 7.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMG---LHMLR--------SRLTIIP--- 1390
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadaLAQLRrehfgfifQRYHLLShlt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1391 -----QDPVLFSGSLRinldpfeiKTDDEIWKALeLSHLksfvkslaaGLNHEIAEGGENLSVGQRQLVCLARALLRKTK 1465
Cdd:PRK10535 103 aaqnvEVPAVYAGLER--------KQRLLRAQEL-LQRL---------GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1466 VLVLDEATAAVDLETDD---LIQKTIRTefKECTVLTIAHRLNTILDSDKVIVLDKGQIIEfASPTELLDNPKSAFYSMA 1542
Cdd:PRK10535 165 VILADEPTGALDSHSGEevmAILHQLRD--RGHTVIIVTHDPQVAAQAERVIEIRDGEIVR-NPPAQEKVNVAGGTEPVV 241
|
...
gi 45552357 1543 KDA 1545
Cdd:PRK10535 242 NTA 244
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
657-860 |
8.49e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 56.27 E-value: 8.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 657 SWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGeMEKlagvvNTVGKLAY----VPQQAwIQNatvRDNILFG 732
Cdd:PRK11432 15 RFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAG-LEK-----PTEGQIFIdgedVTHRS-IQQ---RDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 733 QTY----------------------DRKRYNKVIDACALRadidilsagDLTEIGEKGIN-LSGGQKQRISLARAVYSDA 789
Cdd:PRK11432 85 QSYalfphmslgenvgyglkmlgvpKEERKQRVKEALELV---------DLAGFEDRYVDqISGGQQQRVALARALILKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 790 DLYLLDDPLSAVDAHVGKHIFE---EVIGPKGIlarkSRVLVTHGVTFLPQV-DSIYVIKMGEISESGTFDQLVK 860
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREkirELQQQFNI----TSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQELYR 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
650-853 |
9.01e-08 |
|
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: 54.51 E-value: 9.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 650 SIENGEFSWGDEITLRNINIEVKKGsLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG------------KLAYVPQQ 717
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 718 -AWIQNATVRDNIlfgqtydrkRYN---KVIDACALRADID-ILSAGDLTEIGEKGIN-LSGGQKQRISLARAVYSDADL 791
Cdd:cd03264 81 fGVYPNFTVREFL---------DYIawlKGIPSKEVKARVDeVLELVNLGDRAKKKIGsLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 792 YLLDDPLSAVDAhvgkhifEEVIGPKGILAR----KSRVLVTHGVTflpQVDSIY----VIKMGEISESG 853
Cdd:cd03264 152 LIVDEPTAGLDP-------EERIRFRNLLSElgedRIVILSTHIVE---DVESLCnqvaVLNKGKLVFEG 211
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
664-847 |
1.03e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 53.48 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAflgemeklagVVNTVGKLAYVPqqawiqnatvrdnilFGQTYDrkrYNKV 743
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNE----------GLYASGKARLIS---------------FLPKFS---RNKL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 744 IDACALRADIDiLSAGDLTeIGEKGINLSGGQKQRISLARAVYSDAD--LYLLDDPLSAVDaHVGKHIFEEVIgpKGILA 821
Cdd:cd03238 63 IFIDQLQFLID-VGLGYLT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH-QQDINQLLEVI--KGLID 137
|
170 180
....*....|....*....|....*..
gi 45552357 822 RKSRV-LVTHGVTFLPQVDsiYVIKMG 847
Cdd:cd03238 138 LGNTViLIEHNLDVLSSAD--WIIDFG 162
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
664-860 |
1.04e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.57 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSS-------VVQAFLGEME--------------KLAGVvntvgklAYVPQQ-AWIQ 721
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTlmkilsgVYQPDSGEILldgepvrfrsprdaQAAGI-------AIIHQElNLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 722 NATVRDNILFGQ------TYDRKRYNKviDACAL--RADIDIlsagDL-TEIGEkginLSGGQKQRISLARAVYSDADLY 792
Cdd:COG1129 93 NLSVAENIFLGReprrggLIDWRAMRR--RARELlaRLGLDI----DPdTPVGD----LSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 793 LLDDPLSAVDAHVGKHIFEevigpkgILAR-KSR----VLVTHgvtFLPQV----DSIYVIKMGEISESG-----TFDQL 858
Cdd:COG1129 163 ILDEPTASLTEREVERLFR-------IIRRlKAQgvaiIYISH---RLDEVfeiaDRVTVLRDGRLVGTGpvaelTEDEL 232
|
..
gi 45552357 859 VK 860
Cdd:COG1129 233 VR 234
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
664-801 |
1.09e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.33 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG--------KLAY------VPQQ-AWIQNATVRDN 728
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhKLAAqlgigiIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552357 729 ILFGQTYDRKRYN-KVIDACALR--ADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAV 801
Cdd:PRK09700 101 LYIGRHLTKKVCGvNIIDWREMRvrAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1445-1523 |
1.24e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 56.34 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1445 NLSVGQRQLVCLARALLRKTKVLVLDEATAAVDlETD-----DLIqktirTEFKE--CTVLTIAHRLNTILD-SDKVIVL 1516
Cdd:NF040905 139 DIGVGKQQLVEIAKALSKDVKLLILDEPTAALN-EEDsaallDLL-----LELKAqgITSIIISHKLNEIRRvADSITVL 212
|
....*..
gi 45552357 1517 DKGQIIE 1523
Cdd:NF040905 213 RDGRTIE 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1326-1521 |
1.26e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 54.11 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1326 LRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMG---LHMLRSRLTIIPQD-PVLFSGSLR 1401
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRRQIGMIFQDhHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1402 INLD-PFEIK--TDDEIWKALELSHLKsfVKSLAAGLNHEIaeggeNLSVGQRQLVCLARALLRKTKVLVLDEATAAVDl 1478
Cdd:PRK10908 98 DNVAiPLIIAgaSGDDIRRRVSAALDK--VGLLDKAKNFPI-----QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD- 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 45552357 1479 etDDLIQKTIR--TEFKE--CTVLTIAHRLNTILDSD-KVIVLDKGQI 1521
Cdd:PRK10908 170 --DALSEGILRlfEEFNRvgVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1326-1531 |
1.35e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.79 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1326 LRGVSFNIQG-------------GEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQD 1392
Cdd:PRK10575 14 LRNVSFRVPGrtllhplsltfpaGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1393 -PVLFSGSLR----INLDP-------FEIKTDDEIWKALELSHLKSFVKSLAaglnheiaeggENLSVGQRQLVCLARAL 1460
Cdd:PRK10575 94 lPAAEGMTVRelvaIGRYPwhgalgrFGAADREKVEEAISLVGLKPLAHRLV-----------DSLSGGERQRAWIAMLV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552357 1461 LRKTKVLVLDEATAAVDL----ETDDLIQKTIRTefKECTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELL 1531
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDIahqvDVLALVHRLSQE--RGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELM 236
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
1032-1279 |
1.95e-07 |
|
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: 54.37 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1032 LGVYGAFGFGQVFSYIGSVVIVYLGaligtRKIFIQL----FGNILHAPQAYFDIKPRARILDRLaNDIYKLDVVLPELI 1107
Cdd:cd18570 46 IGLILLYLFQSLLSYIRSYLLLKLS-----QKLDIRLilgyFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1108 RVFNSQVFRVLAT-IVVISLSTPIFLAVIVPI---AFLYYFAQRFYVATSRQLMRLESVsrspIYSHFSETVTGASTIRA 1183
Cdd:cd18570 120 ISLFLDLLMVIISgIILFFYNWKLFLITLLIIplyILIILLFNKPFKKKNREVMESNAE----LNSYLIESLKGIETIKS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1184 YNVGDRFIEESDAKVDK--NQVCKYpSVIANRWLAIR--LEMVGNLIILFASLFAVLGGQTNPG-LVGLsvsYALQV--T 1256
Cdd:cd18570 196 LNAEEQFLKKIEKKFSKllKKSFKL-GKLSNLQSSIKglISLIGSLLILWIGSYLVIKGQLSLGqLIAF---NALLGyfL 271
|
250 260
....*....|....*....|...
gi 45552357 1257 QTLNWLVRMSSDIETNIVSVERI 1279
Cdd:cd18570 272 GPIENLINLQPKIQEAKVAADRL 294
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1326-1522 |
2.01e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 55.60 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1326 LRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRI---------IEAAGGRISIDGV-DIASMGLHMLRSRLTIIPQDPVL 1395
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgtwdgeIYWSGSPLKASNIrDTERAGIVIIHQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1396 ---FSGSlRINLdPFEIKTDDEIWkaLELSHLKSFVKSLAAGLNHEIAEGGenlsVGQRQLVCLARALLRKTKVLVLDEA 1472
Cdd:TIGR02633 97 eniFLGN-EITL-PGGRMAYNAMY--LRAKNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 45552357 1473 TAAV-DLETDDLIQKTIRTEFKECTVLTIAHRLNTILD-SDKVIVLDKGQII 1522
Cdd:TIGR02633 169 SSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1326-1533 |
2.01e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 54.63 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1326 LRGVSFNIQGGEKVGIVGRTGAGKSS---LTLALfrIIEAAGGRISIDGVDIASMG----LHMLRSRLTIIPQDP--VLF 1396
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTmiqLTNGL--IISETGQTIVGDYAIPANLKkikeVKRLRKEIGLVFQFPeyQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1397 SGSLR--INLDPFEIKTD-DEIWKAL-ELSHLKSFVKSLAAGLNHEiaeggenLSVGQRQLVCLARALLRKTKVLVLDEA 1472
Cdd:PRK13645 105 QETIEkdIAFGPVNLGENkQEAYKKVpELLKLVQLPEDYVKRSPFE-------LSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 1473 TAAVDLE-TDDLIQKTIR--TEFKEcTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDN 1533
Cdd:PRK13645 178 TGGLDPKgEEDFINLFERlnKEYKK-RIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
649-802 |
2.26e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.03 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 649 MSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK------------LAYVPQ 716
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlctyqkqLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 717 QAWIQ-NATVRDNILFGQTYDRKryNKVIDACalradIDILSAGDLTEIgEKGInLSGGQKQRISLARAVYSDADLYLLD 795
Cdd:PRK13540 82 RSGINpYLTLRENCLYDIHFSPG--AVGITEL-----CRLFSLEHLIDY-PCGL-LSSGQKRQVALLRLWMSKAKLWLLD 152
|
....*..
gi 45552357 796 DPLSAVD 802
Cdd:PRK13540 153 EPLVALD 159
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
664-851 |
2.71e-07 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 53.21 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSV--------------VQAF------LGEmEKLAGVVNtvGKLAYVpQQAW--IQ 721
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLlgllagldrptsgtVRLAgqdlfaLDE-DARARLRA--RHVGFV-FQSFqlLP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 722 NATVRDNI-----LFGQTYDRKRYNKVIDACALRADIDILSAGdlteigekginLSGGQKQRISLARAVYSDADLYLLDD 796
Cdd:COG4181 104 TLTALENVmlpleLAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFADE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45552357 797 PLSAVDAHVGKHI----FEevigpkgiLARKSR---VLVTHGVTFLPQVDSIYVIKMGEISE 851
Cdd:COG4181 173 PTGNLDAATGEQIidllFE--------LNRERGttlVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1322-1529 |
2.91e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 54.50 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1322 LDLVLRGVSfniqggekvGIVGRTGAGKSSLTLALFRIIEAAGGRISIDG---VDIAS-MGLHMLRSRLTIIPQDPVLF- 1396
Cdd:PRK11144 19 LTLPAQGIT---------AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgICLPPEKRRIGYVFQDARLFp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1397 ----SGSLRINLDPFEIKTDDEIWKALELSH-LKSFVKSLAaglnheiaeGGEnlsvgqRQLVCLARALLRKTKVLVLDE 1471
Cdd:PRK11144 90 hykvRGNLRYGMAKSMVAQFDKIVALLGIEPlLDRYPGSLS---------GGE------KQRVAIGRALLTAPELLLMDE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 1472 ATAAVD----------LETddlIQKTIRTefkecTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTE 1529
Cdd:PRK11144 155 PLASLDlprkrellpyLER---LAREINI-----PILYVSHSLDEILRlADRVVVLEQGKVKAFGPLEE 215
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
664-804 |
2.95e-07 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 52.55 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLG--EMEKLAGVVNTVGK----------LAYVPQQ-AWIQNATVRDNIL 730
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRpldkrsfrkiIGYVPQDdILHPTLTVRETLM 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45552357 731 FgqtydrkrynkvidACALRadidilsagdlteigekgiNLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAH 804
Cdd:cd03213 105 F--------------AAKLR-------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
664-804 |
3.03e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.68 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEK--LAGVVNTVGKL-------------------AYVPQQAwiQN 722
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGggAPRGARVTGDVtlngeplaaidaprlarlrAVLPQAA--QP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 723 A---TVRDNILFGQTYDRKR------YNKVIDACAL-RADIDILSAGDLTeigekgiNLSGGQKQRISLARAV------- 785
Cdd:PRK13547 95 AfafSAREIVLLGRYPHARRagalthRDGEIAWQALaLAGATALVGRDVT-------TLSGGELARVQFARVLaqlwpph 167
|
170 180
....*....|....*....|..
