|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-1528 |
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: 3085.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 7 CSSDGSDPLWDWNVTWHTSNPDFTKCFQNTVLTWVPCFYLWSCFPLYFLYLSRHDRGYIQMTHLNKAKTALGFFLWIICW 86
Cdd:TIGR00957 1 CSADGSDPLWDWNVTWHTSNPDFTKCFQNTVLAWVPCFYLWVCFPCYFLYLSRHDRGYIQMTHLNKTKTALGFLLWIVCW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 87 ADLFYSFWERSQGMLLAPVLLVSPTLLGITMLLATFLIQFERRKGVQSSGIMLTFWLVALLCALAILRSKIISALKKDAQ 166
Cdd:TIGR00957 81 ADLFYSFWERSHGRAPAPVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALVCALAILRSKILLALKEDAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 167 VDMFRDSAFYLYFTLVFIQLVLSCFSDSSPLFSETVRDPNPCPESSASFLSRITFWWITGMMVQGYRQPLKSSDLWSLNK 246
Cdd:TIGR00957 161 VDPFRDTTFYIYFALVLSQLVLSCFSDKSPLFSETNHDPNPCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 247 EDTSEEVVPVLVNNWKKECVKSRKQPVRIVYAPpKDPTKPKGSSQLDVNEEVEALIVKSSHKDRDPSLFKVLYKTFGPYF 326
Cdd:TIGR00957 241 EDTSEMVVPVLVENWKKECKKTRKQPVSAVYGK-KDPSKPKGSSQLDANEEVEALIVKSPHKPRKPSLFKVLYKTFGPYF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 327 LMSFLYKALHDLMMFAGPEILELIINFVNDREAPDWQGYLYTALLFVSACLQTLALHQYFHICFVTGMRIKTAVVGAVYR 406
Cdd:TIGR00957 320 LMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 407 KALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVTLALYFLWLNLGPSVLAGVAVMILMVPFNAVMAM 486
Cdd:TIGR00957 400 KALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAM 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 487 KTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMNIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTF 566
Cdd:TIGR00957 480 KTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITF 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 567 AVFVTVDEKNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERWSIKDGGGmNSIT 646
Cdd:TIGR00957 560 AVYVTVDENNILDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEG-NSIT 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 647 VKNATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIQNDSLREN 726
Cdd:TIGR00957 639 VHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLREN 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 727 ILFGRPLQEHCYKAVMEACALLPDLEILPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKH 806
Cdd:TIGR00957 719 ILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 807 IFEKVVGPMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFVRTYANTEQDLASEDD---S 883
Cdd:TIGR00957 799 IFEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEDSwtaL 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 884 VSGLGKESKPVENGILVTDAVGKPLQRHLSNSSSHSVVTNQQHSSTAELQKSGVKEETWKLMEADKAQTGQVKLSVYWNY 963
Cdd:TIGR00957 879 VSGEGKEAKLIENGMLVTDVVGKQLQRQLSASSSDSGDQSRHHGSSAELQKAEAKEETWKLMEADKAQTGQVELSVYWDY 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 964 MKAIGLCISFLSIFLFLCNHVSALASNYWLSLWTDDrPAVNGTQENRNFRLSVYGALGILQGVAVFGYSMAVSIGGIFAS 1043
Cdd:TIGR00957 959 MKAIGLFITFLSIFLFVCNHVSALASNYWLSLWTDD-PMVNGTQNNTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQAS 1037
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1044 RRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLV 1123
Cdd:TIGR00957 1038 RVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLL 1117
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1124 YFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWLAVRLEC 1203
Cdd:TIGR00957 1118 YFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLEC 1197
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1204 VGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYSETEKEASWQIQETAPPS 1283
Cdd:TIGR00957 1198 VGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPS 1277
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1284 TWPHSGRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHN 1363
Cdd:TIGR00957 1278 GWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD 1357
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1364 LRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALL 1443
Cdd:TIGR00957 1358 LRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALL 1437
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1444 RKTKILVLDEATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELLQQRGVFYSMA 1523
Cdd:TIGR00957 1438 RKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMA 1517
|
....*
gi 1958656469 1524 KDAGL 1528
Cdd:TIGR00957 1518 KDAGL 1522
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
102-1527 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 1056.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 102 LAPVLLVSPTLLGITMLLATFLIQFERRKGVQSSGIMLTFWLVALLCALAILRSKIISaLKkdaqvDMFRDSAFYLYFTL 181
Cdd:PLN03130 107 LPPFEIVSLIVEALTWCSMLVMIGVETKIYIREFRWYVRFAVIYVLVGDAVMLNLVLS-VK-----EYYSSFVLYLYISE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 182 VFIQLVLSCF-----------SDSSPLFSETVRD---------PNPCPESSASFLSRITFWWITGMMVQGYRQPLKSSDL 241
Cdd:PLN03130 181 VAAQVLFGILllvyfpnldpyPGYTPIGSESVDDyeyeelpggEQICPERHANIFSRIFFGWMTPLMQLGYKRPLTEKDV 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 242 WSLNKEDTSEEVVPVLVNNWKKECvksrkqpvrivyappkdpTKPKgssqldvneevealivksshkdrdPSLFKVLYKT 321
Cdd:PLN03130 261 WKLDTWDQTETLYRSFQKCWDEEL------------------KKPK------------------------PWLLRALNNS 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 322 FGPYFLMSFLYKALHDLMMFAGPEILELIINFVNDREaPDWQGYLYTALLFVSACLQTLALHQYFHICFVTGMRIKTAVV 401
Cdd:PLN03130 299 LGGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQNGE-PAWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLV 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 402 GAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVTLALYFLWLNLGPSVLAGVAVMILMVPFN 481
Cdd:PLN03130 378 AAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQ 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 482 AVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMNIRQEELKVLKKSAYLAAVGTFTWVCTPFLV 561
Cdd:PLN03130 458 TFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNSIPVLV 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 562 ALSTFAVFVTVDEKniLDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEE--LEPD-SIERwsikd 638
Cdd:PLN03130 538 TVVSFGVFTLLGGD--LTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEErvLLPNpPLEP----- 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 639 ggGMNSITVKNATFTW-ARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVE-GHVTLKGSVAYVPQQA 716
Cdd:PLN03130 611 --GLPAISIKNGYFSWdSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTVAYVPQVS 688
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 717 WIQNDSLRENILFGRPLQEHCYKAVMEACALLPDLEILPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPL 796
Cdd:PLN03130 689 WIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 797 SAVDAHVGKHIFEKVVgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFVRTyANTEQD 876
Cdd:PLN03130 769 SALDAHVGRQVFDKCI--KDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMEN-AGKMEE 845
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 877 LASEDDSVSGLGKESKPVENGilvtdaVGKPLQRhlsNSSShsvvtnqqhsstaelqKSGVKEETWKLMEADKAQTGQVK 956
Cdd:PLN03130 846 YVEENGEEEDDQTSSKPVANG------NANNLKK---DSSS----------------KKKSKEGKSVLIKQEERETGVVS 900
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 957 LSVYWNYMKAIGLciSFLSIFLFLC---NHVSALASNYWLSLWTDdrpAVNGTQENRNFRLSVYGALGILQGVAVFGYSM 1033
Cdd:PLN03130 901 WKVLERYKNALGG--AWVVMILFLCyvlTEVFRVSSSTWLSEWTD---QGTPKTHGPLFYNLIYALLSFGQVLVTLLNSY 975
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1034 AVSIGGIFASRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIA 1113
Cdd:PLN03130 976 WLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTIS 1055
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1114 AVIIPPLGLVYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVA 1193
Cdd:PLN03130 1056 LWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSS 1135
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1194 NRWLAVRLECVGNCIVLFAALFAVI-----SRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYSET 1268
Cdd:PLN03130 1136 NRWLAIRLETLGGLMIWLTASFAVMqngraENQAAFASTMGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDL 1215
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1269 EKEASWQIQETAPPSTWPHSGRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGE 1348
Cdd:PLN03130 1216 PSEAPLVIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGR 1295
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1349 IIIDGINIAKIGLHNLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENL 1428
Cdd:PLN03130 1296 ILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENF 1375
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1429 SVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGA 1508
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDT 1455
|
1450 1460
....*....|....*....|
gi 1958656469 1509 PSELLQ-QRGVFYSMAKDAG 1527
Cdd:PLN03130 1456 PENLLSnEGSAFSKMVQSTG 1475
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
206-1527 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 959.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 206 NPCPESSASFLSRITFWWITGMMVQGYRQPLKSSDLWSLNKEDTSEEVVPVLVNNWKKEcvkSRKqpvrivyappkdptk 285
Cdd:PLN03232 225 NICPERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEE---SRR--------------- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 286 PKgssqldvneevealivksshkdrdPSLFKVLYKTFGPYFLMSFLYKALHDLMMFAGPEILELIINFVNDREaPDWQGY 365
Cdd:PLN03232 287 PK------------------------PWLLRALNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMQEGD-PAWVGY 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 366 LYTALLFVSACLQTLALHQYFHICFVTGMRIKTAVVGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMI 445
Cdd:PLN03232 342 VYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGL 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 446 WSAPLQVTLALYFLWLNLGPSVLAGVAVMILMVPFNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAF 525
Cdd:PLN03232 422 WSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSF 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 526 QDKVMNIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFAVFVTVDEKniLDAKKAFVSLALFNILRFPLNILPMVIS 605
Cdd:PLN03232 502 ESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFVLLGGD--LTPARAFTSLSLFAVLRSPLNMLPNLLS 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 606 SIVQASVSLKRLR-IFLSHEE-------LEPdsierwsikdggGMNSITVKNATFTW-ARDEPPTLNGITFAIPDGALVA 676
Cdd:PLN03232 580 QVVNANVSLQRIEeLLLSEERilaqnppLQP------------GAPAISIKNGYFSWdSKTSKPTLSDINLEIPVGSLVA 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 677 VVGQVGCGKSSLLSALLAEMDKVE-GHVTLKGSVAYVPQQAWIQNDSLRENILFGRPLQEHCYKAVMEACALLPDLEILP 755
Cdd:PLN03232 648 IVGGTGEGKTSLISAMLGELSHAEtSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLP 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 756 SGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIFEKVVGPMglLKNKTRILVTHGISYLPQ 835
Cdd:PLN03232 728 GRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDE--LKGKTRVLVTNQLHFLPL 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 836 VDVIIVMSGGKISEMGSYQELLDRDGAFAEFVRTYANTE--QDLASEDDSVSGLGkeskpvengilvtdavgkplqrhls 913
Cdd:PLN03232 806 MDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKMDatQEVNTNDENILKLG------------------------- 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 914 nSSSHSVVTNQQHSSTaelqKSGvKEETWKLMEADKAQTGQVKLSVYWNYMKAIG-LCISFLSIFLFLCNHVSALASNYW 992
Cdd:PLN03232 861 -PTVTIDVSERNLGST----KQG-KRGRSVLVKQEERETGIISWNVLMRYNKAVGgLWVVMILLVCYLTTEVLRVSSSTW 934
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 993 LSLWTDdrpavNGTQENRN--FRLSVYGALGILQGVAVFGYSMAVSIGGIFASRRLHLDLLQNVLRSPMSFFERTPSGNL 1070
Cdd:PLN03232 935 LSIWTD-----QSTPKSYSpgFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRV 1009
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1071 VNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRFYVASSRQLKRLESVSRSPVY 1150
Cdd:PLN03232 1010 INRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIY 1089
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1151 SHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVI-----SRHSLSA 1225
Cdd:PLN03232 1090 AQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLrngnaENQAGFA 1169
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1226 GLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYSETEKEASWQIQETAPPSTWPHSGRVEFRDYCLRYREDLD 1305
Cdd:PLN03232 1170 STMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLP 1249
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1306 LVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITIIPQDPVLFSGSLRMN 1385
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFN 1329
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1386 LDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDL 1465
Cdd:PLN03232 1330 IDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSL 1409
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958656469 1466 IQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELLQQRG-VFYSMAKDAG 1527
Cdd:PLN03232 1410 IQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVHSTG 1472
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
313-1527 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 786.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 313 SLFKVLYKTFGPYFLMSFLYKALHDLMMFAGPEILELIINFVNDREAPDWQGYLYTALLFVSACLQTLALHQYFHICFVT 392
Cdd:PTZ00243 233 SLLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRFYYISIRC 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 393 GMRIKTAVVGAVYRKALVITNS--ARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVTLALYFLWLNLGPSVLAG 470
Cdd:PTZ00243 313 GLQYRSALNALIFEKCFTISSKslAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALMA 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 471 VAVMILMVPFNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMNIRQEELKVLKKSAYLAAVG 550
Cdd:PTZ00243 393 VAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVAT 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 551 TFTWVCTPFLVALSTFAVFVTVDEKniLDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFL--------- 621
Cdd:PTZ00243 473 SFVNNATPTLMIAVVFTVYYLLGHE--LTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLecdnatcst 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 622 --------------------------------------------------------------------------SHEELE 627
Cdd:PTZ00243 551 vqdmeeywreqrehstacqlaavlenvdvtafvpvklprapkvktsllsralrmlcceqcrptkrhpspsvvveDTDYGS 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 628 PDSIERWSIKDG-GGMN---------SITVKNATFTWARDEPPTL-NGITFAIPDGALVAVVGQVGCGKSSLLSALLAEM 696
Cdd:PTZ00243 631 PSSASRHIVEGGtGGGHeatptsersAKTPKMKTDDFFELEPKVLlRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQF 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 697 DKVEGHVTLKGSVAYVPQQAWIQNDSLRENILFGRPLQEHCYKAVMEACALLPDLEILPSGDLTEIGEKGVNLSGGQKQR 776
Cdd:PTZ00243 711 EISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKAR 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 777 VSLARAVYCNSDIYLLDDPLSAVDAHVGKHIFEKVVgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYqel 856
Cdd:PTZ00243 791 VSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF--LGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSS--- 865
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 857 ldrdgafAEFVRTyaNTEQDLASEddsvsglGKESKPVENGILVTDAVGKPLQRHLSNSSSHSVVTNQQHSSTAELQKSG 936
Cdd:PTZ00243 866 -------ADFMRT--SLYATLAAE-------LKENKDSKEGDADAEVAEVDAAPGGAVDHEPPVAKQEGNAEGGDGAALD 929
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 937 VkeETWKLMEADKAQTGQVKLSVYWNYMKAIG-LCISFLSIFLFLCNHVSALASNYWLSLWTDDRPAVNGTQEnrnfrLS 1015
Cdd:PTZ00243 930 A--AAGRLMTREEKASGSVPWSTYVAYLRFCGgLHAAGFVLATFAVTELVTVSSGVWLSMWSTRSFKLSAATY-----LY 1002
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1016 VYgaLGI-LQGVAVFGYSMAVSIGGI-FASRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFM 1093
Cdd:PTZ00243 1003 VY--LGIvLLGTFSVPLRFFLSYEAMrRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLL 1080
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1094 GSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFI 1173
Cdd:PTZ00243 1081 QCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVM 1160
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1174 RQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVI------SRHSLsaGLVGLSVSYSLQITAYLNWLVR 1247
Cdd:PTZ00243 1161 QEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGVIgtmlraTSQEI--GLVSLSLTMAMQTTATLNWLVR 1238
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1248 MSSEMETNIVAVERLKEYS-ETEKEA-----------------------SWQIQETAPPSTWPH---SGRVEFRDYCLRY 1300
Cdd:PTZ00243 1239 QVATVEADMNSVERLLYYTdEVPHEDmpeldeevdalerrtgmaadvtgTVVIEPASPTSAAPHpvqAGSLVFEGVQMRY 1318
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1301 REDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITIIPQDPVLFSG 1380
Cdd:PTZ00243 1319 REGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDG 1398
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1381 SLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRK-TKILVLDEATAAVD 1459
Cdd:PTZ00243 1399 TVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFILMDEATANID 1478
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656469 1460 LETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELLQQR-GVFYSMAKDAG 1527
Cdd:PTZ00243 1479 PALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRqSIFHSMVEALG 1547
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
329-617 |
8.68e-170 |
|
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: 510.86 E-value: 8.68e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 329 SFLYKALHDLMMFAGPEILELIINFVNDREAPDWQGYLYTALLFVSACLQTLALHQYFHICFVTGMRIKTAVVGAVYRKA 408
Cdd:cd18595 2 AALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 409 LVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVTLALYFLWLNLGPSVLAGVAVMILMVPFNAVMAMKT 488
Cdd:cd18595 82 LRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 489 KTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMNIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFAV 568
Cdd:cd18595 162 KKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFAT 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1958656469 569 FVTVDEKNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd18595 242 YVLSDPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
972-1266 |
2.98e-169 |
|
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: 509.71 E-value: 2.98e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 972 SFLSIFLFLCNHVSALASNYWLSLWTDDRP-AVNGTQENRNFRLSVYGALGILQGVAVFGYSMAVSIGGIFASRRLHLDL 1050
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPAlNGTQDTEQRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1051 LQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRF 1130
Cdd:cd18603 81 LHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1131 YVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVL 1210
Cdd:cd18603 161 YVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 1211 FAALFAVISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYS 1266
Cdd:cd18603 241 FAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
209-1519 |
4.42e-168 |
|
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: 546.05 E-value: 4.42e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 209 PESSASFLSRITFWWITGMMVQGYRQPLKSSDLWSLNKEDTSEEVVPVLVNNWKKECVKSRKqpvrivyappkdptkpkg 288
Cdd:TIGR01271 5 PVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAKK------------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 289 ssqldvneevealivksshkdrDPSLFKVLYKTFGPYFLMSFLYKALHDLMMFAGPEILELIINFVNDREAPDWQGYLYT 368
Cdd:TIGR01271 67 ----------------------NPKLLNALRRCFFWRFVFYGILLYFGEATKAVQPLLLGRIIASYDPFNAPEREIAYYL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 369 A----LLFVsacLQTLALHQYFHICFVTGMRIKTAVVGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINM 444
Cdd:TIGR01271 125 AlglcLLFI---VRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHF 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 445 IWSAPLQVTLALYFLWLNLGPSVLAGVAVMILMVPFNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELA 524
Cdd:TIGR01271 202 VWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 525 FQDKVMNIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFAVFVTVdeKNILdAKKAFVSLALFNILRFPLN-ILPMV 603
Cdd:TIGR01271 282 MEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVVFLSVVPYALI--KGII-LRRIFTTISYCIVLRMTVTrQFPGA 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 604 ISSIVQASVSLKRLRIFLSHEELEpdsierwSIKDGGGMNSITVKNATFTW----------------ARDEP-------- 659
Cdd:TIGR01271 359 IQTWYDSLGAITKIQDFLCKEEYK-------TLEYNLTTTEVEMVNVTASWdegigelfekikqnnkARKQPngddglff 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 660 --------PTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIQNDSLRENILFGR 731
Cdd:TIGR01271 432 snfslyvtPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGL 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 732 PLQEHCYKAVMEACALLPDLEILPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIFEKV 811
Cdd:TIGR01271 512 SYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESC 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 812 VgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFV-------------RTYANTE--QD 876
Cdd:TIGR01271 592 L--CKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLlgleafdnfsaerRNSILTEtlRR 669
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 877 LASEDDSVSGLGKESK-------PVE------------------------------NGILVTDAVGKPLQRHLS------ 913
Cdd:TIGR01271 670 VSIDGDSTVFSGPETIkqsfkqpPPEfaekrkqsiilnpiasarkfsfvqmgpqkaQATTIEDAVREPSERKFSlvpede 749
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 914 ---------NSSSH----------SVVTNQQHSSTAELQKSGVKEETWKLMEADKAQTGQVKLSVY-------------- 960
Cdd:TIGR01271 750 qgeeslprgNQYHHglqhqaqrrqSVLQLMTHSNRGENRREQLQTSFRKKSSITQQNELASELDIYsrrlskdsvyeise 829
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 961 -----------------------WN-YMKAIGL--CISFLSIFLFLCNHVSALASNYWLSLWTDDRPAVNGTQENRNFRL 1014
Cdd:TIGR01271 830 eineedlkecfaderenvfetttWNtYLRYITTnrNLVFVLIFCLVIFLAEVAASLLGLWLITDNPSAPNYVDQQHANAS 909
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1015 S--VYGALGILQGVAVFGYSMAVSIG------GIF-----------ASRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFS 1075
Cdd:TIGR01271 910 SpdVQKPVIITPTSAYYIFYIYVGTAdsvlalGFFrglplvhtlltVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFT 989
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1076 KELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRFYVASSRQLKRLESVSRSPVYSHFNE 1155
Cdd:TIGR01271 990 KDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLIT 1069
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1156 TLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWLAVRLECVgncIVLF--AALFAVISRHSLSAGLVGLSVS 1233
Cdd:TIGR01271 1070 SLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDII---FVFFfiAVTFIAIGTNQDGEGEVGIILT 1146
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1234 YSLQITAYLNWLVRMSSEMETNIVAVERLKEYSETEKEASWQIQETAP--PST------------WPHSGRVEFRDYCLR 1299
Cdd:TIGR01271 1147 LAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRPSGGGGKyqLSTvlvienphaqkcWPSGGQMDVQGLTAK 1226
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1300 YREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRInESAEGEIIIDGINIAKIGLHNLRFKITIIPQDPVLFS 1379
Cdd:TIGR01271 1227 YTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFS 1305
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1380 GSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1459
Cdd:TIGR01271 1306 GTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
1450 1460 1470 1480 1490 1500
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1460 LETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELLQQRGVF 1519
Cdd:TIGR01271 1386 PVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1289-1509 |
5.63e-132 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 407.26 E-value: 5.63e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1289 GRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKI 1368
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1369 TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKI 1448
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958656469 1449 LVLDEATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAP 1509
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
328-617 |
1.15e-127 |
|
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: 398.51 E-value: 1.15e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 328 MSFLYKALHDLMMFAGPEILELIINFVNDREAPDWQGYLYTALLFVSACLQTLALHQYFHICFVTGMRIKTAVVGAVYRK 407
Cdd:cd18559 1 SFLLIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 408 ALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVTLALYFLWLNLGPSVLAGVAVMILMVPFNAVMAMK 487
Cdd:cd18559 81 ALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 488 TKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMNIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFA 567
Cdd:cd18559 161 SRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1958656469 568 VFVTVDEKNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd18559 241 AYVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
945-1524 |
6.14e-124 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 399.54 E-value: 6.14e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 945 MEADKAQTGQVKLSVYWNYMKAIglcisFLSIFLFLCNHVSALASNYWLSLWTDDrpAVNGTQENRNFRLS-VYGALGIL 1023
Cdd:COG1132 1 MSKSPRKLLRRLLRYLRPYRGLL-----ILALLLLLLSALLELLLPLLLGRIIDA--LLAGGDLSALLLLLlLLLGLALL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1024 QGVAVFGYSMAVSIGGIFASRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAV 1103
Cdd:COG1132 74 RALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1104 IIILLATPIAAVIIPPLGLVYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDEN 1183
Cdd:COG1132 154 VVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1184 QKAYYPSIVANRWLAVRLECVGNCIVLFAALFAV--ISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVER 1261
Cdd:COG1132 234 RRANLRAARLSALFFPLMELLGNLGLALVLLVGGllVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAER 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1262 LKEYSETEKEaswqIQETA-PPSTWPHSGRVEFRDYCLRYREDlDLVLKHINVTIEGGEKVGIVGRTGAGKSSLT---LG 1337
Cdd:COG1132 314 IFELLDEPPE----IPDPPgAVPLPPVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVnllLR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1338 LFRINEsaeGEIIIDGINIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWMALELAHLKGFVSALP 1414
Cdd:COG1132 389 FYDPTS---GRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAKAAQAHEFIEALP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1415 DKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYTR 1494
Cdd:COG1132 464 DGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADR 543
|
570 580 590
....*....|....*....|....*....|
gi 1958656469 1495 VIVLDKGEIRECGAPSELLQQRGVFYSMAK 1524
Cdd:COG1132 544 ILVLDDGRIVEQGTHEELLARGGLYARLYR 573
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
329-617 |
1.69e-118 |
|
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: 373.36 E-value: 1.69e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 329 SFLYKALHDLMMFAGPEILELIINFVNDREAPD-WQGYLYTALLFVSACLQTLALHQYFHICFVTGMRIKTAVVGAVYRK 407
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPlSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 408 ALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVTLALYFLWLNLGPSVLAGVAVMILMVPFNAVMAMK 487
Cdd:cd18579 82 ALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 488 TKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMNIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFA 567
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1958656469 568 VFVTVDekNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd18579 242 TYVLLG--NPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
972-1266 |
3.61e-118 |
|
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: 372.70 E-value: 3.61e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 972 SFLSIFLFLCNHVSALASNYWLSLWTDDrpAVNGTQENRNFRLSVYGALGILQGVAVFGYSMAVSIGGIFASRRLHLDLL 1051
Cdd:cd18559 1 SFLLIKLVLCNHVFSGPSNLWLLLWFDD--PVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1052 QNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIpPLGLVYFFVQRFY 1131
Cdd:cd18559 79 HKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGI-PLGLLYVPVNRVY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1132 VASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDeNQKAYYPSIVANRWLAVRLECVGNCIVLF 1211
Cdd:cd18559 158 AASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIVLF 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 1212 AALFAVISRHSLsAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYS 1266
Cdd:cd18559 237 ASFFAYVSRHSL-AGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
972-1266 |
1.23e-114 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 362.98 E-value: 1.23e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 972 SFLSIFLFLCNHVSALASNYWLSLWTDDrpAVNGTQENRNFRLSVYGALGILQGVA-VFGYSMAVSIGGIFASRRLHLDL 1050
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSD--WSSSPNSSSGYYLGVYAALLVLASVLlVLLRWLLFVLAGLRASRRLHDKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1051 LQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRF 1130
Cdd:cd18580 79 LRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1131 YVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVL 1210
Cdd:cd18580 159 YLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLAL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 1211 FAALFAVISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYS 1266
Cdd:cd18580 239 VVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
645-846 |
1.73e-113 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 356.01 E-value: 1.73e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDE---PPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIQND 721
Cdd:cd03250 1 ISVEDASFTWDSGEqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 722 SLRENILFGRPLQEHCYKAVMEACALLPDLEILPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDA 801
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958656469 802 HVGKHIFEKVVGPMgLLKNKTRILVTHGISYLPQVDVIIVMSGGK 846
Cdd:cd03250 161 HVGRHIFENCILGL-LLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
973-1266 |
2.29e-111 |
|
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: 353.70 E-value: 2.29e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 973 FLSIFLFLCNHVSALASNYWLSLWTDDRPavngtQENRNFRLSVYGALGILQGVAVFGYSMAVSIGGIFASRRLHLDLLQ 1052
Cdd:cd18606 2 PLLLLLLILSQFAQVFTNLWLSFWTEDFF-----GLSQGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1053 NVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRFYV 1132
Cdd:cd18606 77 RVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1133 ASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFA 1212
Cdd:cd18606 157 ASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLIV 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1958656469 1213 ALFAVISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYS 1266
Cdd:cd18606 237 ALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1018-1524 |
1.46e-97 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 330.64 E-value: 1.46e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1018 GALGILQGVAVFGYSMAVSIGGIFASRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSkELDTVDSMIP-QVIKMFMGSL 1096
Cdd:COG2274 203 LLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTgSLLTALLDLL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1097 FSVIGAVIIILLATPIAAV---IIPPLGLVYFFVQRFYVASSRQlkrlESVSRSPVYSHFNETLLGVSVIRAFEEQERFI 1173
Cdd:COG2274 282 FVLIFLIVLFFYSPPLALVvllLIPLYVLLGLLFQPRLRRLSRE----ESEASAKRQSLLVETLRGIETIKALGAESRFR 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1174 RQSDLKVDE----NQKAYYPSIVANRWLAVrLECVGNCIVLFAALFAVISRHsLSAG-LVGlSVSYSLQITAYLNWLVRM 1248
Cdd:COG2274 358 RRWENLLAKylnaRFKLRRLSNLLSTLSGL-LQQLATVALLWLGAYLVIDGQ-LTLGqLIA-FNILSGRFLAPVAQLIGL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1249 SSEMETNIVAVERLKEYSETEKEASWQIQETAPPstwPHSGRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTG 1328
Cdd:COG2274 435 LQRFQDAKIALERLDDILDLPPEREEGRSKLSLP---RLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSG 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1329 AGKSSLT---LGLFRINEsaeGEIIIDGINIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWMALE 1402
Cdd:COG2274 512 SGKSTLLkllLGLYEPTS---GRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDP--DATDEEIIEAAR 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1403 LAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDSTVLTI 1482
Cdd:COG2274 587 LAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIII 666
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1958656469 1483 AHRLNTIMDYTRVIVLDKGEIRECGAPSELLQQRGVFYSMAK 1524
Cdd:COG2274 667 AHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1285-1509 |
2.01e-97 |
|
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: 311.65 E-value: 2.01e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1285 WPHSGRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNL 1364
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1365 RFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELahlkgfvsalpdklnhecAEGGENLSVGQRQLVCLARALLR 1444
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALRV------------------SEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 1445 KTKILVLDEATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAP 1509
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
973-1266 |
1.21e-92 |
|
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: 301.69 E-value: 1.21e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 973 FLSIFLFLCNHVSALASNYWLSLWT---DDRPAVNGTQENRNFRLSVYGALGILQGVAVFGYSMAVSIGGIFASRRLHLD 1049
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWAsayETSSALPPSEVSVLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1050 LLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQR 1129
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1130 FYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIV 1209
Cdd:cd18604 162 LYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFS 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656469 1210 LFAALFAViSRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYS 1266
Cdd:cd18604 242 FATAALLV-YGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
973-1266 |
1.74e-88 |
|
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: 290.66 E-value: 1.74e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 973 FLSIFLFLCNHVSALASNYWLSLWTDDRPAVNGTQENRN----------FRLSVYGALGILQGVAVFGYSMAVSIGGIFA 1042
Cdd:cd18602 2 ALVLALALLKQGLRVATDFWLADWTEANHDVASVVFNITsssleddevsYYISVYAGLSLGAVILSLVTNLAGELAGLRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1043 SRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGL 1122
Cdd:cd18602 82 ARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIII 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1123 VYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWLAVRLE 1202
Cdd:cd18602 162 VYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLD 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 1203 CVGNCIVLFAALFAVISRH--SLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYS 1266
Cdd:cd18602 242 YLGAVIVFLAALSSLTAALagYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
970-1265 |
3.20e-87 |
|
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: 286.73 E-value: 3.20e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 970 CISFLsIFLFLCnHVSALASNYWLSLWTDDR--PAVNGTQENRNFRLSVYGALGILQGVAVFGYSMAVSIGGIFASRRLH 1047
Cdd:cd18605 1 LILIL-LSLILM-QASRNLIDFWLSYWVSHSnnSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1048 LDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFV 1127
Cdd:cd18605 79 NKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1128 QRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWLAVRLECVGNC 1207
Cdd:cd18605 159 QRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVL 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958656469 1208 IVLFAALFAVISRH---SLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEY 1265
Cdd:cd18605 239 IVTFVALTAVVQHFfglSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQY 299
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
330-617 |
3.25e-84 |
|
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: 278.61 E-value: 3.25e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 330 FLYKALHDLMMFAGPEILELIINFV-NDREAPDWQGYLYTALLFVSACLQTLALHQYFHICFVTGMRIKTAVVGAVYRKA 408
Cdd:cd18596 3 ALLAVLSSVLSFAPPFFLNRLLRYLeDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 409 LVITNSA-------------------RKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVTLALYFLWLNLGPSVLA 469
Cdd:cd18596 83 LRRRDKSgssksseskkkdkeededeKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 470 GVAVMILMVPFNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMNIRQEELKVLKKSAYLAAV 549
Cdd:cd18596 163 GLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 550 GTFTWVCTPFLVALSTFAVFvTVDEKNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd18596 243 LSLLWFLIPILVTVVTFATY-TLVMGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1289-1524 |
3.33e-84 |
|
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: 276.40 E-value: 3.33e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1289 GRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKI 1368
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1369 TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKI 1448
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656469 1449 LVLDEATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELL-QQRGVFYSMAK 1524
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLVR 254
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
331-617 |
2.50e-80 |
|
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: 266.34 E-value: 2.50e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 331 LYKALHDLMMFAGPEILELIINFVNDREAPDWQGYLYTALLFVSACLQTLALHQYFHICFVTGMRIKTAVVGAVYRKALV 410
Cdd:cd18598 4 LLKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRKALR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 411 ITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVTLALYFLWLNLGPSVLAGVAVMILMVPFNAVMAMKTKT 490
Cdd:cd18598 84 VRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRIGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 491 YQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMNIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFAVFV 570
Cdd:cd18598 164 LSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPVLISILTFATYV 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958656469 571 TVdeKNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd18598 244 LM--GNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
328-617 |
9.32e-80 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350041 [Multi-domain] Cd Length: 293 Bit Score: 265.09 E-value: 9.32e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 328 MSFLYKALHDLMMFAGPEILELIINFVNDREA-----PDWQGYLYTALLFVSACLQTLALHQYFHICFVTGMRIKTAVVG 402
Cdd:cd18597 1 LAGLLKLLADVLQVLSPLLLKYLINFVEDAYLggpppSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 403 AVYRKALVITNSARKSSTVGEIVNLMSVDAQRfMDLA-TYINMIWSAPLQVTLALYFLWLNLGPSVLAGVAVMILMVPFN 481
Cdd:cd18597 81 AIYRKSLRLSGKSRHEFPNGKITNLMSTDLSR-IDFAlGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 482 AVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMNIRQEELKVLKKSAYLAAVGTFTWVCTPFLV 561
Cdd:cd18597 160 GFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 562 ALSTFAVFVTVdeKNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd18597 240 SMLSFITYYAT--GHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
308-874 |
2.49e-77 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 268.19 E-value: 2.49e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 308 KDRDPSLFKVLYKTFGPY---FLMSFLYKALHDLMMFAGPEILELIINFV---NDREAPDWQGYLYTALLFVSACLQTLA 381
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYrglLILALLLLLLSALLELLLPLLLGRIIDALlagGDLSALLLLLLLLLGLALLRALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 382 LHQYFHICFVTGMRIKTAVvgavYRKALVITNSARKSSTVGEIVNLMSVDAQRFMD-LATYINMIWSAPLQVTLALYFL- 459
Cdd:COG1132 82 RYLLARLAQRVVADLRRDL----FEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQfLAHGLPQLVRSVVTLIGALVVLf 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 460 WLN--LGpsvLAGVAVMILMVPFNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYA---WELA-FQDKVMNIR 533
Cdd:COG1132 158 VIDwrLA---LIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGreeRELErFREANEELR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 534 QEELKVLKKSA-YLAAVGTFTWVCTPFLVALSTFAVF---VTVDEknildakkaFVS-LALFNILRFPLNILPMVISSIV 608
Cdd:COG1132 235 RANLRAARLSAlFFPLMELLGNLGLALVLLVGGLLVLsgsLTVGD---------LVAfILYLLRLFGPLRQLANVLNQLQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 609 QASVSLKRLRIFLSHEELEPDSIERWSIKDGGGmnSITVKNATFTWArDEPPTLNGITFAIPDGALVAVVGQVGCGKSSL 688
Cdd:COG1132 306 RALASAERIFELLDEPPEIPDPPGAVPLPPVRG--EIEFENVSFSYP-GDRPVLKDISLTIPPGETVALVGPSGSGKSTL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 689 LSALLAEMDKVEGHVTLKG-------------SVAYVPQQAWIQNDSLRENILFGRP---LQEhcykaVMEACA---LLP 749
Cdd:COG1132 383 VNLLLRFYDPTSGRILIDGvdirdltleslrrQIGVVPQDTFLFSGTIRENIRYGRPdatDEE-----VEEAAKaaqAHE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 750 DLEILPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHG 829
Cdd:COG1132 458 FIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL---ERLMKGRTTIVIAHR 534
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1958656469 830 ISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFVRTYANTE 874
Cdd:COG1132 535 LSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFGEE 579
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1019-1517 |
3.71e-77 |
|
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: 267.39 E-value: 3.71e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1019 ALGILQGVAVFGYSMAVSIGGIFASRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFskeLDTVDSM-------IPQVIKM 1091
Cdd:COG4988 66 AVLLLRALLAWLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLL---TEGVEALdgyfaryLPQLFLA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1092 FMGSLfsVIGAVI--------IILLATpiaAVIIPplgLVYFFVQRFY-VASSRQLKRLESVSrspvySHFNETLLGVSV 1162
Cdd:COG4988 143 ALVPL--LILVAVfpldwlsgLILLVT---APLIP---LFMILVGKGAaKASRRQWRALARLS-----GHFLDRLRGLTT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1163 IRAF----EEQERFIRQSD---------LKVdenqkAYYPSIVanrwlavrLECVGnciVLFAALFAVISRHSLSAGLVG 1229
Cdd:COG4988 210 LKLFgrakAEAERIAEASEdfrkrtmkvLRV-----AFLSSAV--------LEFFA---SLSIALVAVYIGFRLLGGSLT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1230 LSVSYSLQITA---YL-------NWLVRMSsemetNIVAVERLKEYSETEKEASWQIQETAPpstWPHSGRVEFRDYCLR 1299
Cdd:COG4988 274 LFAALFVLLLApefFLplrdlgsFYHARAN-----GIAAAEKIFALLDAPEPAAPAGTAPLP---AAGPPSIELEDVSFS 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1300 YrEDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITIIPQDPVLFS 1379
Cdd:COG4988 346 Y-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1380 GSLRMNL---DPfsQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1456
Cdd:COG4988 425 GTIRENLrlgRP--DASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTA 502
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958656469 1457 AVDLETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELLQQRG 1517
Cdd:COG4988 503 HLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1289-1517 |
3.04e-75 |
|
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: 249.45 E-value: 3.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1289 GRVEFRDYCLRYREDlDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKI 1368
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1369 TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWM-ALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTK 1447
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIeAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1448 ILVLDEATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELLQQRG 1517
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1020-1522 |
1.39e-73 |
|
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: 257.34 E-value: 1.39e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1020 LGILQGVAVFGYSMAVSIGGIFASRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSV 1099
Cdd:TIGR02203 63 LAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1100 IGAVIIILLA----TPIAAVIIPPLGLVyffvqrfyvaSSRQLKRLESVSRSPVYSH------FNETLLGVSVIRAF--- 1166
Cdd:TIGR02203 143 IGLFIVLLYYswqlTLIVVVMLPVLSIL----------MRRVSKRLRRISKEIQNSMgqvttvAEETLQGYRVVKLFggq 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1167 -EEQERF------IRQSDLKVDENQKAYYPSI--VANRWLAVrlecvgnciVLFAALFAVISRHSLSAGLVGLSVSySLQ 1237
Cdd:TIGR02203 213 aYETRRFdavsnrNRRLAMKMTSAGSISSPITqlIASLALAV---------VLFIALFQAQAGSLTAGDFTAFITA-MIA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1238 ITAYLNWLVRMSSEMETNIVAVERLKEYSETEKEAswQIQETAPPSTwphSGRVEFRDYCLRYREDLDLVLKHINVTIEG 1317
Cdd:TIGR02203 283 LIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEK--DTGTRAIERA---RGDVEFRNVTFRYPGRDRPALDSISLVIEP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1318 GEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL---DPfSQYSD 1394
Cdd:TIGR02203 358 GETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT-EQADR 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1395 EEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQF 1474
Cdd:TIGR02203 437 AEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLM 516
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1958656469 1475 EDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELLQQRGVF---YSM 1522
Cdd:TIGR02203 517 QGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYaqlHNM 567
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
968-1266 |
1.88e-72 |
|
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: 244.78 E-value: 1.88e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 968 GLCISFLSIFLFLCNHVSALASNYWLSLW----------TDDRPAVNGTQENRNFRLSVYgalgilqgVAVFGYSMAVSI 1037
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWlkqgsgnttnNVDNSTVDSGNISDNPDLNFY--------QLVYGGSILVIL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1038 ------GGIF------ASRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVII 1105
Cdd:cd18599 73 llslirGFVFvkvtlrASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLII 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1106 ILLATPIAAVIIPPLGLVYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQK 1185
Cdd:cd18599 153 IAIVFPWFLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1186 AYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEY 1265
Cdd:cd18599 233 AFFLFNCAMRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEY 312
|
.
gi 1958656469 1266 S 1266
Cdd:cd18599 313 I 313
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
331-617 |
4.38e-72 |
|
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: 243.68 E-value: 4.38e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 331 LYKALHDLMMFAGPEILELIINFVNDREAPDWQ------------------GYLYTALLFVSACLQTLALHQYFHICFVT 392
Cdd:cd18591 4 ILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNstdklsvsyvtveeffsnGYVLAVILFLALLLQATFSQASYHIVIRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 393 GMRIKTAVVGAVYRKALVIT--NSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVTLALYFLWLNLGPSVLAG 470
Cdd:cd18591 84 GIRLKTALQAMIYEKALRLSswNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 471 VAVMILMVPFNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMNIRQEELKVLKKSAYLAAVG 550
Cdd:cd18591 164 AALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSLM 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656469 551 TFTWVCTPFLVALSTFAVFVTVDEKNiLDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd18591 244 TFLTQASPILVTLVTFGLYPYLEGEP-LTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1045-1524 |
5.04e-72 |
|
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: 252.38 E-value: 5.04e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1045 RLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIkmfmgslFSVIGAVIIILLATPIAAVIIPPLGLVY 1124
Cdd:COG4987 89 DLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVL-------LPLLVALLVILAAVAFLAFFSPALALVL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1125 F------------FVQRFYVASSRQLKRLesvsRSPVYSHFNETLLGVSVIRAFEEQERFIRQsdlkVDENQKAYypsiV 1192
Cdd:COG4987 162 AlglllaglllplLAARLGRRAGRRLAAA----RAALRARLTDLLQGAAELAAYGALDRALAR----LDAAEARL----A 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1193 ANRWLAVRLECVGNCIVLFAALFAVI----------SRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERL 1262
Cdd:COG4987 230 AAQRRLARLSALAQALLQLAAGLAVVavlwlaaplvAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1263 KEYSETEKeaswQIQETAPPSTWPHSGRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRIN 1342
Cdd:COG4987 310 NELLDAPP----AVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1343 ESAEGEIIIDGINIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWMALELAHLKGFVSALPDKLNH 1419
Cdd:COG4987 386 DPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGLGDWLAALPDGLDT 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1420 ECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLD 1499
Cdd:COG4987 464 WLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLE 543
|
490 500
....*....|....*....|....*
gi 1958656469 1500 KGEIRECGAPSELLQQRGVFYSMAK 1524
Cdd:COG4987 544 DGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
349-617 |
2.29e-66 |
|
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: 226.36 E-value: 2.29e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 349 LIINFVNDREAPDWQGYLYTALLFVSACLQTLALHQYFHICFVTGMRIKTAVVGAVYRKALVITNSARKSSTVGEIVNLM 428
Cdd:cd18594 23 LVAYFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTLKLSSSALSKITTGHIVNLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 429 SVDAQRFMDLATYINMIWSAPLQVTLALYFLWLNLGPSVLAGVAVMILMVPFNAVMAMKTKTYQVAHMKSKDNRIKLMNE 508
Cdd:cd18594 103 SNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGLTDERVKIMNE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 509 ILNGIKVLKLYAWELAFQDKVMNIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFAVFVTVdeKNILDAKKAFVSLA 588
Cdd:cd18594 183 IISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVLT--GNTLTARKVFTVIS 260
|
250 260 270
....*....|....*....|....*....|
gi 1958656469 589 LFNILRFPLNI-LPMVISSIVQASVSLKRL 617
Cdd:cd18594 261 LLNALRMTITRfFPESIQTLSESRVSLKRI 290
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1291-1522 |
3.80e-66 |
|
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: 223.65 E-value: 3.80e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITI 1370
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1371 IPQDPVLFSGSLRMNLdpfsQY-----SDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRK 1445
Cdd:cd03251 81 VSQDVFLFNDTVAENI----AYgrpgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656469 1446 TKILVLDEATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELLQQRGVFYSM 1522
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
391-868 |
9.73e-66 |
|
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: 237.81 E-value: 9.73e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 391 VTGMRIKTAVVGAVYRKALVITNSARKSSTVGEIVNlmsvdaqRFMDLATYINMIWSAPLQVTLALYFLWLNL------- 463
Cdd:COG2274 222 RLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLAS-------RFRDVESIREFLTGSLLTALLDLLFVLIFLivlffys 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 464 GPSVLAGVAVMILMVPFNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMNIRQEELKVLKKS 543
Cdd:COG2274 295 PPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 544 AYLAAVGTFTwvcTPFLVALSTFAVFVT----VDEKNI-LDAKKAFVSLalfnILRF--PLNILPMVISSIVQASVSLKR 616
Cdd:COG2274 375 RRLSNLLSTL---SGLLQQLATVALLWLgaylVIDGQLtLGQLIAFNIL----SGRFlaPVAQLIGLLQRFQDAKIALER 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 617 LRIFLSHEELEPDSIERWSIKDGGGmnSITVKNATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEM 696
Cdd:COG2274 448 LDDILDLPPEREEGRSKLSLPRLKG--DIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLY 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 697 DKVEGHVTLKG-------------SVAYVPQQAWIQNDSLRENILFGRPlqEHCYKAVMEAC---ALLPDLEILPSGDLT 760
Cdd:COG2274 526 EPTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGTIRENITLGDP--DATDEEIIEAArlaGLHDFIEALPMGYDT 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 761 EIGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYLPQVDVII 840
Cdd:COG2274 604 VVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENL---RRLLKGRTVIIIAHRLSTIRLADRII 680
|
490 500
....*....|....*....|....*...
gi 1958656469 841 VMSGGKISEMGSYQELLDRDGAFAEFVR 868
Cdd:COG2274 681 VLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
968-1266 |
4.44e-65 |
|
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: 223.74 E-value: 4.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 968 GLCISFLSIFLFLCNHVSALASNYWLSLW----------TDDRPAVNGTQE-----NRNFRLSVYGALGILQGVAVFGYS 1032
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWanleeklndtTDRVQGENSTNVdiedlDRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1033 MAVSIGGIFASRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPI 1112
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1113 AAVIIPPLGLVYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIV 1192
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958656469 1193 ANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYS 1266
Cdd:cd18601 241 TSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEYS 314
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1044-1522 |
7.65e-65 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 232.30 E-value: 7.65e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1044 RRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLfSVIGAVIIILLATP-----IAAVIIP 1118
Cdd:PRK10790 98 QQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSA-ALIGAMLVAMFSLDwrmalVAIMIFP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1119 PLGLVYFFVQRFyvaSSRQLKRLESVsRSPVYSHFNETLLGVSVIRAFEEQERFIRqsdlKVDENQKAYYPSivanRWLA 1198
Cdd:PRK10790 177 AVLVVMVIYQRY---STPIVRRVRAY-LADINDGFNEVINGMSVIQQFRQQARFGE----RMGEASRSHYMA----RMQT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1199 VRLE--CVGNCIVLFAALF--AVISRHSLSA-GLVGLSVSYslqitAYLNWLVRMS----------SEMETNIVAVERLK 1263
Cdd:PRK10790 245 LRLDgfLLRPLLSLFSALIlcGLLMLFGFSAsGTIEVGVLY-----AFISYLGRLNeplielttqqSMLQQAVVAGERVF 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1264 EYSETEKeaswqiQETAPPSTWPHSGRVEFRDYCLRYREDlDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINE 1343
Cdd:PRK10790 320 ELMDGPR------QQYGNDDRPLQSGRIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1344 SAEGEIIIDGINIAKIGLHNLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAE 1423
Cdd:PRK10790 393 LTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGE 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1424 GGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEI 1503
Cdd:PRK10790 473 QGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQA 552
|
490
....*....|....*....
gi 1958656469 1504 RECGAPSELLQQRGVFYSM 1522
Cdd:PRK10790 553 VEQGTHQQLLAAQGRYWQM 571
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
645-845 |
1.94e-64 |
|
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: 217.97 E-value: 1.94e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDePPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTL-----------------KG 707
Cdd:cd03290 1 VQVTNGYFSWGSG-LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWsnknesepsfeatrsrnRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 708 SVAYVPQQAWIQNDSLRENILFGRPLQEHCYKAVMEACALLPDLEILPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNS 787
Cdd:cd03290 80 SVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 788 DIYLLDDPLSAVDAHVGKHIFEKvvGPMGLLKN--KTRILVTHGISYLPQVDVIIVMSGG 845
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQE--GILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1291-1522 |
1.14e-63 |
|
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: 216.71 E-value: 1.14e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLDlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITI 1370
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1371 IPQDPVLFSGSLRMNLdpfsQY-----SDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRK 1445
Cdd:cd03253 80 VPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656469 1446 TKILVLDEATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELLQQRGVFYSM 1522
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
362-617 |
3.23e-63 |
|
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: 217.47 E-value: 3.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 362 WQGYLYTALLFVSACLQTLALHQYFHICFVTGMRIKTAVVGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATY 441
Cdd:cd18593 37 TEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIYRKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 442 INMIWSAPLQVTLALYFLWLNLGPSVLAGVAVMILMVPFNAVMAmktktYQVAHMKSK-----DNRIKLMNEILNGIKVL 516
Cdd:cd18593 117 LHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFG-----KLFSKLRRKtaartDKRIRIMNEIINGIRVI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 517 KLYAWELAFQDKVMNIRQEELKVLKKSAYLAAV-GTFTWVCTPfLVALSTFAVFVTVDekNILDAKKAFVSLALFNILRF 595
Cdd:cd18593 192 KMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALnMGLFFVSSK-LILFLTFLAYILLG--NILTAERVFVTMALYNAVRL 268
|
250 260
....*....|....*....|...
gi 1958656469 596 PLNI-LPMVISSIVQASVSLKRL 617
Cdd:cd18593 269 TMTLfFPFAIQFGSELSVSIRRI 291
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1291-1502 |
7.72e-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: 208.78 E-value: 7.72e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITI 1370
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1371 IPQDPVLFSGSLRMNLdpfsqysdeevwmalelahlkgfvsalpdklnhecaeggenLSVGQRQLVCLARALLRKTKILV 1450
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958656469 1451 LDEATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGE 1502
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1291-1524 |
1.37e-60 |
|
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: 207.78 E-value: 1.37e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRY--REDLdLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKI 1368
Cdd:cd03249 1 IEFKNVSFRYpsRPDV-PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1369 TIIPQDPVLFSGSLRMNL-----DPfsqySDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALL 1443
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIrygkpDA----TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1444 RKTKILVLDEATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELLQQRGVFYSMA 1523
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
|
.
gi 1958656469 1524 K 1524
Cdd:cd03249 236 K 236
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1218-1522 |
1.63e-59 |
|
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: 216.61 E-value: 1.63e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1218 ISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYSETEKEaswqIQET--APPSTwPHSGRVEFRD 1295
Cdd:COG5265 288 VVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPE----VADApdAPPLV-VGGGEVRFEN 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1296 YCLRYREDlDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITIIPQDP 1375
Cdd:COG5265 363 VSFGYDPE-RPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDT 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1376 VLFSGSLRMNLdpfsQY-----SDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILV 1450
Cdd:COG5265 442 VLFNDTIAYNI----AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILI 517
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958656469 1451 LDEATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELLQQRGVFYSM 1522
Cdd:COG5265 518 FDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1038-1522 |
1.78e-59 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 219.21 E-value: 1.78e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1038 GGIF------ASRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATP 1111
Cdd:TIGR00958 222 GGSFnytmarINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSP 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1112 IAAVI----IPPLGLVYFFVQRFYVASSRQLKrlESVSRSPVYSHfnETLLGVSVIRAF--EEQE--RFIRQSDLKVDEN 1183
Cdd:TIGR00958 302 RLTMVtlinLPLVFLAEKVFGKRYQLLSEELQ--EAVAKANQVAE--EALSGMRTVRSFaaEEGEasRFKEALEETLQLN 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1184 QK---AYYPSIVANRWLAVRLECvgncIVLFAALFAVISRHSLSAGLVGLsVSYSLQITAYLNWLVRMSSEMETNIVAVE 1260
Cdd:TIGR00958 378 KRkalAYAGYLWTTSVLGMLIQV----LVLYYGGQLVLTGKVSSGNLVSF-LLYQEQLGEAVRVLSYVYSGMMQAVGASE 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1261 RLKEYSETEKeaswQIQET---APPstwPHSGRVEFRDYCLRY--REDLdLVLKHINVTIEGGEKVGIVGRTGAGKSSLT 1335
Cdd:TIGR00958 453 KVFEYLDRKP----NIPLTgtlAPL---NLEGLIEFQDVSFSYpnRPDV-PVLKGLTFTLHPGEVVALVGPSGSGKSTVA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1336 LGLFRINESAEGEIIIDGINIAKIGLHNLRFKITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWMALELAHLKGFVSALP 1414
Cdd:TIGR00958 525 ALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPDEEIMAAAKAANAHDFIMEFP 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1415 DKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTirTQFEDSTVLTIAHRLNTIMDYTR 1494
Cdd:TIGR00958 605 NGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQ 682
|
490 500
....*....|....*....|....*...
gi 1958656469 1495 VIVLDKGEIRECGAPSELLQQRGVFYSM 1522
Cdd:TIGR00958 683 ILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1019-1519 |
6.87e-58 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 211.42 E-value: 6.87e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1019 ALGILQGVAVF--GYSMA-VSIGGIFASRRlhlDLLQNVLRSPMSFFERTPSGNLVNRFskeldTVDSmiPQVIKMFMGS 1095
Cdd:PRK11176 73 GLMILRGITSFisSYCISwVSGKVVMTMRR---RLFGHMMGMPVSFFDKQSTGTLLSRI-----TYDS--EQVASSSSGA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1096 LFSVI--GAVIIILLA----------------TPIAAVIIpplGLVyffVQRFyvassRQLKRLESVSRSPVYSHFNETL 1157
Cdd:PRK11176 143 LITVVreGASIIGLFImmfyyswqlsliliviAPIVSIAI---RVV---SKRF-----RNISKNMQNTMGQVTTSAEQML 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1158 LGVSVIRAF----EEQERF------IRQSDLKVDENQKAYYPSI--VANRWLAVrlecvgnciVLFAALFAVIsRHSLSA 1225
Cdd:PRK11176 212 KGHKEVLIFggqeVETKRFdkvsnrMRQQGMKMVSASSISDPIIqlIASLALAF---------VLYAASFPSV-MDTLTA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1226 GLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEY--SETEKEASWQIQETAppstwphSGRVEFRDYCLRYRED 1303
Cdd:PRK11176 282 GTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAIldLEQEKDEGKRVIERA-------KGDIEFRNVTFTYPGK 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1304 LDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITIIPQDPVLFSGSLR 1383
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1384 MNLDPFS--QYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1461
Cdd:PRK11176 435 NNIAYARteQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTE 514
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 1462 TDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELLQQRGVF 1519
Cdd:PRK11176 515 SERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVY 572
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
452-868 |
4.07e-57 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 208.85 E-value: 4.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 452 VTLALYFLWLNLGPSVLAGVAVMILMVPFNAVMAMKTKTYQVAHMKSkDNRIKLMnEILNGIKVLKLY-AWElAFQDKVM 530
Cdd:COG4987 146 AVAFLAFFSPALALVLALGLLLAGLLLPLLAARLGRRAGRRLAAARA-ALRARLT-DLLQGAAELAAYgALD-RALARLD 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 531 NIRQEELKVLKKSAYLAAVGTFTwvcTPFLVALSTFAVFVTVD---EKNILDAKK----AFVSLALFNILRfPLnilPMV 603
Cdd:COG4987 223 AAEARLAAAQRRLARLSALAQAL---LQLAAGLAVVAVLWLAAplvAAGALSGPLlallVLAALALFEALA-PL---PAA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 604 ISSIVQASVSLKRLRIFLSHEELEPDSIERWSIKDGGgmnSITVKNATFTWARDEPPTLNGITFAIPDGALVAVVGQVGC 683
Cdd:COG4987 296 AQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGP---SLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGS 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 684 GKSSLLSALLAEMDKVEGHVTLKG-------------SVAYVPQQAWIQNDSLRENILFGRP------LqehcyKAVMEA 744
Cdd:COG4987 373 GKSTLLALLLRFLDPQSGSITLGGvdlrdldeddlrrRIAVVPQRPHLFDTTLRENLRLARPdatdeeL-----WAALER 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 745 CALLPDLEILPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRI 824
Cdd:COG4987 448 VGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADL---LEALAGRTVL 524
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1958656469 825 LVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFVR 868
Cdd:COG4987 525 LITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1289-1519 |
2.38e-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: 191.22 E-value: 2.38e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1289 GRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRInESAEGEIIIDGINIAKIGLHNLRFKI 1368
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1369 TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKI 1448
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958656469 1449 LVLDEATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELLQQRGVF 1519
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1291-1522 |
2.81e-54 |
|
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: 189.62 E-value: 2.81e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITI 1370
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1371 IPQDPVLFSGSLRMNL---DPfsQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTK 1447
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 1448 ILVLDEATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELLQQRGVFYSM 1522
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
341-617 |
4.05e-53 |
|
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: 188.15 E-value: 4.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 341 FAGPEIL-ELIINFVNDREAPDWQGYLYTALLFVSACLQTLALHQYFHICFVTGMRIKTAVVGAVYRKALVITNSARKSs 419
Cdd:cd18592 14 FIGPTILiRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKILRLRSLGDKS- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 420 tVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVTLALYFLWLNLGPSVLAGVAVMILMVPFNAVMAMKTKTYQVAHMKSK 499
Cdd:cd18592 93 -VGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVIT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 500 DNRIKLMNEILNGIKVLKLYAWELAFQDKVMNIRQEELKVLKKSAYLAAVGTftwVCTPFLVALSTFAVFVT-VDEKNIL 578
Cdd:cd18592 172 DKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISI---SLAPIVPVIASVVTFLAhVALGNDL 248
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958656469 579 DAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd18592 249 TAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1289-1503 |
1.21e-52 |
|
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: 184.33 E-value: 1.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1289 GRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDGINIAKIGLHNLR 1365
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLkllAGLYK---PTSGSVLLDGTDIRQLDPADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1366 FKITIIPQDPVLFSGSLRMNLDPFSQY-SDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLR 1444
Cdd:cd03245 78 RNIGYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656469 1445 KTKILVLDEATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEI 1503
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
644-861 |
7.98e-51 |
|
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: 189.97 E-value: 7.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 644 SITVKNATFTWArDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVA 710
Cdd:COG4988 336 SIELEDVSFSYP-GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpaswrrQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 711 YVPQQAWIQNDSLRENILFGRP------LQehcykAVMEACALLPDLEILPSGDLTEIGEKGVNLSGGQKQRVSLARAVY 784
Cdd:COG4988 415 WVPQNPYLFAGTIRENLRLGRPdasdeeLE-----AALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALL 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656469 785 CNSDIYLLDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDG 861
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETEAEILQAL---RRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1022-1522 |
6.76e-50 |
|
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: 190.34 E-value: 6.76e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1022 ILQGVAVFGYSMAVSIGGIFASRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMG-SLFSVI 1100
Cdd:TIGR01193 207 IIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDmWILVIV 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1101 GAVI---------IILLATPIAAVIIpplglvYFFVQRFYVASSRQLKrlesvSRSPVYSHFNETLLGVSVIRAF-EEQE 1170
Cdd:TIGR01193 287 GLFLvrqnmllflLSLLSIPVYAVII------ILFKRTFNKLNHDAMQ-----ANAVLNSSIIEDLNGIETIKSLtSEAE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1171 RFIRQSDLKVDENQKA--YYPSIVANRWLAVRLECVGNCIVLFAALFAVIsRHSLSAGLVglsVSYSLQITAYLNWL--- 1245
Cdd:TIGR01193 356 RYSKIDSEFGDYLNKSfkYQKADQGQQAIKAVTKLILNVVILWTGAYLVM-RGKLTLGQL---ITFNALLSYFLTPLeni 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1246 VRMSSEMETNIVAVERLKE--YSETEKEASWQIQETAPPStwphsGRVEFRDYCLRYREDlDLVLKHINVTIEGGEKVGI 1323
Cdd:TIGR01193 432 INLQPKLQAARVANNRLNEvyLVDSEFINKKKRTELNNLN-----GDIVINDVSYSYGYG-SNILSDISLTIKMNSKTTI 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1324 VGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITIIPQDPVLFSGSLRMNLDPFSQ--YSDEEVWMAL 1401
Cdd:TIGR01193 506 VGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKenVSQDEIWAAC 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1402 ELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIrTQFEDSTVLT 1481
Cdd:TIGR01193 586 EIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNL-LNLQDKTIIF 664
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1958656469 1482 IAHRLNTIMDYTRVIVLDKGEIRECGAPSELLQQRGVFYSM 1522
Cdd:TIGR01193 665 VAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
973-1242 |
2.84e-49 |
|
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: 176.68 E-value: 2.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 973 FLSIFLFLCNHVSALASNYWLSLWTDDRPAVNGTQENR-NFRLSVYGALGILQGVAVFGYSMAVSIGGIFASRRLHLDLL 1051
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQAlNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1052 QNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRFY 1131
Cdd:pfam00664 82 KKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1132 VASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLF 1211
Cdd:pfam00664 162 AKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYAL 241
|
250 260 270
....*....|....*....|....*....|...
gi 1958656469 1212 AALFAV--ISRHSLSAGLVGLSVSYSLQITAYL 1242
Cdd:pfam00664 242 ALWFGAylVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
660-884 |
3.51e-49 |
|
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: 176.59 E-value: 3.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 660 PTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIQNDSLRENILFGRPLQEHCYK 739
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 740 AVMEACALLPDLEILPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIFEKVVgpMGLLK 819
Cdd:cd03291 131 SVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCV--CKLMA 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 820 NKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFVRTYANTEQDLASEDDSV 884
Cdd:cd03291 209 NKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGYDTFDQFSAERRNSI 273
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1055-1524 |
6.40e-49 |
|
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: 186.70 E-value: 6.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1055 LRSPMSFFERTPSGNLVNRfskeLDTVDSMIPQ----VIKMFMGSLFSVIGAVII-------ILLATPIAAVIIpplgLV 1123
Cdd:TIGR03797 220 LRLPVSFFRQYSTGDLASR----AMGISQIRRIlsgsTLTTLLSGIFALLNLGLMfyyswklALVAVALALVAI----AV 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1124 YFFVQRFYVASSRQLKRLESVSRSPVYSHFNetllGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWLAVRLec 1203
Cdd:TIGR03797 292 TLVLGLLQVRKERRLLELSGKISGLTVQLIN----GISKLRVAGAENRAFARWAKLFSRQRKLELSAQRIENLLTVFN-- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1204 VGNCIVLFAALFAVISRHSLSAGL-VGLSVSYSLQITAYLNWLVRMSSEMeTNIVAV----ERLKEYSETEKEASwqiQE 1278
Cdd:TIGR03797 366 AVLPVLTSAALFAAAISLLGGAGLsLGSFLAFNTAFGSFSGAVTQLSNTL-ISILAViplwERAKPILEALPEVD---EA 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1279 TAPPStwPHSGRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSL---TLGlFRINESaeGEIIIDGIN 1355
Cdd:TIGR03797 442 KTDPG--KLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLlrlLLG-FETPES--GSVFYDGQD 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1356 IAKIGLHNLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQL 1435
Cdd:TIGR03797 517 LAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQR 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1436 VCLARALLRKTKILVLDEATAAVDLETDDLI-QSTIRTQfedSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELLQ 1514
Cdd:TIGR03797 597 LLIARALVRKPRILLFDEATSALDNRTQAIVsESLERLK---VTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMA 673
|
490
....*....|
gi 1958656469 1515 QRGVFYSMAK 1524
Cdd:TIGR03797 674 REGLFAQLAR 683
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
645-865 |
1.13e-48 |
|
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: 173.57 E-value: 1.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWArDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAY 711
Cdd:cd03253 1 IEFENVTFAYD-PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 712 VPQQAWIQNDSLRENILFGRP--LQEHCYKAVmEACALLPDLEILPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSDI 789
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPdaTDEEVIEAA-KAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 790 YLLDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAE 865
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAAL---RDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAE 231
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1054-1529 |
5.96e-48 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 182.08 E-value: 5.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1054 VLRSPMSFFERTPSGNLVNRFskeLDTVDSMIpQVIKMFMGSLFSVIGAVIIILlatPIA-------AVIIPPLGLVYFF 1126
Cdd:PRK13657 99 IIQLPLAWHSQRGSGRALHTL---LRGTDALF-GLWLEFMREHLATLVALVVLL---PLAlfmnwrlSLVLVVLGIVYTL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1127 VQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAF---EEQERFIRQSdlkVDENQKAYYPsiVANRW-LAVRLE 1202
Cdd:PRK13657 172 ITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYnriEAETQALRDI---ADNLLAAQMP--VLSWWaLASVLN 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1203 CVGNCIVLFAALF---AVISRHSLSAGLVGLSVSYSlqiTAYLNWLVRMSSEMETNIVAVERLKEYSETEkEASWQIQEt 1279
Cdd:PRK13657 247 RAASTITMLAILVlgaALVQKGQLRVGEVVAFVGFA---TLLIGRLDQVVAFINQVFMAAPKLEEFFEVE-DAVPDVRD- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1280 aPPSTWPH---SGRVEFRDYCLRY---REDLDlvlkHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG 1353
Cdd:PRK13657 322 -PPGAIDLgrvKGAVEFDDVSFSYdnsRQGVE----DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDG 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1354 INIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL-----DPfsqySDEEVWMALELAHLKGFVSALPDKLNHECAEGGENL 1428
Cdd:PRK13657 397 TDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIrvgrpDA----TDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQL 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1429 SVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGA 1508
Cdd:PRK13657 473 SGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGS 552
|
490 500
....*....|....*....|.
gi 1958656469 1509 PSELLQQRGVFYSMAKDAGLV 1529
Cdd:PRK13657 553 FDELVARGGRFAALLRAQGML 573
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
645-865 |
5.61e-47 |
|
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: 168.56 E-value: 5.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAY 711
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 712 VPQQAWIQNDSLRENILFGRPLQEHcyKAVMEAC--ALLPDL-EILPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSD 788
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATR--EEVEEAAraANAHEFiMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 789 IYLLDDPLSAVDAHVGKHI---FEKvvgpmgLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAE 865
Cdd:cd03251 159 ILILDEATSALDTESERLVqaaLER------LMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1019-1486 |
1.46e-45 |
|
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: 173.70 E-value: 1.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1019 ALGILQGVAVF-----GYSMAVSIGGifasrRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIkmfm 1093
Cdd:TIGR02868 61 AFGIGRAVFRYlerlvGHDAALRSLG-----ALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVI---- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1094 gslFSVIGAVIIILLATPIAAVIIPPLGLV--------YFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRA 1165
Cdd:TIGR02868 132 ---VPAGVALVVGAAAVAAIAVLSVPAALIlaaglllaGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1166 FEEQERFIRQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAV--ISRHSLSAGLVGLSVSYSLQITAYLN 1243
Cdd:TIGR02868 209 SGALPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGpaVADGRLAPVTLAVLVLLPLAAFEAFA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1244 WLVRMSSEMETNIVAVERLKEYSETEKEASWQIQETAPPSTwPHSGRVEFRDYCLRYrEDLDLVLKHINVTIEGGEKVGI 1323
Cdd:TIGR02868 289 ALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVG-LGKPTLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAI 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1324 VGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWMA 1400
Cdd:TIGR02868 367 LGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLrlaRP--DATDEELWAA 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1401 LELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDSTVL 1480
Cdd:TIGR02868 445 LERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVV 524
|
....*.
gi 1958656469 1481 TIAHRL 1486
Cdd:TIGR02868 525 LITHHL 530
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1289-1503 |
8.86e-45 |
|
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: 161.87 E-value: 8.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1289 GRVEFRDYCLRYREDLD-LVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFK 1367
Cdd:cd03248 10 GIVKFQNVTFAYPTRPDtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1368 ITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKT 1446
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656469 1447 KILVLDEATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEI 1503
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
645-868 |
9.19e-45 |
|
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: 162.32 E-value: 9.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTW-ARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS-------------VA 710
Cdd:cd03249 1 IEFKNVSFRYpSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 711 YVPQQAWIQNDSLRENILFGRPLQEHcyKAVMEAC--ALLPD-LEILPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNS 787
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAkkANIHDfIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 788 DIYLLDDPLSAVDAHVGKHIFEKVVGPMgllKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFV 867
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAM---KGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
|
.
gi 1958656469 868 R 868
Cdd:cd03249 236 K 236
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1018-1498 |
1.01e-44 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 170.93 E-value: 1.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1018 GALGILQGVAVFGYSMAVSiggifasRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDS----MIPQVIKMFM 1093
Cdd:TIGR02857 58 ALLGWLQERAAARAAAAVK-------SQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGyfarYLPQLVLAVI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1094 GSLfsVIGAVIiiLLATPIAAVII---PPLgLVYFFVQRFYVASSRQLKRLESVSRspVYSHFNETLLGVSVIRAF---- 1166
Cdd:TIGR02857 131 VPL--AILAAV--FPQDWISGLILlltAPL-IPIFMILIGWAAQAAARKQWAALSR--LSGHFLDRLRGLPTLKLFgrak 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1167 EEQERFIRQSD---------LKVdenqkAYYPSIVanrwlavrLEcvgncivLFA----ALFAVISRHSLSAGLVGLSVS 1233
Cdd:TIGR02857 204 AQAAAIRRSSEeyrertmrvLRI-----AFLSSAV--------LE-------LFAtlsvALVAVYIGFRLLAGDLDLATG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1234 YSLQITA---YLNwLVRMSSEMETNIVAVERLKEYSETEKEASWQIQETAPpSTWPHSGRVEFRDYCLRYrEDLDLVLKH 1310
Cdd:TIGR02857 264 LFVLLLApefYLP-LRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAP-VTAAPASSLEFSGVSVAY-PGRRPALRP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1311 INVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL---D 1387
Cdd:TIGR02857 341 VSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaR 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1388 PFSqySDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQ 1467
Cdd:TIGR02857 421 PDA--SDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVL 498
|
490 500 510
....*....|....*....|....*....|.