gi 45552357 786 --YSDADLYLLDDPLSAVD-AH 804
Cdd:PRK13547 168 daAQPPRYLLLDEPTAALDlAH 189
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
650-804 |
3.25e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.50 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 650 SIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK------------LAYVPQQ 717
Cdd:PRK13538 3 EARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEpirrqrdeyhqdLLYLGHQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 718 AWIQNA-TVRDNILFgqtydrkrynkvidACALRADID---ILSAgdLTEIGEKGI------NLSGGQKQRISLARAVYS 787
Cdd:PRK13538 83 PGIKTElTALENLRF--------------YQRLHGPGDdeaLWEA--LAQVGLAGFedvpvrQLSAGQQRRVALARLWLT 146
|
170
....*....|....*..
gi 45552357 788 DADLYLLDDPLSAVDAH 804
Cdd:PRK13538 147 RAPLWILDEPFTAIDKQ 163
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
647-853 |
4.05e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.20 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 647 HPMSIENGEFSWGDEI-TLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLAYVPQQAWIQN--- 722
Cdd:PRK13647 3 NIIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSkvg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 723 ------------ATVRDNILFG---QTYDRKRYNKVIDAcALRADidilsagDLTEIGEKG-INLSGGQKQRISLARAVY 786
Cdd:PRK13647 83 lvfqdpddqvfsSTVWDDVAFGpvnMGLDKDEVERRVEE-ALKAV-------RMWDFRDKPpYHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45552357 787 SDADLYLLDDPLSAVDAHVGKHIFEevigpkgILAR-----KSRVLVTHGVTFLPQ-VDSIYVIKMGEISESG 853
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLME-------ILDRlhnqgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEG 220
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1309-1530 |
4.27e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.21 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYREGLDL---VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMG----LHM 1381
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1382 LRSRLTIIPQDP--VLFSGSL--RINLDP--FEIKTDDEIWKALELSHLksfvkslaAGLNHEIAEGGE-NLSVGQRQLV 1454
Cdd:PRK13649 83 IRKKVGLVFQFPesQLFEETVlkDVAFGPqnFGVSQEEAEALAREKLAL--------VGISESLFEKNPfELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1455 CLARALLRKTKVLVLDEATAAVDLETddliQKTIRTEFKEC-----TVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPT 1528
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKG----RKELMTLFKKLhqsgmTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPK 230
|
..
gi 45552357 1529 EL 1530
Cdd:PRK13649 231 DI 232
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1326-1522 |
4.63e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.35 E-value: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1326 LRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDI--------ASMGLHMLRSRLTIIPQDPVLfs 1397
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksskeaLENGISMVHQELNLVLQRSVM-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1398 gslrinldpfeiktdDEIW------KALELSHLKSF--VKSLAAGLNHEI--AEGGENLSVGQRQLVCLARALLRKTKVL 1467
Cdd:PRK10982 92 ---------------DNMWlgryptKGMFVDQDKMYrdTKAIFDELDIDIdpRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 1468 VLDEATAAV-DLETDDLIqkTIRTEFKE--CTVLTIAHRLNTILD-SDKVIVLDKGQII 1522
Cdd:PRK10982 157 IMDEPTSSLtEKEVNHLF--TIIRKLKErgCGIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
1043-1279 |
4.71e-07 |
|
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: 53.33 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1043 VFSYIGSVVIVYLGALIgTRKIFIQLFGNILHAPQAYFDIKPRARILDRLANDIYKL-DVVLPELIRVFNSQVFRVLATI 1121
Cdd:cd18557 51 VFTFVRYYLFNIAGERI-VARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLqSAVTDNLSQLLRNILQVIGGLI 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1122 VVISLS---TPIFLAVIVPIAFLYYFAQRFYVATSRQLmrLESVSRSPiySHFSETVTGASTIRAYNVGDRFIEESDAKV 1198
Cdd:cd18557 130 ILFILSwklTLVLLLVIPLLLIASKIYGRYIRKLSKEV--QDALAKAG--QVAEESLSNIRTVRSFSAEEKEIRRYSEAL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1199 DKNQVCKYPSVIAN---RWLAIRLEMVGNLIILFASLFAVLGGQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVS 1275
Cdd:cd18557 206 DRSYRLARKKALANalfQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGA 285
|
....
gi 45552357 1276 VERI 1279
Cdd:cd18557 286 SERV 289
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
660-802 |
4.88e-07 |
|
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: 51.39 E-value: 4.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 660 DEITLRNINIEVKKGSLVALVGTVGSGKSSVVQA-------FLGEMEKLAGvvntvGKLAYVPQQAWIQNATVRDNILFg 732
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAlaglwpwGSGRIGMPEG-----EDLLFLPQRPYLPLGTLREQLIY- 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 733 qTYDRKrynkvidacalradidilsagdlteigekginLSGGQKQRISLARAVYSDADLYLLDDPLSAVD 802
Cdd:cd03223 87 -PWDDV--------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
336-569 |
5.74e-07 |
|
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: 52.95 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 336 GALMKLFTDTLTFAQPQVLSLII-SFVEAQDAEPEWKGILYAVLLFVLAAAQTFILGQYFHrmfIVGLRIRTALINAIYR 414
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIdTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFN---IAGERIVARLRRDLFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 415 KALRISNSTKKESTVGEIVNLMAVDAQRFME-LTTYLNMIWSAPLQIGLALYFLW---QQLGPsvlaglaVMIILIPVNg 490
Cdd:cd18557 78 SLLRQEIAFFDKHKTGELTSRLSSDTSVLQSaVTDNLSQLLRNILQVIGGLIILFilsWKLTL-------VLLLVIPLL- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 491 VIASRIKTYQIRQM--KYKDERVKLM---NEVLSGIKVLKLYAWEP----SFEKQVLDIRDKEIATLRSTAYLNAGTSFL 561
Cdd:cd18557 150 LIASKIYGRYIRKLskEVQDALAKAGqvaEESLSNIRTVRSFSAEEkeirRYSEALDRSYRLARKKALANALFQGITSLL 229
|
....*...
gi 45552357 562 WSCAPFLV 569
Cdd:cd18557 230 IYLSLLLV 237
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1336-1519 |
6.17e-07 |
|
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: 50.45 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1336 GEKVGIVGRTGAGKSSLTLALFRIIEAAGGRIsidgvdiasmglhmlrsrltiipqdpvlfsgsLRINLDPFEIKTDDEI 1415
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------------IYIDGEDILEEVLDQL 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1416 WkalelshlksfvkslaaglNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKE- 1494
Cdd:smart00382 50 L-------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLl 110
|
170 180 190
....*....|....*....|....*....|....*..
gi 45552357 1495 ------CTVLTIAHRLNTILD------SDKVIVLDKG 1519
Cdd:smart00382 111 lkseknLTVILTTNDEKDLGPallrrrFDRRIVLLLI 147
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1298-1523 |
6.86e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.82 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1298 NKPKNWPqegRVEFQNFQVRYREGlDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASM 1377
Cdd:PRK10522 315 QAFPDWQ---TLELRNVTFAYQDN-GFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1378 GLHMLRSRLTIIPQDPVLFSGSLriNLDPFEIKTDD-EIW-KALELSHLKSFVkslaaglNHEIAEggENLSVGQRQLVC 1455
Cdd:PRK10522 391 QPEDYRKLFSAVFTDFHLFDQLL--GPEGKPANPALvEKWlERLKMAHKLELE-------DGRISN--LKLSKGQKKRLA 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 1456 LARALLRKTKVLVLDEATAAVDletddliqKTIRTEF--------KEC--TVLTIAHRLNTILDSDKVIVLDKGQIIE 1523
Cdd:PRK10522 460 LLLALAEERDILLLDEWAADQD--------PHFRREFyqvllpllQEMgkTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
452-851 |
7.10e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.82 E-value: 7.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 452 MIWSAPLQIGLALYFLWqqLGPSVLAGLAV-MIILIPVNGVIASRIKTYqIRQMKYKDERV-KLMNEVLSGIKVLKL--- 526
Cdd:PRK10522 128 LVQGIILTLGSAAYLAW--LSPKMLLVTAIwMAVTIWGGFVLVARVYKH-MATLRETEDKLyNDYQTVLEGRKELTLnre 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 527 ---YAWEPSFEKQVLDIRDKeiATLRSTAYLNAGTsflWSCAPFL--VSLVTF-------------ATYVLTseanqlsv 588
Cdd:PRK10522 205 raeYVFENEYEPDAQEYRHH--IIRADTFHLSAVN---WSNIMMLgaIGLVFYmanslgwadtnvaATYSLT-------- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 589 ekvlvsiALFdlMKLPLT----ILPMLsvdiAETQVSVNRINKFlnseELDPNSvlHDSSKPHP------MSIENGEFSW 658
Cdd:PRK10522 272 -------LLF--LRTPLLsavgALPTL----LSAQVAFNKLNKL----ALAPYK--AEFPRPQAfpdwqtLELRNVTFAY 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 659 GDE-ITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK-LAYVPQQAWIQ--NATVRDNILFGQT 734
Cdd:PRK10522 333 QDNgFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKpVTAEQPEDYRKlfSAVFTDFHLFDQL 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 735 YDRKryNKVIDACALRADIDILSAGDLTEIGE---KGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVgKHIFE 811
Cdd:PRK10522 413 LGPE--GKPANPALVEKWLERLKMAHKLELEDgriSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF-RREFY 489
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 45552357 812 EVIGPKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEISE 851
Cdd:PRK10522 490 QVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
660-858 |
7.48e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 52.36 E-value: 7.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 660 DEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLAYVPQQAWIQNA---------------- 723
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAiklrkevgmvfqqpnp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 724 ----TVRDNILF----GQTYDRKRYNKVIDACalradidILSAGDLTEIGEK----GINLSGGQKQRISLARAVYSDADL 791
Cdd:PRK14246 102 fphlSIYDNIAYplksHGIKEKREIKKIVEEC-------LRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45552357 792 YLLDDPLSAVDAhVGKHIFEEVIGPkgILARKSRVLVTHGVTFLPQV-DSIYVIKMGEISESGTFDQL 858
Cdd:PRK14246 175 LLMDEPTSMIDI-VNSQAIEKLITE--LKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEI 239
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1329-1521 |
1.04e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.38 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1329 VSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDG--VDIASMGlHMLRSRLTIIPQD-------PVLfsgS 1399
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPR-DAIRAGIMLCPEDrkaegiiPVH---S 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1400 LRINLD----PFEIKTDDEIWKALELSHLKSFVKSLA---AGLNHEIAeggeNLSVGQRQLVCLARALLRKTKVLVLDEA 1472
Cdd:PRK11288 348 VADNINisarRHHLRAGCLINNRWEAENADRFIRSLNiktPSREQLIM----NLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 45552357 1473 TAAVDL----ETDDLIQKTIRtefKECTVLTIAHRLNTILD-SDKVIVLDKGQI 1521
Cdd:PRK11288 424 TRGIDVgakhEIYNVIYELAA---QGVAVLFVSSDLPEVLGvADRIVVMREGRI 474
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
649-859 |
1.21e-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: 52.88 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 649 MSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLG--EMEKLAGVVntVGKLAYVPQQAWIQ----- 721