gi 1958656469 1468 STIRTQFEDSTVLTIAHRLNTIMDYTRVIVL 1498
Cdd:TIGR02857 499 EALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1311-1522 |
1.50e-43 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 168.87 E-value: 1.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1311 INVTIEGGEKVGIVGRTGAGKSSLT---LGLFrineSAEGEIIIDGINIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL- 1386
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLnalLGFL----PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVl 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1387 --DPfsQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDD 1464
Cdd:PRK11174 445 lgNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQ 522
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 1465 LIQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELLQQRGVFYSM 1522
Cdd:PRK11174 523 LVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
645-861 |
1.68e-42 |
|
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: 155.46 E-value: 1.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDEPpTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAY 711
Cdd:cd03254 3 IEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 712 VPQQAWIQNDSLRENILFGRPLQEHcyKAVMEACALL-PDLEI--LPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSD 788
Cdd:cd03254 82 VLQDTFLFSGTIMENIRLGRPNATD--EEVIEAAKEAgAHDFImkLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958656469 789 IYLLDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDG 861
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEAL---EKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1256-1522 |
1.54e-41 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 162.30 E-value: 1.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1256 IVAVERLKEYSETEKEASWQIQETAPPStwphSGRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLT 1335
Cdd:PRK11160 308 IASARRINEITEQKPEVTFPTTSTAAAD----QVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1336 LGLFRINESAEGEIIIDGINIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWMALELAHLKGFVSA 1412
Cdd:PRK11160 384 QLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKLLED 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1413 lPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRLNTI--M 1490
Cdd:PRK11160 462 -DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLeqF 540
|
250 260 270
....*....|....*....|....*....|..
gi 1958656469 1491 DytRVIVLDKGEIRECGAPSELLQQRGVFYSM 1522
Cdd:PRK11160 541 D--RICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
645-846 |
2.21e-41 |
|
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: 150.23 E-value: 2.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAY 711
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 712 VPQQAWIQNDSLRENILfgrplqehcykavmeacallpdleilpsgdlteigekgvnlSGGQKQRVSLARAVYCNSDIYL 791
Cdd:cd03228 81 VPQDPFLFSGTIRENIL-----------------------------------------SGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 792 LDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGK 846
Cdd:cd03228 120 LDEATSALDPETEALILEAL---RALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
326-597 |
1.21e-40 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 151.64 E-value: 1.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 326 FLMSFLYKALHDLMMFAGPEILELIINFVNDREAPDWQGYLYTALLFVSACL-QTLALHQYFHICFVTGMRIKTAVVGAV 404
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLaQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 405 YRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVTLALYFLWLNLGPSV-LAGVAVMILMVPFNAV 483
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLtLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 484 MAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMNIRQEELKV-LKKSAYLAAVGTFTWVCTPFLVA 562
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAgIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....*
gi 1958656469 563 LSTFAVFVTVDeKNILDAKKAFVSLALFNILRFPL 597
Cdd:pfam00664 241 LALWFGAYLVI-SGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
644-847 |
2.16e-39 |
|
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: 146.20 E-value: 2.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 644 SITVKNATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVA 710
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 711 YVPQQAWIQNDSLRENILFGRPLQEHcyKAVMEACALL---PDLEILPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNS 787
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLADD--ERILRAAELAgvtDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 788 DIYLLDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKI 847
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERL---RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1291-1516 |
6.98e-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: 145.17 E-value: 6.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDlDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTL---GLFRINEsaeGEIIIDGINIAKIGLHNLRFK 1367
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRllnGLLKPTS---GEVLVDGKDITKKNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1368 ITIIPQDPV--LFSGSLR-------MNLdpfsQYSDEE----VWMALELAHLKGFvsalpdkLNHECAEggenLSVGQRQ 1434
Cdd:COG1122 77 VGLVFQNPDdqLFAPTVEedvafgpENL----GLPREEirerVEEALELVGLEHL-------ADRPPHE----LSGGQKQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1435 LVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRT-QFEDSTVLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSEL 1512
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAELAdRVIVLDDGRIVADGTPREV 221
|
....
gi 1958656469 1513 LQQR 1516
Cdd:COG1122 222 FSDY 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
644-842 |
2.68e-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: 148.97 E-value: 2.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 644 SITVKNATFTWaRDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVA 710
Cdd:TIGR02857 321 SLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 711 YVPQQAWIQNDSLRENILFGRPLQ-EHCYKAVMEACALLPDLEILPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSDI 789
Cdd:TIGR02857 400 WVPQHPFLFAGTIAENIRLARPDAsDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958656469 790 YLLDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYLPQVDVIIVM 842
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEAL---RALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
642-1526 |
5.07e-36 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 149.79 E-value: 5.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 642 MNSITVKNATFTW-ARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS------------ 708
Cdd:PTZ00265 380 IKKIQFKNVRFHYdTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwr 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 709 --VAYVPQQAWIQNDSLRENILF------------------GRPLQEHCYK--AVMEACA-------------------- 746
Cdd:PTZ00265 460 skIGVVSQDPLLFSNSIKNNIKYslyslkdlealsnyynedGNDSQENKNKrnSCRAKCAgdlndmsnttdsneliemrk 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 747 ---LLPDLEI---------------LPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDaHVGKHIF 808
Cdd:PTZ00265 540 nyqTIKDSEVvdvskkvlihdfvsaLPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLV 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 809 EKVVGPMGLLKNKTRILVTHGISYLPQVDVIIVMS--------------------------------------------- 843
Cdd:PTZ00265 619 QKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSnrergstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkin 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 844 --GGKISEMGSYQELL-DRDGAFAEFV-------RTYANTEQDLASedDSVSGLGKESkpvENGILVTDAVGkpLQRHLS 913
Cdd:PTZ00265 699 naGSYIIEQGTHDALMkNKNGIYYTMInnqkvssKKSSNNDNDKDS--DMKSSAYKDS---ERGYDPDEMNG--NSKHEN 771
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 914 NSSSHSVVTNQQHSSTAELQKSGVKEETWKLMEADKAQTGQVKLsVY---WNYMKAIglCISFLSIFLF--LCNHVSALA 988
Cdd:PTZ00265 772 ESASNKKSCKMSDENASENNAGGKLPFLRNLFKRKPKAPNNLRI-VYreiFSYKKDV--TIIALSILVAggLYPVFALLY 848
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 989 SNYWLSLWTddrpaVNGTQENRNfRLSVYgalgilqgVAVFGYSMAVS---------IGGIFASRRLHLDLLQNVLRSPM 1059
Cdd:PTZ00265 849 AKYVSTLFD-----FANLEANSN-KYSLY--------ILVIAIAMFISetlknyynnVIGEKVEKTMKRRLFENILYQEI 914
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1060 SFFER---TPsGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIippLGLVYFFVQRFYVASSR 1136
Cdd:PTZ00265 915 SFFDQdkhAP-GLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVAAV---LTGTYFIFMRVFAIRAR 990
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1137 -------QLKRLESVSRSPVYSH-----------FNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWLA 1198
Cdd:PTZ00265 991 ltankdvEKKEINQPGTVFAYNSddeifkdpsflIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLW 1070
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1199 VRLECVGNCIVLFAALFA--VISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLkeYSETEKEASWQI 1276
Cdd:PTZ00265 1071 GFSQSAQLFINSFAYWFGsfLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKY--YPLIIRKSNIDV 1148
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1277 QETAP---PSTWPHSGRVEFRDYCLRYREDLDL-VLKHINVTIEGGEKVGIVGRTGAGKSSL------------------ 1334
Cdd:PTZ00265 1149 RDNGGiriKNKNDIKGKIEIMDVNFRYISRPNVpIYKDLTFSCDSKKTTAIVGETGSGKSTVmsllmrfydlkndhhivf 1228
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1335 --------------------TLGLFRINESA----------------EGEIIIDGINIAKIGLHNLRFKITIIPQDPVLF 1378
Cdd:PTZ00265 1229 knehtndmtneqdyqgdeeqNVGMKNVNEFSltkeggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLF 1308
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1379 SGSLRMNLDpFSQ--YSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1456
Cdd:PTZ00265 1309 NMSIYENIK-FGKedATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATS 1387
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 1457 AVDLETDDLIQSTIR--TQFEDSTVLTIAHRLNTIMDYTRVIVLDKGE-----IRECGAPSELLQ-QRGVFYSMAKDA 1526
Cdd:PTZ00265 1388 SLDSNSEKLIEKTIVdiKDKADKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSvQDGVYKKYVKLA 1465
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
395-828 |
2.51e-35 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 142.88 E-value: 2.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 395 RIKTAVVGAVYRKALVITNSARKSSTVGEIVNLMS--VDAQRFMDLATYINMIWSAPL--QVTLALYFLWLNLGPSVLAG 470
Cdd:TIGR02868 83 RSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGadVDALQDLYVRVIVPAGVALVVgaAAVAAIAVLSVPAALILAAG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 471 VAVMILMVPFNAVMAMKTKTYQVAHMKSKDNRiKLMnEILNGIKVLKLYAWELAFQDKVMNIRQEELKVLKKSAYLAAVG 550
Cdd:TIGR02868 163 LLLAGFVAPLVSLRAARAAEQALARLRGELAA-QLT-DALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 551 T--FTWVCTpfLVALSTFAVFVTVDEKNILD----AKKAFVSLALFNilrfPLNILPMVISSIVQASVSLKRLriflshE 624
Cdd:TIGR02868 241 AalTLLAAG--LAVLGALWAGGPAVADGRLApvtlAVLVLLPLAAFE----AFAALPAAAQQLTRVRAAAERI------V 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 625 ELEPDSIERWSIKD------GGGMNSITVKNATFTWArDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDK 698
Cdd:TIGR02868 309 EVLDAAGPVAEGSApaagavGLGKPTLELRDLSAGYP-GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 699 VEGHVTLKGS-------------VAYVPQQAWIQNDSLRENILFGRP--LQEHCYKAvMEACALLPDLEILPSGDLTEIG 763
Cdd:TIGR02868 388 LQGEVTLDGVpvssldqdevrrrVSVCAQDAHLFDTTVRENLRLARPdaTDEELWAA-LERVGLADWLRALPDGLDTVLG 466
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 764 EKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIFEKVVGPMgllKNKTRILVTH 828
Cdd:TIGR02868 467 EGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAAL---SGRTVVLITH 528
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
645-868 |
3.54e-34 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 140.15 E-value: 3.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAY 711
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlaslrnQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 712 VPQQAWIQNDSLRENILFGRplQEHCYKAVMEACALLPD----LEILPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNS 787
Cdd:PRK11176 422 VSQNVHLFNDTIANNIAYAR--TEQYSREQIEEAARMAYamdfINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 788 DIYLLDDPLSAVDAHVGKHI---FEKvvgpmgLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFA 864
Cdd:PRK11176 500 PILILDEATSALDTESERAIqaaLDE------LQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYA 573
|
....
gi 1958656469 865 EFVR 868
Cdd:PRK11176 574 QLHK 577
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
645-867 |
1.18e-33 |
|
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: 130.30 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSAL----LAEMDKV--EGH-------VTLKGSVAY 711
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIqrfyVPENGRVlvDGHdlaladpAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 712 VPQQAWIQNDSLRENILFGRPLQEhcYKAVMEACALLPDLEI---LPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSD 788
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMS--MERVIEAAKLAGAHDFiseLPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656469 789 IYLLDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFV 867
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNM---HDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLY 234
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1292-1502 |
1.23e-33 |
|
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: 129.51 E-value: 1.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1292 EFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITII 1371
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1372 PQDP------------VLFsgSLRmNLdpfsQYSDEEVWMALELAhLKGFvsALPDKLNHECAEggenLSVGQRQLVCLA 1439
Cdd:cd03225 81 FQNPddqffgptveeeVAF--GLE-NL----GLPEEEIEERVEEA-LELV--GLEGLRDRSPFT----LSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 1440 RALLRKTKILVLDEATAAVDLETDDLIQSTIRT-QFEDSTVLTIAHRLNTIMDY-TRVIVLDKGE 1502
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
644-866 |
2.05e-33 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 137.65 E-value: 2.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 644 SITVKNATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVA 710
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiadyseaalrqAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 711 YVPQQAWIQNDSLRENILFGRP-LQEHCYKAVMEACALlpdleilpsGDLTE--------IGEKGVNLSGGQKQRVSLAR 781
Cdd:PRK11160 418 VVSQRVHLFSATLRDNLLLAAPnASDEALIEVLQQVGL---------EKLLEddkglnawLGEGGRQLSGGEQRRLGIAR 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 782 AVYCNSDIYLLDDPLSAVDAHVGKHIFEkvvgpmgLL----KNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELL 857
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERQILE-------LLaehaQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
....*....
gi 1958656469 858 DRDGAFAEF 866
Cdd:PRK11160 562 AQQGRYYQL 570
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1291-1507 |
2.06e-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: 127.43 E-value: 2.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLtLGLFRINESA-EGEIIIDGINIAKIGlHNLRFKIT 1369
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTL-LQLLTGDLKPqQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1370 IIPQDPVLFSGSLRMNLdpfsqysdeevwmalelahlkgfvsalpdklnhecaegGENLSVGQRQLVCLARALLRKTKIL 1449
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 1450 VLDEATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECG 1507
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1292-1503 |
2.39e-33 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 127.33 E-value: 2.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1292 EFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDGINIAKIGLHNLRFKI 1368
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLArliLGLLR---PTSGRVRLDGADISQWDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1369 TIIPQDPVLFSGSLRMNLdpfsqysdeevwmalelahlkgfvsalpdklnhecaeggenLSVGQRQLVCLARALLRKTKI 1448
Cdd:cd03246 79 GYLPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 1449 LVLDEATAAVDLETDDLIQSTI-RTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEI 1503
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIaALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
620-868 |
2.60e-33 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 137.67 E-value: 2.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 620 FLSHEELEPDSIERwSIKDGGGmNSITVKNATFTwARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMdKV 699
Cdd:PRK11174 327 FLETPLAHPQQGEK-ELASNDP-VTIEAEDLEIL-SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PY 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 700 EGHVTLKG------SVAYVPQQ-AWI-QN-----DSLRENILFGRP-LQEHCYKAVMEACALLPDLEILPSGDLTEIGEK 765
Cdd:PRK11174 403 QGSLKINGielrelDPESWRKHlSWVgQNpqlphGTLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQ 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 766 GVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIFEKVVGPMgllKNKTRILVTHGISYLPQVDVIIVMSGG 845
Cdd:PRK11174 483 AAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS---RRQTTLMVTHQLEDLAQWDQIWVMQDG 559
|
250 260
....*....|....*....|...
gi 1958656469 846 KISEMGSYQELLDRDGAFAEFVR 868
Cdd:PRK11174 560 QIVQQGDYAELSQAGGLFATLLA 582
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
583-893 |
2.77e-33 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 137.40 E-value: 2.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 583 AFVSLALFNILRfplniLPMVISSIVQASVSLKRLRIFLSHEELEPDSIERWSIKDGGGMN-SITVKNATFTWArDEPPT 661
Cdd:PRK13657 277 AFVGFATLLIGR-----LDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDLGRVKgAVEFDDVSFSYD-NSRQG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAYVPQQAWIQNDSLRENIL 728
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtvtraslrrNIAVVFQDAGLFNRSIEDNIR 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 729 FGRP--LQEHCYKAvMEACALLPDLEILPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGkh 806
Cdd:PRK13657 431 VGRPdaTDEEMRAA-AERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETE-- 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 807 ifEKVVGPM-GLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFVRTyanteQDLASEDDSVS 885
Cdd:PRK13657 508 --AKVKAALdELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRA-----QGMLQEDERRK 580
|
....*...
gi 1958656469 886 GLGKESKP 893
Cdd:PRK13657 581 QPAAEGAN 588
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
597-886 |
6.55e-33 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 136.00 E-value: 6.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 597 LNILPMV----ISSIVQ-ASVSLKRLRIFLSHEELEPDSIErwSIKDGGGMNSITVKnaTFTWARDEPPTLNGITFAIPD 671
Cdd:PRK10789 265 LMIWPMLalawMFNIVErGSAAYSRIRAMLAEAPVVKDGSE--PVPEGRGELDVNIR--QFTYPQTDHPALENVNFTLKP 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 672 GALVAVVGQVGCGKSSLLSALLAEMDKVEGHVT-------------LKGSVAYVPQQAWIQNDSLRENILFGRP--LQEH 736
Cdd:PRK10789 341 GQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRfhdipltklqldsWRSRLAVVSQTPFLFSDTVANNIALGRPdaTQQE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 737 CYKAVMEACaLLPDLEILPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIfekvvgpmg 816
Cdd:PRK10789 421 IEHVARLAS-VHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQI--------- 490
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656469 817 lLKN-------KTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFVRtYANTEQDLASEDDSVSG 886
Cdd:PRK10789 491 -LHNlrqwgegRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYR-YQQLEAALDDAPEIREE 565
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
644-852 |
1.63e-32 |
|
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: 126.45 E-value: 1.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 644 SITVKNATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVT-------------LKGSVA 710
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILidgvdiskiglhdLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 711 YVPQQAWIQNDSLRENIlfgRPLQEHCYKAVMEA---CALLPDLEILPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNS 787
Cdd:cd03244 82 IIPQDPVLFSGTIRSNL---DPFGEYSDEELWQAlerVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 788 DIYLLDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGS 852
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTI---REAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1307-1507 |
2.24e-32 |
|
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: 126.47 E-value: 2.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG---LHNLRFKITIIPQDPvlfSGSL- 1382
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVFQDP---MSSLn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1383 -RMN-----LDPF------SQYSDEEVWMALELAHLkGFVSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILV 1450
Cdd:cd03257 97 pRMTigeqiAEPLrihgklSKKEARKEAVLLLLVGV-GLPEEVLNRYPHE-------LSGGQRQRVAIARALALNPKLLI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958656469 1451 LDEATAAVDLETDDLIQST---IRTQFeDSTVLTIAHRLNTIMDYT-RVIVLDKGEIRECG 1507
Cdd:cd03257 169 ADEPTSALDVSVQAQILDLlkkLQEEL-GLTLLFITHDLGVVAKIAdRVAVMYAGKIVEEG 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
642-860 |
3.36e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 126.36 E-value: 3.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 642 MNSITVKNATFtwARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG--------SVAYVP 713
Cdd:COG1121 4 MPAIELENLTV--SYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 714 QQAWIQND---SLRENILFGR--------PLQEHCYKAVMEACALLpdleilpsgDLTE-----IGEkgvnLSGGQKQRV 777
Cdd:COG1121 82 QRAEVDWDfpiTVRDVVLMGRygrrglfrRPSRADREAVDEALERV---------GLEDladrpIGE----LSGGQQQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 778 SLARAVYCNSDIYLLDDPLSAVDAHVGKHIFEkvvgpmgLLK-----NKTRILVTHGISYLPQ-VDVIIVMSGGKISEmG 851
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYE-------LLRelrreGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-G 220
|
....*....
gi 1958656469 852 SYQELLDRD 860
Cdd:COG1121 221 PPEEVLTPE 229
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1292-1502 |
7.89e-32 |
|
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: 122.35 E-value: 7.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1292 EFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITII 1371
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1372 PQdpvlfsgslrmnldpfsqysdeevwmalelahlkgfvsalpdklnhecaeggenLSVGQRQLVCLARALLRKTKILVL 1451
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958656469 1452 DEATAAVDLETDDLIQSTIRTQFED-STVLTIAHRLNTIMDYT-RVIVLDKGE 1502
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAAdRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1290-1513 |
3.37e-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: 123.62 E-value: 3.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1290 RVEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKIT 1369
Cdd:COG1120 1 MLEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1370 IIPQDPVL-FSGSLR----M----NLDPFSQYSDEE---VWMALELAHLkgfvSALPDKLNHEcaeggenLSVGQRQLVC 1437
Cdd:COG1120 79 YVPQEPPApFGLTVRelvaLgrypHLGLFGRPSAEDreaVEEALERTGL----EHLADRPVDE-------LSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1438 LARALLRKTKILVLDEATAAVDL----ETDDLIQSTIRTQfeDSTVLTIAHRLNTIMDY-TRVIVLDKGEIRECGAPSEL 1512
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARER--GRTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGPPEEV 225
|
.
gi 1958656469 1513 L 1513
Cdd:COG1120 226 L 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1291-1515 |
4.32e-31 |
|
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: 129.64 E-value: 4.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTL---GLFRINESAEGEIIIDGINIAKIGLHNLRFK 1367
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALalmGLLPHGGRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1368 ITIIPQDP------------VLFsgSLRMNLDPFSQySDEEVWMALELAHLKGFVSALPdklnHEcaeggenLSVGQRQL 1435
Cdd:COG1123 85 IGMVFQDPmtqlnpvtvgdqIAE--ALENLGLSRAE-ARARVLELLEAVGLERRLDRYP----HQ-------LSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1436 VCLARALLRKTKILVLDEATAAVDLETDDLIQSTIR--TQFEDSTVLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSEL 1512
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEIAdRVVVMDDGRIVEDGPPEEI 230
|
...
gi 1958656469 1513 LQQ 1515
Cdd:COG1123 231 LAA 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
596-865 |
6.64e-31 |
|
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: 130.33 E-value: 6.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 596 PLNILPMVISSIVQASVSLKRLriF-LSHEELEP-DSIERWSIKDGGGmnSITVKNATFTWaRDEPPTLNGITFAIPDGA 673
Cdd:COG5265 311 PLNFLGFVYREIRQALADMERM--FdLLDQPPEVaDAPDAPPLVVGGG--EVRFENVSFGY-DPERPILKGVSFEVPAGK 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 674 LVAVVGQVGCGKSSLLSALLAEMDKVEG----------HVT---LKGSVAYVPQQAWIQNDSLRENILFGRPlqeHCYKA 740
Cdd:COG5265 386 TVAIVGPSGAGKSTLARLLFRFYDVTSGrilidgqdirDVTqasLRAAIGIVPQDTVLFNDTIAYNIAYGRP---DASEE 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 741 VMEACALLPDL----EILPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIFE--KVVGp 814
Cdd:COG5265 463 EVEAAARAAQIhdfiESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAalREVA- 541
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958656469 815 mgllKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAE 865
Cdd:COG5265 542 ----RGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQ 588
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1308-1456 |
9.87e-31 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 118.90 E-value: 9.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1308 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITIIPQDPVLFSGS-----L 1382
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLtvrenL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 1383 RMNLDPFSQYSDE-EVWMALELAHLKgfvsaLPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1456
Cdd:pfam00005 81 RLGLLLKGLSKREkDARAEEALEKLG-----LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1291-1522 |
7.20e-30 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 126.75 E-value: 7.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYClrYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITI 1370
Cdd:PRK10789 316 VNIRQFT--YPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1371 IPQDPVLFSGSLRMNL---DPfsQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTK 1447
Cdd:PRK10789 394 VSQTPFLFSDTVANNIalgRP--DATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAE 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 1448 ILVLDEATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELLQQRGVFYSM 1522
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDM 546
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
660-865 |
1.37e-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: 127.16 E-value: 1.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 660 PTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------TLKGSVAYVPQQAWIQNDSLREN 726
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEIllngfslkdidrhTLRQFINYLPQEPYIFSGSILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 727 ILFG--RPLQEHCYKAVMEACALLPDLEILPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVG 804
Cdd:TIGR01193 568 LLLGakENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958656469 805 KHIFEKVVGpmglLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAE 865
Cdd:TIGR01193 648 KKIVNNLLN----LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYAS 704
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
645-847 |
3.66e-29 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 115.01 E-value: 3.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS-------------VAY 711
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 712 VPQQAWIQNDSLRENILfgrplqehcykavmeacallpdleilpsgdlteigekgvnlSGGQKQRVSLARAVYCNSDIYL 791
Cdd:cd03246 81 LPQDDELFSGSIAENIL-----------------------------------------SGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 792 LDDPLSAVDaHVGKHIFEKVVGPMGlLKNKTRILVTHGISYLPQVDVIIVMSGGKI 847
Cdd:cd03246 120 LDEPNSHLD-VEGERALNQAIAALK-AAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
645-867 |
4.02e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 125.60 E-value: 4.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTW-ARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVA 710
Cdd:TIGR00958 479 IEFQDVSFSYpNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 711 YVPQQAWIQNDSLRENILFG--RPLQEHCYKAVMEACALLPDLEiLPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSD 788
Cdd:TIGR00958 559 LVGQEPVLFSGSVRENIAYGltDTPDEEIMAAAKAANAHDFIME-FPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPR 637
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656469 789 IYLLDDPLSAVDAHVgkhifEKVVGPMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFV 867
Cdd:TIGR00958 638 VLILDEATSALDAEC-----EQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
647-846 |
6.47e-29 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 115.64 E-value: 6.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 647 VKNATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAYVP 713
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelrrKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 714 QQAWIQ--NDSLRENILFGrPLQEHCYKAVMEACAllpdLEILPSGDLTEIGEKGV-NLSGGQKQRVSLARAVYCNSDIY 790
Cdd:cd03225 82 QNPDDQffGPTVEEEVAFG-LENLGLPEEEIEERV----EEALELVGLEGLRDRSPfTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656469 791 LLDDPLSAVDAHVGKHIFEKVVGpmglLKN--KTRILVTHGISYLPQV-DVIIVMSGGK 846
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKK----LKAegKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
645-847 |
8.39e-29 |
|
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: 115.66 E-value: 8.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDEPPT--LNGITFAIPDGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKG-------------- 707
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVRVDGtdisklsekelaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 708 ---SVAYVPQQ-AWIQNDSLRENILF-----GRPLQEHCYKAvmeacallpdLEILPSGDLTEIGEKGVN-LSGGQKQRV 777
Cdd:cd03255 80 rrrHIGFVFQSfNLLPDLTALENVELplllaGVPKKERRERA----------EELLERVGLGDRLNHYPSeLSGGQQQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 778 SLARAVYCNSDIYLLDDPLSAVDAHVGKHIfekvvgpMGLLK------NKTRILVTHGISYLPQVDVIIVMSGGKI 847
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEV-------MELLRelnkeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1291-1515 |
1.14e-28 |
|
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: 122.32 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRD----YCLRYREDLDlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG---LHN 1363
Cdd:COG1123 261 LEVRNlskrYPVRGKGGVR-AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1364 LRFKITIIPQDPvlfSGSL--RMN--------LDPFSQYSDEEVW-MALELAHLKGFVSALPDKLNHEcaeggenLSVGQ 1432
Cdd:COG1123 340 LRRRVQMVFQDP---YSSLnpRMTvgdiiaepLRLHGLLSRAERReRVAELLERVGLPPDLADRYPHE-------LSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1433 RQLVCLARALLRKTKILVLDEATAAVDLetddLIQSTIRTQFED------STVLTIAHRLNTIMDYT-RVIVLDKGEIRE 1505
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDV----SVQAQILNLLRDlqrelgLTYLFISHDLAVVRYIAdRVAVMYDGRIVE 485
|
250
....*....|
gi 1958656469 1506 CGAPSELLQQ 1515
Cdd:COG1123 486 DGPTEEVFAN 495
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
647-847 |
2.07e-28 |
|
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: 114.55 E-value: 2.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 647 VKNATFTWarDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG--------SVAYVPQQAWI 718
Cdd:cd03235 2 VEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 719 QND---SLRENIL--------FGRPLQEHCYKAVMEAcallpdLEILPSGDLTE--IGEkgvnLSGGQKQRVSLARAVYC 785
Cdd:cd03235 80 DRDfpiSVRDVVLmglyghkgLFRRLSKADKAKVDEA------LERVGLSELADrqIGE----LSGGQQQRVLLARALVQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 786 NSDIYLLDDPLSAVDAHVGKHIFEkvvgpmgLLK-----NKTRILVTHGI-SYLPQVDVIIVMSGGKI 847
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYE-------LLRelrreGMTILVVTHDLgLVLEYFDRVLLLNRTVV 210
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1291-1502 |
6.40e-28 |
|
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: 112.56 E-value: 6.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRY---REDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLfrINESA--EGEIIIDGiniakiglhnlr 1365
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGELEklSGSVSVPG------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1366 fKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRK 1445
Cdd:cd03250 67 -SIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958656469 1446 TKILVLDEATAAVDLET-----DDLIQSTIRtqfEDSTVLTIAHRLNTIMDYTRVIVLDKGE 1502
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVgrhifENCILGLLL---NNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1307-1514 |
1.12e-27 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 113.36 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITIIPQDPvlfSGSL--RM 1384
Cdd:COG1124 20 VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDP---YASLhpRH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1385 NLD-----PFS----QYSDEEVWMALELAHLKgfvSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEAT 1455
Cdd:COG1124 97 TVDrilaePLRihglPDREERIAELLEQVGLP---PSFLDRYPHQ-------LSGGQRQRVAIARALILEPELLLLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 1456 AAVDL----ETDDLIQStIRTQfEDSTVLTIAHRLNTImDY--TRVIVLDKGEIRECGAPSELLQ 1514
Cdd:COG1124 167 SALDVsvqaEILNLLKD-LREE-RGLTYLFVSHDLAVV-AHlcDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1291-1512 |
1.63e-27 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 112.27 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINES-----AEGEIIIDGINIAKIGLH--N 1363
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1364 LRFKITIIPQDPVLFSGSLRMNLDpfsqYS------------DEEVWMALELAHLKGFVSalpDKLNhecaegGENLSVG 1431
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVA----YGlrlhgiklkeelDERVEEALRKAALWDEVK---DRLH------ALGLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1432 QRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRLNT---IMDYTrvIVLDKGEIRECGA 1508
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQaarVADRT--AFLLNGRLVEFGP 223
|
....
gi 1958656469 1509 PSEL 1512
Cdd:cd03260 224 TEQI 227
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
606-859 |
1.91e-27 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 119.08 E-value: 1.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 606 SIVQASVSLKRLRIFLSHEELEPDsierwsikdggGM------NSITVKNATFTWARDEPPTLNGITFAIPDGALVAVVG 679
Cdd:COG4618 297 QFVSARQAYRRLNELLAAVPAEPE-----------RMplprpkGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIG 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 680 QVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAYVPQQAWIQNDSLRENI-LFGRPLQEhcykAVMEAC 745
Cdd:COG4618 366 PSGSGKSTLARLLVGVWPPTAGSVRLDGadlsqwdreelgrHIGYLPQDVELFDGTIAENIaRFGDADPE----KVVAAA 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 746 AL--LPDLeI--LPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAhvgkhifekvVGPMGLL--- 818
Cdd:COG4618 442 KLagVHEM-IlrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD----------EGEAALAaai 510
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1958656469 819 -----KNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDR 859
Cdd:COG4618 511 ralkaRGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1259-1501 |
2.51e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 119.14 E-value: 2.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1259 VERLKEYSETEKEASwQIQETAPPSTWPHSGRVEFRDYCLRyREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLtlgl 1338
Cdd:COG4178 332 VDRLAGFEEALEAAD-ALPEAASRIETSEDGALALEDLTLR-TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTL---- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1339 FR----INESAEGEIII-DGINIAkiglhnlrfkitIIPQDPVLFSGSLRMNL---DPFSQYSDEEVWMALELAHLkgfv 1410
Cdd:COG4178 406 LRaiagLWPYGSGRIARpAGARVL------------FLPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGL---- 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1411 SALPDKLnHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRlNTIM 1490
Cdd:COG4178 470 GHLAERL-DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR-STLA 547
|
250
....*....|..
gi 1958656469 1491 DY-TRVIVLDKG 1501
Cdd:COG4178 548 AFhDRVLELTGD 559
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1291-1514 |
4.59e-27 |
|
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: 111.05 E-value: 4.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDGINIAK---IGLHNL 1364
Cdd:cd03261 1 IELRGLTKSFGGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLrliVGLLR---PDSGEVLIDGEDISGlseAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1365 RFKITIIPQDPVLFSG-SLRMN----LDPFSQYSDEE----VWMALELAHLKGFVSALPDklnhecaeggeNLSVGQRQL 1435
Cdd:cd03261 76 RRRMGMLFQSGALFDSlTVFENvafpLREHTRLSEEEireiVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1436 VCLARALLRKTKILVLDEATAAVD----LETDDLIQSTIRTQfeDSTVLTIAHRLNTIM---DytRVIVLDKGEIRECGA 1508
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDpiasGVIDDLIRSLKKEL--GLTSIMVTHDLDTAFaiaD--RIAVLYDGKIVAEGT 220
|
....*.
gi 1958656469 1509 PSELLQ 1514
Cdd:cd03261 221 PEELRA 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
662-797 |
5.00e-27 |
|
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: 108.12 E-value: 5.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAYVPQQAWIQND-SLRENI 727
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958656469 728 LFGRPLQEHCYKAV-MEACALLPDLEILPSGDlTEIGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLS 797
Cdd:pfam00005 81 RLGLLLKGLSKREKdARAEEALEKLGLGDLAD-RPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1307-1517 |
6.82e-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: 111.10 E-value: 6.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRfKITIIPQDPVLFSG-SLRMN 1385
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARR-QIGVLPDERGLYDRlTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1386 LD---PFSQYSDEEVWMALE-LAHLKGfvsaLPDKLNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1461
Cdd:COG4555 95 IRyfaELYGLFDEELKKRIEeLIELLG----LEEFLDRRVGE----LSTGMKKKVALARALVHDPKVLLLDEPTNGLDVM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 1462 TDDLIQSTIRTQF-EDSTVLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSELLQQRG 1517
Cdd:COG4555 167 ARRLLREILRALKkEGKTVLFSSHIMQEVEALCdRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
961-1262 |
6.84e-27 |
|
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: 113.36 E-value: 6.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 961 WN-YMKAIGLCISFLsIFLFLCNHVSAL---ASNYWLSLWTDDRPAVNGTQENRNFR--------LSVYGALGILQGVAV 1028
Cdd:cd18600 3 WNtYLRYITSHKSLI-FVLILCLVIFAIevaASLVGLWLLRSQADRVNTTRPESSSNtyavivtfTSSYYVFYIYVGVAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1029 FGYSMAVSIG------GIFASRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGA 1102
Cdd:cd18600 82 SLLAMGFFRGlplvhtLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1103 VIIILLATPIAAVIIPPLGLVYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDE 1182
Cdd:cd18600 162 ITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALNL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1183 NQKAYYPSIVANRWLAVRLECVgncIVLF--AALFAVISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVE 1260
Cdd:cd18600 242 HTANWFLYLSTLRWFQMRIEMI---FVIFftAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVS 318
|
..
gi 1958656469 1261 RL 1262
Cdd:cd18600 319 RI 320
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1291-1515 |
1.01e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 110.56 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSL---TLGLFRInesAEGEIIIDGINIAK----IG--- 1360
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLlkaILGLLPP---TSGTVRLFGKPPRRarrrIGyvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1361 ---LHNLRFKITIipQDPVLfsgslrMNLDP----FSQYSDEE---VWMALELAHLKGF----VSALpdklnhecaegge 1426
Cdd:COG1121 82 qraEVDWDFPITV--RDVVL------MGRYGrrglFRRPSRADreaVDEALERVGLEDLadrpIGEL------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1427 nlSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRT-QFEDSTVLTIAHRLNTIMDY-TRVIVLDKGEIR 1504
Cdd:COG1121 141 --SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREYfDRVLLLNRGLVA 218
|
250
....*....|.
gi 1958656469 1505 eCGAPSELLQQ 1515
Cdd:COG1121 219 -HGPPEEVLTP 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
645-849 |
1.11e-26 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 110.95 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDEPPT--LNGITFAIPDGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKG--------SVAYVP 713
Cdd:COG1116 8 LELRGVSKRFPTGGGGVtaLDDVSLTVAAGEFVALVGPSGCGKSTLLR-LIAGLEKPtSGEVLVDGkpvtgpgpDRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 714 QQawiqnDSL------RENILFGRPLQ----EHCYKAVMEAcallpdleilpsgdLTEIGEKGV------NLSGGQKQRV 777
Cdd:COG1116 87 QE-----PALlpwltvLDNVALGLELRgvpkAERRERAREL--------------LELVGLAGFedayphQLSGGMRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656469 778 SLARAVYCNSDIYLLDDPLSAVDAHVGKHIFEKVvgpMGLLK--NKTRILVTHGIS---YLpqVDVIIVMSG--GKISE 849
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDALTRERLQDEL---LRLWQetGKTVLFVTHDVDeavFL--ADRVVVLSArpGRIVE 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1307-1507 |
1.47e-26 |
|
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: 107.91 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITIIPQdpvlfsgSLRmnl 1386
Cdd:cd03214 14 VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ-------ALE--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1387 dpfsqysdeevwmALELAHLKgfvsalpDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDL----ET 1462
Cdd:cd03214 84 -------------LLGLAHLA-------DRPFNE-------LSGGERQRVLLARALAQEPPILLLDEPTSHLDIahqiEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958656469 1463 DDLIQSTIRTqfEDSTVLTIAHRLNTIMDY-TRVIVLDKGEIRECG 1507
Cdd:cd03214 137 LELLRRLARE--RGKTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
645-860 |
2.74e-26 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 109.36 E-value: 2.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFtwARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAY 711
Cdd:COG1120 2 LEAENLSV--GYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 712 VPQQAwIQNDSL--RENILFGR--------PLQEHCYKAVMEACALLpdleilpsgDLTEIGEKGVN-LSGGQKQRVSLA 780
Cdd:COG1120 80 VPQEP-PAPFGLtvRELVALGRyphlglfgRPSAEDREAVEEALERT---------GLEHLADRPVDeLSGGERQRVLIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 781 RAVYCNSDIYLLDDPLSAVDAHvgkHIFEkVvgpMGLLK------NKTRILVTHgisYLPQV----DVIIVMSGGKISEM 850
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLA---HQLE-V---LELLRrlarerGRTVVMVLH---DLNLAaryaDRLVLLKDGRIVAQ 219
|
250
....*....|
gi 1958656469 851 GSYQELLDRD 860
Cdd:COG1120 220 GPPEEVLTPE 229
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1307-1515 |
3.29e-26 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 115.23 E-value: 3.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSL---TLGLFRineSAEGEIIIDGINIA-----KIGLHnlrfkITIIPQDPVLF 1378
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLarlLVGVWP---PTAGSVRLDGADLSqwdreELGRH-----IGYLPQDVELF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1379 SGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAV 1458
Cdd:COG4618 419 DGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 1459 DLETDDLIQSTIRTQFED-STVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELLQQ 1515
Cdd:COG4618 499 DDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1284-1502 |
4.07e-26 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 117.44 E-value: 4.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1284 TWPHSGRVEFRDYCLRY--REDLDlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII-DGINIAKIG 1360
Cdd:PTZ00265 376 KLKDIKKIQFKNVRFHYdtRKDVE-IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDIN 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1361 LHNLRFKITIIPQDPVLFSGSLRMNL-------------------DPFSQYSDEEVWMAL------------------EL 1403
Cdd:PTZ00265 455 LKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdlealsnyyneDGNDSQENKNKRNSCrakcagdlndmsnttdsnEL 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1404 AHLK---------------------GFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 1462
Cdd:PTZ00265 535 IEMRknyqtikdsevvdvskkvlihDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958656469 1463 DDLIQSTIRT--QFEDSTVLTIAHRLNTIMDYTRVIVLDKGE 1502
Cdd:PTZ00265 615 EYLVQKTINNlkGNENRITIIIAHRLSTIRYANTIFVLSNRE 656
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
652-851 |
5.46e-26 |
|
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: 107.61 E-value: 5.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 652 FTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKG-----------SVAYVPQQ-AWI 718
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLR-LIAGLERPdSGEILIDGrdvtgvpperrNIGMVFQDyALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 719 QNDSLRENILFG----RPLQEHCYKAVMEACALLpdleilpsgDLTEIGEKGVN-LSGGQKQRVSLARAVYCNSDIYLLD 793
Cdd:cd03259 85 PHLTVAENIAFGlklrGVPKAEIRARVRELLELV---------GLEGLLNRYPHeLSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958656469 794 DPLSAVDAHVGKHIFEKVVgpmGLLKN--KTRILVTHGIS-YLPQVDVIIVMSGGKISEMG 851
Cdd:cd03259 156 EPLSALDAKLREELREELK---ELQRElgITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1291-1503 |
7.61e-26 |
|
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: 107.19 E-value: 7.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLD--LVLKHINVTIEGGEKVGIVGRTGAGKSSL--TLGLfrINESAEGEIIIDGINIAKIGLHNL-- 1364
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLlnILGG--LDRPTSGEVRVDGTDISKLSEKELaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1365 --RFKITIIPQDPvlfsgslrmNLDP-FSQYsdEEVWMALELAHLKGFVSA-----------LPDKLNHECAEggenLSV 1430
Cdd:cd03255 79 frRRHIGFVFQSF---------NLLPdLTAL--ENVELPLLLAGVPKKERReraeellervgLGDRLNHYPSE----LSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 1431 GQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIR--TQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEI 1503
Cdd:cd03255 144 GQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1307-1516 |
9.34e-26 |
|
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: 107.65 E-value: 9.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG---LHNLRFKITIIPQDP-------- 1375
Cdd:cd03256 16 ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQIGMIFQQFnlierlsv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1376 ---VLfSGSL-RMNLDP--FSQYSDEEVWMALELAHLKGfvsaLPDKLNHECAEggenLSVGQRQLVCLARALLRKTKIL 1449
Cdd:cd03256 96 lenVL-SGRLgRRSTWRslFGLFPKEEKQRALAALERVG----LLDKAYQRADQ----LSGGQQQRVAIARALMQQPKLI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1450 VLDEATAAVDLETDDLIQSTIR--TQFEDSTVLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSELLQQR 1516
Cdd:cd03256 167 LADEPVASLDPASSRQVMDLLKriNREEGITVIVSLHQVDLAREYAdRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1307-1515 |
1.02e-25 |
|
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: 113.60 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL 1386
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1387 DPFSQYSD-EEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDD- 1464
Cdd:TIGR01842 413 ARFGENADpEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQa 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958656469 1465 LIQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELLQQ 1515
Cdd:TIGR01842 493 LANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
645-865 |
1.30e-25 |
|
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: 107.03 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWaRDEPPTLNGITFAIPDGALVAVVGQVGCGKSSL---LSALLAEMdkvEGHVTLKG-------------S 708
Cdd:COG1122 1 IELENLSFSY-PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLlrlLNGLLKPT---SGEVLVDGkditkknlrelrrK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 709 VAYVPQQAWIQ--NDSLRENILFGrPLQ-----EHCYKAVMEACALLpdleilpsgDLTEIGEKGV-NLSGGQKQRVSLA 780
Cdd:COG1122 77 VGLVFQNPDDQlfAPTVEEDVAFG-PENlglprEEIRERVEEALELV---------GLEHLADRPPhELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 781 RAVYCNSDIYLLDDPLSAVDAHVGKHIFEkvvgpmgLLK-----NKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQ 854
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLE-------LLKrlnkeGKTVIIVTHDLDLVAELaDRVIVLDDGRIVADGTPR 219
|
250
....*....|.
gi 1958656469 855 ELLDRDGAFAE 865
Cdd:COG1122 220 EVFSDYELLEE 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
642-859 |
1.33e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 110.16 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 642 MNSITVKNATFTWarDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKG-----------SV 709
Cdd:COG3839 1 MASLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLR-MIAGLEDPtSGEILIGGrdvtdlppkdrNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 710 AYVPQQ-AWIQNDSLRENILFG-----RPLQEHcYKAVMEACALLpdleilpsgDLTEIGEKGV-NLSGGQKQRVSLARA 782
Cdd:COG3839 78 AMVFQSyALYPHMTVYENIAFPlklrkVPKAEI-DRRVREAAELL---------GLEDLLDRKPkQLSGGQRQRVALGRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 783 VYCNSDIYLLDDPLSAVDAHvgkhifekvvgpmglLKNKTR--------------ILVTHGisylpQV------DVIIVM 842
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDAK---------------LRVEMRaeikrlhrrlgtttIYVTHD-----QVeamtlaDRIAVM 207
|
250
....*....|....*..
gi 1958656469 843 SGGKISEMGSYQELLDR 859
Cdd:COG3839 208 NDGRIQQVGTPEELYDR 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
645-865 |
1.77e-25 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 112.69 E-value: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSA---LLAEMDKVEGHVTLKG-------------S 708
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALAlmgLLPHGGRISGEVLLDGrdllelsealrgrR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 709 VAYVPQQAWIQNDSLR--ENILFGrPLQEHCYKAVMEACALlpdlEILPSGDLTEIGEKGVN-LSGGQKQRVSLARAVYC 785
Cdd:COG1123 85 IGMVFQDPMTQLNPVTvgDQIAEA-LENLGLSRAEARARVL----ELLEAVGLERRLDRYPHqLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 786 NSDIYLLDDPLSAVDAHVGKHIFEkvvgpmgLLK------NKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLD 858
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILD-------LLRelqrerGTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEILA 232
|
....*..
gi 1958656469 859 RDGAFAE 865
Cdd:COG1123 233 APQALAA 239
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
645-847 |
2.61e-25 |
|
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: 105.63 E-value: 2.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDEPPT--LNGITFAIPDGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKG--------SVAYVP 713
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLR-IIAGLERPtSGEVLVDGepvtgpgpDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 714 QQA----WIqndSLRENILFGRPLQEHCYKAVMEACALLpdleilpsgdLTEIGEKGV------NLSGGQKQRVSLARAV 783
Cdd:cd03293 80 QQDallpWL---TVLDNVALGLELQGVPKAEARERAEEL----------LELVGLSGFenayphQLSGGMRQRVALARAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958656469 784 YCNSDIYLLDDPLSAVDAHVGKHIFEKvvgpmgLLK-----NKTRILVTHGIS---YLPqvDVIIVMSG--GKI 847
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEE------LLDiwretGKTVLLVTHDIDeavFLA--DRVVVLSArpGRI 212
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
652-828 |
4.22e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 104.90 E-value: 4.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 652 FTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAYVPQQAWI 718
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYVPQEPAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 719 QNDSLRENILFgrPLQEHCYKAVME-ACALLPDLEiLPSGDLteigEKGV-NLSGGQKQRVSLARAVYCNSDIYLLDDPL 796
Cdd:COG4619 86 WGGTVRDNLPF--PFQLRERKFDRErALELLERLG-LPPDIL----DKPVeRLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190
....*....|....*....|....*....|..
gi 1958656469 797 SAVDAHvGKHIFEKVVGPMGLLKNKTRILVTH 828
Cdd:COG4619 159 SALDPE-NTRRVEELLREYLAEEGRAVLWVSH 189
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1307-1513 |
5.26e-25 |
|
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: 105.36 E-value: 5.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKI---GLHNLRFKITIIPQDPVLFSgslr 1383
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgkELRKARRRIGMIFQHFNLLS---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1384 mnldpfSQYSDEEVWMALELAHLKG------------FVsALPDKLNHECAeggeNLSVGQRQLVCLARALLRKTKILVL 1451
Cdd:cd03258 96 ------SRTVFENVALPLEIAGVPKaeieervlelleLV-GLEDKADAYPA----QLSGGQKQRVGIARALANNPKVLLC 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 1452 DEATAAVDLETDDLIQSTIRT--QFEDSTVLTIAHRLNTIMDY-TRVIVLDKGEIRECGAPSELL 1513
Cdd:cd03258 165 DEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEVF 229
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
644-886 |
5.71e-25 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 111.73 E-value: 5.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 644 SITVKNATFTWaRDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVA 710
Cdd:PRK10790 340 RIDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsslshsvlrqGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 711 YVPQQAWIQNDSLRENILFGRPLQEHCYKAVMEACALLPDLEILPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSDIY 790
Cdd:PRK10790 419 MVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQIL 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 791 LLDDPLSAVDAHVGKHIFEKVVgpmGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGafaefvRTY 870
Cdd:PRK10790 499 ILDEATANIDSGTEQAIQQALA---AVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQG------RYW 569
|
250
....*....|....*.
gi 1958656469 871 ANTEQDLASEDDSVSG 886
Cdd:PRK10790 570 QMYQLQLAGEELAASV 585
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
645-851 |
6.09e-25 |
|
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: 103.16 E-value: 6.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS------------VAYV 712
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 713 PQQAWIQNDSLRENIlfgrplqehcykavmeacallpdleilpsgdlteigekGVNLSGGQKQRVSLARAVYCNSDIYLL 792
Cdd:cd03247 81 NQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656469 793 DDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMG 851
Cdd:cd03247 123 DEPTVGLDPITERQLLSLI---FEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
646-847 |
1.23e-24 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 102.51 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 646 TVKNATFtwARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLkgsvayvpqqawiqndslre 725
Cdd:cd03214 1 EVENLSV--GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL-------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 726 nilFGRPLQEHCYKAVMEACALLPD-LEILpsgDLTEIGEKGVN-LSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHV 803
Cdd:cd03214 59 ---DGKDLASLSPKELARKIAYVPQaLELL---GLAHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAH 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958656469 804 GKHIFEKVVGpMGLLKNKTRILVTHGISYLPQV-DVIIVMSGGKI 847
Cdd:cd03214 133 QIELLELLRR-LARERGKTVVMVLHDLNLAARYaDRVILLKDGRI 176
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1292-1501 |
2.61e-24 |
|
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: 102.61 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1292 EFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDGINIAKIglhnlRFKI 1368
Cdd:cd03235 1 EVEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLkaiLGLLK---PTSGSIRVFGKPLEKE-----RKRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1369 TIIPQ----D---PVLFSGSLRMNLDP----FSQYSDEE---VWMALELAHLKGFvsalpdkLNHECAEggenLSVGQRQ 1434
Cdd:cd03235 71 GYVPQrrsiDrdfPISVRDVVLMGLYGhkglFRRLSKADkakVDEALERVGLSEL-------ADRQIGE----LSGGQQQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656469 1435 LVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRT-QFEDSTVLTIAHRLNTIMDYT-RVIVLDKG 1501
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYFdRVLLLNRT 208
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
648-847 |
2.73e-24 |
|
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: 102.93 E-value: 2.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 648 KNATFTW-ARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS-------------VAYVP 713
Cdd:cd03248 15 QNVTFAYpTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 714 QQAWIQNDSLRENILFGrpLQEHCYKAVMEACALL---PDLEILPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSDIY 790
Cdd:cd03248 95 QEPVLFARSLQDNIAYG--LQSCSFECVKEAAQKAhahSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656469 791 LLDDPLSAVDAHvGKHIFEKVVgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKI 847
Cdd:cd03248 173 ILDEATSALDAE-SEQQVQQAL--YDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
645-859 |
3.19e-24 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 103.34 E-value: 3.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKN--ATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS-------------V 709
Cdd:COG1124 2 LEVRNlsVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRpvtrrrrkafrrrV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 710 AYVPQQA-------WIQNDSLREnilfgrPLQEHCYKAVME-ACALLPDLEiLPSGDLTEIGEKgvnLSGGQKQRVSLAR 781
Cdd:COG1124 82 QMVFQDPyaslhprHTVDRILAE------PLRIHGLPDREErIAELLEQVG-LPPSFLDRYPHQ---LSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 782 AVYCNSDIYLLDDPLSAVDAHVGKHIfekvvgpMGLLK------NKTRILVTHG---ISYLpqVDVIIVMSGGKISEMGS 852
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEI-------LNLLKdlreerGLTYLFVSHDlavVAHL--CDRVAVMQNGRIVEELT 222
|
....*..
gi 1958656469 853 YQELLDR 859
Cdd:COG1124 223 VADLLAG 229
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1307-1503 |
4.34e-24 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 100.55 E-value: 4.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLT---LGLFRINEsaeGEIIIDGINIAKIGlHNLRFKITIIPQDPVLFSgslr 1383
Cdd:cd03230 15 ALDDISLTVEKGEIYGLLGPNGAGKTTLIkiiLGLLKPDS---GEIKVLGKDIKKEP-EEVKRRIGYLPEEPSLYE---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1384 mnldpfsqysdeevwmalelaHLKGFvsalpdklnhecaeggENL--SVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1461
Cdd:cd03230 87 ---------------------NLTVR----------------ENLklSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958656469 1462 TDDLIQSTIRT-QFEDSTVLTIAHRLNTIMDY-TRVIVLDKGEI 1503
Cdd:cd03230 130 SRREFWELLRElKKEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
642-859 |
7.44e-24 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 104.79 E-value: 7.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 642 MNSITVKNATFTWarDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKG-----------SV 709
Cdd:COG3842 3 MPALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLR-MIAGFETPdSGRILLDGrdvtglppekrNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 710 AYVPQqawiqNDSL------RENILFGrpLQEHCYKA------VMEACALLpdleilpsgDLTEIGEKGVN-LSGGQKQR 776
Cdd:COG3842 80 GMVFQ-----DYALfphltvAENVAFG--LRMRGVPKaeirarVAELLELV---------GLEGLADRYPHqLSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 777 VSLARAVYCNSDIYLLDDPLSAVDAHVG-------KHIFEKVvgpmgllkNKTRILVTH------GISylpqvDVIIVMS 843
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALDAKLReemreelRRLQREL--------GITFIYVTHdqeealALA-----DRIAVMN 210
|
250
....*....|....*.
gi 1958656469 844 GGKISEMGSYQELLDR 859
Cdd:COG3842 211 DGRIEQVGTPEEIYER 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
642-849 |
1.08e-23 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 101.27 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 642 MNS-ITVKNATFTWARDEPPT--LNGITFAIPDGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKG---------- 707
Cdd:COG1136 1 MSPlLELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVLIDGqdisslsere 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 708 -------SVAYVPQQA-WIQNDSLRENILF-----GRPLQEhCYKAVMEAcallpdLEILpsgDLTEIGEKGVN-LSGGQ 773
Cdd:COG1136 80 larlrrrHIGFVFQFFnLLPELTALENVALplllaGVSRKE-RRERAREL------LERV---GLGDRLDHRPSqLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 774 KQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIFEkvvgpmgLLK------NKTRILVTHGISYLPQVDVIIVMSGGKI 847
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLE-------LLRelnrelGTTIVMVTHDPELAARADRVIRLRDGRI 222
|
..
gi 1958656469 848 SE 849
Cdd:COG1136 223 VS 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
644-859 |
1.31e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 104.07 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 644 SITVKNATFTWARDepPTLNGITFAIPDGALVAVVGQVGCGKSSLLSAL--LAEMDkvEGHVTLKGSVAYV---PQQAWI 718
Cdd:COG1118 2 SIEVRNISKRFGSF--TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIagLETPD--SGRIVLNGRDLFTnlpPRERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 719 ----QNDSL------RENILFG---RPLQEHCYKA-VMEACAL--LPDLE-ILPSgdlteigekgvNLSGGQKQRVSLAR 781
Cdd:COG1118 78 gfvfQHYALfphmtvAENIAFGlrvRPPSKAEIRArVEELLELvqLEGLAdRYPS-----------QLSGGQRQRVALAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 782 AVYCNSDIYLLDDPLSAVDAHVGKHIfEKVVgpMGLLK--NKTRILVTH------GISylpqvDVIIVMSGGKISEMGSY 853
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDAKVRKEL-RRWL--RRLHDelGGTTVFVTHdqeealELA-----DRVVVMNQGRIEQVGTP 218
|
....*.
gi 1958656469 854 QELLDR 859
Cdd:COG1118 219 DEVYDR 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1291-1511 |
1.86e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 100.51 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLDlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKI---GLHNLRFK 1367
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1368 ITIIPQDP-----------VLFsgSLR-MNLDPfsQYSDEEVWMALELAHLKGFVSALPdklnHEcaeggenLSVGQRQL 1435
Cdd:COG2884 81 IGVVFQDFrllpdrtvyenVAL--PLRvTGKSR--KEIRRRVREVLDLVGLSDKAKALP----HE-------LSGGEQQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1436 VCLARALLRKTKILVLDEATAAVDLET-DDLIQstirtQFED-----STVLtIA-HRLNTIMDY-TRVIVLDKGEIRECG 1507
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETsWEIME-----LLEEinrrgTTVL-IAtHDLELVDRMpKRVLELEDGRLVRDE 219
|
....
gi 1958656469 1508 APSE 1511
Cdd:COG2884 220 ARGV 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1291-1513 |
2.65e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 101.22 E-value: 2.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITI 1370
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1371 IPQDP-VLFSGSLRMNLDPFS----QYSDEEVW-MALELAHLKGfvsaLPDKLNHEcaegGENLSVGQRQLVCLARALLR 1444
Cdd:PRK13632 88 IFQNPdNQFIGATVEDDIAFGlenkKVPPKKMKdIIDDLAKKVG----MEDYLDKE----PQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958656469 1445 KTKILVLDEATAAVDLETDDLIQSTIRT--QFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELL 1513
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1308-1515 |
3.36e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 101.66 E-value: 3.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1308 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIA--KIGLHNLRFKITIIPQDP--VLFS---- 1379
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQYPeyQLFEetie 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1380 -----GSLRMNLdpfsqySDEEVWM----ALELAHLKgfVSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILV 1450
Cdd:PRK13637 103 kdiafGPINLGL------SEEEIENrvkrAMNIVGLD--YEDYKDKSPFE-------LSGGQKRRVAIAGVVAMEPKILI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 1451 LDEATAAVDLETDDLIQSTIRTQFE--DSTVLTIAHRLNTIMDY-TRVIVLDKGEIRECGAPSELLQQ 1515
Cdd:PRK13637 168 LDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKLaDRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1307-1502 |
3.86e-23 |
|
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: 98.03 E-value: 3.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHN--LRFKITIIPQDPVLFSG-SLR 1383
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIGMVFQDFALFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1384 MNLdpfsqysdeevwmalelahlkgfvsALPdklnhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD 1463
Cdd:cd03229 95 ENI-------------------------ALG-------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958656469 1464 DLIQSTIRTQFEDS--TVLTIAHRLNTIMDYT-RVIVLDKGE 1502
Cdd:cd03229 137 REVRALLKSLQAQLgiTVVLVTHDLDEAARLAdRVVVLRDGK 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1291-1507 |
3.87e-23 |
|
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: 99.13 E-value: 3.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLtL----GLFRInesAEGEIIIDGINIAKIGLHnlRF 1366
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTL-LrliaGLERP---DSGEILIDGRDVTGVPPE--RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1367 KITIIPQDPVLF----------SGsLRMNLDPFSQySDEEVWMALELAHLKGFVSALPDKLnhecaeggenlSVGQRQLV 1436
Cdd:cd03259 73 NIGMVFQDYALFphltvaeniaFG-LKLRGVPKAE-IRARVRELLELVGLEGLLNRYPHEL-----------SGGQQQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958656469 1437 CLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFE--DSTVLTIAHRLNTIMDYT-RVIVLDKGEIRECG 1507
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALALAdRIAVMNEGRIVQVG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
646-846 |
1.03e-22 |
|
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: 96.16 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 646 TVKNATFTWarDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLkgsvayvpqqawiqndslre 725
Cdd:cd00267 1 EIENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI-------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 726 nilFGRPLQEHCYKAVMEACALLPDLeilpsgdlteigekgvnlSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHvGK 805
Cdd:cd00267 59 ---DGKDIAKLPLEELRRRIGYVPQL------------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPA-SR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958656469 806 HIFEKVVGPMgLLKNKTRILVTHGISYLPQV-DVIIVMSGGK 846
Cdd:cd00267 117 ERLLELLREL-AEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
644-852 |
1.79e-22 |
|
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: 97.10 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 644 SITVKNATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVA 710
Cdd:cd03369 6 EIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 711 YVPQQAWIQNDSLRENIlfgRPLQEHCYKAVMEAcallpdleilpsgdlTEIGEKGVNLSGGQKQRVSLARAVYCNSDIY 790
Cdd:cd03369 86 IIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGA---------------LRVSEGGLNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958656469 791 LLDDPLSAVDAHVgKHIFEKVVgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGS 852
Cdd:cd03369 148 VLDEATASIDYAT-DALIQKTI--REEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
662-859 |
2.57e-22 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 97.44 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG------------SVAYVPQQAWIQND-SLRENI- 727
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALYPDlTVRENLr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 728 ----LFGRPLQEhCYKAVMEACALLpdleilpsgDLTEIGEKGV-NLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAH 802
Cdd:COG1131 96 ffarLYGLPRKE-ARERIDELLELF---------GLTDAADRKVgTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 803 VGKHIFEkvvgpmgLLK-----NKTRILVTHgisYLPQV----DVIIVMSGGKISEMGSYQELLDR 859
Cdd:COG1131 166 ARRELWE-------LLRelaaeGKTVLLSTH---YLEEAerlcDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
645-851 |
2.92e-22 |
|
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: 97.19 E-value: 2.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKN--ATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG--------------- 707
Cdd:cd03257 2 LEVKNlsVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 708 -SVAYVPQQAwiqNDSL--RENI--LFGRPLQEHCYKAVMEA-----CALLPDLEiLPSGDLT----EigekgvnLSGGQ 773
Cdd:cd03257 82 kEIQMVFQDP---MSSLnpRMTIgeQIAEPLRIHGKLSKKEArkeavLLLLVGVG-LPEEVLNryphE-------LSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 774 KQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIfekvvgpMGLLK------NKTRILVTHGISYLPQV-DVIIVMSGGK 846
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQI-------LDLLKklqeelGLTLLFITHDLGVVAKIaDRVAVMYAGK 223
|
....*
gi 1958656469 847 ISEMG 851
Cdd:cd03257 224 IVEEG 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1308-1516 |
5.24e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 96.36 E-value: 5.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1308 LKHINVTIEGGEKVGIVGRTGAGKSSLtLGL---FRinESAEGEIIIDGINIAKIGLHNlRfKITIIPQDPVLFSG-SLR 1383
Cdd:COG3840 15 PLRFDLTIAAGERVAILGPSGAGKSTL-LNLiagFL--PPDSGRILWNGQDLTALPPAE-R-PVSMLFQENNLFPHlTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1384 MN----LDPFSQYSDEE---VWMALELAHLKGFVSALPdklnhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATA 1456
Cdd:COG3840 90 QNiglgLRPGLKLTAEQraqVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 1457 AVD----LETDDLIQSTIRTQfeDSTVLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSELLQQR 1516
Cdd:COG3840 159 ALDpalrQEMLDLVDELCRER--GLTVLMVTHDPEDAARIAdRVLLVADGRIAADGPTAALLDGE 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1290-1515 |
6.86e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 97.39 E-value: 6.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1290 RVEFRDYclRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDGINIAKIGLHNLRF 1366
Cdd:PRK13635 7 RVEHISF--RYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAkllNGLLL---PEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1367 KITIIPQDP------------VLFSgsLRMNLDPFSQYSdEEVWMALELAHLKGFvsalpdkLNHECAeggeNLSVGQRQ 1434
Cdd:PRK13635 82 QVGMVFQNPdnqfvgatvqddVAFG--LENIGVPREEMV-ERVDQALRQVGMEDF-------LNREPH----RLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1435 LVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRT--QFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSEL 1512
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
...
gi 1958656469 1513 LQQ 1515
Cdd:PRK13635 228 FKS 230
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
645-861 |
7.67e-22 |
|
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: 96.47 E-value: 7.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWarDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG------------SVAYV 712
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 713 PQQAWI-QNDSLRENILF---GRPLQEHCYKAVMEacallpdlEILPSGDLTEIGEKGV-NLSGGQKQRVSLARAVYCNS 787
Cdd:COG4555 80 PDERGLyDRLTVRENIRYfaeLYGLFDEELKKRIE--------ELIELLGLEEFLDRRVgELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656469 788 DIYLLDDPLSAVDAhVGKHIFEKVvgpMGLLKN--KTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLDRDG 861
Cdd:COG4555 152 KVLLLDEPTNGLDV-MARRLLREI---LRALKKegKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1291-1521 |
8.17e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 97.23 E-value: 8.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYrEDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--INIAKIGLHNLRFKI 1368
Cdd:PRK13636 6 LKVEELNYNY-SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1369 TIIPQDP--VLFSGSLR-------MNLdpfsQYSDEEVWMALELAHLKGFVSALPDKLNHEcaeggenLSVGQRQLVCLA 1439
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYqdvsfgaVNL----KLPEDEVRKRVDNALKRTGIEHLKDKPTHC-------LSFGQKKRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1440 RALLRKTKILVLDEATAAVD-LETDDLIQSTIRTQFE-DSTVLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSELLQQR 1516
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDpMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCdNVFVMKEGRVILQGNPKEVFAEK 233
|
....*
gi 1958656469 1517 GVFYS 1521
Cdd:PRK13636 234 EMLRK 238
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
644-858 |
9.09e-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: 95.87 E-value: 9.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 644 SITVKNATFTWARdePPTLNGITFAIPDGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKG-----------SVAY 711
Cdd:cd03296 2 SIEVRNVSKRFGD--FVALDDVSLDIPSGELVALLGPSGSGKTTLLR-LIAGLERPdSGTILFGGedatdvpvqerNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 712 VPQQ-AWIQNDSLRENILFG---RPLQEHCYKAVMEACALlpdlEILPSGDLTEIGEKGVN-LSGGQKQRVSLARAVYCN 786
Cdd:cd03296 79 VFQHyALFRHMTVFDNVAFGlrvKPRSERPPEAEIRAKVH----ELLKLVQLDWLADRYPAqLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 787 SDIYLLDDPLSAVDAHVGKHI---FEKVVGPMGLlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLD 858
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELrrwLRRLHDELHV----TTVFVTHDQEEALEVaDRVVVMNKGRIEQVGTPDEVYD 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1291-1484 |
4.75e-21 |
|
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: 93.31 E-value: 4.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLD--LVLKHINVTIEGGEKVGIVGRTGAGKSSL---TLGLFRInesAEGEIIIDGINIAKIGLHnlr 1365
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLlriIAGLERP---TSGEVLVDGEPVTGPGPD--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1366 fkITIIPQDPVLF---------SGSLRMNLDPFSQySDEEVWMALELAHLKGFVSALPdklnHEcaeggenLSVGQRQLV 1436
Cdd:cd03293 75 --RGYVFQQDALLpwltvldnvALGLELQGVPKAE-ARERAEELLELVGLSGFENAYP----HQ-------LSGGMRQRV 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1437 CLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDS--TVLTIAH 1484
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTH 190
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
645-859 |
5.98e-21 |
|
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: 98.44 E-value: 5.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTW---ARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------- 707
Cdd:COG1123 261 LEVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkdltklsrrslrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 708 --SVAYVPQQAwiqNDSL--RENIL--FGRPLQEHCY----------KAVMEACALLPD-LEILPSGdlteigekgvnLS 770
Cdd:COG1123 341 rrRVQMVFQDP---YSSLnpRMTVGdiIAEPLRLHGLlsraerrervAELLERVGLPPDlADRYPHE-----------LS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 771 GGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIfekvvgpMGLLK------NKTRILVTHGISYLPQV-DVIIVMS 843
Cdd:COG1123 407 GGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQI-------LNLLRdlqrelGLTYLFISHDLAVVRYIaDRVAVMY 479
|
250
....*....|....*.
gi 1958656469 844 GGKISEMGSYQELLDR 859
Cdd:COG1123 480 DGRIVEDGPTEEVFAN 495
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
662-856 |
8.06e-21 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 93.01 E-value: 8.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVTLKGS---------------VAYVPQQAWIQND 721
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKdiydldvdvlelrrrVGMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 722 SLRENILFGRPLQ----EHCYKAVMEAC---ALLPDLEILPSGDLteigekgvNLSGGQKQRVSLARAVYCNSDIYLLDD 794
Cdd:cd03260 96 SIYDNVAYGLRLHgiklKEELDERVEEAlrkAALWDEVKDRLHAL--------GLSGGQQQRLCLARALANEPEVLLLDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 795 PLSAVDAhVGKHIFEKVVgpMGLLKNKTRILVTHGisyLPQV----DVIIVMSGGKISEMGSYQEL 856
Cdd:cd03260 168 PTSALDP-ISTAKIEELI--AELKKEYTIVIVTHN---MQQAarvaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
338-617 |
1.00e-20 |
|
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: 94.15 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 338 LMMFAGPEILELIINFVndREAPDWQGYLYTALLFVSAC-LQTLALHQYFHICFVTGMRIKTAVVGAVYRKALVITNSAR 416
Cdd:cd07346 13 ALGLALPLLTKLLIDDV--IPAGDLSLLLWIALLLLLLAlLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 417 KSSTVGEIVNLMSVDAQRFMDLATY-INMIWSAPLQVTLALYFLwLNLGPSV-LAGVAVMILMVPFNAVMAMKTKTYQVA 494
Cdd:cd07346 91 DRNRTGDLMSRLTSDVDAVQNLVSSgLLQLLSDVLTLIGALVIL-FYLNWKLtLVALLLLPLYVLILRYFRRRIRKASRE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 495 HMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMNIRQEELKVLKKSAYLAAvgtFTWVCTPFLVALSTFAVFV---- 570
Cdd:cd07346 170 VRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSA---LFSPLIGLLTALGTALVLLyggy 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 571 -------TVDEknildakkaFVS-LALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd07346 247 lvlqgslTIGE---------LVAfLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1307-1515 |
2.27e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 94.37 E-value: 2.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSltlgLFR-IN--ESA-EGEIIIDGINIAKI---GLHNLRFKITIIPQDpvlFs 1379
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKST----LIRcINllERPtSGSVLVDGVDLTALserELRAARRKIGMIFQH---F- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1380 gslrmNLdpFSQYSDEE-VWMALELAHLKG------------FVSaLPDKLNHECAEggenLSVGQRQLVCLARALLRKT 1446
Cdd:COG1135 92 -----NL--LSSRTVAEnVALPLEIAGVPKaeirkrvaelleLVG-LSDKADAYPSQ----LSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 1447 KILVLDEATAAVDLETD----DLIQStIRTQFeDSTVLTIAHRLN---TIMDytRVIVLDKGEIRECGAPSELLQQ 1515
Cdd:COG1135 160 KVLLCDEATSALDPETTrsilDLLKD-INREL-GLTIVLITHEMDvvrRICD--RVAVLENGRIVEQGPVLDVFAN 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1291-1503 |
2.49e-20 |
|
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: 91.32 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLdLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKI---GLHNLRFK 1367
Cdd:cd03292 1 IEFINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1368 ITIIPQDPVLFSG---------SLRMNLDPfSQYSDEEVWMALELAHLKGFVSALPdklnhecaeggENLSVGQRQLVCL 1438
Cdd:cd03292 80 IGVVFQDFRLLPDrnvyenvafALEVTGVP-PREIRKRVPAALELVGLSHKHRALP-----------AELSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 1439 ARALLRKTKILVLDEATAAVDLETDDLIqSTIRTQFED--STVLTIAHRLNTIMDYT-RVIVLDKGEI 1503
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEI-MNLLKKINKagTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
1014-1262 |
2.74e-20 |
|
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: 93.00 E-value: 2.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1014 LSVYGALGILQGVAVFGYSMAVSIGGIFASRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFM 1093
Cdd:cd07346 42 ALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1094 GSLFSVIGAVIIILLATP----IAAVIIPPLGLVYFFVQRFYVASSRQLKrlESVSRspVYSHFNETLLGVSVIRAF--- 1166
Cdd:cd07346 122 SDVLTLIGALVILFYLNWkltlVALLLLPLYVLILRYFRRRIRKASREVR--ESLAE--LSAFLQESLSGIRVVKAFaae 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1167 -EEQERFIRQSDLKVDENQKAYYPSIVANRWLAVrLECVGNCIVLFAALFAVIsRHSLSAGLVGLSVSYSLQITAYLNWL 1245
Cdd:cd07346 198 eREIERFREANRDLRDANLRAARLSALFSPLIGL-LTALGTALVLLYGGYLVL-QGSLTIGELVAFLAYLGMLFGPIQRL 275
|
250
....*....|....*..