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRI--IYHVALCEKCGYVErpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 722 ---------------------------NATVRDNILFGQTY----DRKRYNKVIDA---CALRADIDILSAGDLTE---- 763
Cdd:TIGR03269 79 gepcpvcggtlepeevdfwnlsdklrrRIRKRIAIMLQRTFalygDDTVLDNVLEAleeIGYEGKEAVGRAVDLIEmvql 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 764 ---IGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEVIgpKGILARK-SRVLVTHgvtfLPQV- 838
Cdd:TIGR03269 159 shrITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALE--EAVKASGiSMVLTSH----WPEVi 232
|
250 260
....*....|....*....|....*
gi 45552357 839 ----DSIYVIKMGEISESGTFDQLV 859
Cdd:TIGR03269 233 edlsDKAIWLENGEIKEEGTPDEVV 257
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
666-802 |
1.33e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 51.43 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 666 NINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVV--------------NTVGKLAYVPQQAWI-QNATVRDNiL 730
Cdd:PRK10895 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplhaRARRGIGYLPQEASIfRRLSVYDN-L 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45552357 731 FGQTYDRKRYNKviDACALRADiDILSAGDLTEIGEK-GINLSGGQKQRISLARAVYSDADLYLLDDPLSAVD 802
Cdd:PRK10895 100 MAVLQIRDDLSA--EQREDRAN-ELMEEFHIEHLRDSmGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
664-861 |
1.37e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 51.93 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQ---------------------AFLGEMEKLAGVVNTVGKLAYVPQQAWIQN 722
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqtivgdyaipANLKKIKEVKRLRKEIGLVFQFPEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 723 aTVRDNILFGQTY----DRKRYNKV---IDACALRADIdilsagdlteIGEKGINLSGGQKQRISLARAVYSDADLYLLD 795
Cdd:PRK13645 107 -TIEKDIAFGPVNlgenKQEAYKKVpelLKLVQLPEDY----------VKRSPFELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 796 DPLSAVDAHvGKHIFEEVIGPKGILARKSRVLVTHGV-TFLPQVDSIYVIKMGEISESGTFDQLVKN 861
Cdd:PRK13645 176 EPTGGLDPK-GEEDFINLFERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
659-863 |
1.37e-06 |
|
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: 50.60 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 659 GDEItLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAgvvnTVGKLAYVPQqawiqnatvrdNILFGQTYDRK 738
Cdd:cd03217 12 GKEI-LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEV----TEGEILFKGE-----------DITDLPPEERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 739 RyNKVIDACALRADIDILSAGD-LTEIGEkgiNLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEVigpK 817
Cdd:cd03217 76 R-LGIFLAFQYPPEIPGVKNADfLRYVNE---GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVI---N 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 45552357 818 GILARKSRVL-VTHGVTFLPQV--DSIYVIKMGEISESGTFD--QLVKNKG 863
Cdd:cd03217 149 KLREEGKSVLiITHYQRLLDYIkpDRVHVLYDGRIVKSGDKElaLEIEKKG 199
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
664-854 |
1.47e-06 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 52.00 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQ--AFLgemEK-LAGVVnTVG-----------------KLAYVPQQ-AWIQN 722
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRciNLL---ERpTSGSV-LVDgvdltalserelraarrKIGMIFQHfNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 723 ATVRDNILF-----GqtYDRKRynkvIDAcalRADiDILsagDLTEIGEKG----INLSGGQKQRISLARAVYSDADLYL 793
Cdd:COG1135 97 RTVAENVALpleiaG--VPKAE----IRK---RVA-ELL---ELVGLSDKAdaypSQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 794 LDDPLSAVDahvgkhifeevigP---KGILA--RKSR-------VLVTH--GVtflpqV----DSIYVIKMGEISESGT 854
Cdd:COG1135 164 CDEATSALD-------------PettRSILDllKDINrelgltiVLITHemDV-----VrricDRVAVLENGRIVEQGP 224
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
670-857 |
1.61e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 49.88 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 670 EVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG-KLAYVPQQawiqnatvrdnilfgqtydrkrynkvidaca 748
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQY------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 749 lradidilsagdlteigekgINLSGGQKQRISLARAVYSDADLYLLDDPLSAVD-------AHVGKHIFEEvigpkgilA 821
Cdd:cd03222 70 --------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrlnaARAIRRLSEE--------G 121
|
170 180 190
....*....|....*....|....*....|....*.
gi 45552357 822 RKSRVLVTHGVTFLPQVDSIYVIKMGEISESGTFDQ 857
Cdd:cd03222 122 KKTALVVEHDLAVLDYLSDRIHVFEGEPGVYGIASQ 157
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1342-1539 |
1.77e-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: 53.09 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1342 VGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASmGLHMLRSRLTIIPQDPVLFSGSLRINLDPFEIKTDDEIWKALEL 1421
Cdd:TIGR01257 962 LGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQL 1040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1422 sHLKSFVKSlaAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIA 1501
Cdd:TIGR01257 1041 -EMEAMLED--TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMST 1117
|
170 180 190
....*....|....*....|....*....|....*....
gi 45552357 1502 HRLNTI-LDSDKVIVLDKGQIIEFASPTELLDNPKSAFY 1539
Cdd:TIGR01257 1118 HHMDEAdLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFY 1156
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1333-1517 |
1.87e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.50 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1333 IQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDgvdiasmglhmlrsrltiipqdpvlfsgsLRINLDPFEIKTD 1412
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-----------------------------LKISYKPQYIKPD 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1413 DEIWKALELSHLK-----SFVKS-LAAGLN-HEIAEGG-ENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLI 1484
Cdd:PRK13409 413 YDGTVEDLLRSITddlgsSYYKSeIIKPLQlERLLDKNvKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 492
|
170 180 190
....*....|....*....|....*....|....*.
gi 45552357 1485 QKTIR--TEFKECTVLTIAHRLNTI-LDSDKVIVLD 1517
Cdd:PRK13409 493 AKAIRriAEEREATALVVDHDIYMIdYISDRLMVFE 528
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
671-828 |
1.99e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.50 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 671 VKKGSLVALVGTVGSGKSSVVQAFLGEM-----------------------------EKLA-GVVNTVGKLAYVPQQAWI 720
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELipnlgdyeeepswdevlkrfrgtelqnyfKKLYnGEIKVVHKPQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 721 QNATVRDniLFGQTYDRKRYNKVIDACALRADIDilsagdlTEIGEkginLSGGQKQRISLARAVYSDADLYLLDDPLSA 800
Cdd:PRK13409 176 FKGKVRE--LLKKVDERGKLDEVVERLGLENILD-------RDISE----LSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180 190
....*....|....*....|....*....|
gi 45552357 801 VDahvgkhIFEEVIGPKGI--LARKSRVLV 828
Cdd:PRK13409 243 LD------IRQRLNVARLIreLAEGKYVLV 266
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
664-814 |
2.30e-06 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 50.44 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG------------KLAYVP-QQAWIQNATVRDNIL 730
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkepaearrRLGFVSdSTGLYDRLTARENLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 731 -FGQTYDRKRYnkvidacALRADIDILSagDLTEIGE----KGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAhV 805
Cdd:cd03266 101 yFAGLYGLKGD-------ELTARLEELA--DRLGMEElldrRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV-M 170
|
....*....
gi 45552357 806 GKHIFEEVI 814
Cdd:cd03266 171 ATRALREFI 179
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
651-802 |
2.52e-06 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 50.52 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 651 IENGEFSWGDEITlrNINIEVKKGSLVALVGTVGSGKS---SVVQAFLGEMEklagvvntvGKLayvpqqaWIQNA---- 723
Cdd:COG3840 4 LDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKStllNLIAGFLPPDS---------GRI-------LWNGQdlta 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 724 ---------------------TVRDNILFGQTYDRKrynkvidacaLRAD-----IDILSAGDLTEIGEK--GInLSGGQ 775
Cdd:COG3840 66 lppaerpvsmlfqennlfphlTVAQNIGLGLRPGLK----------LTAEqraqvEQALERVGLAGLLDRlpGQ-LSGGQ 134
|
170 180
....*....|....*....|....*..
gi 45552357 776 KQRISLARAVYSDADLYLLDDPLSAVD 802
Cdd:COG3840 135 RQRVALARCLVRKRPILLLDEPFSALD 161
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
669-802 |
2.77e-06 |
|
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: 49.80 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 669 IEVKKGSLVALVGTVGSGKSSVVQAFLG-EMEK-----LAGVVNTVGKLAYVPQQAWIQ------NATVRDNILFGQT-- 734
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQsgrvlINGVDVTAAPPADRPVSMLFQennlfaHLTVEQNVGLGLSpg 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45552357 735 -----YDRKRynkvIDACALRADIDILsagDLTEIGEkginLSGGQKQRISLARAVYSDADLYLLDDPLSAVD 802
Cdd:cd03298 99 lkltaEDRQA----IEVALARVGLAGL---EKRLPGE----LSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
657-800 |
2.85e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.85 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 657 SWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQA---------------FLGEMEKLAGVVNTVGK-LAYVPQQ-AW 719
Cdd:PRK13549 14 TFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVlsgvyphgtyegeiiFEGEELQASNIRDTERAgIAIIHQElAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 720 IQNATVRDNILFGQ---TYDRKRYNKVIDACA-----LRADIDIlsagdlteiGEKGINLSGGQKQRISLARAVYSDADL 791
Cdd:PRK13549 94 VKELSVLENIFLGNeitPGGIMDYDAMYLRAQkllaqLKLDINP---------ATPVGNLGLGQQQLVEIAKALNKQARL 164
|
....*....
gi 45552357 792 YLLDDPLSA 800
Cdd:PRK13549 165 LILDEPTAS 173
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
664-797 |
2.92e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.57 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK--------------LAYVPQ----QAWIQNATV 725
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsprerrrlgVAYIPEdrlgRGLVPDMSV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 726 RDNILFGQtYDRKRYNK--VIDACALRA-------DIDILSAGDLTEIGekgiNLSGGQKQRISLARAVYSDADLYLLDD 796
Cdd:COG3845 354 AENLILGR-YRRPPFSRggFLDRKAIRAfaeelieEFDVRTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQ 428
|
.
gi 45552357 797 P 797
Cdd:COG3845 429 P 429
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
657-803 |
3.26e-06 |
|
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: 51.75 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 657 SWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQA---------------FLGEMEKLAGVVNTVGK-LAYVPQQ-AW 719
Cdd:TIGR02633 10 TFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKIlsgvyphgtwdgeiyWSGSPLKASNIRDTERAgIVIIHQElTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 720 IQNATVRDNILFGQTY----DRKRYNKVIDAC-ALRADIDILSAGDLTEIGEKGinlsGGQKQRISLARAVYSDADLYLL 794
Cdd:TIGR02633 90 VPELSVAENIFLGNEItlpgGRMAYNAMYLRAkNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLIL 165
|
....*....