gi 1958656469 1246 VRMSSEMETNIVAVERL 1262
Cdd:cd07346 276 ANLYNQLQQALASLERI 292
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
645-860 |
5.25e-20 |
|
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: 90.64 E-value: 5.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFtwARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS---------------- 708
Cdd:cd03261 1 IELRGLTK--SFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 709 VAYVPQQAWIQND-SLRENILFgrPLQEH-------CYKAVME---ACALLPDLEILPSgdlteigekgvNLSGGQKQRV 777
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAF--PLREHtrlseeeIREIVLEkleAVGLRGAEDLYPA-----------ELSGGMKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 778 SLARAVYCNSDIYLLDDPLSAVDAhVGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQEL 856
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDP-IASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEEL 224
|
....
gi 1958656469 857 LDRD 860
Cdd:cd03261 225 RASD 228
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1290-1471 |
7.91e-20 |
|
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: 89.46 E-value: 7.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1290 RVEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSL--TL-GLFRInesAEGEIIIDGINIAKIGLHnLRF 1366
Cdd:COG4133 2 MLEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLlrILaGLLPP---SAGEVLWNGEPIRDARED-YRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1367 KITIIPQDPVLFSG-SLRMNLDpFSQ------YSDEEVWMALELAHLKGFvsalpdkLNHECAeggeNLSVGQRQLVCLA 1439
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLR-FWAalyglrADREAIDEALEAVGLAGL-------ADLPVR----QLSAGQKRRVALA 143
|
170 180 190
....*....|....*....|....*....|..
gi 1958656469 1440 RALLRKTKILVLDEATAAVDLETDDLIQSTIR 1471
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIA 175
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1308-1515 |
1.23e-19 |
|
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: 94.75 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1308 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESaEGEIIIDGINIAKIG---LHNLRFKITIIPQDPvlFsGSL-- 1382
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--F-GSLsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1383 RMN-----------LDPfsQYSDEE----VWMALELAHLKgfvsalPDKLN---HEcaeggenLSVGQRQLVCLARALLR 1444
Cdd:COG4172 378 RMTvgqiiaeglrvHGP--GLSAAErrarVAEALEEVGLD------PAARHrypHE-------FSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1445 KTKILVLDEATAAVDLetddliqsTIRTQfedstVLT---------------IAHRLN---TIMDytRVIVLDKGEIREC 1506
Cdd:COG4172 443 EPKLLVLDEPTSALDV--------SVQAQ-----ILDllrdlqrehglaylfISHDLAvvrALAH--RVMVMKDGKVVEQ 507
|
....*....
gi 1958656469 1507 GAPSELLQQ 1515
Cdd:COG4172 508 GPTEQVFDA 516
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1307-1503 |
1.35e-19 |
|
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: 87.48 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG-LHNLRFKITIIPQdpvlfsgslrmn 1385
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1386 ldpfsqysdeevwmalelahlkgfvsalpdklnhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDL-ETDD 1464
Cdd:cd03216 83 ------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPaEVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958656469 1465 LIQSTIRTQFEDSTVLTIAHRLNTIMDYT-RVIVLDKGEI 1503
Cdd:cd03216 121 LFKVIRRLRAQGVAVIFISHRLDEVFEIAdRVTVLRDGRV 160
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
645-802 |
3.05e-19 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 87.53 E-value: 3.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFtwARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG------------SVAYV 712
Cdd:COG4133 3 LEAENLSC--RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 713 PQQ-AWIQNDSLRENILF-----GRPLQEhcyKAVMEACAL--LPDLEILPSGdlteigekgvNLSGGQKQRVSLARAVY 784
Cdd:COG4133 81 GHAdGLKPELTVRENLRFwaalyGLRADR---EAIDEALEAvgLAGLADLPVR----------QLSAGQKRRVALARLLL 147
|
170
....*....|....*...
gi 1958656469 785 CNSDIYLLDDPLSAVDAH 802
Cdd:COG4133 148 SPAPLWLLDEPFTALDAA 165
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1308-1501 |
3.45e-19 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 88.16 E-value: 3.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1308 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNL----RFKITIIPQDPVLFSGSLR 1383
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1384 MNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE-T 1462
Cdd:cd03290 97 ENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958656469 1463 DDLIQSTIRTQFEDS--TVLTIAHRLNTIMDYTRVIVLDKG 1501
Cdd:cd03290 177 DHLMQEGILKFLQDDkrTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1307-1514 |
3.76e-19 |
|
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: 87.87 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHN-LRFKITIIPQDPVLFSG----- 1380
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPEltvee 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1381 SLRMNLDPFSQYSDEEVW-MALELahlkgFvSALPDKLNHEcaegGENLSVGQRQLVCLARALLRKTKILVLDEATAA-- 1457
Cdd:cd03224 95 NLLLGAYARRRAKRKARLeRVYEL-----F-PRLKERRKQL----AGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGla 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958656469 1458 ---VDlETDDLIQsTIRTqfEDSTVLTIAHRLNTIMDY-TRVIVLDKGEIRECGAPSELLQ 1514
Cdd:cd03224 165 pkiVE-EIFEAIR-ELRD--EGVTILLVEQNARFALEIaDRAYVLERGRVVLEGTAAELLA 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1307-1505 |
4.37e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 87.79 E-value: 4.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSL--TLGLFrinESA-EGEIIIDGINIAKIG---LHNLRF-KITIIPQDPvlfs 1379
Cdd:COG1136 23 ALRGVSLSIEAGEFVAIVGPSGSGKSTLlnILGGL---DRPtSGEVLIDGQDISSLSereLARLRRrHIGFVFQFF---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1380 gslrmNLDPFsqYSDEE-VWMALELAHLKGFVSA-----------LPDKLNHECAEggenLSVGQRQLVCLARALLRKTK 1447
Cdd:COG1136 96 -----NLLPE--LTALEnVALPLLLAGVSRKERRerarellervgLGDRLDHRPSQ----LSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958656469 1448 ILVLDEATAAVDLETD----DLIQSTIRTQfeDSTVLTIAH--RLNTIMDytRVIVLDKGEIRE 1505
Cdd:COG1136 165 LILADEPTGNLDSKTGeevlELLRELNREL--GTTIVMVTHdpELAARAD--RVIRLRDGRIVS 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1291-1528 |
6.35e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 88.70 E-value: 6.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSS---LTLGLFRINESAEGEIIIDGINIAKIGLHNLRFK 1367
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1368 ITIIPQDP-VLFSGSLRMNLDPFS----QYSDEE----VWMALELAHLKGFVSALPdklnhecaeggENLSVGQRQLVCL 1438
Cdd:PRK13640 86 VGIVFQNPdNQFVGATVGDDVAFGlenrAVPRPEmikiVRDVLADVGMLDYIDSEP-----------ANLSGGQKQRVAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1439 ARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDS--TVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELLQQR 1516
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
250
....*....|..
gi 1958656469 1517 gvfySMAKDAGL 1528
Cdd:PRK13640 235 ----EMLKEIGL 242
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1291-1512 |
7.10e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 88.27 E-value: 7.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITI 1370
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1371 IPQDPV-LFSGSL-----RMNLDPFSQYSDEevwMALELAHLKGFVSALpDKLNHEcaegGENLSVGQRQLVCLARALLR 1444
Cdd:PRK13648 88 VFQNPDnQFVGSIvkydvAFGLENHAVPYDE---MHRRVSEALKQVDML-ERADYE----PNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1445 KTKILVLDEATAAVDLETDDLIQSTIR--TQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSEL 1512
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
642-830 |
1.04e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 87.61 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 642 MNSITVKN--ATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSV--------AY 711
Cdd:COG4525 1 MSMLTVRHvsVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 712 VpqqawIQNDSL------RENILFGRPLQEhCYKAVMEACALlpdlEILPSGDLTEIGEKGV-NLSGGQKQRVSLARAVY 784
Cdd:COG4525 81 V-----FQKDALlpwlnvLDNVAFGLRLRG-VPKAERRARAE----ELLALVGLADFARRRIwQLSGGMRQRVGIARALA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958656469 785 CNSDIYLLDDPLSAVDAHVGKHIFEKvvgpmgLLK-----NKTRILVTHGI 830
Cdd:COG4525 151 ADPRFLLMDEPFGALDALTREQMQEL------LLDvwqrtGKGVFLITHSV 195
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1308-1511 |
1.04e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 89.47 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1308 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKI---GLHNLRFKITIIPQDPVLFSgslrm 1384
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKARRQIGMIFQHFNLLS----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1385 nldpfSQYSDEEVWMALELAHL-KGFVSA----------LPDKLNHECAeggeNLSVGQRQLVCLARALLRKTKILVLDE 1453
Cdd:PRK11153 96 -----SRTVFDNVALPLELAGTpKAEIKArvtellelvgLSDKADRYPA----QLSGGQKQRVAIARALASNPKVLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 1454 ATAAVDLETDDLIQSTIRTQFED--STVLTIAHRlntiMDYT-----RVIVLDKGEIRECGAPSE 1511
Cdd:PRK11153 167 ATSALDPATTRSILELLKDINRElgLTIVLITHE----MDVVkricdRVAVIDAGRLVEQGTVSE 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1286-1505 |
1.27e-18 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 87.45 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1286 PHSGRVEFRDYCLRYREDLD--LVLKHINVTIEGGEKVGIVGRTGAGKSSLtlglFRI----NESAEGEIIIDGINIAKI 1359
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLiaglEKPTSGEVLVDGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1360 GLhnlrfKITIIPQDPVLF----------SGsLRMNLDPFSQYsDEEVWMALELAHLKGFVSALPdklnHEcaeggenLS 1429
Cdd:COG1116 79 GP-----DRGVVFQEPALLpwltvldnvaLG-LELRGVPKAER-RERARELLELVGLAGFEDAYP----HQ-------LS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1430 VGQRQLVCLARALLRKTKILVLDEATAAVDLET-----DDLIQstIRTQfEDSTVLTIAH------RLNtimdyTRVIVL 1498
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDALTrerlqDELLR--LWQE-TGKTVLFVTHdvdeavFLA-----DRVVVL 212
|
....*....
gi 1958656469 1499 DK--GEIRE 1505
Cdd:COG1116 213 SArpGRIVE 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
662-847 |
1.45e-18 |
|
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: 84.76 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLkgsvayvpqqawiqndslrenilFGRPLQEHcYKAV 741
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV-----------------------LGKDIKKE-PEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 742 MEACALLPDLEILPsGDLTeiGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIFEkvvgpmgLLK-- 819
Cdd:cd03230 72 KRRIGYLPEEPSLY-ENLT--VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWE-------LLRel 141
|
170 180 190
....*....|....*....|....*....|..
gi 1958656469 820 ---NKTRILVTHGISYLPQV-DVIIVMSGGKI 847
Cdd:cd03230 142 kkeGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
643-858 |
1.77e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 87.11 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 643 NSITVKNATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVtlkgsvaYVPQQAwIQNDS 722
Cdd:PRK13648 6 SIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI-------FYNNQA-ITDDN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 723 LRE-----NILFGRPLQEHCYKAVMEACALLPDLEILPSGDLTEIGEKGVN--------------LSGGQKQRVSLARAV 783
Cdd:PRK13648 78 FEKlrkhiGIVFQNPDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKqvdmleradyepnaLSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 784 YCNSDIYLLDDPLSAVDAHVGKHIFEkVVGPMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLD 858
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLD-LVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
1016-1194 |
2.44e-18 |
|
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: 87.44 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1016 VYGALGILQGVAVFGYSMAVSIGGIFASRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGS 1095
Cdd:cd18544 46 LYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1096 LFSVIGAVIIIL-----LATpIAAVIIPPLGLVYFFVQRFYVASSRQLKrlESVSRspVYSHFNETLLGVSVIRAFEEQE 1170
Cdd:cd18544 126 LLLLIGILIAMFllnwrLAL-ISLLVLPLLLLATYLFRKKSRKAYREVR--EKLSR--LNAFLQESISGMSVIQLFNREK 200
|
170 180
....*....|....*....|....
gi 1958656469 1171 RFIRQSDLKVDENQKAYYPSIVAN 1194
Cdd:cd18544 201 REFEEFDEINQEYRKANLKSIKLF 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1291-1514 |
2.48e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 85.91 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINI--AKIGLHNLRFKI 1368
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1369 TIIPQDPVLFS----------GSLRMNldpfSQYSDEEVWMALELAHLKGfvsaLPDKLNHECAEggenLSVGQRQLVCL 1438
Cdd:PRK09493 80 GMVFQQFYLFPhltalenvmfGPLRVR----GASKEEAEKQARELLAKVG----LAERAHHYPSE----LSGGQQQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 1439 ARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDS-TVLTIAHRLNTIMDY-TRVIVLDKGEIRECGAPSELLQ 1514
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGmTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1291-1513 |
2.74e-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: 86.29 E-value: 2.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLtLGLF--RINESAEGEIIIDGINIAKIGLHNLRFKI 1368
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTL-LSLItgDLPPTYGNDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1369 ---------TIIPQDPVL------FSGSLrmnlDPFSQYSDEEV-----WMA-LELAHLKgfvsalpDKLNHEcaeggen 1427
Cdd:COG1119 81 glvspalqlRFPRDETVLdvvlsgFFDSI----GLYREPTDEQRerareLLElLGLAHLA-------DRPFGT------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1428 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRT--QFEDSTVLTIAHRLNTIMD-YTRVIVLDKGEIR 1504
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPgITHVLLLKDGRVV 222
|
....*....
gi 1958656469 1505 ECGAPSELL 1513
Cdd:COG1119 223 AAGPKEEVL 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1291-1513 |
2.88e-18 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 85.82 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLDLVlKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITI 1370
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1371 IPQDPVLFSG-SLRMN--LDP-FSQYSDEEV-WMALELAHLKGFVSA-LPDKLNHEcaeggenLSVGQRQLVCLARALLR 1444
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPkLLKWPKEKIrERADELLALVGLDPAeFADRYPHE-------LSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958656469 1445 KTKILVLDEATAAVDLET-DDLIQSTIRTQFE-DSTVLTIAHRLN-TIMDYTRVIVLDKGEIRECGAPSELL 1513
Cdd:cd03295 153 DPPLLLMDEPFGALDPITrDQLQEEFKRLQQElGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
1016-1262 |
3.59e-18 |
|
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: 86.85 E-value: 3.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1016 VYGALGILQGVAVFGYSMAVSIGGIFASRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGS 1095
Cdd:cd18557 41 ILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1096 LFSVIGAVIIILLA----TPIAAVIIPPLGLVYFFVQRFYVASSRQLkrLESVSRSPvySHFNETLLGVSVIRAFEEQER 1171
Cdd:cd18557 121 ILQVIGGLIILFILswklTLVLLLVIPLLLIASKIYGRYIRKLSKEV--QDALAKAG--QVAEESLSNIRTVRSFSAEEK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1172 FIRQSDLKVDENQKAYYPSIVAN---RWLAVRLECVGNCIVLFAALFAVISRHsLSAGLVGLSVSYSLQITAYLNWLVRM 1248
Cdd:cd18557 197 EIRRYSEALDRSYRLARKKALANalfQGITSLLIYLSLLLVLWYGGYLVLSGQ-LTVGELTSFILYTIMVASSVGGLSSL 275
|
250
....*....|....
gi 1958656469 1249 SSEMETNIVAVERL 1262
Cdd:cd18557 276 LADIMKALGASERV 289
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
645-846 |
4.45e-18 |
|
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: 83.39 E-value: 4.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWArdEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG---------------SV 709
Cdd:cd03229 1 LELKNVSKRYG--QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelpplrrRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 710 AYVPQQ-AWIQNDSLRENILFGrplqehcykavmeacallpdleilpsgdlteigekgvnLSGGQKQRVSLARAVYCNSD 788
Cdd:cd03229 79 GMVFQDfALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958656469 789 IYLLDDPLSAVDAHVGKHI---FEKVVGPMGllknKTRILVTHGISYLPQV-DVIIVMSGGK 846
Cdd:cd03229 121 VLLLDEPTSALDPITRREVralLKSLQAQLG----ITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
644-856 |
5.19e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.45 E-value: 5.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 644 SITVKNATFTWARDEppTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS-----------VAYV 712
Cdd:PRK10851 2 SIEIANIKKSFGRTQ--VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 713 PQQ-AWIQNDSLRENILFG--------RPLQEHCYKAVMEAcallpdLEILPSGDLTEigEKGVNLSGGQKQRVSLARAV 783
Cdd:PRK10851 80 FQHyALFRHMTVFDNIAFGltvlprreRPNAAAIKAKVTQL------LEMVQLAHLAD--RYPAQLSGGQKQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958656469 784 YCNSDIYLLDDPLSAVDAHVGKHIFEKVVGPMGLLKNkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQEL 856
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKF-TSVFVTHDQEEAMEVaDRVVVMSQGNIEQAGTPDQV 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
660-807 |
5.54e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.44 E-value: 5.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 660 PTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG--SVAYVPQQAWIqNDSL----RENILFG--- 730
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRSEV-PDSLpltvRDLVAMGrwa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 731 -----RPLQEHCYKAVMEACAL--LPDLEILPsgdlteIGEkgvnLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHV 803
Cdd:NF040873 85 rrglwRRLTRDDRAAVDDALERvgLADLAGRQ------LGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
....
gi 1958656469 804 GKHI 807
Cdd:NF040873 155 RERI 158
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
646-847 |
5.69e-18 |
|
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: 83.85 E-value: 5.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 646 TVKNATFTWaRDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG----------SVAYVPQQ 715
Cdd:cd03226 1 RIENISFSY-KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 716 AWIQ--NDSLRENILFGRPLQehcYKAVMEACALLPDLEILpsgDLTEigEKGVNLSGGQKQRVSLARAVYCNSDIYLLD 793
Cdd:cd03226 80 VDYQlfTDSVREELLLGLKEL---DAGNEQAETVLKDLDLY---ALKE--RHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656469 794 DPLSAVDAH----VGKhIFEKVVGpmgllKNKTRILVTHGISYLPQV-DVIIVMSGGKI 847
Cdd:cd03226 152 EPTSGLDYKnmerVGE-LIRELAA-----QGKAVIVITHDYEFLAKVcDRVLLLANGAI 204
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1307-1515 |
6.59e-18 |
|
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: 86.65 E-value: 6.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLT---LGLFRINESAEGEIIIDGINIAKIG---LHNLRFK-ITIIPQDPvlfs 1379
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLAraiLGLLPPPGITSGEILFDGEDLLKLSekeLRKIRGReIQMIFQDP---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1380 gslrMN-LDP--------------FSQYSDEEVW-MALELAHLKGFVSAlPDKLN---HEcaeggenLSVGQRQLVCLAR 1440
Cdd:COG0444 96 ----MTsLNPvmtvgdqiaeplriHGGLSKAEAReRAIELLERVGLPDP-ERRLDrypHE-------LSGGMRQRVMIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1441 ALLRKTKILVLDEATAAVDLetddLIQSTI-------RTQFeDSTVLTIAHRLNT---IMDytRVIVLDKGEIRECGAPS 1510
Cdd:COG0444 164 ALALEPKLLIADEPTTALDV----TIQAQIlnllkdlQREL-GLAILFITHDLGVvaeIAD--RVAVMYAGRIVEEGPVE 236
|
....*
gi 1958656469 1511 ELLQQ 1515
Cdd:COG0444 237 ELFEN 241
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
662-859 |
7.72e-18 |
|
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: 84.21 E-value: 7.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKG-SVAYVP----------QQ-AWIQNDSLRENIL 728
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLR-LIAGFETPtSGEILLDGkDITNLPphkrpvntvfQNyALFPHLTVFENIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 729 FG---RPLQEHCYKA-VMEACALLpdleilpsgDLTEIGEKGVN-LSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHV 803
Cdd:cd03300 95 FGlrlKKLPKAEIKErVAEALDLV---------QLEGYANRKPSqLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656469 804 GKHIFEKVvgpMGLLKN--KTRILVTHGIS-YLPQVDVIIVMSGGKISEMGSYQELLDR 859
Cdd:cd03300 166 RKDMQLEL---KRLQKElgITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
645-847 |
7.82e-18 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 84.72 E-value: 7.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWArDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG----------------S 708
Cdd:COG3638 3 LELRNLSKRYP-GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGqdvtalrgralrrlrrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 709 VAYVPQQ-AWIQNDSLRENILFGR--------------PLQEhcykaVMEACALLPDLEILPsgdltEIGEKGVNLSGGQ 773
Cdd:COG3638 82 IGMIFQQfNLVPRLSVLTNVLAGRlgrtstwrsllglfPPED-----RERALEALERVGLAD-----KAYQRADQLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 774 KQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIfekvvgpMGLLK------NKTRILVTHgisylpQVDV-------II 840
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQV-------MDLLRriaredGITVVVNLH------QVDLarryadrII 218
|
....*..
gi 1958656469 841 VMSGGKI 847
Cdd:COG3638 219 GLRDGRV 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
645-868 |
9.16e-18 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 84.27 E-value: 9.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWaRDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSAL-----------------LAEMDKVEghvtLKG 707
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMInrlieptsgeifidgedIREQDPVE----LRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 708 SVAYVPQQAWI-QNDSLRENI-----LFGRPlQEHCYKAVMEACAL--LPDLEIL---PSgdlteigekgvNLSGGQKQR 776
Cdd:cd03295 76 KIGYVIQQIGLfPHMTVEENIalvpkLLKWP-KEKIRERADELLALvgLDPAEFAdryPH-----------ELSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 777 VSLARAVYCNSDIYLLDDPLSAVDAHVGKHIFEKVVGPMGLLkNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQE 855
Cdd:cd03295 144 VGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQEL-GKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDE 222
|
250
....*....|...
gi 1958656469 856 LLDRDGafAEFVR 868
Cdd:cd03295 223 ILRSPA--NDFVA 233
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
671-847 |
1.03e-17 |
|
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: 83.50 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 671 DGALVAVVGQVGCGKSSLLSaLLAEMDKVE-GHVTLKGS-----------------VAYVPQQ-AWIQNDSLRENILFGR 731
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLR-CIAGLEKPDgGTIVLNGTvlfdsrkkinlppqqrkIGLVFQQyALFPHLNVRENLAFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 732 PLqehCYKAVMEACALlpdlEILPSGDLTEIGEKGV-NLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVgKHIFEK 810
Cdd:cd03297 101 KR---KRNREDRISVD----ELLDLLGLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL-RLQLLP 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958656469 811 VVGPMGLLKNKTRILVTHGISYLPQV-DVIIVMSGGKI 847
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLaDRIVVMEDGRL 210
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1290-1513 |
1.21e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.04 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1290 RVEFRDYCLryrEDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG-LHNLRFKI 1368
Cdd:PRK13644 3 RLENVSYSY---PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1369 TIIPQDPV-----------LFSGSLRMNLDPFSqySDEEVWMALELAHLKGFVSALPdklnhecaeggENLSVGQRQLVC 1437
Cdd:PRK13644 80 GIVFQNPEtqfvgrtveedLAFGPENLCLPPIE--IRKRVDRALAEIGLEKYRHRSP-----------KTLSGGQGQCVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656469 1438 LARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFED-STVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELL 1513
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
645-857 |
1.26e-17 |
|
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: 84.79 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSL---LSALL-AEmdkvEGHVTLKGSVAYVPQQAW--- 717
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLaklLNGLLlPT----SGKVTVDGLDTLDEENLWeir 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 718 ------IQN-D------SLRENILFGR-----PLQEhCYKAVMEACALLpdleilpsgDLTEIGEKG-VNLSGGQKQRVS 778
Cdd:TIGR04520 77 kkvgmvFQNpDnqfvgaTVEDDVAFGLenlgvPREE-MRKRVDEALKLV---------GMEDFRDREpHLLSGGQKQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 779 LARAVYCNSDIYLLDDPLSAVDAhVGKhifEKVVGPMGLLK---NKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQE 855
Cdd:TIGR04520 147 IAGVLAMRPDIIILDEATSMLDP-KGR---KEVLETIRKLNkeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPRE 222
|
..
gi 1958656469 856 LL 857
Cdd:TIGR04520 223 IF 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
645-857 |
1.29e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 84.66 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSS---LLSALLAEMD---KVEGHVTLKGSVAYVPQQAWI 718
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTiskILTGLLKPQSgeiKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 719 --QND-------SLRENILFGrpLQEHCY-----KAVMEACALLPDLEILpsgdlteIGEKGVNLSGGQKQRVSLARAVY 784
Cdd:PRK13632 88 ifQNPdnqfigaTVEDDIAFG--LENKKVppkkmKDIIDDLAKKVGMEDY-------LDKEPQNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958656469 785 CNSDIYLLDDPLSAVDAHvGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELL 857
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPK-GKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1305-1485 |
1.57e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 81.43 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1305 DLVLKHINVTIEGGEKVGIVGRTGAGKSSLtlglFRInesaegeiiIDGI------NIAKIGLHNLRFkitiIPQDPVLF 1378
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSL----FRA---------LAGLwpwgsgRIGMPEGEDLLF----LPQRPYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1379 SGSLRmnldpfsqysdEEV---WMalelahlkgfvsalpdklnhecaeggENLSVGQRQLVCLARALLRKTKILVLDEAT 1455
Cdd:cd03223 77 LGTLR-----------EQLiypWD--------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEAT 119
|
170 180 190
....*....|....*....|....*....|
gi 1958656469 1456 AAVDLETDDLIQSTIRTQFedSTVLTIAHR 1485
Cdd:cd03223 120 SALDEESEDRLYQLLKELG--ITVISVGHR 147
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1307-1503 |
1.81e-17 |
|
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: 82.58 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINI--AKIGLHNLRFKITIIPQDPVLFSgslRM 1384
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFP---HL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1385 N------LDP---FSQYSDEEVWMALELAHLKGfvsaLPDKLNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEAT 1455
Cdd:cd03262 92 TvlenitLAPikvKGMSKAEAEERALELLEKVG----LADKADAYPAQ----LSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958656469 1456 AAVDLETDDLIQSTIRTQFEDS-TVLTIAHRlntiMDY-----TRVIVLDKGEI 1503
Cdd:cd03262 164 SALDPELVGEVLDVMKDLAEEGmTMVVVTHE----MGFarevaDRVIFMDDGRI 213
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1307-1503 |
2.53e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 83.60 E-value: 2.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLtL----GLFRINEsaeGEIIIDGINIAKIGLHNlRFK-ITIIPQDPVL---F 1378
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTL-LnaiaGSLPPDS---GSILIDGKDVTKLPEYK-RAKyIGRVFQDPMMgtaP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1379 SGSLRMNLDpfsqysdeevwMALELAHLKGFVSALPDKLNHECAE-------GGEN--------LSVGQRQLVCLARALL 1443
Cdd:COG1101 96 SMTIEENLA-----------LAYRRGKRRGLRRGLTKKRRELFREllatlglGLENrldtkvglLSGGQRQALSLLMATL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1444 RKTKILVLDEATAAVD-------LE-TDDLIQstirtqfEDS-TVLTIAHRLNTIMDY-TRVIVLDKGEI 1503
Cdd:COG1101 165 TKPKLLLLDEHTAALDpktaalvLElTEKIVE-------ENNlTTLMVTHNMEQALDYgNRLIMMHEGRI 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
645-857 |
2.84e-17 |
|
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: 82.63 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNAT--FTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVTLKG-------------- 707
Cdd:cd03258 2 IELKNVSkvFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIR-CINGLERpTSGSVLVDGtdltllsgkelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 708 --SVAYVPQQ-AWIQNDSLRENILFgrPLQ-EHCYKAVMEACALlpdlEILPSGDLTEIGEK-GVNLSGGQKQRVSLARA 782
Cdd:cd03258 81 rrRIGMIFQHfNLLSSRTVFENVAL--PLEiAGVPKAEIEERVL----ELLELVGLEDKADAyPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 783 VYCNSDIYLLDDPLSAVDAHVGKHIFEkvvgpmgLLK--NK----TRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQE 855
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILA-------LLRdiNRelglTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEE 227
|
..
gi 1958656469 856 LL 857
Cdd:cd03258 228 VF 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1307-1512 |
2.92e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.00 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSslTL-----GLFRINEsaeGEIIIDGiniAKIGLHN----LRFKITIIPQDPVL 1377
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKS--TLmkilsGVYQPDS---GEILLDG---EPVRFRSprdaQAAGIAIIHQELNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1378 FSgslrmNLdpfsqySDEE-VWMALELAHlKGFVSalPDKLNHECAE-----G--------GENLSVGQRQLVCLARALL 1443
Cdd:COG1129 91 VP-----NL------SVAEnIFLGREPRR-GGLID--WRAMRRRAREllarlGldidpdtpVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958656469 1444 RKTKILVLDEATAAVDL-ETDDLIQsTIRtQFEDS--TVLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSEL 1512
Cdd:COG1129 157 RDARVLILDEPTASLTErEVERLFR-IIR-RLKAQgvAIIYISHRLDEVFEIAdRVTVLRDGRLVGTGPVAEL 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
662-856 |
3.07e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 85.16 E-value: 3.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVTLKGSvaYVPQQAWIQND--------------SLREN 726
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLR-LVAGLEKpTEGQIFIDGE--DVTHRSIQQRDicmvfqsyalfphmSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 727 ILFGRPLQ----EHCYKAVMEACALLpdleilpsgDLTEIGEKGVN-LSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDA 801
Cdd:PRK11432 99 VGYGLKMLgvpkEERKQRVKEALELV---------DLAGFEDRYVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 802 HVGKHIFEKVVGPMGLLkNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQEL 856
Cdd:PRK11432 170 NLRRSMREKIRELQQQF-NITSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1304-1513 |
3.75e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 85.47 E-value: 3.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1304 LDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG---LHNLRFK--------ITIIP 1372
Cdd:PRK10070 40 LSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVRRKkiamvfqsFALMP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1373 QDPVLFSGSLRMNLDPF-SQYSDEEVWMALELAHLKGFVSALPDKlnhecaeggenLSVGQRQLVCLARALLRKTKILVL 1451
Cdd:PRK10070 120 HMTVLDNTAFGMELAGInAEERREKALDALRQVGLENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958656469 1452 DEATAAVDletddliqSTIRTQFEDS----------TVLTIAHRLNTIMDY-TRVIVLDKGEIRECGAPSELL 1513
Cdd:PRK10070 189 DEAFSALD--------PLIRTEMQDElvklqakhqrTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1307-1512 |
4.78e-17 |
|
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: 86.39 E-value: 4.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLtLGLFRINESAE---GEII--------------------------------- 1350
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDQYEptsGRIIyhvalcekcgyverpskvgepcpvcggtlepee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1351 IDGINIAKIGLHNLRFKITIIPQDPVLFSGSLR-----MNLDPFSQYS-DEEVWMALELAHLKgfvsalpdKLNHECAEG 1424
Cdd:TIGR03269 94 VDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTvldnvLEALEEIGYEgKEAVGRAVDLIEMV--------QLSHRITHI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1425 GENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFED---STVLTiAHRLNTIMDYT-RVIVLDK 1500
Cdd:TIGR03269 166 ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsgiSMVLT-SHWPEVIEDLSdKAIWLEN 244
|
250
....*....|..
gi 1958656469 1501 GEIRECGAPSEL 1512
Cdd:TIGR03269 245 GEIKEEGTPDEV 256
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1291-1512 |
5.49e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 82.86 E-value: 5.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLD-LVLKHINVTIEGGEKVGIVGRTGAGKSS---LTLGLFrinESAEGEIIIDGINIAKIGLHNLRF 1366
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLL---EAESGQIIIDGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1367 KITIIPQDP-VLFSGSLRMNLDPFS--------QYSDEEVWMALELAHLKGFVSALPDKLnhecaeggenlSVGQRQLVC 1437
Cdd:PRK13650 82 KIGMVFQNPdNQFVGATVEDDVAFGlenkgiphEEMKERVNEALELVGMQDFKEREPARL-----------SGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 1438 LARALLRKTKILVLDEATAAVDLETD-DLIQS--TIRTQFeDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSEL 1512
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRlELIKTikGIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
645-847 |
8.21e-17 |
|
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: 81.46 E-value: 8.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDEPpTLNGITFAIPDGALVAVVGQVGCGKSSLLSAL--LAEMDKVEGHV------TLKGS-------- 708
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLngLVEPTSGSVLIdgtdinKLKGKalrqlrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 709 VAYVPQQ-AWIQNDSLRENILFGRPLQEHCYKAVM---------EACALLPDLEILPSgdlteIGEKGVNLSGGQKQRVS 778
Cdd:cd03256 80 IGMIFQQfNLIERLSVLENVLSGRLGRRSTWRSLFglfpkeekqRALAALERVGLLDK-----AYQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 779 LARAVYCNSDIYLLDDPLSAVDAHVGKHIfekvvgpMGLLK------NKTRILVTHgisylpQVDV-------IIVMSGG 845
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQV-------MDLLKrinreeGITVIVSLH------QVDLareyadrIVGLKDG 221
|
..
gi 1958656469 846 KI 847
Cdd:cd03256 222 RI 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
645-851 |
1.23e-16 |
|
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: 80.38 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWarDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLS--ALLAEMDKveGHVTLKG-----------SVAY 711
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRmiAGLEEPTS--GRIYIGGrdvtdlppkdrDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 712 VPQQ-AWIQNDSLRENILFGRPL----QEHCYKAVMEACALLpDLEILpsgdlteIGEKGVNLSGGQKQRVSLARAVYCN 786
Cdd:cd03301 77 VFQNyALYPHMTVYDNIAFGLKLrkvpKDEIDERVREVAELL-QIEHL-------LDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 787 SDIYLLDDPLSAVDAHVGKHIFEKVVGPMGLLKnKTRILVTHG-ISYLPQVDVIIVMSGGKISEMG 851
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLG-TTTIYVTHDqVEAMTMADRIAVMNDGQIQQIG 213
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1307-1513 |
1.38e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 83.74 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLtlgLFRINES---AEGEIIIDGINIAKIGLHNLRFKITIIPQDPVL---FSG 1380
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTL---LRAINGTltpTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfeFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1381 S--LRMNLDP----FSQYSDEEVwMALELAHLKGFVSALPDKlnhecaeGGENLSVGQRQLVCLARALLRKTKILVLDEA 1454
Cdd:PRK09536 95 RqvVEMGRTPhrsrFDTWTETDR-AAVERAMERTGVAQFADR-------PVTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958656469 1455 TAAVDL----ETDDLIQSTIRtqfEDSTVLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSELL 1513
Cdd:PRK09536 167 TASLDInhqvRTLELVRRLVD---DGKTAVAAIHDLDLAARYCdELVLLADGRVRAAGPPADVL 227
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
645-869 |
1.50e-16 |
|
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: 81.11 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------TLKGSVAY 711
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIvidgidisklplhTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 712 VPQQAWIQNDSLRENILFGRPLQEHCYKAVMEACALLPDLEILPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSDIYL 791
Cdd:cd03288 100 ILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656469 792 LDDPLSAVDAHVgKHIFEKVVgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELL-DRDGAFAEFVRT 869
Cdd:cd03288 180 MDEATASIDMAT-ENILQKVV--MTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLVRT 255
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
645-856 |
1.50e-16 |
|
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: 80.24 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG------------SVAYV 712
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 713 PQqawiqNDSL------RENILF-----GRPLQEhcYKAVMEAcaLLPDLEILPSGDlTEIGekgvNLSGGQKQRVSLAR 781
Cdd:cd03263 81 PQ-----FDALfdeltvREHLRFyarlkGLPKSE--IKEEVEL--LLRVLGLTDKAN-KRAR----TLSGGMKRKLSLAI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 782 AVYCNSDIYLLDDPLSAVDAHVGKHIFEKVVgpmGLLKNKTRILVTHG---ISYLpqVDVIIVMSGGKISEMGSYQEL 856
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLIL---EVRKGRSIILTTHSmdeAEAL--CDRIAIMSDGKLRCIGSPQEL 219
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
643-859 |
1.66e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 81.77 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 643 NSITVKNATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSS---LLSALLAEMDKVEGHVTLKGsVAYVPQQAWiq 719
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDG-ITLTAKTVW-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 720 ndSLREN--ILFGRPLQEHCYKAVMEACAL------LPDLEILP--------SGDLTEIGEKGVNLSGGQKQRVSLARAV 783
Cdd:PRK13640 81 --DIREKvgIVFQNPDNQFVGATVGDDVAFglenraVPRPEMIKivrdvladVGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 784 YCNSDIYLLDDPLSAVDAHvGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDR 859
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPA-GKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1291-1515 |
1.67e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 81.66 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDlDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--INIAKIGLHNLRFKI 1368
Cdd:PRK13639 2 LETRDLKYSYPDG-TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1369 TIIPQDP--VLFSGSLR-------MNLDPFSQYSDEEVWMALELAHLKGFVSALPdklnhecaeggENLSVGQRQLVCLA 1439
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEedvafgpLNLGLSKEEVEKRVKEALKAVGMEGFENKPP-----------HHLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 1440 RALLRKTKILVLDEATAAVD-LETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSELLQQ 1515
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDpMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYAdKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
667-859 |
1.85e-16 |
|
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: 82.84 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 667 FAIPDGALVAVVGQVGCGKSSLLSAL--LAEMDkvEGHVTLKGSV-----------------AYVPQQAwiqndSL---- 723
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIagLERPD--SGRIRLGGEVlqdsargiflpphrrriGYVFQEA-----RLfphl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 724 --RENILFGRPlqehcyKAVMEACALLPDlEILpsgDLTEIG---EKGV-NLSGGQKQRVSLARAVYCNSDIYLLDDPLS 797
Cdd:COG4148 93 svRGNLLYGRK------RAPRAERRISFD-EVV---ELLGIGhllDRRPaTLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958656469 798 AVDAHVGKHI---FEKvvgpmglLKNKTRI---LVTHGisyLPQV----DVIIVMSGGKISEMGSYQELLDR 859
Cdd:COG4148 163 ALDLARKAEIlpyLER-------LRDELDIpilYVSHS---LDEVarlaDHVVLLEQGRVVASGPLAEVLSR 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1291-1513 |
2.77e-16 |
|
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: 80.07 E-value: 2.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREdldLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAkiGLHNLRFKITI 1370
Cdd:cd03299 1 LKVENLSKDWKE---FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1371 IPQDPVLF---------SGSLRMNLDPFSQySDEEVwmaLELAHLKGFVSALPDKlnhecaegGENLSVGQRQLVCLARA 1441
Cdd:cd03299 76 VPQNYALFphmtvykniAYGLKKRKVDKKE-IERKV---LEIAEMLGIDHLLNRK--------PETLSGGEQQRVAIARA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 1442 LLRKTKILVLDEATAAVDLETDDLIQS---TIRTQFeDSTVLTIAHRLNTI-MDYTRVIVLDKGEIRECGAPSELL 1513
Cdd:cd03299 144 LVVNPKILLLDEPFSALDVRTKEKLREelkKIRKEF-GVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
662-847 |
2.95e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.49 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSaLLAEMDKVEGHVTLKGSVAYvpqqAWIQNDSlreNILF--GRPLQehcYK 739
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLR-LLAGLETPSAGELLAGTAPL----AEAREDT---RLMFqdARLLP---WK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 740 AVMEACAL------LPD-LEILPSGDLTE-IGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVG---KHIF 808
Cdd:PRK11247 97 KVIDNVGLglkgqwRDAaLQALAAVGLADrANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRiemQDLI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958656469 809 EKVVGPMGLlknkTRILVTHGISYLPQV-DVIIVMSGGKI 847
Cdd:PRK11247 177 ESLWQQHGF----TVLLVTHDVSEAVAMaDRVLLIEEGKI 212
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1314-1513 |
4.09e-16 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 81.32 E-value: 4.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1314 TIEGGEKVGIVGRTGAGKSslTLG--LFRINESAEGEIIIDGINIAKIG---LHNLRFKITIIPQDPvlfSGSL--RMN- 1385
Cdd:COG4608 40 DIRRGETLGLVGESGCGKS--TLGrlLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP---YASLnpRMTv 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1386 -------LDPFSQYS----DEEVWMALELAHLKgfvsalPDKLN---HEcaeggenLSVGQRQLVCLARALLRKTKILVL 1451
Cdd:COG4608 115 gdiiaepLRIHGLASkaerRERVAELLELVGLR------PEHADrypHE-------FSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958656469 1452 DEATAAVDLEtddlIQSTIRTQFED------STVLTIAHRLNT---IMDytRVIVLDKGEIRECGaPSELL 1513
Cdd:COG4608 182 DEPVSALDVS----IQAQVLNLLEDlqdelgLTYLFISHDLSVvrhISD--RVAVMYLGKIVEIA-PRDEL 245
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
621-868 |
4.23e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 84.70 E-value: 4.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 621 LSHEELEPDSIERWSI--KDGGGMN---------SITVKNATFTW-ARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSL 688
Cdd:PTZ00265 1131 LSFEKYYPLIIRKSNIdvRDNGGIRiknkndikgKIEIMDVNFRYiSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTV 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 689 LSALLAEMD-KVEGHVTLKGS----------------------------------------------------------- 708
Cdd:PTZ00265 1211 MSLLMRFYDlKNDHHIVFKNEhtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfknsgkilldgvdicdyn 1290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 709 -------VAYVPQQAWIQNDSLRENILFGRplQEHCYKAVMEAC---ALLPDLEILPSGDLTEIGEKGVNLSGGQKQRVS 778
Cdd:PTZ00265 1291 lkdlrnlFSIVSQEPMLFNMSIYENIKFGK--EDATREDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIA 1368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 779 LARAVYCNSDIYLLDDPLSAVDAHVGKHIfEKVVGPMGLLKNKTRILVTHGISYLPQVDVIIVM-----SGGKISEMGSY 853
Cdd:PTZ00265 1369 IARALLREPKILLLDEATSSLDSNSEKLI-EKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFnnpdrTGSFVQAHGTH 1447
|
330
....*....|....*.
gi 1958656469 854 QELLD-RDGAFAEFVR 868
Cdd:PTZ00265 1448 EELLSvQDGVYKKYVK 1463
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1308-1515 |
5.31e-16 |
|
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: 80.00 E-value: 5.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1308 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG---LHNLRFK--------ITIIPQDPV 1376
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKkismvfqsFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1377 LFSGSLRMNLDPFSQYSDEEVWM-ALELAHLKGFVSALPDKLnhecaeggenlSVGQRQLVCLARALLRKTKILVLDEAT 1455
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAeALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958656469 1456 AAVDletddliqSTIRTQFEDS----------TVLTIAHRLNTIM---DytRVIVLDKGEIRECGAPSELLQQ 1515
Cdd:cd03294 189 SALD--------PLIRREMQDEllrlqaelqkTIVFITHDLDEALrlgD--RIAIMKDGRLVQVGTPEEILTN 251
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
644-836 |
6.14e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 79.70 E-value: 6.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 644 SITVKNATFTWarDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALlAEMDKVEGHVTLKGSVAYVPQQAW---IQN 720
Cdd:PRK14258 7 AIKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEFFNQNIYerrVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 721 DSLRENI--LFGRP--LQEHCYKAVMEACALL---PDLEI-------LPSGDL-----TEIGEKGVNLSGGQKQRVSLAR 781
Cdd:PRK14258 84 NRLRRQVsmVHPKPnlFPMSVYDNVAYGVKIVgwrPKLEIddivesaLKDADLwdeikHKIHKSALDLSGGQQQRLCIAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 782 AVYCNSDIYLLDDPLSAVDAHVGKHIfEKVVGPMGLLKNKTRILVTHGisyLPQV 836
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKV-ESLIQSLRLRSELTMVIVSHN---LHQV 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1310-1503 |
7.54e-16 |
|
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: 77.92 E-value: 7.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1310 HINVTIEGGEKVGIVGRTGAGKSSLtLGLFRINESAE-GEIIIDGINIAkiGLHNLRFKITIIPQDPVLFSG-------- 1380
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTL-LNLIAGFETPQsGRVLINGVDVT--AAPPADRPVSMLFQENNLFAHltveqnvg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1381 ---SLRMNLDPFSQysdEEVWMALELAHLKGFVSALPDKLnhecaeggenlSVGQRQLVCLARALLRKTKILVLDEATAA 1457
Cdd:cd03298 93 lglSPGLKLTAEDR---QAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958656469 1458 VD----LETDDLIqSTIRTQfEDSTVLTIAHRLNTIMD-YTRVIVLDKGEI 1503
Cdd:cd03298 159 LDpalrAEMLDLV-LDLHAE-TKMTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1290-1512 |
7.78e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 78.93 E-value: 7.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1290 RVEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGINI--AKIGLH 1362
Cdd:COG1117 11 KIEVRNLNVYYGDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlipgaRVEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1363 NLRFKITIIPQDPVLFSGS--------LRMNLDPFSQYSDEEVWMALELAHL----KgfvsalpDKLNhecaEGGENLSV 1430
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSiydnvaygLRLHGIKSKSELDEIVEESLRKAALwdevK-------DRLK----KSALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1431 GQRQLVCLARALLRKTKILVLDEATAAVD-LETD---DLIQStIRTQFedsTVLTIAHRLNT---IMDYTrvIVLDKGEI 1503
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDpISTAkieELILE-LKKDY---TIVIVTHNMQQaarVSDYT--AFFYLGEL 231
|
....*....
gi 1958656469 1504 RECGAPSEL 1512
Cdd:COG1117 232 VEFGPTEQI 240
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
645-849 |
8.29e-16 |
|
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: 78.63 E-value: 8.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFT-WARDEPPT-LNGITFAIPDGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKG-------------- 707
Cdd:COG4181 9 IELRGLTKTvGTGAGELTiLKGISLEVEAGESVAIVGASGSGKSTLLG-LLAGLDRPtSGTVRLAGqdlfaldedararl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 708 ---SVAYVpQQAW--IQNDSLRENilfgrplqehcykaVMeacalLPdLEILPSGDLTEIGEK-----GVN--------- 768
Cdd:COG4181 88 rarHVGFV-FQSFqlLPTLTALEN--------------VM-----LP-LELAGRRDARARARAllervGLGhrldhypaq 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 769 LSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIfekvvgpMGLL--KNKTR----ILVTHGISYLPQVDVIIVM 842
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQI-------IDLLfeLNRERgttlVLVTHDPALAARCDRVLRL 219
|
....*..
gi 1958656469 843 SGGKISE 849
Cdd:COG4181 220 RAGRLVE 226
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1307-1521 |
8.35e-16 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 79.52 E-value: 8.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGiniakiglhnlrfKITIIPQDPVLFSGSLRMNL 1386
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1387 DPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD-DL 1465
Cdd:cd03291 119 IFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEkEI 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 1466 IQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELLQQRGVFYS 1521
Cdd:cd03291 199 FESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSS 254
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1307-1511 |
9.11e-16 |
|
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: 78.25 E-value: 9.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSslTL-----GLFRINEsaeGEIIIDGINI--------AKIGLHnlR-FKITIIP 1372
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKT--TLfnlisGFLRPTS---GSVLFDGEDItglppheiARLGIG--RtFQIPRLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1373 QD---------PVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGfvsaLPDKLNHECAeggeNLSVGQRQLVCLARALL 1443
Cdd:cd03219 88 PEltvlenvmvAAQARTGSGLLLARARREEREARERAEELLERVG----LADLADRPAG----ELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1444 RKTKILVLDEATAAVDL-ETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDY-TRVIVLDKGEIRECGAPSE 1511
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPeETEELAELIRELRERGITVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDE 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1308-1502 |
1.15e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.00 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1308 LKHINVTIEGGEKVGIVGRTGAGKSslTL-----GLFRINEsaeGEIIIDGiniAKIGLHN----LRFKITIIPQDPVLF 1378
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKS--TLmkilyGLYQPDS---GEILIDG---KPVRIRSprdaIALGIGMVHQHFMLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1379 sgslrmnlDPFSQYsdEEVWMALElaHLKGFVSALpDKLNHE----CAEGG---------ENLSVGQRQLVCLARALLRK 1445
Cdd:COG3845 93 --------PNLTVA--ENIVLGLE--PTKGGRLDR-KAARARirelSERYGldvdpdakvEDLSVGEQQRVEILKALYRG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958656469 1446 TKILVLDEATaAV--DLETDDLIQsTIRtQF--EDSTVLTIAHRLNTIMDYT-RVIVLDKGE 1502
Cdd:COG3845 160 ARILILDEPT-AVltPQEADELFE-ILR-RLaaEGKSIIFITHKLREVMAIAdRVTVLRRGK 218
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1307-1511 |
1.18e-15 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 78.54 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSL----TlGLFRINEsaeGEIIIDGINI--------AKIGLhnLR-FKIT-IIP 1372
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLfnliT-GFYRPTS---GRILFDGRDItglpphriARLGI--ARtFQNPrLFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1373 QDPVL----------FSGSLRMNLDPFSQYSDEEVWM---ALELAHLKGfvsaLPDKLNHECAeggeNLSVGQRQLVCLA 1439
Cdd:COG0411 93 ELTVLenvlvaaharLGRGLLAALLRLPRARREEREArerAEELLERVG----LADRADEPAG----NLSYGQQRRLEIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 1440 RALLRKTKILVLDEATAAVDL-ETDDLIQsTIRT--QFEDSTVLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSE 1511
Cdd:COG0411 165 RALATEPKLLLLDEPAAGLNPeETEELAE-LIRRlrDERGITILLIEHDMDLVMGLAdRIVVLDFGRVIAEGTPAE 239
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
657-855 |
1.21e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 80.76 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 657 DEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKG-SVAYVPQQ-----------AWIQNDSL 723
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLR-LIAGFETPdSGRIMLDGqDITHVPAEnrhvntvfqsyALFPHMTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 724 RENILFG-----RPLQEhCYKAVMEACALLpdleilpsgDLTEIGE-KGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLS 797
Cdd:PRK09452 104 FENVAFGlrmqkTPAAE-ITPRVMEALRMV---------QLEEFAQrKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 798 AVDAHVGKHifekvvgpMGL-LK------NKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQE 855
Cdd:PRK09452 174 ALDYKLRKQ--------MQNeLKalqrklGITFVFVTHDQeEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1307-1515 |
1.45e-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: 80.14 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLtL----GLFRINEsaeGEIIIDGINIAKIGLHNlRfKITIIPQDPVLFS--- 1379
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTL-LrmiaGFETPDS---GRILLDGRDVTGLPPEK-R-NVGMVFQDYALFPhlt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1380 -------GsLRM-NLDPfsQYSDEEVWMALELAHLKGFVSALPdklnHEcaeggenLSVGQRQLVCLARALLRKTKILVL 1451
Cdd:COG3842 94 vaenvafG-LRMrGVPK--AEIRARVAELLELVGLEGLADRYP----HQ-------LSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656469 1452 DEATAAVDLETDDLIQSTIRTQFEDS--TVLTIAHRLN---TIMDytRVIVLDKGEIRECGAPSELLQQ 1515
Cdd:COG3842 160 DEPLSALDAKLREEMREELRRLQRELgiTFIYVTHDQEealALAD--RIAVMNDGRIEQVGTPEEIYER 226
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
1000-1177 |
1.74e-15 |
|
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: 78.62 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1000 RPAVNGTQENRNFRLSVYGALGI-----LQGVAVFGYSMAVSIGGIFASRRLHLDLLQNVLRSPMSFFERTPSGNLVNRF 1074
Cdd:cd18552 23 KPLLDDIFVEKDLEALLLVPLAIiglflLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1075 SKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLA----TPIAAVIIPPLGL-VYFFVQRFYVASSRQLKRLESVSrspv 1149
Cdd:cd18552 103 TNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLdwklTLIALVVLPLAALpIRRIGKRLRKISRRSQESMGDLT---- 178
|
170 180 190
....*....|....*....|....*....|..
gi 1958656469 1150 ySHFNETLLGVSVIRAF----EEQERFIRQSD 1177
Cdd:cd18552 179 -SVLQETLSGIRVVKAFgaedYEIKRFRKANE 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1291-1512 |
2.18e-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: 77.28 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYreDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHnlRFKITI 1370
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1371 IPQDPVLF---------SGSLRMNLDPfSQYSDEEVWMALELAHLKGFVSALPDKLnhecaeggenlSVGQRQLVCLARA 1441
Cdd:cd03300 77 VFQNYALFphltvfeniAFGLRLKKLP-KAEIKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656469 1442 LLRKTKILVLDEATAAVDLETDDLIQSTIRtQFEDSTVLTIAHRLN------TIMDytRVIVLDKGEIRECGAPSEL 1512
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELK-RLQKELGITFVFVTHdqeealTMSD--RIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
662-867 |
2.73e-15 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 76.99 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS-----------VAYVPQQ-AWIQNDSLRENILF 729
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 730 G----RPLQEHCYKAVMEACALLPDLEILPSGDLTeigekgvnLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAhvgk 805
Cdd:cd03299 95 GlkkrKVDKKEIERKVLEIAEMLGIDHLLNRKPET--------LSGGEQQRVAIARALVVNPKILLLDEPFSALDV---- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 806 HIFEKVVGPMGLLKNK---TRILVTHGIS-YLPQVDVIIVMSGGKISEMGSYQELLDR--DGAFAEFV 867
Cdd:cd03299 163 RTKEKLREELKKIRKEfgvTVLHVTHDFEeAWALADKVAIMLNGKLIQVGKPEEVFKKpkNEFVAEFL 230
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1307-1515 |
3.10e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 77.50 E-value: 3.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLtLGLFrineSAE-----GEIIIDGINIAKIGLHNLRFKITIIPQDPVL-FSG 1380
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTL-LRAL----SGElspdsGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1381 S----LRMNLDPFSQYSDE-----EVWMAL-ELAHLKGfvsalpdKLNHEcaeggenLSVGQRQLVCLARALLR------ 1444
Cdd:PRK13548 92 TveevVAMGRAPHGLSRAEddalvAAALAQvDLAHLAG-------RDYPQ-------LSGGEQQRVQLARVLAQlwepdg 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 1445 KTKILVLDEATAAVDL----ETDDLIQStiRTQFEDSTVLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSELLQQ 1515
Cdd:PRK13548 158 PPRWLLLDEPTSALDLahqhHVLRLARQ--LAHERGLAVIVVLHDLNLAARYAdRIVLLHQGRLVADGTPAEVLTP 231
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1307-1507 |
3.17e-15 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 76.08 E-value: 3.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGeKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIaKIGLHNLRFKITIIPQDpvlFSGSLRMNL 1386
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQPQKLRRRIGYLPQE---FGVYPNFTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1387 DPFSQY-----------SDEEVWMALELAHLKGFVSalpDKLNhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEAT 1455
Cdd:cd03264 90 REFLDYiawlkgipskeVKARVDEVLELVNLGDRAK---KKIG--------SLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958656469 1456 AAVDLETDDLIQSTIRTQFEDSTVLTIAHRLNTIMD-YTRVIVLDKGEIRECG 1507
Cdd:cd03264 159 AGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
645-865 |
3.67e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 77.75 E-value: 3.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVaYVPQQAW------- 717
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV-LSEETVWdvrrqvg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 718 --IQN-------DSLRENILFGrplqehcykavMEACALlPDLEILPSGD--LTEIG------EKGVNLSGGQKQRVSLA 780
Cdd:PRK13635 85 mvFQNpdnqfvgATVQDDVAFG-----------LENIGV-PREEMVERVDqaLRQVGmedflnREPHRLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 781 RAVYCNSDIYLLDDPLSAVDAhVGKhifEKVVGPMGLLKNKTRILV---THGISYLPQVDVIIVMSGGKISEMGSYQELL 857
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDP-RGR---REVLETVRQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEEGTPEEIF 228
|
....*...
gi 1958656469 858 DRDGAFAE 865
Cdd:PRK13635 229 KSGHMLQE 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
642-857 |
4.04e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 76.71 E-value: 4.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 642 MNSITVKNATFTWARDEppTLNGITFAIPDGALVAVVGQVGCGKSSLLSA--LLAEMD----KVeGHVTLKGSVAYVPQQ 715
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQT--VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCinLLEQPEagtiRV-GDITIDTARSLSQQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 716 AWIQNdsLRENILFgrplqehcykaVMEACALLPDLEIL-------------PSGDLTEIGEK-----GVN--------- 768
Cdd:PRK11264 78 GLIRQ--LRQHVGF-----------VFQNFNLFPHRTVLeniiegpvivkgePKEEATARAREllakvGLAgketsyprr 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 769 LSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAH-VGkhifeKVVGPMGLL--KNKTRILVTHGISYLPQV-DVIIVMSG 844
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPElVG-----EVLNTIRQLaqEKRTMVIVTHEMSFARDVaDRAIFMDQ 219
|
250
....*....|...
gi 1958656469 845 GKISEMGSYQELL 857
Cdd:PRK11264 220 GRIVEQGPAKALF 232
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
645-860 |
5.35e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 76.69 E-value: 5.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTwaRDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAY 711
Cdd:COG4559 2 LEAENLSVR--LGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaawspwelarRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 712 VPQQAWIQND-SLRENILFGR----PLQEHCYKAVMEACALLpDLEILPSGDLTEigekgvnLSGGQKQRVSLARA---V 783
Cdd:COG4559 80 LPQHSSLAFPfTVEEVVALGRaphgSSAAQDRQIVREALALV-GLAHLAGRSYQT-------LSGGEQQRVQLARVlaqL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 784 YCNSD----IYLLDDPLSAVD-AHvgKHIFekvvgpMGLLKNKTR-----ILVTHGISYLPQV-DVIIVMSGGKISEMGS 852
Cdd:COG4559 152 WEPVDggprWLFLDEPTSALDlAH--QHAV------LRLARQLARrgggvVAVLHDLNLAAQYaDRILLLHQGRLVAQGT 223
|
....*...
gi 1958656469 853 YQELLDRD 860
Cdd:COG4559 224 PEEVLTDE 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
645-870 |
5.44e-15 |
|
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: 76.17 E-value: 5.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFtwARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-SVAYVPQQAWI----- 718
Cdd:COG1127 6 IEVRNLTK--SFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqDITGLSEKELYelrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 719 -----QN----DSL--RENILFgrPLQEH-------CYKAVMEACAL--LPDLEIL-PSgdlteigEkgvnLSGGQKQRV 777
Cdd:COG1127 84 igmlfQGgalfDSLtvFENVAF--PLREHtdlseaeIRELVLEKLELvgLPGAADKmPS-------E----LSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 778 SLARAVYCNSDIYLLDDPLSAVDAHVGKHIFE---KVVGPMGLlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSY 853
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITSAVIDElirELRDELGL----TSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTP 226
|
250
....*....|....*..
gi 1958656469 854 QELLDRDgafAEFVRTY 870
Cdd:COG1127 227 EELLASD---DPWVRQF 240
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
662-859 |
7.31e-15 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 77.40 E-value: 7.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSA---LLAEMDKVEGHVTLKGS-----------------VAYVPQqawiqnD 721
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAilgLLPPPGITSGEILFDGEdllklsekelrkirgreIQMIFQ------D 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 722 ---SL--RENI--LFGRPLQEHCY---KAVME-ACALLPDLEILPSGDLteigekgVN-----LSGGQKQRVSLARAVYC 785
Cdd:COG0444 95 pmtSLnpVMTVgdQIAEPLRIHGGlskAEARErAIELLERVGLPDPERR-------LDrypheLSGGMRQRVMIARALAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 786 NSDIYLLDDPLSAVDAHVGKHIfekvvgpMGLLK------NKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLD 858
Cdd:COG0444 168 EPKLLIADEPTTALDVTIQAQI-------LNLLKdlqrelGLAILFITHDLGVVAEIaDRVAVMYAGRIVEEGPVEELFE 240
|
.
gi 1958656469 859 R 859
Cdd:COG0444 241 N 241
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
644-851 |
7.84e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.46 E-value: 7.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 644 SITVKNATFTWaRDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS----------VAYVP 713
Cdd:PRK15056 6 GIVVNDVTVTW-RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 714 QQA---WIQNDSLRENILFGR--------PLQEHCYKAVMEACALLPDLEILPSgdltEIGEkgvnLSGGQKQRVSLARA 782
Cdd:PRK15056 85 QSEevdWSFPVLVEDVVMMGRyghmgwlrRAKKRDRQIVTAALARVDMVEFRHR----QIGE----LSGGQKKRVFLARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958656469 783 VYCNSDIYLLDDPLSAVDAHVGKhifeKVVGPMGLLKN--KTRILVTHGISYLPQVDVIIVMSGGKISEMG 851
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEA----RIISLLRELRDegKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1307-1516 |
7.97e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.21 E-value: 7.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITIIPQDPVLFSG-SLR-- 1383
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRel 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1384 --------MNL-DPFSQYSDEEVWMALELAHlkgfVSALPDKLnhecaegGENLSVGQRQLVCLARALLRKTKILVLDEA 1454
Cdd:PRK11231 97 vaygrspwLSLwGRLSAEDNARVNQAMEQTR----INHLADRR-------LTDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656469 1455 TAAVDL----ETDDLIQstiRTQFEDSTVLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSELLQQR 1516
Cdd:PRK11231 166 TTYLDInhqvELMRLMR---ELNTQGKTVVTVLHDLNQASRYCdHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
662-859 |
8.16e-15 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 75.80 E-value: 8.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSAL--LAEMDkvEGHVTLKGSVAYVPQQAWIQndsLRENI--------LF-- 729
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCInlLEEPD--SGTITVDGEDLTDSKKDINK---LRRKVgmvfqqfnLFph 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 730 ---------------GRPLQEhcykAVMEACALLpdleilpsgDLTEIGEKG----VNLSGGQKQRVSLARAVYCNSDIY 790
Cdd:COG1126 92 ltvlenvtlapikvkKMSKAE----AEERAMELL---------ERVGLADKAdaypAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958656469 791 LLDDPLSAVDAH-VGkhifEkVVGPMGLLKNK--TRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLDR 859
Cdd:COG1126 159 LFDEPTSALDPElVG----E-VLDVMRDLAKEgmTMVVVTHEMGFAREVaDRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
645-858 |
1.22e-14 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 75.41 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDEPpTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG----------------S 708
Cdd:TIGR02315 2 LEVENLSKVYPNGKQ-ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGtditklrgkklrklrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 709 VAYVPQQ-AWIQNDSLRENILFGR------------PLQEHCYkavMEACALLPDLEILPSGDLteigeKGVNLSGGQKQ 775
Cdd:TIGR02315 81 IGMIFQHyNLIERLTVLENVLHGRlgykptwrsllgRFSEEDK---ERALSALERVGLADKAYQ-----RADQLSGGQQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 776 RVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIfekvvgpMGLLKnktRILVTHGISY---LPQVDV-------IIVMSGG 845
Cdd:TIGR02315 153 RVAIARALAQQPDLILADEPIASLDPKTSKQV-------MDYLK---RINKEDGITViinLHQVDLakkyadrIVGLKAG 222
|
250
....*....|...
gi 1958656469 846 KISEMGSYQELLD 858
Cdd:TIGR02315 223 EIVFDGAPSELDD 235
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
645-852 |
1.41e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 77.04 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNA--TFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLS--ALLAEMDkvEGHVTLKG------------- 707
Cdd:COG1135 2 IELENLskTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRciNLLERPT--SGSVLVDGvdltalserelra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 708 ---SVAYVPQQAwiqndSL------RENILFgrPLQ------EHCYKAVMEacaLLpdleilpsgDLTEIGEKG----VN 768
Cdd:COG1135 80 arrKIGMIFQHF-----NLlssrtvAENVAL--PLEiagvpkAEIRKRVAE---LL---------ELVGLSDKAdaypSQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 769 LSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIFEkvvgpmgLLK--NK----TRILVTHgisylpQVDVI--I 840
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILD-------LLKdiNRelglTIVLITH------EMDVVrrI 207
|
250
....*....|....*..
gi 1958656469 841 -----VMSGGKISEMGS 852
Cdd:COG1135 208 cdrvaVLENGRIVEQGP 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
665-859 |
1.74e-14 |
|
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: 76.69 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 665 ITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-----------------SVAYVPQQAWI-QNDSLREN 726
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrkgiflppekrRIGYVFQEARLfPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 727 ILFGR-----PLQEHCYKAVMEACALLPDLEILPSgdlteigekgvNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDA 801
Cdd:TIGR02142 96 LRYGMkrarpSERRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 802 HVGKHIfekvvgpMGLLKNKTR------ILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLDR 859
Cdd:TIGR02142 165 PRKYEI-------LPYLERLHAefgipiLYVSHSLQEVLRLaDRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
662-847 |
1.79e-14 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 74.10 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSAL--LAEMDkvEGHVTLKGSVAYVPQQAWIQndsLRENI--------LFgr 731
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlLEEPD--SGTIIIDGLKLTDDKKNINE---LRQKVgmvfqqfnLF-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 732 plqEHcyKAVMEACALLP-DLEILPSGDLTEIGEK-----GV---------NLSGGQKQRVSLARAVYCNSDIYLLDDPL 796
Cdd:cd03262 89 ---PH--LTVLENITLAPiKVKGMSKAEAEERALEllekvGLadkadaypaQLSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958656469 797 SAVDAHVGKhifeKVVGPMGLL--KNKTRILVTHGISYLPQV-DVIIVMSGGKI 847
Cdd:cd03262 164 SALDPELVG----EVLDVMKDLaeEGMTMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
662-857 |
1.95e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.05 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAYVPQQAWIQND-SLRENI 727
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTPEGiTVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 728 LFGRP--------LQEHCYKAVMEAcalLPDLEIlpsgdlTEIGEKGV-NLSGGQKQRVSLARAVYCNSDIYLLDDPLSA 798
Cdd:PRK11231 98 AYGRSpwlslwgrLSAEDNARVNQA---MEQTRI------NHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 799 VDAHvgkHIFEkVVGPMGLLKN--KTRILVTHGIS----YlpqVDVIIVMSGGKISEMGSYQELL 857
Cdd:PRK11231 169 LDIN---HQVE-LMRLMRELNTqgKTVVTVLHDLNqasrY---CDHLVVLANGHVMAQGTPEEVM 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1291-1513 |
2.24e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.13 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLDL-VLKHINVTIEGGEKVGIVGRTGAGKSS---LTLGLFrinESAEGEIIIDGINIAKIGLHNLRF 1366
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTtarLIDGLF---EEFEGKVKIDGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1367 KITIIPQDP-VLFSGSLRMNLDPFSQYSD----EEVWMALELAHLKgfVSALPDKLNHECaeggeNLSVGQRQLVCLARA 1441
Cdd:PRK13642 82 KIGMVFQNPdNQFVGATVEDDVAFGMENQgiprEEMIKRVDEALLA--VNMLDFKTREPA-----RLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 1442 LLRKTKILVLDEATAAVDLETDDLIQSTIRtQFEDS---TVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELL 1513
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIH-EIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
1019-1262 |
2.30e-14 |
|
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: 75.55 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1019 ALGILQGVAVFGYSMAVSIGGIFASRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFS 1098
Cdd:cd18542 47 GVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1099 VIGAVIIIL-----LATpIAAVIIPPLGLV-YFF---VQRFYVASSRQLKRLESVsrspvyshFNETLLGVSVIRAF--- 1166
Cdd:cd18542 127 FIGALIIMFsinwkLTL-ISLAIIPFIALFsYVFfkkVRPAFEEIREQEGELNTV--------LQENLTGVRVVKAFare 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1167 -EEQERFIRQSDLKVDENQKA------YYPSIVAnrwlavrLECVGNCIVLFAALFAVIsRHSLSAG-LVGLSvSYslqi 1238
Cdd:cd18542 198 dYEIEKFDKENEEYRDLNIKLakllakYWPLMDF-------LSGLQIVLVLWVGGYLVI-NGEITLGeLVAFI-SY---- 264
|
250 260
....*....|....*....|....*...