gi 45552357 795 DDPLSAVDA 803
Cdd:TIGR02633 166 DEPSSSLTE 174
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
667-803 |
4.22e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 50.61 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 667 INIEVKKGSLVALVGTVGSGKSSVVQ--AFL-----GEMEkLAG-VVNTVG----KLAYVpqqawIQN------ATVRDN 728
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRmvAGLeritsGEIW-IGGrVVNELEpadrDIAMV-----FQNyalyphMSVREN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 729 ILFGqtydrkrynkvidacaL------RADID--ILSAGDLTEIGE----KGINLSGGQKQRISLARAVYSDADLYLLDD 796
Cdd:PRK11650 97 MAYG----------------LkirgmpKAEIEerVAEAARILELEPlldrKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
....*..
gi 45552357 797 PLSAVDA 803
Cdd:PRK11650 161 PLSNLDA 167
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
652-802 |
4.28e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 49.98 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 652 ENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAG----------------VVNTVGKLAyvp 715
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGhvwldgehiqhyaskeVARRIGLLA--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 716 qqawiQNATVRDNILFGQTYDRKRY---------NKVIDACALRAdidiLSAGDLTEIGEKGIN-LSGGQKQRISLARAV 785
Cdd:PRK10253 88 -----QNATTPGDITVQELVARGRYphqplftrwRKEDEEAVTKA----MQATGITHLADQSVDtLSGGQRQRAWIAMVL 158
|
170
....*....|....*..
gi 45552357 786 YSDADLYLLDDPLSAVD 802
Cdd:PRK10253 159 AQETAIMLLDEPTTWLD 175
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
664-871 |
5.15e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 51.20 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEK---------LAGVVNTVGKL----AYVPQQ-AWIQNATVRDNI 729
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkgsgsvlLNGMPIDAKEMraisAYVQQDdLFIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 730 LF----------GQTYDRKRYNKVIDACALR--ADIDILSAGDLteigeKGinLSGGQKQRISLARAVYSDADLYLLDDP 797
Cdd:TIGR00955 121 MFqahlrmprrvTKKEKRERVDEVLQALGLRkcANTRIGVPGRV-----KG--LSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 798 LSAVDAHVGKHIFEEVIGpkgiLARKSR--VLVTH--GVTFLPQVDSIYVIKMGEISESGTFDQLVK--NKGAF------ 865
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKG----LAQKGKtiICTIHqpSSELFELFDKIILMAEGRVAYLGSPDQAVPffSDLGHpcpeny 269
|
....*...
gi 45552357 866 --ADFIIQ 871
Cdd:TIGR00955 270 npADFYVQ 277
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
667-854 |
5.91e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.55 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 667 INIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK------------LAYVPQQAWI-QNATVRDNILF-G 732
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdietnldavrqsLGMCPQHNILfHHLTVAEHILFyA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 733 QTYDRKRYNKVIDACALRADidilsAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEE 812
Cdd:TIGR01257 1029 QLKGRSWEEAQLEMEAMLED-----TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 45552357 813 VIGPKgilARKSRVLVTHGVTFLPQV-DSIYVIKMGEISESGT 854
Cdd:TIGR01257 1104 LLKYR---SGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGT 1143
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
649-797 |
7.93e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 49.11 E-value: 7.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 649 MSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK--------------LAYV 714
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKditdwqtakimreaVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 715 PQQAWI-QNATVRDNILFGQTY-DRKRYN----KVIDACALRADIDILSAGdlteigekgiNLSGGQKQRISLARAVYSD 788
Cdd:PRK11614 86 PEGRRVfSRMTVEENLAMGGFFaERDQFQerikWVYELFPRLHERRIQRAG----------TMSGGEQQMLAIGRALMSQ 155
|
....*....
gi 45552357 789 ADLYLLDDP 797
Cdd:PRK11614 156 PRLLLLDEP 164
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
987-1279 |
8.40e-06 |
|
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: 49.43 E-value: 8.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 987 GIFLSVatLVLNFVFQAFQIGsNLWLTQWANDQ-NVANDTGLRDMY-LGVYGAFGFGQVFSYIGSVVIVYLGALIgTRKI 1064
Cdd:cd18555 2 KLLISI--LLLSLLLQLLTLL-IPILTQYVIDNvIVPGNLNLLNVLgIGILILFLLYGLFSFLRGYIIIKLQTKL-DKSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1065 FIQLFGNILHAPQAYFDIKPRARILDRlANDIYKLDVVLPE-LIRVFNSQVFRVLATIVVISLSTPIFLAVIVpIAFLYY 1143
Cdd:cd18555 78 MSDFFEHLLKLPYSFFENRSSGDLLFR-ANSNVYIRQILSNqVISLIIDLLLLVIYLIYMLYYSPLLTLIVLL-LGLLIV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1144 FAQRFYVATSRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGDRFIEESDaKVDKNQVCKYPSviANRWLAI------ 1217
Cdd:cd18555 156 LLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWE-NLFKKQLKAFKK--KERLSNIlnsiss 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45552357 1218 RLEMVGNLIILFASLFAVLGGQ-TNPGLVGLSvSYALQVTQTLNWLVRMSSDIETNIVSVERI 1279
Cdd:cd18555 233 SIQFIAPLLILWIGAYLVINGElTLGELIAFS-SLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
995-1279 |
1.09e-05 |
|
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: 49.00 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 995 LVLNFVFQAFQIGSNL---WLTQWANDQNVAN-DTGLRDMYLGVYGAFGFGQVFSYIGSVVIVylgALIGTRKIF---IQ 1067
Cdd:cd18545 2 LLLALLLMLLSTAASLagpYLIKIAIDEYIPNgDLSGLLIIALLFLALNLVNWVASRLRIYLM---AKVGQRILYdlrQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1068 LFGNILHAPQAYFDIKPRARILDRLANDIYKL-DVVLPELIRVFnSQVFrVLATIVVISLSTPIFLA----VIVPIAFL- 1141
Cdd:cd18545 79 LFSHLQKLSFSFFDSRPVGKILSRVINDVNSLsDLLSNGLINLI-PDLL-TLVGIVIIMFSLNVRLAlvtlAVLPLLVLv 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1142 -YYFAQRfyvatSRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGDRFIEESDAKVDKNqvckypsVIANRWlAIRLE 1220
Cdd:cd18545 157 vFLLRRR-----ARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNREN-------RKANMR-AVRLN 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1221 -----------MVGNLIILFASLFAVLGGQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERI 1279
Cdd:cd18545 224 alfwplvelisALGTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
664-810 |
1.15e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK--------------LAYVPQQA-WIQNATVRDN 728
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfksskealengISMVHQELnLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 729 ILFGQT------YDRKRYNKVIDACALRADIDIlsagdltEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVD 802
Cdd:PRK10982 94 MWLGRYptkgmfVDQDKMYRDTKAIFDELDIDI-------DPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
....*...
gi 45552357 803 AHVGKHIF 810
Cdd:PRK10982 167 EKEVNHLF 174
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
642-858 |
1.16e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.94 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 642 DSSKPhPMSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAG------------------ 703
Cdd:PRK14271 16 DAAAP-AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdvllggrsifnyr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 704 -VVNTVGKLAYVPQQAWIQNATVRDNILFGQtydrkRYNKVIDACALRAdidiLSAGDLTEIG----------EKGINLS 772
Cdd:PRK14271 95 dVLEFRRRVGMLFQRPNPFPMSIMDNVLAGV-----RAHKLVPRKEFRG----VAQARLTEVGlwdavkdrlsDSPFRLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 773 GGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIfEEVIgpKGILARKSRVLVTHGVTFLPQV-DSIYVIKMGEISE 851
Cdd:PRK14271 166 GGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI-EEFI--RSLADRLTVIIVTHNLAQAARIsDRAALFFDGRLVE 242
|
....*..
gi 45552357 852 SGTFDQL 858
Cdd:PRK14271 243 EGPTEQL 249
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1325-1535 |
1.37e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 48.93 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASM------------------------GLH 1380
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekekvleklviqktrfkkikKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1381 MLRSRLTIIPQ--DPVLFSGSLR--INLDPFEIKTDDEiwKALELShlKSFVKSLaaGLNHEIAEGGE-NLSVGQRQLVC 1455
Cdd:PRK13651 102 EIRRRVGVVFQfaEYQLFEQTIEkdIIFGPVSMGVSKE--EAKKRA--AKYIELV--GLDESYLQRSPfELSGGQKRRVA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1456 LARALLRKTKVLVLDEATAAVDLE-TDDL--IQKTIRTEFKecTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELL 1531
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQgVKEIleIFDNLNKQGK--TIILVTHDLDNVLEwTKRTIFFKDGKIIKDGDTYDIL 253
|
....
gi 45552357 1532 DNPK 1535
Cdd:PRK13651 254 SDNK 257
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
664-830 |
1.38e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 48.27 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVG-----------------KLAYVPQ-QAWIQNATV 725
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklssaakaelrnqKLGFIYQfHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 726 RDNI----LFGqtydrkrynKVIDACALRADIDILSAGDLTEIGE-KGINLSGGQKQRISLARAVYSDADLYLLDDPLSA 800
Cdd:PRK11629 105 LENVamplLIG---------KKKPAEINSRALEMLAAVGLEHRANhRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190
....*....|....*....|....*....|
gi 45552357 801 VDAHVGKHIFeEVIGPKGILARKSRVLVTH 830
Cdd:PRK11629 176 LDARNADSIF-QLLGELNRLQGTAFLVVTH 204
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1012-1279 |
1.41e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 48.63 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1012 LTQWANDQNVANDT--GLRdMYLGVYGAFGFGQVFSYIGSVvivYLGALIGT---RKIFIQLFGNILHAPQAYFDIKPRA 1086
Cdd:cd18540 24 LTKYAIDHFITPGTldGLT-GFILLYLGLILIQALSVFLFI---RLAGKIEMgvsYDLRKKAFEHLQTLSFSYFDKTPVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1087 RILDRLANDIYKL-DVVLPELIRVFNSQVFRVLATIVVISLS---TPIFLAVIVPIAFLYYFAQRFYVATSRQLMRLESV 1162
Cdd:cd18540 100 WIMARVTSDTQRLgEIISWGLVDLVWGITYMIGILIVMLILNwklALIVLAVVPVLAVVSIYFQKKILKAYRKVRKINSR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1163 srspIYSHFSETVTGASTIRAYNVGDRFIEESDAKVDKnqvCKYPSVIANRWLAIRLEMVGNL------IILFASLFAVL 1236
Cdd:cd18540 180 ----ITGAFNEGITGAKTTKTLVREEKNLREFKELTEE---MRRASVRAARLSALFLPIVLFLgsiataLVLWYGGILVL 252
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 45552357 1237 GGQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERI 1279
Cdd:cd18540 253 AGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
664-858 |
2.17e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 48.91 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGeMEKLAGVVNTVGK-LAYVPQQAW------IQ------NA------T 724
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQdLDGLSRRALrplrrrMQvvfqdpFGslsprmT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 725 VRDNI-----LFGQTYDRK-RYNKVIDAcalradidilsagdLTEIG-----------EkginLSGGQKQRISLARAVYS 787
Cdd:COG4172 381 VGQIIaeglrVHGPGLSAAeRRARVAEA--------------LEEVGldpaarhryphE----FSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 788 DADLYLLDDPLSAVDAHVGKHIFEevigpkgILARKSRvlvTHGVTFL-----PQV-----DSIYVIKMGEISESGTFDQ 857
Cdd:COG4172 443 EPKLLVLDEPTSALDVSVQAQILD-------LLRDLQR---EHGLAYLfishdLAVvralaHRVMVMKDGKVVEQGPTEQ 512
|
.