gi 1958656469 1239 TAYLNWLVRMS----SEMETNIVAVERL 1262
Cdd:cd18542 265 LWMLIWPVRQLgrliNDMSRASASAERI 292
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
662-857 |
2.86e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 74.42 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAYVPQQAwiqndSL----- 723
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHS-----SLsfpft 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 724 -RENILFGR-PLQEHCYK------AVMEACallpDLEILPSGDLTEigekgvnLSGGQKQRVSLARA---VYCNSD---I 789
Cdd:PRK13548 93 vEEVVAMGRaPHGLSRAEddalvaAALAQV----DLAHLAGRDYPQ-------LSGGEQQRVQLARVlaqLWEPDGpprW 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656469 790 YLLDDPLSAVD-AHvgKHIFekvvgpMGLLKNKTR------ILVTHGIS----YlpqVDVIIVMSGGKISEMGSYQELL 857
Cdd:PRK13548 162 LLLDEPTSALDlAH--QHHV------LRLARQLAHerglavIVVLHDLNlaarY---ADRIVLLHQGRLVADGTPAEVL 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1307-1513 |
3.05e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 74.18 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGINIAKIGLHNLRFKITIIPQDP------ 1375
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnpipnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1376 -VLFSGSLRMNLDPFSQYSDE---EVWMALELAHLKGFVSalpDKLNhecAEGGEnLSVGQRQLVCLARALLRKTKILVL 1451
Cdd:PRK14247 98 sIFENVALGLKLNRLVKSKKElqeRVRWALEKAQLWDEVK---DRLD---APAGK-LSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 1452 DEATAAVDLETDDLIQSTIRTQFEDSTVLTIAH---RLNTIMDYtrVIVLDKGEIRECGAPSELL 1513
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqQAARISDY--VAFLYKGQIVEWGPTREVF 233
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1307-1513 |
4.20e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 74.34 E-value: 4.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAK--------------------IGLHNLRF 1366
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnraqrkafrrdiqmvfqdsISAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1367 KITIIPQDPvlfsgsLR--MNLDPFSQYSdeevwMALELAHLKGFVSALPDKLNHEcaeggenLSVGQRQLVCLARALLR 1444
Cdd:PRK10419 107 TVREIIREP------LRhlLSLDKAERLA-----RASEMLRAVDLDDSVLDKRPPQ-------LSGGQLQRVCLARALAV 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656469 1445 KTKILVLDEATAAVDLetddLIQSTI-------RTQFeDSTVLTIAHRLNTIMDY-TRVIVLDKGEIRECGAPSELL 1513
Cdd:PRK10419 169 EPKLLILDEAVSNLDL----VLQAGVirllkklQQQF-GTACLFITHDLRLVERFcQRVMVMDNGQIVETQPVGDKL 240
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
660-859 |
4.59e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 73.59 E-value: 4.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 660 PTLNGITFAIPDGALVAVVGQVGCGKSSLLSAL--LAEMDK----VEGHVTLKGSV---------AYVPQQAWI--QNDS 722
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITSgdliVDGLKVNDPKVderlirqeaGMVFQQFYLfpHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 723 LrENILFGrPLQ-EHCYKAVMEACALlpdlEILPSGDLTE-IGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVD 800
Cdd:PRK09493 95 L-ENVMFG-PLRvRGASKEEAEKQAR----ELLAKVGLAErAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958656469 801 AHVgKHIFEKVvgpMGLLKNK--TRILVTHGISYLPQVDV-IIVMSGGKISEMGSYQELLDR 859
Cdd:PRK09493 169 PEL-RHEVLKV---MQDLAEEgmTMVIVTHEIGFAEKVASrLIFIDKGRIAEDGDPQVLIKN 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1307-1504 |
4.67e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.64 E-value: 4.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSltlgLFRI----NESAEGEIIIDGiniakiglhnlRFKITIIPQDPVLFSG-S 1381
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKST----LLKIlageLEPDSGEVSIPK-----------GLRIGYLPQEPPLDDDlT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1382 LRmnldpfsqysdEEVWMAL-----------ELAHLKGFVSALPDK---LNHECAEGGE--------------------- 1426
Cdd:COG0488 78 VL-----------DTVLDGDaelraleaeleELEAKLAEPDEDLERlaeLQEEFEALGGweaearaeeilsglgfpeedl 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1427 -----NLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTqfEDSTVLTIAH-R--LNTIMdyTRVIVL 1498
Cdd:COG0488 147 drpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN--YPGTVLVVSHdRyfLDRVA--TRILEL 222
|
....*.
gi 1958656469 1499 DKGEIR 1504
Cdd:COG0488 223 DRGKLT 228
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
662-851 |
4.92e-14 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 72.95 E-value: 4.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKGSVAYVPQ-QAWIQND-SLRENILF-----GRPL 733
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLR-LLAGIYPPdSGTVTVRGRVSSLLGlGGGFNPElTGRENIYLngrllGLSR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 734 QEhcYKAVMEacallpdlEILpsgDLTEIGEKG----VNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAH----VGK 805
Cdd:cd03220 117 KE--IDEKID--------EII---EFSELGDFIdlpvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfqekCQR 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958656469 806 HIFEKVvgpmglLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMG 851
Cdd:cd03220 184 RLRELL------KQGKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1291-1513 |
5.22e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 74.00 E-value: 5.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLDlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITI 1370
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1371 IPQDP--VLFS---------GSLRMNLDPfsQYSDEEVWMALELAHLKgfvsALPDKLNHecaeggeNLSVGQRQLVCLA 1439
Cdd:PRK13647 84 VFQDPddQVFSstvwddvafGPVNMGLDK--DEVERRVEEALKAVRMW----DFRDKPPY-------HLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 1440 RALLRKTKILVLDEATAAVDLETDDLIQSTI-RTQFEDSTVLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSELL 1513
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILdRLHNQGKTVIVATHDVDLAAEWAdQVIVLKEGRVLAEGDKSLLT 226
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1045-1453 |
5.64e-14 |
|
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: 76.76 E-value: 5.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1045 RLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVdSMIPQVIKMFMGSLFSVIGAVI-IILLATPIAAVIIPPLGLV 1123
Cdd:COG4615 82 RLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTI-SQAFVRLPELLQSVALVLGCLAyLAWLSPPLFLLTLVLLGLG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1124 yFFVQRFYVASSRQLKRLESVSRSPVYSHFNetllgvSVIRAFEE----QER--FIRQSDLKV------DENQKAYYPSI 1191
Cdd:COG4615 161 -VAGYRLLVRRARRHLRRAREAEDRLFKHFR------ALLEGFKElklnRRRrrAFFDEDLQPtaeryrDLRIRADTIFA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1192 VANRWlavrlecvGNCIVLFA---ALFAVISRHSLSAGLVglsVSYSL----------QITAYLNWLVRMSsemetniVA 1258
Cdd:COG4615 234 LANNW--------GNLLFFALiglILFLLPALGWADPAVL---SGFVLvllflrgplsQLVGALPTLSRAN-------VA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1259 VERLKEYSETEKEASWQIQETAPPSTWPHSGRVEFRDYCLRYREDLD---LVLKHINVTIEGGEKVGIVGRTGAGKSSLT 1335
Cdd:COG4615 296 LRKIEELELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGdegFTLGPIDLTIRRGELVFIVGGNGSGKSTLA 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1336 ---LGLFRineSAEGEIIIDGINIAKIGLHNLRFKITIIPQDPVLFSGslrmNLDPFSQYSDEEV--WMA-LELAHLKGF 1409
Cdd:COG4615 376 kllTGLYR---PESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR----LLGLDGEADPARAreLLErLELDHKVSV 448
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1958656469 1410 vsalpdklnhecaEGGE----NLSVGQRQLVCLARALLRKTKILVLDE 1453
Cdd:COG4615 449 -------------EDGRfsttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
642-859 |
6.71e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 74.88 E-value: 6.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 642 MNSITVKNATFTWARDEPpTLNGITFAIPDGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKGSV----------- 709
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQ-VIKGIDLDVADGEFIVLVGPSGCGKSTLLR-MVAGLERItSGEIWIGGRVvnelepadrdi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 710 AYVpqqawIQNDSL------RENILFG---RPL-QEHCYKAVMEACALLpdleilpsgdltEIGE----KGVNLSGGQKQ 775
Cdd:PRK11650 79 AMV-----FQNYALyphmsvRENMAYGlkiRGMpKAEIEERVAEAARIL------------ELEPlldrKPRELSGGQRQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 776 RVSLARAVYCNSDIYLLDDPLSAVDAhvgkhifeKVVGPMGL-LK------NKTRILVTHGisylpQV------DVIIVM 842
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLDA--------KLRVQMRLeIQrlhrrlKTTSLYVTHD-----QVeamtlaDRVVVM 208
|
250
....*....|....*..
gi 1958656469 843 SGGKISEMGSYQELLDR 859
Cdd:PRK11650 209 NGGVAEQIGTPVEVYEK 225
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
662-828 |
7.23e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 73.15 E-value: 7.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVTLKG---------------SVAYVPQQAwiqN- 720
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndLIPGARVEGEILLDGediydpdvdvvelrrRVGMVFQKP---Np 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 721 --DSLRENILFGRPLQEhcykavmeacallpdleILPSGDLTEIGEK------------------GVNLSGGQKQRVSLA 780
Cdd:COG1117 104 fpKSIYDNVAYGLRLHG-----------------IKSKSELDEIVEEslrkaalwdevkdrlkksALGLSGGQQQRLCIA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958656469 781 RAVYCNSDIYLLDDPLSAVD----AHVGKHIFEkvvgpmglLKNK-TRILVTH 828
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDpistAKIEELILE--------LKKDyTIVIVTH 211
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
645-846 |
7.30e-14 |
|
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: 70.17 E-value: 7.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWarDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTL--KGSVAYVPQqawiqnds 722
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWgsTVKIGYFEQ-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 723 lrenilfgrplqehcykavmeacallpdleilpsgdlteigekgvnLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAH 802
Cdd:cd03221 71 ----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958656469 803 vGKHIFEkvvgpmGLLKN--KTRILVTHGISYLPQV-DVIIVMSGGK 846
Cdd:cd03221 105 -SIEALE------EALKEypGTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
645-865 |
8.37e-14 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 73.35 E-value: 8.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLaEMDKVEGHVTLKG-------------SVAY 711
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwrkAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 712 VPQQAWIQNDSLRENI-LFGRPLQEHCYKaVMEACALLPDLEILPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSDIY 790
Cdd:cd03289 82 IPQKVFIFSGTFRKNLdPYGKWSDEEIWK-VAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 791 LLDDPLSAVDAhVGKHIFEKVVGPMglLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAE 865
Cdd:cd03289 161 LLDEPSAHLDP-ITYQVIRKTLKQA--FADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1306-1528 |
9.38e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.58 E-value: 9.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1306 LVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG-LHNLRFKITIIPQDP--------- 1375
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQNPdnqivativ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1376 ---VLFsGSLRMNLDPfsqysdEEVWMALELAHLKGFVSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLD 1452
Cdd:PRK13633 104 eedVAF-GPENLGIPP------EEIRERVDESLKKVGMYEYRRHAPHL-------LSGGQKQRVAIAGILAMRPECIIFD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 1453 EATAAVDLETDDLIQSTIRTQFEDS--TVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELLQQrgvfYSMAKDAGL 1528
Cdd:PRK13633 170 EPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE----VEMMKKIGL 243
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
545-865 |
9.44e-14 |
|
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: 76.87 E-value: 9.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 545 YLAAVGTFTWVCTPFLVALSTFAVFVTVDEKnilDAKKAFVSLalfnILRFPLNILPM----VISSIVQASVSLKRLRIF 620
Cdd:TIGR01271 1104 YLSTLRWFQMRIDIIFVFFFIAVTFIAIGTN---QDGEGEVGI----ILTLAMNILSTlqwaVNSSIDVDGLMRSVSRVF 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 621 ----LSHEELEPDS------------IERWSIKD----GGGMnsiTVKNATFTWARDEPPTLNGITFAIPDGALVAVVGQ 680
Cdd:TIGR01271 1177 kfidLPQEEPRPSGgggkyqlstvlvIENPHAQKcwpsGGQM---DVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGR 1253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 681 VGCGKSSLLSALLaEMDKVEGHVTLKG-------------SVAYVPQQAWIQNDSLRENI-LFGRPLQEHCYKaVMEACA 746
Cdd:TIGR01271 1254 TGSGKSTLLSALL-RLLSTEGEIQIDGvswnsvtlqtwrkAFGVIPQKVFIFSGTFRKNLdPYEQWSDEEIWK-VAEEVG 1331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 747 LLPDLEILPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAhVGKHIFEKVVGPMglLKNKTRILV 826
Cdd:TIGR01271 1332 LKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP-VTLQIIRKTLKQS--FSNCTVILS 1408
|
330 340 350
....*....|....*....|....*....|....*....
gi 1958656469 827 THGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAE 865
Cdd:TIGR01271 1409 EHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQ 1447
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1298-1488 |
1.02e-13 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 71.62 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1298 LRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSL--TL-GLFRineSAEGEIIIDGINIAKIglhnlrfkiTIIPQD 1374
Cdd:TIGR01189 6 LACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLlrILaGLLR---PDSGEVRWNGTPLAEQ---------RDEPHE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1375 PVLFSG---------SLRMNLD---PFSQYSDEEVWMALELAHLKGFvSALPdklnheCAEggenLSVGQRQLVCLARAL 1442
Cdd:TIGR01189 74 NILYLGhlpglkpelSALENLHfwaAIHGGAQRTIEDALAAVGLTGF-EDLP------AAQ----LSAGQQRRLALARLW 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958656469 1443 LRKTKILVLDEATAAVDLETDDLIQSTIR--TQFEDSTVLTIAHRLNT 1488
Cdd:TIGR01189 143 LSRRPLWILDEPTTALDKAGVALLAGLLRahLARGGIVLLTTHQDLGL 190
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1307-1515 |
1.10e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 74.37 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSS---LTLGLfriNESAEGEIIIDGINIAKIGLHNLrfKITIIPQDPVLFSG--- 1380
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTvlrLVAGL---EKPTEGQIFIDGEDVTHRSIQQR--DICMVFQSYALFPHmsl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1381 ------SLRMNLDPFSQYSdEEVWMALELAHLKGFVSALPDKLnhecaeggenlSVGQRQLVCLARALLRKTKILVLDEA 1454
Cdd:PRK11432 96 genvgyGLKMLGVPKEERK-QRVKEALELVDLAGFEDRYVDQI-----------SGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958656469 1455 TAAVDLETDDLIQSTIR---TQFeDSTVLTIAHrlntimDYTR-------VIVLDKGEIRECGAPSELLQQ 1515
Cdd:PRK11432 164 LSNLDANLRRSMREKIRelqQQF-NITSLYVTH------DQSEafavsdtVIVMNKGKIMQIGSPQELYRQ 227
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1307-1522 |
1.11e-13 |
|
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: 76.49 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGiniakiglhnlrfKITIIPQDPVLFSGSLRMNL 1386
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1387 DPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD-DL 1465
Cdd:TIGR01271 508 IFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEkEI 587
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656469 1466 IQSTIRTQFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPSELLQQRGVFYSM 1522
Cdd:TIGR01271 588 FESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSL 644
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1291-1515 |
1.24e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.91 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLDlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITI 1370
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1371 IPQDP--VLFSGSLRMNL--DPFSQYSDEEV--WMALELAHLKGfVSALPDKLNHecaeggeNLSVGQRQLVCLARALLR 1444
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDIafGPINLGLDEETvaHRVSSALHMLG-LEELRDRVPH-------HLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 1445 KTKILVLDEATAAVDLE-TDDLIQSTIRTQFE-DSTVLTIAHRLNTI---MDYtrVIVLDKGEIRECGAPSELLQQ 1515
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQgVKELIDFLNDLPETyGMTVIFSTHQLDLVpemADY--IYVMDKGRIVAYGTVEEIFLQ 228
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
642-859 |
1.41e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 72.25 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 642 MNSITVKNATFTWARDEppTLNGITFAIPDGALVAVVGQVGCGKSSLLSAL--LAEM---DKVEGHVTLKGS-------- 708
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVE--VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELypeARVSGEVYLDGQdifkmdvi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 709 --------VAYVPQQawIQNDSLRENILFG----------RPLQEHCYKAvMEACALLPDLEilpsgdlTEIGEKGVNLS 770
Cdd:PRK14247 79 elrrrvqmVFQIPNP--IPNLSIFENVALGlklnrlvkskKELQERVRWA-LEKAQLWDEVK-------DRLDAPAGKLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 771 GGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHgisYLPQV----DVIIVMSGGK 846
Cdd:PRK14247 149 GGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLF---LELKKDMTIVLVTH---FPQQAarisDYVAFLYKGQ 222
|
250
....*....|...
gi 1958656469 847 ISEMGSYQELLDR 859
Cdd:PRK14247 223 IVEWGPTREVFTN 235
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1307-1504 |
1.57e-13 |
|
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: 71.16 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIA-----KIGL----HNLRFKITIIPQdpVL 1377
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDiaarnRIGYlpeeRGLYPKMKVIDQ--LV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1378 FSGSLR-MNLDPFSQYSDEevWM-ALELAHLKGfvsalpDKLnhecaeggENLSVGQRQLVCLARALLRKTKILVLDEAT 1455
Cdd:cd03269 93 YLAQLKgLKKEEARRRIDE--WLeRLELSEYAN------KRV--------EELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958656469 1456 AAVDLETDDLIQSTIRTQFED-STVLTIAHRLNTIMDY-TRVIVLDKGEIR 1504
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELcDRVLLLNKGRAV 207
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
642-856 |
1.65e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.91 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 642 MNSITVKNATFTWarDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLS--ALLAE------------MDKVEghvTLKG 707
Cdd:PRK11000 1 MASVTLRNVTKAY--GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRmiAGLEDitsgdlfigekrMNDVP---PAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 708 SVAYVPQQ-AWIQNDSLRENILFGRPL----QEHCYKAVMEACallpdlEILPSGDLTEIGEKGvnLSGGQKQRVSLARA 782
Cdd:PRK11000 76 GVGMVFQSyALYPHLSVAENMSFGLKLagakKEEINQRVNQVA------EVLQLAHLLDRKPKA--LSGGQRQRVAIGRT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 783 VYCNSDIYLLDDPLSAVDA--HVGKHI----FEKVVGpmgllknKTRILVTHG-ISYLPQVDVIIVMSGGKISEMGSYQE 855
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLDAalRVQMRIeisrLHKRLG-------RTMIYVTHDqVEAMTLADKIVVLDAGRVAQVGKPLE 220
|
.
gi 1958656469 856 L 856
Cdd:PRK11000 221 L 221
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
660-801 |
1.72e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.04 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 660 PTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVP---QQAWIQNDSL------RENILFG 730
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPgaeRGVVFQNEGLlpwrnvQDNVAFG 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958656469 731 RPLQeHCYKAVMEACALlpdlEILPSGDLTEIGEKGV-NLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDA 801
Cdd:PRK11248 95 LQLA-GVEKMQRLEIAH----QMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
973-1261 |
1.84e-13 |
|
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: 72.82 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 973 FLSIFLFLCNHVSALASNYWLSLWTDDRPAVNGTQENRNFRlSVYGALGILQGV----AVFGYSMAVSIGGI--FASRRL 1046
Cdd:cd18547 2 ILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFS-GLLRILLLLLGLyllsALFSYLQNRLMARVsqRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1047 HLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATP----IAAVIIPPLGL 1122
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPlltlIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1123 VYFFV----QRFYVASSRQLKRLEsvsrspvySHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWL- 1197
Cdd:cd18547 161 VTKFIakrsQKYFRKQQKALGELN--------GYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLm 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656469 1198 -AVRLecVGN----CIVLFAALFAVisRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVER 1261
Cdd:cd18547 233 pIMNF--INNlgyvLVAVVGGLLVI--NGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAER 297
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
662-847 |
2.23e-13 |
|
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: 71.15 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSAL---LAEMDKVEGHVTLKG----------SVAYVPQQ-AWIQNDSLRENI 727
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGqprkpdqfqkCVAYVRQDdILLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 728 LFGR--PLQEHC---YKAVMEACALLPDLEILPSGdlteiGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAH 802
Cdd:cd03234 103 TYTAilRLPRKSsdaIRKKRVEDVLLRDLALTRIG-----GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958656469 803 VGKHIfekvvgpMGLLK-----NKTRILVTH--GISYLPQVDVIIVMSGGKI 847
Cdd:cd03234 178 TALNL-------VSTLSqlarrNRIVILTIHqpRSDLFRLFDRILLLSSGEI 222
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1307-1513 |
2.27e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 72.00 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGI------NIAKIGLHNLRFKITIIPQDPVLFSG 1380
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1381 -SLRMNLD-PFSQY---SDEEVWMALELAHLK-GFVSALPDKLNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEA 1454
Cdd:PRK14246 105 lSIYDNIAyPLKSHgikEKREIKKIVEECLRKvGLWKEVYDRLNSPASQ----LSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958656469 1455 TAAVDLETDDLIQSTIRTQFEDSTVLTIAH---RLNTIMDYtrVIVLDKGEIRECGAPSELL 1513
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEIAIVIVSHnpqQVARVADY--VAFLYNGELVEWGSSNEIF 240
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
644-851 |
2.32e-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: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 644 SITVKNATFT----WARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSAL--LAEMDKVEGHVTLKG---------- 707
Cdd:cd03213 3 TLSFRNLTVTvkssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGrpldkrsfrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 708 SVAYVPQQ-AWIQNDSLRENILFGRPLQehcykavmeacallpdleilpsgdlteigekgvNLSGGQKQRVSLARAVYCN 786
Cdd:cd03213 83 IIGYVPQDdILHPTLTVRETLMFAAKLR---------------------------------GLSGGERKRVSIALELVSN 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958656469 787 SDIYLLDDPLSAVDAHVGKHIfekvvgpMGLLK-----NKTRILVTHGISYL--PQVDVIIVMSGGKISEMG 851
Cdd:cd03213 130 PSLLFLDEPTSGLDSSSALQV-------MSLLRrladtGRTIICSIHQPSSEifELFDKLLLLSQGRVIYFG 194
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
653-795 |
2.48e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 74.33 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 653 TWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG--SVAYVPQQAWIQND-SLRENILF 729
Cdd:COG0488 5 SKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDDDlTVLDTVLD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 730 G-RPLQ------EHCYKAVMEACALLPDLEILpSGDLTEIGE-------KGV----------------NLSGGQKQRVSL 779
Cdd:COG0488 85 GdAELRaleaelEELEAKLAEPDEDLERLAEL-QEEFEALGGweaearaEEIlsglgfpeedldrpvsELSGGWRRRVAL 163
|
170
....*....|....*.
gi 1958656469 780 ARAVYCNSDIYLLDDP 795
Cdd:COG0488 164 ARALLSEPDLLLLDEP 179
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1307-1507 |
3.05e-13 |
|
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: 70.64 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLhNLRFKITIIPQDPVLFSGSLrMNL 1386
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGL-GGGFNPELTGRENIYLNGRL-LGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1387 DPfsQYSDEEVWMALELAHLKGFVSaLPDKlnhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLI 1466
Cdd:cd03220 115 SR--KEIDEKIDEIIEFSELGDFID-LPVK----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKC 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958656469 1467 QSTIRTQFED-STVLTIAHRLNTIMDY-TRVIVLDKGEIRECG 1507
Cdd:cd03220 182 QRRLRELLKQgKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
642-887 |
3.33e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 73.34 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 642 MNSITVKNATFTWArdEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------S 708
Cdd:PRK09536 1 MPMIDVSDLSVEFG--DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 709 VAYVPQQAWIQND-SLRENILFGR--------PLQEHCYKAVMEAcallpdleiLPSGDLTEIGEKGV-NLSGGQKQRVS 778
Cdd:PRK09536 79 VASVPQDTSLSFEfDVRQVVEMGRtphrsrfdTWTETDRAAVERA---------MERTGVAQFADRPVtSLSGGERQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 779 LARAVYCNSDIYLLDDPLSAVDAHVGKHIFEKVvgpMGLLKN-KTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQEL 856
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQVRTLELV---RRLVDDgKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADV 226
|
250 260 270
....*....|....*....|....*....|..
gi 1958656469 857 LDRDGAFAEF-VRTYANTeqDLASEDDSVSGL 887
Cdd:PRK09536 227 LTADTLRAAFdARTAVGT--DPATGAPTVTPL 256
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
590-801 |
3.43e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 74.07 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 590 FNILRFPLNILPMVISSIVQASVSLKRLRIF---LSHEELEPDSIERWSIKDGGGmnsITVKNATFTWARDEPpTLNGIT 666
Cdd:COG4178 308 FGQVQGALSWFVDNYQSLAEWRATVDRLAGFeeaLEAADALPEAASRIETSEDGA---LALEDLTLRTPDGRP-LLEDLS 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 667 FAIPDGALVAVVGQVGCGKSSLLSAlLAEM-DKVEGHVTL--KGSVAYVPQQAWIQNDSLRENILFgrPLQEHCY----- 738
Cdd:COG4178 384 LSLKPGERLLITGPSGSGKSTLLRA-IAGLwPYGSGRIARpaGARVLFLPQRPYLPLGTLREALLY--PATAEAFsdael 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958656469 739 KAVMEACAlLPDLeilpSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDA 801
Cdd:COG4178 461 REALEAVG-LGHL----AERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1307-1512 |
4.27e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.55 E-value: 4.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG-LHNLRFKITIIPQDPVLFSG-SLRM 1384
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLVPQEPLLFPNlSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1385 NLD---PFSQYSDEEvwmalelahLKGFVSALPDKLNHECAEGgeNLSVGQRQLVCLARALLRKTKILVLDEATAAVD-L 1460
Cdd:PRK15439 106 NILfglPKRQASMQK---------MKQLLAALGCQLDLDSSAG--SLEVADRQIVEILRGLMRDSRILILDEPTASLTpA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958656469 1461 ETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSEL 1512
Cdd:PRK15439 175 ETERLFSRIRELLAQGVGIVFISHKLPEIRQLAdRISVMRDGTIALSGKTADL 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1307-1513 |
4.76e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 70.93 E-value: 4.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSL--TLGLFRINESAE---GEIIIDG---INIAKIGLHNLRFKITIIPQDPVLF 1378
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLlrCINLLEQPEAGTirvGDITIDTarsLSQQKGLIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1379 ----------SGSLRMNLDPfsqySDEEVWMALEL---AHLKGFVSALPDKlnhecaeggenLSVGQRQLVCLARALLRK 1445
Cdd:PRK11264 98 phrtvleniiEGPVIVKGEP----KEEATARARELlakVGLAGKETSYPRR-----------LSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1446 TKILVLDEATAAVDLETDDLIQSTIRTQFEDS-TVLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSELL 1513
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDVAdRAIFMDQGRIVEQGPAKALF 232
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
657-855 |
5.13e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.13 E-value: 5.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 657 DEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS-------------VAYVPQQAWIQNDSL 723
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrqqVSYCAQTPTLFGDTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 724 RENILFgrPLQehCYKAVMEACALLPDLEI--LPSgdltEIGEKGVN-LSGGQKQRVSLARAVYCNSDIYLLDDPLSAVD 800
Cdd:PRK10247 98 YDNLIF--PWQ--IRNQQPDPAIFLDDLERfaLPD----TILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 801 AHvGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQVDVIIVMSggkiSEMGSYQE 855
Cdd:PRK10247 170 ES-NKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQ----PHAGEMQE 219
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
653-801 |
5.77e-13 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 69.31 E-value: 5.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 653 TWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG------------SVAYVPQQAWIQN 720
Cdd:TIGR01189 7 ACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplaeqrdepheNILYLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 721 D-SLRENILFGRPLQEHCYKAVMEACAL--LPDLEILPSGdlteigekgvNLSGGQKQRVSLARAVYCNSDIYLLDDPLS 797
Cdd:TIGR01189 87 ElSALENLHFWAAIHGGAQRTIEDALAAvgLTGFEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
....
gi 1958656469 798 AVDA 801
Cdd:TIGR01189 157 ALDK 160
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1289-1512 |
6.72e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 72.03 E-value: 6.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1289 GRVEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLtL----GLFRINEsaeGEIIIDGINIAkiGLHNL 1364
Cdd:COG3839 2 ASLELENVSKSYGGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTL-LrmiaGLEDPTS---GEILIGGRDVT--DLPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1365 RFKITIIPQDPVLF----------SGsLRMnldpfSQYSDEEV-----WMA--LELAHLkgfvsalpdkLNHECAEggen 1427
Cdd:COG3839 74 DRNIAMVFQSYALYphmtvyeniaFP-LKL-----RKVPKAEIdrrvrEAAelLGLEDL----------LDRKPKQ---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1428 LSVGQRQLVCLARALLRKTKILVLDEATAAVD----LETddliqstiRTQfedstvltIA---HRLNTIMDY-------- 1492
Cdd:COG3839 134 LSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEM--------RAE--------IKrlhRRLGTTTIYvthdqvea 197
|
250 260
....*....|....*....|....
gi 1958656469 1493 ----TRVIVLDKGEIRECGAPSEL 1512
Cdd:COG3839 198 mtlaDRIAVMNDGRIQQVGTPEEL 221
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
662-856 |
6.75e-13 |
|
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: 69.80 E-value: 6.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVTLKGSVAYVP---QQAWIQNDSL------RENIlfgr 731
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLN-LISGLAQpTSGGVILEGKQITEPgpdRMVVFQNYSLlpwltvRENI---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 732 plqehcYKAVMEACALLPDLE-------ILPSGDLTEIGEKGVN-LSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHV 803
Cdd:TIGR01184 76 ------ALAVDRVLPDLSKSErraiveeHIALVGLTEAADKRPGqLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 804 GKHIFEKVvgpMGLLKNK--TRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQEL 856
Cdd:TIGR01184 150 RGNLQEEL---MQIWEEHrvTVLMVTHDVdEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
644-851 |
7.68e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 70.04 E-value: 7.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 644 SITVKNATFTWARDEppTLNGITFAIPDGALVAVVGQVGCGKSSLLSAL-LAEMDK-----VEGH-------------VT 704
Cdd:COG4161 2 SIQLKNINCFYGSHQ--ALFDINLECPSGETLVLLGPSGAGKSSLLRVLnLLETPDsgqlnIAGHqfdfsqkpsekaiRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 705 LKGSVAYVPQQ--AWiQNDSLRENIL------FGRPLQEhcykAVMEACALLPDLEilpsgdLTEIGEK-GVNLSGGQKQ 775
Cdd:COG4161 80 LRQKVGMVFQQynLW-PHLTVMENLIeapckvLGLSKEQ----AREKAMKLLARLR------LTDKADRfPLHLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656469 776 RVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIFE--KVVGPMGLlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMG 851
Cdd:COG4161 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQVVEiiRELSQTGI----TQVIVTHEVEFARKVaSQVVYMEKGRIIEQG 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
662-868 |
7.73e-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: 70.37 E-value: 7.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-----------------SVAYVPQQ-AWIQNDSL 723
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrelrrkKISMVFQSfALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 724 RENILF-----GRPLQEHCYKA--VMEACALLPDLEILPSgdlteigekgvNLSGGQKQRVSLARAVYCNSDIYLLDDPL 796
Cdd:cd03294 120 LENVAFglevqGVPRAEREERAaeALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 797 SAVDAHVGKHIFEKVVGPMGLLKnKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLDR--DGAFAEFVR 868
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAELQ-KTIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEEILTNpaNDYVREFFR 262
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1310-1515 |
7.84e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 69.61 E-value: 7.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1310 HINVTIEGGEKVGIVGRTGAGKSSLtLGL---FRINESaeGEIIIDGINiakiglHNL----RFKITIIPQDPVLFSG-S 1381
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTL-LNLiagFLTPAS--GSLTLNGQD------HTTtppsRRPVSMLFQENNLFSHlT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1382 LRMN----LDPFSQYSDEEVWMALELAHLKGfVSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAA 1457
Cdd:PRK10771 88 VAQNiglgLNPGLKLNAAQREKLHAIARQMG-IEDLLARLPGQ-------LSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958656469 1458 VD----LETDDLIQSTIRTQfeDSTVLTIAHRLNTIMDY-TRVIVLDKGEIRECGAPSELLQQ 1515
Cdd:PRK10771 160 LDpalrQEMLTLVSQVCQER--QLTLLMVSHSLEDAARIaPRSLVVADGRIAWDGPTDELLSG 220
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1311-1521 |
9.57e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 71.79 E-value: 9.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1311 INVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHnlRFKITIIPQDPVLF---------SGS 1381
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPINMMFQSYALFphmtveqniAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1382 LRMNLDPFSQYSDEEVWMaLELAHLKGFVSALPdklnHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1461
Cdd:PRK11607 116 LKQDKLPKAEIASRVNEM-LGLVHMQEFAKRKP----HQ-------LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958656469 1462 TDDLIQSTIRTQFE--DSTVLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSELLQQRGVFYS 1521
Cdd:PRK11607 184 LRDRMQLEVVDILErvGVTCVMVTHDQEEAMTMAgRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
640-858 |
1.03e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 71.40 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 640 GGMNSITVKNATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGsvAYVPQQAWI- 718
Cdd:PRK13536 35 GSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG--VPVPARARLa 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 719 --------QNDSL------RENIL-FGRplqeHCYKAVMEACALLPDLeiLPSGDLTEIGEKGV-NLSGGQKQRVSLARA 782
Cdd:PRK13536 113 rarigvvpQFDNLdleftvRENLLvFGR----YFGMSTREIEAVIPSL--LEFARLESKADARVsDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 783 VYCNSDIYLLDDPLSAVDAHVGKHIFEKVVGPmgLLKNKTRILVTHGISYLPQV-DVIIVMSGG-KISEmGSYQELLD 858
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSL--LARGKTILLTTHFMEEAERLcDRLCVLEAGrKIAE-GRPHALID 261
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1307-1518 |
1.05e-12 |
|
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: 69.24 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNL-RFKITIIPQDPVLFSG-SLRM 1384
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1385 NLD--PFSQYSDEEVWMALELAH-----LKgfvsalpDKLNHEcaeGGeNLSVGQRQLVCLARALLRKTKILVLDEATAA 1457
Cdd:COG0410 98 NLLlgAYARRDRAEVRADLERVYelfprLK-------ERRRQR---AG-TLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656469 1458 -----VDlETDDLIQsTIRTqfEDSTVLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSELLQQRGV 1518
Cdd:COG0410 167 lapliVE-EIFEIIR-RLNR--EGVTILLVEQNARFALEIAdRAYVLERGRIVLEGTAAELLADPEV 229
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1308-1459 |
1.05e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 68.66 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1308 LKHINVTIEGGEKVGIVGRTGAGKSSL---TLGLFRINESAEGEIIIDGINIAKIGLHnlRFKITIIPQDPVLFS----- 1379
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLlaaIAGTLSPAFSASGEVLLNGRRLTALPAE--QRRIGILFQDDLLFPhlsvg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1380 GSLRMNLDPFSQYSD--EEVWMALELAHLKGFVSALPDklnhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAA 1457
Cdd:COG4136 95 ENLAFALPPTIGRAQrrARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
..
gi 1958656469 1458 VD 1459
Cdd:COG4136 164 LD 165
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
642-858 |
1.10e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 69.87 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 642 MNSITVKNATFTWARDEppTLNGITFAIPDGALVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVTLKGSVAYVPQQA 716
Cdd:PRK14267 2 KFAIETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 717 WIQndsLRENI--LFGRPlQEHCYKAVMEACALLPDLEIL--PSGDLTEIGE------------------KGVNLSGGQK 774
Cdd:PRK14267 80 PIE---VRREVgmVFQYP-NPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEwalkkaalwdevkdrlndYPSNLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 775 QRVSLARAVYCNSDIYLLDDPLSAVDAhVGKHIFEKVVgpMGLLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSY 853
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDP-VGTAKIEELL--FELKKEYTIVLVTHSPAQAARVsDYVAFLYLGKLIEVGPT 232
|
....*
gi 1958656469 854 QELLD 858
Cdd:PRK14267 233 RKVFE 237
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1308-1486 |
1.25e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 69.42 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1308 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGINI--AKIGLHNLRFKITIIPQDPVLFSG 1380
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1381 S--------LRMNLDPFSQYSDEEVWMALELAHLKGFVSalpDKLnHECAEGgenLSVGQRQLVCLARALLRKTKILVLD 1452
Cdd:PRK14239 101 SiyenvvygLRLKGIKDKQVLDEAVEKSLKGASIWDEVK---DRL-HDSALG---LSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190
....*....|....*....|....*....|....