gi 45552357 858 L 858
Cdd:COG4172 513 V 513
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1329-1534 |
2.40e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 47.62 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1329 VSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAgGRISIDGVDIASMGLHML-RSRLTIIPQDPVLFsgslriNLDpf 1407
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPF------AMP-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1408 eiktddeIWKALELSHLKSFVKSLAAGLNHEIAE----------GGENLSVGQRQLVCLARALLR-------KTKVLVLD 1470
Cdd:PRK03695 86 -------VFQYLTLHQPDKTRTEAVASALNEVAEalglddklgrSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 1471 EATAAVDLETDDLIQKTIRtEFKEC--TVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNP 1534
Cdd:PRK03695 159 EPMNSLDVAQQAALDRLLS-ELCQQgiAVVMSSHDLNHTLRhADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
334-625 |
2.57e-05 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 47.80 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 334 LFGALMKLFTDTLTFAQPQVLSLIISFVeaqdaepewkgilyAVLLFVLAAaqtfiLGQYFHRMFI--VGLRIRTALINA 411
Cdd:cd18552 17 ALAWLLKPLLDDIFVEKDLEALLLVPLA--------------IIGLFLLRG-----LASYLQTYLMayVGQRVVRDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 412 IYRKALRISNSTKKESTVGEIVNLMAVDAQRFME-LTTYLNMIWSAPLQ-IGLALYFLWQ--QLgpSVLAGLAVMIILIP 487
Cdd:cd18552 78 LFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNaLTSALTVLVRDPLTvIGLLGVLFYLdwKL--TLIALVVLPLAALP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 488 VnGVIASRIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPS----FEKQVLDIRDKEIATLRSTAYLNAGTSFLWS 563
Cdd:cd18552 156 I-RRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYeikrFRKANERLRRLSMKIARARALSSPLMELLGA 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45552357 564 CApfLVSLVTFATY-VLtseANQLSVEKVLVSIALFDLMKLPLTILPMLSVDIAETQVSVNRI 625
Cdd:cd18552 235 IA--IALVLWYGGYqVI---SGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
650-804 |
2.68e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 47.47 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 650 SIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVV------------QAFLGEmEKLAGVVNTV--GKLAYVP 715
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLkmlgrhqppsegEILLDA-QPLESWSSKAfaRKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 716 QQ-AWIQNATVRDNILFGQ-----------TYDRKRYNKVIDACALRAdidilSAGDLTEigekgiNLSGGQKQRISLAR 783
Cdd:PRK10575 92 QQlPAAEGMTVRELVAIGRypwhgalgrfgAADREKVEEAISLVGLKP-----LAHRLVD------SLSGGERQRAWIAM 160
|
170 180
....*....|....*....|..
gi 45552357 784 AVYSDADLYLLDDPLSAVD-AH 804
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDiAH 182
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
664-858 |
2.88e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.51 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGK--------------LAYVPQQAWI-QNATVRDN 728
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLfPNLSVKEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 729 ILFGQTYDRKRYNKVID-----ACALRADIdilSAGDLtEIGEkginlsggqKQRISLARAVYSDADLYLLDDPLSAVDA 803
Cdd:PRK15439 107 ILFGLPKRQASMQKMKQllaalGCQLDLDS---SAGSL-EVAD---------RQIVEILRGLMRDSRILILDEPTASLTP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 804 HVGKHIFeevigpkgilaRKSRVLVT--HGVTF----LPQV----DSIYVIKMGEISESGTFDQL 858
Cdd:PRK15439 174 AETERLF-----------SRIRELLAqgVGIVFishkLPEIrqlaDRISVMRDGTIALSGKTADL 227
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
664-861 |
2.94e-05 |
|
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: 47.34 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQA-------------FLGE------MEKLA--GVVNTvgklayvpqqawIQN 722
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLitgfyrptsgrilFDGRditglpPHRIArlGIART------------FQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 723 A------TVRDNILFGQTYDRK-----------RYNKVIDACALRADiDILSAGDLTEI-GEKGINLSGGQKQRISLARA 784
Cdd:COG0411 88 PrlfpelTVLENVLVAAHARLGrgllaallrlpRARREEREARERAE-ELLERVGLADRaDEPAGNLSYGQQRRLEIARA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 785 VYSDADLYLLDDPLSAVdAHVGKHIFEEVIgpKGILARKSR--VLVTHGVTFLPQV-DSIYVIKMGEISESGTFDQLVKN 861
Cdd:COG0411 167 LATEPKLLLLDEPAAGL-NPEETEELAELI--RRLRDERGItiLLIEHDMDLVMGLaDRIVVLDFGRVIAEGTPAEVRAD 243
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
671-802 |
3.02e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 47.36 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 671 VKKGSLVALVGTVGSGKSSVVQAFLGEM-----------------------------EKL-AGVVNTVGKLAYV---PQQ 717
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLkpnlgkfddppdwdeildefrgselqnyfTKLlEGDVKVIVKPQYVdliPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 718 AwiqNATVRDniLFGQTYDRKRYNKVIDACalradidilsagDLTEIGEKGI-NLSGGQKQRISLARAVYSDADLYLLDD 796
Cdd:cd03236 103 V---KGKVGE--LLKKKDERGKLDELVDQL------------ELRHVLDRNIdQLSGGELQRVAIAAALARDADFYFFDE 165
|
....*.
gi 45552357 797 PLSAVD 802
Cdd:cd03236 166 PSSYLD 171
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1309-1502 |
3.05e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.39 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1309 VEFQNFQVRYreGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSltlaLFRII----EAAGGRISI-DGVDIASMGlhmlR 1383
Cdd:TIGR03719 323 IEAENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKST----LFRMItgqeQPDSGTIEIgETVKLAYVD----Q 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1384 SRLTIIPQDPV----------LFSGSLRIN----LDPFEIKTDDEIWKALELShlksfvkslaaglnheiaeGGEnlsvg 1449
Cdd:TIGR03719 393 SRDALDPNKTVweeisggldiIKLGKREIPsrayVGRFNFKGSDQQKKVGQLS-------------------GGE----- 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 45552357 1450 qRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIrTEFKECTVLtIAH 1502
Cdd:TIGR03719 449 -RNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEAL-LNFAGCAVV-ISH 498
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1327-1538 |
3.06e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 48.10 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1327 RGVSFNIQGGEKVGIVGRTGAGKSSLtlalFRIIeaAG------GRISIDG-----VDIASMGLHMLRSRLTIIPQDPVL 1395
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTL----LRMI--AGleditsGDLFIGEkrmndVPPAERGVGMVFQSYALYPHLSVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1396 FSGSLRINL---DPFEI-KTDDEIWKALELSHLksfvkslaagLNHEIAEggenLSVGQRQLVCLARALLRKTKVLVLDE 1471
Cdd:PRK11000 94 ENMSFGLKLagaKKEEInQRVNQVAEVLQLAHL----------LDRKPKA----LSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552357 1472 ATAAVD--------LETDDLIQKTirtefkECTVLTIAH-RLNTILDSDKVIVLDKGQIIEFASPTELLDNPKSAF 1538
Cdd:PRK11000 160 PLSNLDaalrvqmrIEISRLHKRL------GRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRF 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1325-1502 |
3.34e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 47.39 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1325 VLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGlhmlRSRLTIIPQDPVLfsgslrinl 1404
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG----AERGVVFQNEGLL--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1405 dPFEiKTDDEIWKALELSHLKSFVKSLAAG--LNHEIAEGGEN-----LSVGQRQLVCLARALLRKTKVLVLDEATAAVD 1477
Cdd:PRK11248 83 -PWR-NVQDNVAFGLQLAGVEKMQRLEIAHqmLKKVGLEGAEKryiwqLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180
....*....|....*....|....*..
gi 45552357 1478 LETDDLIQKTIRTEFKEC--TVLTIAH 1502
Cdd:PRK11248 161 AFTREQMQTLLLKLWQETgkQVLLITH 187
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
659-854 |
4.71e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 47.05 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 659 GDE-ITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAG----------------VVNTVGKLAYVPQQAWIq 721
Cdd:PRK13648 19 SDAsFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGeifynnqaitddnfekLRKHIGIVFQNPDNQFV- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 722 NATVRDNILFGQ-----TYDR--KRYNKVIDacalraDIDILSAGDlteigEKGINLSGGQKQRISLARAVYSDADLYLL 794
Cdd:PRK13648 98 GSIVKYDVAFGLenhavPYDEmhRRVSEALK------QVDMLERAD-----YEPNALSGGQKQRVAIAGVLALNPSVIIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45552357 795 DDPLSAVDAHVGKHIFE---EVIGPKGIlarkSRVLVTHGVTFLPQVDSIYVIKMGEISESGT 854
Cdd:PRK13648 167 DEATSMLDPDARQNLLDlvrKVKSEHNI----TIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
664-803 |
5.57e-05 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 45.72 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTV---------------GKLAYVPQQAW-IQNATVRD 727
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIhyngipykefaekypGEIIYVSEEDVhFPTLTVRE 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552357 728 NILFgqtydrkrynkvidACALRADiDILsagdlteigeKGInlSGGQKQRISLARAVYSDADLYLLDDPLSAVDA 803
Cdd:cd03233 103 TLDF--------------ALRCKGN-EFV----------RGI--SGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
1036-1237 |
5.90e-05 |
|
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: 46.66 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1036 GAFGFGQVFSYIGSVVIVYLGALIgTRKIFIQLFGNILHAPQAYFDIKPRARILDRLANDIYKL----DVVLPELIrvfn 1111
Cdd:cd18551 44 ALFLLQAVLSALSSYLLGRTGERV-VLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLreliTSGLPQLV---- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1112 SQVFRVLATIVV-ISLSTPIFLAVI--VPIAFL--YYFAQRFYVATSRQLMRLESVSrspiySHFSETVTGASTIRAYNV 1186
Cdd:cd18551 119 TGVLTVVGAVVLmFLLDWVLTLVTLavVPLAFLiiLPLGRRIRKASKRAQDALGELS-----AALERALSAIRTVKASNA 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 45552357 1187 GDRFIEESDAKVDKnqvCKYPSVIANRWLAIrLEMVGNLIIlFASLFAVLG 1237
Cdd:cd18551 194 EERETKRGGEAAER---LYRAGLKAAKIEAL-IGPLMGLAV-QLALLVVLG 239
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
988-1279 |
6.40e-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: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 988 IFLsvATLVLNFVFQAFQIgsnlwLTQWANDQNVANDTG--LRDMYLGVYGAFGFGQVFSYIGSVVIVYLGALIGTrKIF 1065
Cdd:cd18568 7 ILL--ASLLLQLLGLALPL-----FTQIILDRVLVHKNIslLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDL-SLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1066 IQLFGNILHAPQAYFDIKPRARILDRLANDiykldvvlpELIRVFNSQ-----------VFRVLATIVVISLS-TPIFLA 1133
Cdd:cd18568 79 SDFYKHLLSLPLSFFASRKVGDIITRFQEN---------QKIRRFLTRsalttildllmVFIYLGLMFYYNLQlTLIVLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1134 VIVPIAFLYYFAQRFYVATSRQLMRLESVSrspiYSHFSETVTGASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVIanr 1213
Cdd:cd18568 150 FIPLYVLLTLLSSPKLKRNSREIFQANAEQ----QSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQK--- 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45552357 1214 wLAIRLEMVGNLI-------ILFASLFAVLGGQTNPG-LVGLSVSYALqVTQTLNWLVRMSSDIETNIVSVERI 1279
Cdd:cd18568 223 -LSIVLQLISSLInhlgtiaVLWYGAYLVISGQLTIGqLVAFNMLFGS-VINPLLALVGLWDELQETRISVERL 294
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
769-802 |
6.58e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.18 E-value: 6.58e-05
10 20 30
....*....|....*....|....*....|....
gi 45552357 769 INLSGGQKQRISLARAVYSDADLYLLDDPLSAVD 802
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
664-803 |
7.35e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.42 E-value: 7.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVV-------QAFLGEMEKLAGVvnTVGklaYVPQQAWI-QNATVRDNIL--FGQ 733
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLrimagvdKEFEGEARPAPGI--KVG---YLPQEPQLdPEKTVRENVEegVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 734 TYD-RKRYNKVIDACA---------------LRADIDILSAGDLT---EI---------GEKGI-NLSGGQKQRISLARA 784
Cdd:PRK11819 98 VKAaLDRFNEIYAAYAepdadfdalaaeqgeLQEIIDAADAWDLDsqlEIamdalrcppWDAKVtKLSGGERRRVALCRL 177
|
170
....*....|....*....
gi 45552357 785 VYSDADLYLLDDPLSAVDA 803
Cdd:PRK11819 178 LLEKPDMLLLDEPTNHLDA 196
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
771-861 |
7.39e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 46.37 E-value: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 771 LSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHI---FEEVIGPKGIlarkSRVLVTHGVTFLPQV-DSIYVIKM 846
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIinlMLELQEKLGI----SYIYVSQHLGIVKHIsDKVLVMHQ 225
|
90
....*....|....*
gi 45552357 847 GEISESGTFDQLVKN 861
Cdd:COG4167 226 GEVVEYGKTAEVFAN 240
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
664-804 |
7.71e-05 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 45.79 E-value: 7.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLAYVPQQAWIQNATVrdniLFGQ---------- 733
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGV----VFGQktqlwwdlpv 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 734 --TYD--RKRYNkvIDACALRADIDILSAG-DLTEIGEKGI-NLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAH 804
Cdd:cd03267 113 idSFYllAAIYD--LPPARFKKRLDELSELlDLEELLDTPVrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1326-1393 |
8.51e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 46.07 E-value: 8.51e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 1326 LRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDG-----VDIASMGL----HMLRSRLTIIPQDP 1393
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEaerrRLLRTEWGFVHQHP 98
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
659-858 |
8.55e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 46.33 E-value: 8.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 659 GDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVV----------------NTVGkLAYVPQQAWIQN 722
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVlirgepitkenirevrKFVG-LVFQNPDDQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 723 ATVRDNILFGQTydrkryNKVIDACALRADID-ILSAGDLTEIGEKGIN-LSGGQKQRISLARAVYSDADLYLLDDPLSA 800
Cdd:PRK13652 94 PTVEQDIAFGPI------NLGLDEETVAHRVSsALHMLGLEELRDRVPHhLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 801 VDAHVGKHIFeEVIGPKGILARKSRVLVTHGVTFLPQV-DSIYVIKMGEISESGTFDQL 858
Cdd:PRK13652 168 LDPQGVKELI-DFLNDLPETYGMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEI 225
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
770-854 |
9.13e-05 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 46.33 E-value: 9.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 770 NLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEevigpkgILARKSR------VLVTHGVTFLPQV-DSIY 842
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILE-------LLKDINRelgltiVLITHEMDVVKRIcDRVA 212
|
90
....*....|..
gi 45552357 843 VIKMGEISESGT 854
Cdd:PRK11153 213 VIDAGRLVEQGT 224
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
1063-1279 |
9.52e-05 |
|
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: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1063 KIFIQLFGNILHAPQAYFDIKPRARILDRLANDIYKL-DVVLPELIRVFNSQVFRVLATIVVISLSTPIFLA--VIVPIA 1139
Cdd:cd18554 80 DIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTkDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVslVIFPFY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1140 FL--YYFAQRFyvatsRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGDRFIEESDakvDKNQVCKYPSVIANRWLAI 1217
Cdd:cd18554 160 ILavKYFFGRL-----RKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFD---KRNGHFLTRALKHTRWNAK 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 1218 RLEMVGN-------LIILFASLFAVLGGQTNPGLVGLsVSYALQVTQTLNWLVRMSSDIETNIVSVERI 1279
Cdd:cd18554 232 TFSAVNTitdlaplLVIGFAAYLVIEGNLTVGTLVAF-VGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
1011-1243 |
1.03e-04 |
|
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: 45.94 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1011 WLTQWANDQNVAndTGLRDMYLGVYGAFGFGQVFSYIGSVVIVYLGALIGTRKIF---IQLFGNILHAPQAYFDIKPRAR 1087
Cdd:cd18546 20 LLVRYGIDSGVR--AGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYdlrLRVFAHLQRLSLDFHERETSGR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1088 ILDRLANDIYKLDVVLPE-LIRVFNSQVFRVLATIVVISLSTPIFL---AVIVPIAFLYYFAQRFYVATSRQlMRlESVS 1163
Cdd:cd18546 98 IMTRMTSDIDALSELLQTgLVQLVVSLLTLVGIAVVLLVLDPRLALvalAALPPLALATRWFRRRSSRAYRR-AR-ERIA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1164 RspIYSHFSETVTGASTIRAYN----VGDRFIEESDAKVDKNqvckypsVIANRWLAIR---LEMVGNL---IILFASLF 1233
Cdd:cd18546 176 A--VNADLQETLAGIRVVQAFRrerrNAERFAELSDDYRDAR-------LRAQRLVAIYfpgVELLGNLataAVLLVGAW 246
|
250
....*....|
gi 45552357 1234 AVLGGQTNPG 1243
Cdd:cd18546 247 RVAAGTLTVG 256
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1042-1279 |
1.07e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 45.96 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1042 QVFSYIGSVVIVYLGALIGTRKIF---IQLFGNILHAPQAYFDIKPRARILDRLANDIYKLDVVLPELIRVFNSQVFRVL 1118
Cdd:cd18563 53 YVLSALLGILRGRLLARLGERITAdlrRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMII 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1119 ATIVV-ISLSTPIFLAVIVPIAFLYYFAQRFYVAtSRQLMRLESVSRSPIYSHFSETVTGASTIRAYN----VGDRFIEE 1193
Cdd:cd18563 133 GIGVVlFSLNWKLALLVLIPVPLVVWGSYFFWKK-IRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGqekrEIKRFDEA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1194 SDAKVDKNQVckypsvIANRWLAIR-----LEMVGNLIILFASLFAVLGGQTNPGLVGLSVSYALQVTQTLNWLVRMSSD 1268
Cdd:cd18563 212 NQELLDANIR------AEKLWATFFplltfLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNW 285
|
250
....*....|.
gi 45552357 1269 IETNIVSVERI 1279
Cdd:cd18563 286 ITRALTSAERI 296
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
333-625 |
1.28e-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: 45.89 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 333 FLFGALMKLFTDTLTFAQPQVLSLII-SFVEAQDAEPEWkgiLYAVLLFVLAAAQTFIlgQYFHRMFI------VGLRIR 405
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIdSVIGGGLRELLW---LLALLILGVALLRGVF--RYLQGYLAekasqkVAYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 406 taliNAIYRKALRISNSTKKESTVGEIVNLMAVDA---QRFmeLTTYLNMIWSAPLQIGLALYFLWqqlgpSVLAGLA-V 481
Cdd:cd18542 76 ----NDLYDHLQRLSFSFHDKARTGDLMSRCTSDVdtiRRF--LAFGLVELVRAVLLFIGALIIMF-----SINWKLTlI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 482 MIILIPVNGVIASRIKTyQIRQMKYK-DERVKLMN----EVLSGIKVLKLYAWEPS----FEKQVLDIRDKEIATLRSTA 552
Cdd:cd18542 145 SLAIIPFIALFSYVFFK-KVRPAFEEiREQEGELNtvlqENLTGVRVVKAFAREDYeiekFDKENEEYRDLNIKLAKLLA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 553 YLNAGTSFLWSCAPFLV----------------SLVTFATYVLtseanqlsvekvlvsialfdLMKLPLTILPMLSVDIA 616
Cdd:cd18542 224 KYWPLMDFLSGLQIVLVlwvggylvingeitlgELVAFISYLW--------------------MLIWPVRQLGRLINDMS 283
|
....*....
gi 45552357 617 ETQVSVNRI 625
Cdd:cd18542 284 RASASAERI 292
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
659-811 |
1.29e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.62 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 659 GDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFL------GEMEKLAGVVNTVGKLAYVPQQAWIQnatvrdnILFG 732
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLrlinsqGEIWFDGQPLHNLNRRQLLPVRHRIQ-------VVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 733 QTYD--RKRYNKV-IDACALRADIDILSAGDLTE-----IGEKGIN----------LSGGQKQRISLARAVYSDADLYLL 794
Cdd:PRK15134 370 DPNSslNPRLNVLqIIEEGLRVHQPTLSAAQREQqviavMEEVGLDpetrhrypaeFSGGQRQRIAIARALILKPSLIIL 449
|
170
....*....|....*..
gi 45552357 795 DDPLSAVDAHVGKHIFE 811
Cdd:PRK15134 450 DEPTSSLDKTVQAQILA 466
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
664-803 |
1.32e-04 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 44.54 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSV--VQAFLGEMEKLAGVVNTVGKL---------AYVPQQ-AWIQNATVRDNILF 731
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLldVLAGRKTAGVITGEILINGRPldknfqrstGYVEQQdVHSPNLTVREALRF 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45552357 732 gqtydrkrynkvidACALRAdidilsagdlteigekginLSGGQKQRISLARAVYSDADLYLLDDPLSAVDA 803
Cdd:cd03232 103 --------------SALLRG-------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1333-1517 |
1.42e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 46.32 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1333 IQGGEKVGIVGRTGAGKSslTLAlfRIIeaaGGRISIDGVDIasmglhmlrsrltiipqdpvlfSGSLRINLDPFEIKTD 1412
Cdd:COG1245 363 IREGEVLGIVGPNGIGKT--TFA--KIL---AGVLKPDEGEV----------------------DEDLKISYKPQYISPD 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1413 -DEIWKALELSHLKSFVKSlaAGLNHEIAEG----------GENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETD 1481
Cdd:COG1245 414 yDGTVEEFLRSANTDDFGS--SYYKTEIIKPlgleklldknVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 491
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 45552357 1482 DLIQKTIR--TEFKECTVLTIAHRLnTILD--SDKVIVLD 1517
Cdd:COG1245 492 LAVAKAIRrfAENRGKTAMVVDHDI-YLIDyiSDRLMVFE 530
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
659-802 |
1.61e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.27 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 659 GDEITLRNINIEVKKGSLVALVGTVGSGKSS---------VVQAflGEMEKLAGVV------NTVG-KLAYVPQ---QAW 719
Cdd:NF033858 12 GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSllsliagarKIQQ--GRVEVLGGDMadarhrRAVCpRIAYMPQglgKNL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 720 IQNATVRDNI-----LFGQtydrkrynkviDACALRADID-ILSAGDLTEIGEK--GiNLSGGQKQRISLARAVYSDADL 791
Cdd:NF033858 90 YPTLSVFENLdffgrLFGQ-----------DAAERRRRIDeLLRATGLAPFADRpaG-KLSGGMKQKLGLCCALIHDPDL 157
|
170
....*....|.
gi 45552357 792 YLLDDPLSAVD 802
Cdd:NF033858 158 LILDEPTTGVD 168
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
986-1200 |
1.64e-04 |
|
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: 45.54 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 986 VGIFLSVA--------TLVLNFVFQAFQIGSNLWLTQwANDQNVANDTGLRDMYLGVyGAFgfgqVFSYIGSVVIVYLGA 1057
Cdd:cd18577 3 IGLLAAIAagaalplmTIVFGDLFDAFTDFGSGESSP-DEFLDDVNKYALYFVYLGI-GSF----VLSYIQTACWTITGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1058 LIgTRKIFIQLFGNILHAPQAYFDIKPRARILDRLANDIykldvvlpELIRVFNSQ----VFRVLATIV---VISLS--- 1127
Cdd:cd18577 77 RQ-ARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDT--------NLIQDGIGEklglLIQSLSTFIagfIIAFIysw 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 1128 --TPIFLAVIVPIAFLYYFAQRFYVATSRQLMRLESVSrspiYSHFSETVTGASTIRAYNVGDRFIEESDAKVDK 1200
Cdd:cd18577 148 klTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKA----GSIAEEALSSIRTVKAFGGEEKEIKRYSKALEK 218
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
333-632 |
1.71e-04 |
|
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: 45.52 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 333 FLFGALMKLFTdtLTFAQpqvlsLIISFVEAQDAEPEWKGILYAVLLFVLAAAQ---TFILGQYFHRM-FIVGLRIRTAL 408
Cdd:cd18578 19 IIAGAVFPVFA--ILFSK-----LISVFSLPDDDELRSEANFWALMFLVLAIVAgiaYFLQGYLFGIAgERLTRRLRKLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 409 INAIYRKalRISNSTKKESTVGEIVNLMAVDAQRFMELT-----TYLNMIWSAPLQIGLALYFLWqQLGpsvLAGLAVMI 483
Cdd:cd18578 92 FRAILRQ--DIAWFDDPENSTGALTSRLSTDASDVRGLVgdrlgLILQAIVTLVAGLIIAFVYGW-KLA---LVGLATVP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 484 ILIpvnGVIASRIKTYQIRQMKYKDERV---KLMNEVLSGIKVLKLYAWEPSFEKQVLDIRDKEIATLRSTAYLNAGTSF 560
Cdd:cd18578 166 LLL---LAGYLRMRLLSGFEEKNKKAYEessKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFG 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 561 LWSCAPFLVSLVTF---ATYVLTSEANQLSVEKVLVSIaLFDLMKL--PLTILPmlsvDIAETQVSVNRINKFLNSE 632
Cdd:cd18578 243 LSQSLTFFAYALAFwygGRLVANGEYTFEQFFIVFMAL-IFGAQSAgqAFSFAP----DIAKAKAAAARIFRLLDRK 314
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
333-625 |
1.97e-04 |
|
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: 45.08 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 333 FLFGALMKLFTDTLTFAQPQVLSLII-SFVEAQDAEPEWKgilYAVLLFVLAAAQTF--ILGQYFhrMFIVGLRIRTALI 409
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIdEGIANGDLSYILR---TGLLMLLLALLGLIagILAGYF--AAKASQGFGRDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 410 NAIYRKALRISNSTKKESTVGEIVNLMAVDA---QRFMELTtyLNMIWSAPLQIGLALYFLWQ---QLGPSVLAGLAVMI 483
Cdd:cd18548 76 KDLFEKIQSFSFAEIDKFGTSSLITRLTNDVtqvQNFVMML--LRMLVRAPIMLIGAIIMAFRinpKLALILLVAIPILA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 484 ILIpvnGVIASR-IKTYQIRQMKYkDERVKLMNEVLSGIKVLKLYAWEP----SFEKQVLDIRDKEIATLRSTAYLNAGT 558
Cdd:cd18548 154 LVV---FLIMKKaIPLFKKVQKKL-DRLNRVVRENLTGIRVIRAFNREDyeeeRFDKANDDLTDTSLKAGRLMALLNPLM 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 559 SFLWSCApfLVSLVTFATYVLtsEANQLSVEKVLVSIALFDLMKLPLTILPMLSVDIAETQVSVNRI 625
Cdd:cd18548 230 MLIMNLA--IVAILWFGGHLI--NAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
995-1185 |
2.15e-04 |
|
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: 45.14 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 995 LVLNFVFQAFQIGSNLwLTQWANDQN-VANDTGLrdmyLGVYgAFGFG------QVFSYIGSVVIVYLGALIGtrkifIQ 1067
Cdd:cd18567 8 LLLSLALELFALASPL-YLQLVIDEViVSGDRDL----LTVL-AIGFGlllllqALLSALRSWLVLYLSTSLN-----LQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1068 LFGNI----LHAPQAYF------DIKPR----ARILDRLANDIYK--LDVVLpelirvfnsqvfrVLATIVVISLSTPIf 1131
Cdd:cd18567 77 WTSNLfrhlLRLPLSYFekrhlgDIVSRfgslDEIQQTLTTGFVEalLDGLM-------------AILTLVMMFLYSPK- 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 45552357 1132 LAVIVPIAFLYYFAQRFyvATSRQLMRLES---VSRSPIYSHFSETVTGASTIRAYN 1185
Cdd:cd18567 143 LALIVLAAVALYALLRL--ALYPPLRRATEeqiVASAKEQSHFLETIRGIQTIKLFG 197
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
986-1279 |
2.30e-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: 45.11 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 986 VGIFLSVATLVLNFVfqafqigsNLWLTQWANDQN-VANDTGLRDMYLGVYGAFGFGQ-VFSYIGSvvivYLGALIGTRK 1063
Cdd:cd18542 3 LAILALLLATALNLL--------IPLLIRRIIDSViGGGLRELLWLLALLILGVALLRgVFRYLQG----YLAEKASQKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1064 IFI---QLFGNILHAPQAYFDikpRAR---ILDRLANDIykldvvlpELIRVFNSQVFR---------VLATIVVISLST 1128
Cdd:cd18542 71 AYDlrnDLYDHLQRLSFSFHD---KARtgdLMSRCTSDV--------DTIRRFLAFGLVelvravllfIGALIIMFSINW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1129 P---IFLAVIVPIAFL-YYFAQRF---YVATSRQLMRLESVsrspiyshFSETVTGASTIRAYNVGD----RFIEESDAK 1197
Cdd:cd18542 140 KltlISLAIIPFIALFsYVFFKKVrpaFEEIREQEGELNTV--------LQENLTGVRVVKAFAREDyeieKFDKENEEY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1198 VDKNqvckypsVIANRWLAIR------LEMVGNLIILFASLFAVLGGQTNPG-LVGLSvSYALQvtqtLNWLVRMS---- 1266
Cdd:cd18542 212 RDLN-------IKLAKLLAKYwplmdfLSGLQIVLVLWVGGYLVINGEITLGeLVAFI-SYLWM----LIWPVRQLgrli 279
|
330
....*....|...
gi 45552357 1267 SDIETNIVSVERI 1279
Cdd:cd18542 280 NDMSRASASAERI 292
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
651-797 |
2.41e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.71 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 651 IENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKL--AYVPQ--QAWIQNATVR 726
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLevAYFDQhrAELDPEKTVM 401
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 727 DNILFG-QTYD---RKRYnkvidacALRADIDILSAGDLTEIGEKGinLSGGQKQRISLARAVYSDADLYLLDDP 797
Cdd:PRK11147 402 DNLAEGkQEVMvngRPRH-------VLGYLQDFLFHPKRAMTPVKA--LSGGERNRLLLARLFLKPSNLLILDEP 467
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
664-862 |
2.45e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 45.08 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSSVVQ---AFL----GEME---------------KLAGVVNTVGK----------- 710
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEhlnALLlpdtGTIEwifkdeknkkktkekEKVLEKLVIQKtrfkkikkike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 711 ----LAYVPQQAWIQ--NATVRDNILFG-------QTYDRKRYNKVIDACALraDIDILSagdlteigEKGINLSGGQKQ 777
Cdd:PRK13651 103 irrrVGVVFQFAEYQlfEQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGL--DESYLQ--------RSPFELSGGQKR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 778 RISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEevIGPKGILARKSRVLVTHGV-TFLPQVDSIYVIKMGEISESG-TF 855
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLdNVLEWTKRTIFFKDGKIIKDGdTY 250
|
....*..
gi 45552357 856 DQLVKNK 862
Cdd:PRK13651 251 DILSDNK 257
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
668-802 |
2.48e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 44.19 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 668 NIEVKKGSLVALVGTVGSGKS---SVVQAFL----GEMeKLAGVVNTVGKLAYVPQQAWIQ------NATVRDNILFG-- 732
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKStllNLIAGFLtpasGSL-TLNGQDHTTTPPSRRPVSMLFQennlfsHLTVAQNIGLGln 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45552357 733 -----QTYDRKRYNKVIDACALRADIDILSAgdlteigekgiNLSGGQKQRISLARAVYSDADLYLLDDPLSAVD 802
Cdd:PRK10771 98 pglklNAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
647-829 |
3.06e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 45.26 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 647 HPMSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEK--LAGVV---------NTVGKLAYVP 715
Cdd:PLN03211 67 HKPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGnnFTGTIlannrkptkQILKRTGFVT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 716 QQAWI-QNATVRDNILFGQTY----DRKRYNKVIDACALRADIDILSAGDlTEIGEKGIN-LSGGQKQRISLARAVYSDA 789
Cdd:PLN03211 147 QDDILyPHLTVRETLVFCSLLrlpkSLTKQEKILVAESVISELGLTKCEN-TIIGNSFIRgISGGERKRVSIAHEMLINP 225
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 45552357 790 DLYLLDDPLSAVDAHVGKHIFEEVIGpkgiLARKSRVLVT 829
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTLGS----LAQKGKTIVT 261
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
772-805 |
3.64e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 44.57 E-value: 3.64e-04
10 20 30
....*....|....*....|....*....|....
gi 45552357 772 SGGQKQRISLARAVYSDADLYLLDDPLSAVDAHV 805
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
672-802 |
4.16e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.78 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 672 KKGSLVALVGTVGSGKSSVVQAFLGEM-----------------------------EKLA-GVVNTVGKLAYV---PQQA 718
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELkpnlgdydeepswdevlkrfrgtelqdyfKKLAnGEIKVAHKPQYVdliPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 719 wiqNATVRDniLFGQTYDRKRYNKVIDACALRADIDilsagdlTEIGEkginLSGGQKQRISLARAVYSDADLYLLDDPL 798
Cdd:COG1245 177 ---KGTVRE--LLEKVDERGKLDELAEKLGLENILD-------RDISE----LSGGELQRVAIAAALLRDADFYFFDEPS 240
|
....
gi 45552357 799 SAVD 802
Cdd:COG1245 241 SYLD 244
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
664-803 |
5.64e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.52 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 664 LRNINIEVKKGSLVALVGTVGSGKSS--------------------VVQAFLGEMEKL-AGVVNTVGKLAYVPqqawiqN 722
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTllkilsgnyqpdagsilidgQEMRFASTTAALaAGVAIIYQELHLVP------E 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 723 ATVRDNILFGQTYDRKrynKVIDACALRADidilSAGDLTEIGE------KGINLSGGQKQRISLARAVYSDADLYLLDD 796
Cdd:PRK11288 94 MTVAENLYLGQLPHKG---GIVNRRLLNYE----AREQLEHLGVdidpdtPLKYLSIGQRQMVEIAKALARNARVIAFDE 166
|
....*..
gi 45552357 797 PLSAVDA 803
Cdd:PRK11288 167 PTSSLSA 173
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1300-1477 |
5.73e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1300 PKNWPQEGRV--EFQNFQVRYREGLD-LVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALF------RIieaaGGRISID 1370
Cdd:NF040905 247 PERTPKIGEVvfEVKNWTVYHPLHPErKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgrsygrNI----SGTVFKD 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1371 G--VDIASM------GLHML---RSRLTIIPQDPVLFSGSLrINLDPF----------EIKTDDEIWKALelsHLKSfvk 1429
Cdd:NF040905 323 GkeVDVSTVsdaidaGLAYVtedRKGYGLNLIDDIKRNITL-ANLGKVsrrgvideneEIKVAEEYRKKM---NIKT--- 395
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 45552357 1430 slaaglnHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVD 1477
Cdd:NF040905 396 -------PSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1329-1534 |
7.23e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 43.64 E-value: 7.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1329 VSFNIQGGEKVGIVGRTGAGKSSLTLALFRI----IEAAGGRISIDGVDIASMGLHMLRS----RLTIIPQDPvlfsgsl 1400
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPRERRKlvghNVSMIFQEP------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1401 RINLDPFEIKTDDEI-----------------WK---ALELSH---LKSFvKSLAAGLNHEIAEGgenlsvgQRQLVCLA 1457
Cdd:PRK15093 99 QSCLDPSERVGRQLMqnipgwtykgrwwqrfgWRkrrAIELLHrvgIKDH-KDAMRSFPYELTEG-------ECQKVMIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1458 RALLRKTKVLVLDEATAAVDLETDDLIQKTIR--TEFKECTVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNP 1534
Cdd:PRK15093 171 IALANQPRLLIADEPTNAMEPTTQAQIFRLLTrlNQNNNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELVTTP 250
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
373-625 |
9.20e-04 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 43.20 E-value: 9.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 373 ILYAVLLFVLAAAQTFIlgQYFHRMFIV--GLRIRTALINAIYRKALR--ISN-STKKestVGEIVNLMAvDAQRFMELT 447
Cdd:cd18570 42 NIISIGLILLYLFQSLL--SYIRSYLLLklSQKLDIRLILGYFKHLLKlpLSFfETRK---TGEIISRFN-DANKIREAI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 448 TylNMIWSAPLQI------GLALYFLWQQLGPSVLAGLAVMIILIpvnGVIASRIKTYQIRQMKYKDERVKLMNEVLSGI 521
Cdd:cd18570 116 S--STTISLFLDLlmviisGIILFFYNWKLFLITLLIIPLYILII---LLFNKPFKKKNREVMESNAELNSYLIESLKGI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 522 KVLKLYAWEPSFEKQVLDIRDKEIATLRSTAYLNAGTSFLWSCAPFLVSLVTF---ATYVLtseANQLSVEKVLVSIALF 598
Cdd:cd18570 191 ETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILwigSYLVI---KGQLSLGQLIAFNALL 267
|
250 260
....*....|....*....|....*..
gi 45552357 599 DLMKLPLTILPMLSVDIAETQVSVNRI 625
Cdd:cd18570 268 GYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1029-1200 |
1.01e-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: 43.21 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1029 DMYLGVYGAFGFGQVFSYIGSVvivYLGALIG---TRKIFIQLFGNILHAPQAYFDiKPR---ARILDRLANDiykldvv 1102
Cdd:cd18578 52 NFWALMFLVLAIVAGIAYFLQG---YLFGIAGerlTRRLRKLAFRAILRQDIAWFD-DPEnstGALTSRLSTD------- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1103 lPELIRVFNS----QVFRVLATIV---VISLS-----TPIFLAVIVPIAFLYYFaqRFYVATSRQLMRLESVSRSPiySH 1170
Cdd:cd18578 121 -ASDVRGLVGdrlgLILQAIVTLVaglIIAFVygwklALVGLATVPLLLLAGYL--RMRLLSGFEEKNKKAYEESS--KI 195
|
170 180 190
....*....|....*....|....*....|
gi 45552357 1171 FSETVTGASTIRAYNVGDRFIEESDAKVDK 1200
Cdd:cd18578 196 ASEAVSNIRTVASLTLEDYFLEKYEEALEE 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
621-853 |
1.05e-03 |
|
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: 43.64 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 621 SVNRINKFLNSEELDPNSVLHDSSKpHPMSIENGEFSWGDeitlrNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEK 700
Cdd:TIGR03269 263 GVSEVEKECEVEVGEPIIKVRNVSK-RYISVDRGVVKAVD-----NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEP 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 701 LAGVVNT-VGklayvpqQAWIQ----------NATVRDNILFgQTYDRKRYNKVI------------DACALRADIDILS 757
Cdd:TIGR03269 337 TSGEVNVrVG-------DEWVDmtkpgpdgrgRAKRYIGILH-QEYDLYPHRTVLdnlteaiglelpDELARMKAVITLK 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 758 AGDLTEIGEKGI------NLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAhvgkhiFEEVIGPKGIL-ARK----SRV 826
Cdd:TIGR03269 409 MVGFDEEKAEEIldkypdELSEGERHRVALAQVLIKEPRIVILDEPTGTMDP------ITKVDVTHSILkAREemeqTFI 482
|
250 260
....*....|....*....|....*...
gi 45552357 827 LVTHGVTFLPQV-DSIYVIKMGEISESG 853
Cdd:TIGR03269 483 IVSHDMDFVLDVcDRAALMRDGKIVKIG 510
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
772-861 |
1.20e-03 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 42.77 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 772 SGGQKQRISLARAVYSDADLYLLDDPLSAVDAhvgkHIFEEVIGPKGILARK---SRVLVTHGVTFLPQV-DSIYVIKMG 847
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDV----SIQAQVVNLLQQLQREmglSLIFIAHDLAVVKHIsDRVLVMYLG 238
|
90
....*....|....
gi 45552357 848 EISESGTFDQLVKN 861
Cdd:PRK15079 239 HAVELGTYDEVYHN 252
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
771-802 |
1.26e-03 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 42.80 E-value: 1.26e-03
10 20 30
....*....|....*....|....*....|..
gi 45552357 771 LSGGQKQRISLARAVYSDADLYLLDDPLSAVD 802
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
1043-1279 |
1.88e-03 |
|
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: 42.00 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1043 VFSYIGSVVIVYLGALIGT---RKIFIQLFGNILHAPQAYFDIKPRARILDRLANDIYKLDVVLPELIRVFnsqvFR--- 1116
Cdd:cd18548 50 LLGLIAGILAGYFAAKASQgfgRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRML----VRapi 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1117 --VLATIVVISLS---TPIFLAVIVPIAFLYYF----AQRFYVATSRQLMRLESVSRspiyshfsETVTGASTIRAYNVG 1187
Cdd:cd18548 126 mlIGAIIMAFRINpklALILLVAIPILALVVFLimkkAIPLFKKVQKKLDRLNRVVR--------ENLTGIRVIRAFNRE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1188 D----RFIEESDAKVDKNqvckypsVIANRWLAIR---LEMVGNLIILFASLFA---VLGGQTNPG-LVGLsVSYALQVT 1256
Cdd:cd18548 198 DyeeeRFDKANDDLTDTS-------LKAGRLMALLnplMMLIMNLAIVAILWFGghlINAGSLQVGdLVAF-INYLMQIL 269
|
250 260
....*....|....*....|...
gi 45552357 1257 QTLNWLVRMSSDIETNIVSVERI 1279
Cdd:cd18548 270 MSLMMLSMVFVMLPRASASAKRI 292
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1410-1516 |
2.51e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.49 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1410 KTD-----DEIWKALELSHLksfvkslaagLNHEIaeggENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLI 1484
Cdd:PRK13409 186 KVDergklDEVVERLGLENI----------LDRDI----SELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNV 251
|
90 100 110
....*....|....*....|....*....|....
gi 45552357 1485 QKTIRTEFKECTVLTIAHRLnTILD--SDKVIVL 1516
Cdd:PRK13409 252 ARLIRELAEGKYVLVVEHDL-AVLDylADNVHIA 284
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
772-838 |
3.22e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 3.22e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 772 SGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVgkhifeeVIGPKGILAR--KSRVLVTHGVTFLPQV 838
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA-------VLWLETYLLKwpKTFIVVSHAREFLNTV 407
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
772-804 |
3.76e-03 |
|
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: 40.50 E-value: 3.76e-03
10 20 30
....*....|....*....|....*....|...
gi 45552357 772 SGGQKQRISLARAVYSDADLYLLDDPLSAVDAH 804
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAA 186
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1324-1503 |
4.12e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 40.32 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1324 LVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIAsmglhmlRSRLTIipQDPVLFSGSlRIN 1403
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK-------KDLCTY--QKQLCFVGH-RSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1404 LDP---------FEIKTD------DEIWKALELSHLKSFvkslAAGLnheiaeggenLSVGQRQLVCLARALLRKTKVLV 1468
Cdd:PRK13540 85 INPyltlrenclYDIHFSpgavgiTELCRLFSLEHLIDY----PCGL----------LSSGQKRQVALLRLWMSKAKLWL 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 45552357 1469 LDEATAAVDLETDDLIQKTIRTEFKE-CTVLTIAHR 1503
Cdd:PRK13540 151 LDEPLVALDELSLLTIITKIQEHRAKgGAVLLTSHQ 186
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
771-802 |
5.10e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 40.22 E-value: 5.10e-03
10 20 30
....*....|....*....|....*....|..
gi 45552357 771 LSGGQKQRISLARAVYSDADLYLLDDPLSAVD 802
Cdd:PRK13543 138 LSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1393-1516 |
5.19e-03 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 40.43 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1393 PVLFSGSLRINLDpfeiKTD-----DEIWKALELSHLksfvkslaagLNHEIaeggENLSVGQRQLVCLARALLRKTKVL 1467
Cdd:cd03236 100 PKAVKGKVGELLK----KKDergklDELVDQLELRHV----------LDRNI----DQLSGGELQRVAIAAALARDADFY 161
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 45552357 1468 VLDEATAAVDLETDDLIQKTIRTEFKEC-TVLTIAHRLnTILD--SDKVIVL 1516
Cdd:cd03236 162 FFDEPSSYLDIKQRLNAARLIRELAEDDnYVLVVEHDL-AVLDylSDYIHCL 212
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1316-1534 |
5.97e-03 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 40.52 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1316 VRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASM---GLHMLRSRLTIIPQd 1392
Cdd:PRK11831 13 VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMsrsRLYTVRKRMSMLFQ- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1393 pvlfSGSLRINLDPFeiktDDEIWKALELSHL-----KSFV--KSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTK 1465
Cdd:PRK11831 92 ----SGALFTDMNVF----DNVAYPLREHTQLpapllHSTVmmKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45552357 1466 VLVLDEATAAVDLETDDLIQKTIrTEFKEC---TVLTIAHRLNTILD-SDKVIVLDKGQIIEFASPTELLDNP 1534
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLI-SELNSAlgvTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALQANP 235
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
771-860 |
6.11e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.50 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 771 LSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEVIGpkgiLARK---SRVLVTHGVTFLPQV-DSIYVIKM 846
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLE----LQQKenmALVLITHDLALVAEAaHKIIVMYA 229
|
90
....*....|....
gi 45552357 847 GEISESGTFDQLVK 860
Cdd:PRK11022 230 GQVVETGKAHDIFR 243
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
986-1196 |
6.71e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 40.21 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 986 VGIFLSVATLVLNFVFQafqigsnlWLTQWANDQ--NVANDTG-LRDMYLGVYGAFGFGQVFSYIGSVVIVYLGALIgTR 1062
Cdd:cd18778 3 LTLLCALLSTLLGLVPP--------WLIRELVDLvtIGSKSLGlLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKV-VA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1063 KIFIQLFGNILHAPQAYFDIKPRARILDRLANDIYKLDVVLPELIRVFNSQVFRVL-ATIVVISLSTPIFLAVIVPIAFL 1141
Cdd:cd18778 74 DLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVgVAIILFSINPKLALLTLIPIPFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45552357 1142 YYFAqRFYVATSRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGD----RFIEESDA 1196
Cdd:cd18778 154 ALGA-WLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEeeakRFEALSRR 211
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1316-1376 |
9.05e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.88 E-value: 9.05e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45552357 1316 VRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLtLALF---RIIEAagGRISIDGVDIAS 1376
Cdd:NF033858 7 VSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSL-LSLIagaRKIQQ--GRVEVLGGDMAD 67
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
1030-1155 |
9.60e-03 |
|
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: 39.83 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552357 1030 MYLGVYGAFGFGQ-VFSYIGSVVIVYLGALIgTRKIFIQLFGNILHAPQAYFDIKPRARILDRLANDIYKLDVVLPELIR 1108
Cdd:cd18572 37 RAVLLLLLLSVLSgLFSGLRGGCFSYAGTRL-VRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLN 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 45552357 1109 VFNSQVFRVLATIVV-------ISLSTpifLAVIVPIAFLYYFAQRFYVATSRQ 1155
Cdd:cd18572 116 VFLRNLVQLVGGLAFmfslswrLTLLA---FITVPVIALITKVYGRYYRKLSKE 166
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