gi 1958656469 1453 EATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRL 1486
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1298-1493 |
1.47e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 69.68 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1298 LRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINEsAEGEIIIDG--------INIAKIGLHNLRFKIT 1369
Cdd:PRK14258 13 LSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrveffnqnIYERRVNLNRLRRQVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1370 IIPQDPVLFsgslrmnldPFSQYSDEEVWMALELAH----LKGFVSA------LPDKLNHECAEGGENLSVGQRQLVCLA 1439
Cdd:PRK14258 92 MVHPKPNLF---------PMSVYDNVAYGVKIVGWRpkleIDDIVESalkdadLWDEIKHKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656469 1440 RALLRKTKILVLDEATAAVD----LETDDLIQS-TIRTQFEDSTVLTIAHRLNTIMDYT 1493
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDpiasMKVESLIQSlRLRSELTMVIVSHNLHQVSRLSDFT 221
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
662-886 |
1.52e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 69.43 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVTLKGSVAYVPQqawIQNDSLRENI--LFGRPlq 734
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYAPD---VDPVEVRRRIgmVFQKP-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 735 EHCYKAVMEACALLPDLEILpSGDLTEIGEK------------------GVNLSGGQKQRVSLARAVYCNSDIYLLDDPL 796
Cdd:PRK14243 101 NPFPKSIYDNIAYGARINGY-KGDMDELVERslrqaalwdevkdklkqsGLSLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 797 SAVDAHVGKHIFEKvvgpMGLLKNK-TRILVTHGISYLPQVDVIIVMSGGKISEMGSyqelldRDGAFAEFVRTYA--NT 873
Cdd:PRK14243 180 SALDPISTLRIEEL----MHELKEQyTIIIVTHNMQQAARVSDMTAFFNVELTEGGG------RYGYLVEFDRTEKifNS 249
|
250
....*....|...
gi 1958656469 874 EQDLASEdDSVSG 886
Cdd:PRK14243 250 PQQQATR-DYVSG 261
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
645-849 |
1.73e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 68.54 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDePPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG---------SVAY---- 711
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlkrrEIPYlrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 712 ---VPQQAW-IQNDSLRENILF-----GRPLQEhCYKAVMEACallpdleilpsgDLTEIGEKG----VNLSGGQKQRVS 778
Cdd:COG2884 81 igvVFQDFRlLPDRTVYENVALplrvtGKSRKE-IRRRVREVL------------DLVGLSDKAkalpHELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656469 779 LARAVYCNSDIYLLDDPLSAVDAHVGKHIfekvvgpMGLLK--NK---TRILVTHGISYLPQVDV-IIVMSGGKISE 849
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEI-------MELLEeiNRrgtTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
644-855 |
1.88e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 69.69 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 644 SITVKNATFTWARDEP---PTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG------------- 707
Cdd:PRK13637 2 SIKIENLTHIYMEGTPfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 708 --SVAYVPQQAWIQ--NDSLRENILFG-RPL---QEHCYKAVMEACALLpdleilpsG-DLTEIGEKG-VNLSGGQKQRV 777
Cdd:PRK13637 82 rkKVGLVFQYPEYQlfEETIEKDIAFGpINLglsEEEIENRVKRAMNIV--------GlDYEDYKDKSpFELSGGQKRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656469 778 SLARAVYCNSDIYLLDDPLSAVDAHVGKHIFEKvVGPMGLLKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQE 855
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNK-IKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1298-1507 |
2.03e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 71.66 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1298 LRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESaEGEIIIDGINiakigLHNL--------RFKIT 1369
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDGQP-----LHNLnrrqllpvRHRIQ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1370 IIPQDPvlfSGSL--RMNLDPF-------------SQYSDEEVWMALELAHLKgfvsalPDKLNHECAEggenLSVGQRQ 1434
Cdd:PRK15134 366 VVFQDP---NSSLnpRLNVLQIieeglrvhqptlsAAQREQQVIAVMEEVGLD------PETRHRYPAE----FSGGQRQ 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 1435 LVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRT--QFEDSTVLTIAHRLNTIMDYT-RVIVLDKGEIRECG 1507
Cdd:PRK15134 433 RIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSlqQKHQLAYLFISHDLHVVRALChQVIVLRQGEVVEQG 508
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
645-857 |
2.09e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 69.25 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWArDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQawIQNDSLR 724
Cdd:PRK13644 2 IRLENVSYSYP-DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSK--LQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 725 ENILFGRPLQEHCYKAVMEACAL------LPDLEILPSGD--LTEIG-EK-----GVNLSGGQKQRVSLARAVYCNSDIY 790
Cdd:PRK13644 79 VGIVFQNPETQFVGRTVEEDLAFgpenlcLPPIEIRKRVDraLAEIGlEKyrhrsPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656469 791 LLDDPLSAVDAHVGKHIFEKVVGPMGllKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELL 857
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHE--KGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
645-859 |
2.26e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 69.65 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDEP---PTLNGITFAIPDGALVAVVGQVGCGKSSLLS------------------ALLAEMDKVEGHV 703
Cdd:PRK13645 7 IILDNVSYTYAKKTPfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqtivgdyAIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 704 TLKGSVAYV---PQQAWIQnDSLRENILFGrPL-----QEHCYKAVMEacalLPDLEILPSgdlTEIGEKGVNLSGGQKQ 775
Cdd:PRK13645 87 RLRKEIGLVfqfPEYQLFQ-ETIEKDIAFG-PVnlgenKQEAYKKVPE----LLKLVQLPE---DYVKRSPFELSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 776 RVSLARAVYCNSDIYLLDDPLSAVDAHvGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMG--- 851
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPK-GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIaDEVIVMHEGKVISIGspf 236
|
250
....*....|.
gi 1958656469 852 ---SYQELLDR 859
Cdd:PRK13645 237 eifSNQELLTK 247
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1257-1459 |
2.28e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.54 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1257 VAVERLKEYSETEKEASWQIqeTAPPSTWPhsgRVEFRDYCLRYrEDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTL 1336
Cdd:PRK10522 294 VAFNKLNKLALAPYKAEFPR--PQAFPDWQ---TLELRNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAM 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1337 GLFRINESAEGEIIIDGINIAKIGLHNLRFKITIIPQDPVLFSgslRMnLDPFSQYSDEEV---WmaleLAHLKgfvsaL 1413
Cdd:PRK10522 368 LLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFD---QL-LGPEGKPANPALvekW----LERLK-----M 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1414 PDKLNHecaEGGE----NLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1459
Cdd:PRK10522 435 AHKLEL---EDGRisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
643-860 |
2.40e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.99 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 643 NSITVKNATFTWaRDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIQNds 722
Cdd:PRK13647 3 NIIEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRS-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 723 lRENILFGRPLQEHCYKAVMEACALLP-DLEILPSGDLTEIGE--KGVN-----------LSGGQKQRVSLARAVYCNSD 788
Cdd:PRK13647 80 -KVGLVFQDPDDQVFSSTVWDDVAFGPvNMGLDKDEVERRVEEalKAVRmwdfrdkppyhLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 789 IYLLDDPLSAVDAHVGKHIFEKVVGpmglLKN--KTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELLDRD 860
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDR----LHNqgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1306-1507 |
2.66e-12 |
|
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: 67.78 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1306 LVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRfKITIIPQDPVLFSG-SLRM 1384
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARR-RLGFVSDSTGLYDRlTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1385 NLDPFSQYsdeevwMALELAHLKGFVSALPDKL--NHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 1462
Cdd:cd03266 98 NLEYFAGL------YGLKGDELTARLEELADRLgmEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958656469 1463 DDLIQSTIRTQFED-STVLTIAHRLNTIMDYT-RVIVLDKGEIRECG 1507
Cdd:cd03266 172 TRALREFIRQLRALgKCILFSTHIMQEVERLCdRVVVLHRGRVVYEG 218
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
645-828 |
2.96e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 68.26 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDEppTLNGITFAIPDGALVAVVGQVGCGKSSLLSALlAEMDKVEGHVTLKGSVAY------------- 711
Cdd:PRK14239 6 LQVSDLSVYYNKKK--ALNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGSIVYnghniysprtdtv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 712 --------VPQQAWIQNDSLRENILFGRPLQEHCYKAVMEAcALLPDLEILPSGDLTE--IGEKGVNLSGGQKQRVSLAR 781
Cdd:PRK14239 83 dlrkeigmVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDE-AVEKSLKGASIWDEVKdrLHDSALGLSGGQQQRVCIAR 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958656469 782 AVYCNSDIYLLDDPLSAVDAHVGKHIFEKVVGpmglLKNK-TRILVTH 828
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLLG----LKDDyTMLLVTR 205
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
655-802 |
3.40e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.21 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 655 ARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLL---SALLAemdKVEGHVTLKG----------SVAYV-PQQAWIQN 720
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLrliAGLLP---PAAGTIKLDGgdiddpdvaeACHYLgHRNAMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 721 DSLRENILFGRPLQ-EHCYKAVMEACAL-LPDLEILPSGdlteigekgvNLSGGQKQRVSLARAVYCNSDIYLLDDPLSA 798
Cdd:PRK13539 88 LTVAENLEFWAAFLgGEELDIAAALEAVgLAPLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
....
gi 1958656469 799 VDAH 802
Cdd:PRK13539 158 LDAA 161
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1307-1518 |
3.49e-12 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 67.95 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSL---TLGLFRINEsaeGEIIIDGINIAKIGLHN-LRFKITIIPQDPVLFSG-S 1381
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTfymIVGLVKPDS---GKILLDGQDITKLPMHKrARLGIGYLPQEASIFRKlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1382 LRMNLDPF--SQYSDEEVWMA-----LELAHLkgfvSALPDKLnhecaegGENLSVGQRQLVCLARALLRKTKILVLDEA 1454
Cdd:cd03218 92 VEENILAVleIRGLSKKEREEkleelLEEFHI----THLRKSK-------ASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656469 1455 TAAVDLETDDLIQSTIRtQFEDST--VLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSELLQQRGV 1518
Cdd:cd03218 161 FAGVDPIAVQDIQKIIK-ILKDRGigVLITDHNVRETLSITdRAYIIYEGKVLAEGTPEEIAANELV 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
653-801 |
3.50e-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: 67.13 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 653 TWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG------------SVAYVPQQAWIQN 720
Cdd:cd03231 7 TCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgpldfqrdsiarGLLYLGHAPGIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 721 D-SLRENILFGRPLqeHCYKAVMEAcallpdleiLPSGDLTEIGEKGVN-LSGGQKQRVSLARAVYCNSDIYLLDDPLSA 798
Cdd:cd03231 87 TlSVLENLRFWHAD--HSDEQVEEA---------LARVGLNGFEDRPVAqLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
...
gi 1958656469 799 VDA 801
Cdd:cd03231 156 LDK 158
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1308-1512 |
3.69e-12 |
|
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: 67.75 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1308 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAK-------IGL---HNLRFK-ITIIpqDPV 1376
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDvpvqernVGFvfqHYALFRhMTVF--DNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1377 LFSgsLRM---NLDPFSQYSDEEVWMALELAHLKGFVSALPdklnhecaeggENLSVGQRQLVCLARALLRKTKILVLDE 1453
Cdd:cd03296 96 AFG--LRVkprSERPPEAEIRAKVHELLKLVQLDWLADRYP-----------AQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958656469 1454 ATAAVDLETDDLIQSTIRtQFEDSTVLT---IAHRLNTIMDYT-RVIVLDKGEIRECGAPSEL 1512
Cdd:cd03296 163 PFGALDAKVRKELRRWLR-RLHDELHVTtvfVTHDQEEALEVAdRVVVMNKGRIEQVGTPDEV 224
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1307-1513 |
4.09e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.47 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL 1386
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1387 DPFSQYSDEEVWMALELAHLKGFVSAL-PDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD-- 1463
Cdd:PRK10253 102 VARGRYPHQPLFTRWRKEDEEAVTKAMqATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQid 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958656469 1464 --DLIQSTIRTQfeDSTVLTIAHRLNTIMDY-TRVIVLDKGEIRECGAPSELL 1513
Cdd:PRK10253 182 llELLSELNREK--GYTLAAVLHDLNQACRYaSHLIALREGKIVAQGAPKEIV 232
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1307-1518 |
4.25e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 67.61 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLH-NLRFKITIIPQDPVLFS------ 1379
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRARRGIGYLPQEASIFRrlsvyd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1380 ---GSLRMNLDPFSQYSDEEVWMALELAHlkgfVSALPDKLnhecaegGENLSVGQRQLVCLARALLRKTKILVLDEATA 1456
Cdd:PRK10895 98 nlmAVLQIRDDLSAEQREDRANELMEEFH----IEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656469 1457 AVD----LETDDLIQstirtQFEDS--TVLTIAHRLNTIMDY-TRVIVLDKGEIRECGAPSELLQQRGV 1518
Cdd:PRK10895 167 GVDpisvIDIKRIIE-----HLRDSglGVLITDHNVRETLAVcERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
642-859 |
4.90e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 68.22 E-value: 4.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 642 MNSITVKNATFTWARD-EPPTLNGITFAIPDGALVAVVGQVGCGKSS---LLSALL-AEMDK--VEGHVTLKGSVAYVPQ 714
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLLeAESGQiiIDGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 715 QAWI--QND-------SLRENILFGR-----PLQEhCYKAVMEAcallpdLEILPSGDLTEigEKGVNLSGGQKQRVSLA 780
Cdd:PRK13650 82 KIGMvfQNPdnqfvgaTVEDDVAFGLenkgiPHEE-MKERVNEA------LELVGMQDFKE--REPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656469 781 RAVYCNSDIYLLDDPLSAVDAHvGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDR 859
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPE-GRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1301-1513 |
5.15e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.89 E-value: 5.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1301 REDLDLVlKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGiniakiglHNLRF--------KITIIP 1372
Cdd:PRK15112 23 RQTVEAV-KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD--------HPLHFgdysyrsqRIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1373 QDPV-----------LFSGSLRMNLDPFSQYSDEEVWMALELahlkgfVSALPDKLNHEcaegGENLSVGQRQLVCLARA 1441
Cdd:PRK15112 94 QDPStslnprqrisqILDFPLRLNTDLEPEQREKQIIETLRQ------VGLLPDHASYY----PHMLAPGQKQRLGLARA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656469 1442 LLRKTKILVLDEATAAVDLET-DDLIQSTIRTQFED--STVLTIAH--RLNTIMDytRVIVLDKGEIRECGAPSELL 1513
Cdd:PRK15112 164 LILRPKVIIADEALASLDMSMrSQLINLMLELQEKQgiSYIYVTQHlgMMKHISD--QVLVMHQGEVVERGSTADVL 238
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
1019-1252 |
5.78e-12 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 68.28 E-value: 5.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1019 ALGILQGVAVFGYSMAVSIGGIFASRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVD---SMIPqvikMFMGS 1095
Cdd:cd18543 47 ALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQrflAFGP----FLLGN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1096 LFSVIGAVIIILLATP----IAAVIIPPLGLV-YFFVQRFYVASSRQLKRLESVSrspvySHFNETLLGVSVIRAF---- 1166
Cdd:cd18543 123 LLTLVVGLVVMLVLSPplalVALASLPPLVLVaRRFRRRYFPASRRAQDQAGDLA-----TVVEESVTGIRVVKAFgrer 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1167 EEQERFIRQSD-LKVDENQKAyypSIVANRWLAVR-LECVGNCIVLFAALFAVIsRHSLSAG-LVGLSvSYSLQitayLN 1243
Cdd:cd18543 198 RELDRFEAAARrLRATRLRAA---RLRARFWPLLEaLPELGLAAVLALGGWLVA-NGSLTLGtLVAFS-AYLTM----LV 268
|
....*....
gi 1958656469 1244 WLVRMSSEM 1252
Cdd:cd18543 269 WPVRMLGWL 277
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
662-847 |
6.40e-12 |
|
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: 65.14 E-value: 6.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGsvayvpqqawiqndslrenilfgrplQEHCYKAV 741
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--------------------------KEVSFASP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 742 MEACALlpdleilpsgdlteigekGVN----LSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIFEKvvgpMGL 817
Cdd:cd03216 70 RDARRA------------------GIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKV----IRR 127
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958656469 818 LKN--KTRILVTHgisYLPQV----DVIIVMSGGKI 847
Cdd:cd03216 128 LRAqgVAVIFISH---RLDEVfeiaDRVTVLRDGRV 160
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1307-1503 |
7.72e-12 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 66.04 E-value: 7.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSL--TLGLFRINESAEGEIIIDGINIakiGLHNLRFKITIIPQDPVLFSgslrm 1384
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLlnALAGRRTGLGVSGEVLINGRPL---DKRSFRKIIGYVPQDDILHP----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1385 NLDPFsqysdEEVWMAlelAHLKGfvsalpdklnhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDD 1464
Cdd:cd03213 96 TLTVR-----ETLMFA---AKLRG-------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958656469 1465 LIQSTIRtQFEDS--TVLTIAHRLNTIMDYT--RVIVLDKGEI 1503
Cdd:cd03213 149 QVMSLLR-RLADTgrTIICSIHQPSSEIFELfdKLLLLSQGRV 190
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1308-1515 |
7.85e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.88 E-value: 7.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1308 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINI-AKIG---LHNLRFKITIIPQDP--VLFSGS 1381
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKdkyIRPVRKRIGMVFQFPesQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1382 L-----------RMNLDPFSQYSDEevwMALELAHLKGFVSALPDKlnhecaeggenLSVGQRQLVCLARALLRKTKILV 1450
Cdd:PRK13646 103 VereiifgpknfKMNLDEVKNYAHR---LLMDLGFSRDVMSQSPFQ-----------MSGGQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 1451 LDEATAAVDLETDDLIQSTIRT-QFEDS-TVLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSELLQQ 1515
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKSlQTDENkTIILVSHDMNEVARYAdEVIVMKEGSIVSQTSPKELFKD 236
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
659-847 |
8.47e-12 |
|
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: 65.53 E-value: 8.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 659 PPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS--------------VAYVPQqawiqnDSLR 724
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairagIAYVPE------DRKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 725 ENILFGRPLQEHcykavmeacALLPDLeilpsgdlteigekgvnLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDahVG 804
Cdd:cd03215 87 EGLVLDLSVAEN---------IALSSL-----------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVD--VG 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958656469 805 --KHIFEKVVgpmgLL--KNKTRILVThgiSYLPQV----DVIIVMSGGKI 847
Cdd:cd03215 139 akAEIYRLIR----ELadAGKAVLLIS---SELDELlglcDRILVMYEGRI 182
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
645-856 |
8.48e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 67.41 E-value: 8.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWArDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG--------SVAYVPQQA 716
Cdd:PRK13639 2 LETRDLKYSYP-DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkkSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 717 WI--QN--DSL-----RENILFGrPL-----QEHCYKAVMEAcallpdleilpsgdLTEIGEKGV------NLSGGQKQR 776
Cdd:PRK13639 81 GIvfQNpdDQLfaptvEEDVAFG-PLnlglsKEEVEKRVKEA--------------LKAVGMEGFenkpphHLSGGQKKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 777 VSLARAVYCNSDIYLLDDPLSAVDAHVGKHIfekvvgpMGLLK--NK---TRILVTHGISYLP-QVDVIIVMSGGKISEM 850
Cdd:PRK13639 146 VAIAGILAMKPEIIVLDEPTSGLDPMGASQI-------MKLLYdlNKegiTIIISTHDVDLVPvYADKVYVMSDGKIIKE 218
|
....*.
gi 1958656469 851 GSYQEL 856
Cdd:PRK13639 219 GTPKEV 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
660-795 |
8.58e-12 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 66.30 E-value: 8.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 660 PTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS--------------VAYVPQ-QAWIQNDSLR 724
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEgRRIFPELTVE 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958656469 725 ENILFG-RPLQEHCYKAVME-ACALLPDL-EILpsgdlteiGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDP 795
Cdd:cd03224 94 ENLLLGaYARRRAKRKARLErVYELFPRLkERR--------KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
642-857 |
9.19e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.43 E-value: 9.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 642 MNSI-TVKNATFTWARD-EPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSvAYVPQQAWiq 719
Cdd:PRK13642 1 MNKIlEVENLVFKYEKEsDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVW-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 720 ndSLRENI--LFGRPLQEHCYKAVMEACAL------LPDLEILPSGDLTEIG--------EKGVNLSGGQKQRVSLARAV 783
Cdd:PRK13642 78 --NLRRKIgmVFQNPDNQFVGATVEDDVAFgmenqgIPREEMIKRVDEALLAvnmldfktREPARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958656469 784 YCNSDIYLLDDPLSAVDAhVGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELL 857
Cdd:PRK13642 156 ALRPEIIILDESTSMLDP-TGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
662-828 |
9.86e-12 |
|
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: 69.78 E-value: 9.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSaLLAEMDKVEGHVTLK---GSVAYVPQQAWIQNDSLRENILFGRPLQEHCY 738
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGGRLTKpakGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKR 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 739 KAVMEAcallpDLE-ILPSGDLTEIGEKGVN----------LSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHI 807
Cdd:TIGR00954 547 RGLSDK-----DLEqILDNVQLTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYM 621
|
170 180
....*....|....*....|...
gi 1958656469 808 FEkvvgpmgLLKNK--TRILVTH 828
Cdd:TIGR00954 622 YR-------LCREFgiTLFSVSH 637
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1292-1515 |
1.11e-11 |
|
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: 69.33 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1292 EFRDYCLRYREDLDL--VLKHINVTIEGGEKVGIVGRTGAGKS--SL-TLGLF-RINESAEGEIIIDGINIAKIGLHNLR 1365
Cdd:COG4172 8 SVEDLSVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSvtALsILRLLpDPAAHPSGSILFDGQDLLGLSERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1366 ----FKITIIPQDPvlfsgslrMN-LDPF----SQ----------YSDEEVW-MALELAHLKGfvsaLPD---KLN---H 1419
Cdd:COG4172 88 rirgNRIAMIFQEP--------MTsLNPLhtigKQiaevlrlhrgLSGAAARaRALELLERVG----IPDperRLDaypH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1420 EcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLetddliqsTIRTQF----------EDSTVLTIAHRLNTI 1489
Cdd:COG4172 156 Q-------LSGGQRQRVMIAMALANEPDLLIADEPTTALDV--------TVQAQIldllkdlqreLGMALLLITHDLGVV 220
|
250 260
....*....|....*....|....*..
gi 1958656469 1490 MDYT-RVIVLDKGEIRECGAPSELLQQ 1515
Cdd:COG4172 221 RRFAdRVAVMRQGEIVEQGPTAELFAA 247
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1311-1515 |
1.13e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.45 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1311 INVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG----LHNLRFKITIIPQDP--VLFSGSLRM 1384
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKPVRKKVGVVFQFPesQLFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1385 NL----DPFSQYSDEEVWMALELAHLKGFVSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVD- 1459
Cdd:PRK13643 105 DVafgpQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFE-------LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDp 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1460 ---LETDDLIQSTIRTqfeDSTVLTIAHRLNTIMDYTR-VIVLDKGEIRECGAPSELLQQ 1515
Cdd:PRK13643 178 karIEMMQLFESIHQS---GQTVVLVTHLMDDVADYADyVYLLEKGHIISCGTPSDVFQE 234
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
645-851 |
1.80e-11 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 65.29 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDEppTLNGITFAIPDGaLVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS------------VAYV 712
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 713 PQQ-AWIQNDSLRE-----NILFGRPlQEHCYKAVMEACALLpdleilpsgDLTEIGEKGVN-LSGGQKQRVSLARAVYC 785
Cdd:cd03264 78 PQEfGVYPNFTVREfldyiAWLKGIP-SKEVKARVDEVLELV---------NLGDRAKKKIGsLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958656469 786 NSDIYLLDDPLSAVDAhVGKHIFEKVVGPMGllKNKTRILVTHGISylpqvDV------IIVMSGGKISEMG 851
Cdd:cd03264 148 DPSILIVDEPTAGLDP-EERIRFRNLLSELG--EDRIVILSTHIVE-----DVeslcnqVAVLNKGKLVFEG 211
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
644-858 |
1.89e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.42 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 644 SITVKNATFtWARdePPTL---NGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-SVAYVPQQAW-- 717
Cdd:PRK15079 19 DIKDGKQWF-WQP--PKTLkavDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkDLLGMKDDEWra 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 718 ----IQ---NDSL-----RENI--LFGRPLQEHC-----------YKAVMEACALLPDLeilpsgdlteIGEKGVNLSGG 772
Cdd:PRK15079 96 vrsdIQmifQDPLaslnpRMTIgeIIAEPLRTYHpklsrqevkdrVKAMMLKVGLLPNL----------INRYPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 773 QKQRVSLARAVYCNSDIYLLDDPLSAVDAhvgkHIFEKVVgpmGLLKNKTR------ILVTHGISYLPQV-DVIIVMSGG 845
Cdd:PRK15079 166 QCQRIGIARALILEPKLIICDEPVSALDV----SIQAQVV---NLLQQLQRemglslIFIAHDLAVVKHIsDRVLVMYLG 238
|
250
....*....|...
gi 1958656469 846 KISEMGSYQELLD 858
Cdd:PRK15079 239 HAVELGTYDEVYH 251
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1309-1512 |
2.24e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.04 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1309 KHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG---LHNLRFKITIIPQDPvLFSGSLRMN 1385
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddeWRAVRSDIQMIFQDP-LASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1386 L-----DPFSQY----SDEEVWMALELAHLKgfVSALPDKLN---HEcaeggenLSVGQRQLVCLARALLRKTKILVLDE 1453
Cdd:PRK15079 117 IgeiiaEPLRTYhpklSRQEVKDRVKAMMLK--VGLLPNLINrypHE-------FSGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 1454 ATAAVDLEtddlIQSTI-----RTQFEDSTVLT-IAHRLNT---IMDytRVIVLDKGEIRECGAPSEL 1512
Cdd:PRK15079 188 PVSALDVS----IQAQVvnllqQLQREMGLSLIfIAHDLAVvkhISD--RVLVMYLGHAVELGTYDEV 249
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1017-1188 |
2.35e-11 |
|
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: 66.34 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1017 YGALGILQGVAVFGYSMAVSIGGIFASRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSL 1096
Cdd:cd18577 53 FVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1097 FSVIGAVII----------ILLATpiaaviIPPLGLVYFFVQRFYV-ASSRQLKRLESVSrspvySHFNETLLGVSVIRA 1165
Cdd:cd18577 133 STFIAGFIIafiyswkltlVLLAT------LPLIAIVGGIMGKLLSkYTKKEQEAYAKAG-----SIAEEALSSIRTVKA 201
|
170 180
....*....|....*....|...
gi 1958656469 1166 FEEQERFIRQSDLKVDENQKAYY 1188
Cdd:cd18577 202 FGGEEKEIKRYSKALEKARKAGI 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1300-1498 |
2.44e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.12 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1300 YREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITIIPQDPVLFS 1379
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1380 GSLRMNLDPFSQYSDEEVWMALELAHLKGFvsALPDK-LNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAV 1458
Cdd:PRK10247 95 DTVYDNLIFPWQIRNQQPDPAIFLDDLERF--ALPDTiLTKNIAE----LSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958656469 1459 D----LETDDLIQSTIRTQfeDSTVLTIAHRLNTIMDYTRVIVL 1498
Cdd:PRK10247 169 DesnkHNVNEIIHRYVREQ--NIAVLWVTHDKDEINHADKVITL 210
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1307-1507 |
2.77e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 65.42 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSL--TLGLFRINESAEgeiiidgINIAkiglhNLRFKITIIPQDPVLFSgsLRM 1384
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLlrVLNLLEMPRSGT-------LNIA-----GNHFDFSKTPSDKAIRE--LRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1385 NLD-PFSQYS-----------------------DEEVWMALELA---HLKGFVSALPdklnhecaeggENLSVGQRQLVC 1437
Cdd:PRK11124 83 NVGmVFQQYNlwphltvqqnlieapcrvlglskDQALARAEKLLerlRLKPYADRFP-----------LHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958656469 1438 LARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDS-TVLTIAHRLNTIMDY-TRVIVLDKGEIRECG 1507
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVEVARKTaSRVVYMENGHIVEQG 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1307-1515 |
2.86e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 66.71 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLtL----GLfrinESA-EGEIIIDGiNIAKIGLHNLRFKITIIPQDPVLFS-- 1379
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTL-LriiaGL----ETPdSGRIVLNG-RDLFTNLPPRERRVGFVFQHYALFPhm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1380 --------GsLRMnLDPFSQYSDEEV--WmaLELAHLKGFVSALPDklnhecaeggeNLSVGQRQLVCLARALLRKTKIL 1449
Cdd:COG1118 91 tvaeniafG-LRV-RPPSKAEIRARVeeL--LELVQLEGLADRYPS-----------QLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1450 VLDEATAAVD------LET------DDLIQSTIrtqF-----EDstVLTIAhrlntimDytRVIVLDKGEIRECGAPSEL 1512
Cdd:COG1118 156 LLDEPFGALDakvrkeLRRwlrrlhDELGGTTV---FvthdqEE--ALELA-------D--RVVVMNQGRIEQVGTPDEV 221
|
...
gi 1958656469 1513 LQQ 1515
Cdd:COG1118 222 YDR 224
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
1016-1261 |
2.93e-11 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 65.95 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1016 VYGALGILQGVAVFGYSMAVSIGG---IFASRRlhlDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMF 1092
Cdd:cd18545 45 LFLALNLVNWVASRLRIYLMAKVGqriLYDLRQ---DLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1093 MGSLFSVIGAVIIIL-----LATpIAAVIIPPLGLVYFFVQRFyvasSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFE 1167
Cdd:cd18545 122 IPDLLTLVGIVIIMFslnvrLAL-VTLAVLPLLVLVVFLLRRR----ARKAWQRVRKKISNLNAYLHESISGIRVIQSFA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1168 EQERFIRQSDLKVDENQKAYYPSIVANR--WLAVRL-ECVGNCIVLFAALFAVISrHSLSAGLVGLSVSYSLQITAYLNW 1244
Cdd:cd18545 197 REDENEEIFDELNRENRKANMRAVRLNAlfWPLVELiSALGTALVYWYGGKLVLG-GAITVGVLVAFIGYVGRFWQPIRN 275
|
250
....*....|....*..
gi 1958656469 1245 LVRMSSEMETNIVAVER 1261
Cdd:cd18545 276 LSNFYNQLQSAMASAER 292
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
662-858 |
3.20e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.15 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSAL---LAEMDKVEGHVTLKGSVAYVPQQ----AWIQNDSL-------RENI 727
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrSPKGVKGSGSVLLNGMPIDAKEMraisAYVQQDDLfiptltvREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 728 LFGRPL--QEHCYKAV-MEAC-ALLPDLEILPSGDlTEIGEKGV--NLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDA 801
Cdd:TIGR00955 121 MFQAHLrmPRRVTKKEkRERVdEVLQALGLRKCAN-TRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958656469 802 HVGKHifekVVGPMGLL--KNKTRILVTHGISY--LPQVDVIIVMSGGKISEMGSYQELLD 858
Cdd:TIGR00955 200 FMAYS----VVQVLKGLaqKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
1019-1261 |
3.69e-11 |
|
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: 65.64 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1019 ALGILQGVAVFGYSMAvsigGIFASRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFS 1098
Cdd:cd18572 48 LSGLFSGLRGGCFSYA----GTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1099 VIGAVIIILLATP----IAAVIIPPLGLVYFFVQRFYvassRQLKRLESVSRSPVYSHFNETLLGVSVIRAF--EEQE-- 1170
Cdd:cd18572 124 LVGGLAFMFSLSWrltlLAFITVPVIALITKVYGRYY----RKLSKEIQDALAEANQVAEEALSNIRTVRSFatEEREar 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1171 RFIRQSDLKVDENQK---AYypsiVANRWLAVRLECVGNCIVLFAALFAVISrHSLSAGLVGLSVSYSLQITAYLNWLVR 1247
Cdd:cd18572 200 RYERALDKALKLSVRqalAY----AGYVAVNTLLQNGTQVLVLFYGGHLVLS-GRMSAGQLVTFMLYQQQLGEAFQSLGD 274
|
250
....*....|....
gi 1958656469 1248 MSSEMETNIVAVER 1261
Cdd:cd18572 275 VFSSLMQAVGAAEK 288
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1307-1503 |
3.98e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 65.08 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIdginiAKIGLHNLRFKITIIPQDPVLF-------- 1378
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA-----GTAPLAEAREDTRLMFQDARLLpwkkvidn 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1379 -SGSLRMNLDPFSQYSDEEVwmalelahlkgfvsALPDKLNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAA 1457
Cdd:PRK11247 102 vGLGLKGQWRDAALQALAAV--------------GLADRANEWPAA----LSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958656469 1458 VD----LETDDLIQSTIRTQ-FedsTVLTIAHRLN---TIMDytRVIVLDKGEI 1503
Cdd:PRK11247 164 LDaltrIEMQDLIESLWQQHgF---TVLLVTHDVSeavAMAD--RVLLIEEGKI 212
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1307-1515 |
4.65e-11 |
|
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: 63.70 E-value: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSL--TLGLFRINESAEGEIIIDGINIAKIGLHNlRFK--ITIIPQDPVLFSGsl 1382
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLakTIMGHPKYEVTEGEILFKGEDITDLPPEE-RARlgIFLAFQYPPEIPG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1383 rmnldpfsqysdeevwmaLELAHLKGFVsalpdklnhecaegGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 1462
Cdd:cd03217 92 ------------------VKNADFLRYV--------------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656469 1463 DDLIQSTIRT-QFEDSTVLTIAHRLNtIMDY---TRVIVLDKGEIRECGaPSELLQQ 1515
Cdd:cd03217 140 LRLVAEVINKlREEGKSVLIITHYQR-LLDYikpDRVHVLYDGRIVKSG-DKELALE 194
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1295-1518 |
4.76e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.03 E-value: 4.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1295 DYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--INIAKIGLHNLRFKITIIP 1372
Cdd:PRK13638 6 DLWFRYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1373 QDP---VLFSG-------SLRmNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHecaeggenlsvGQRQLVCLARAL 1442
Cdd:PRK13638 84 QDPeqqIFYTDidsdiafSLR-NLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSH-----------GQKKRVAIAGAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1443 LRKTKILVLDEATAAVDLE-TDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYT-RVIVLDKGEIRECGAP------SELLQ 1514
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAgRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISdAVYVLRQGQILTHGAPgevfacTEAME 231
|
....
gi 1958656469 1515 QRGV 1518
Cdd:PRK13638 232 QAGL 235
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1308-1511 |
5.25e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.90 E-value: 5.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1308 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLrfkITIIPQD-------PVLFSG 1380
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSeevdwsfPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1381 SLRMnldpfSQYSDEEvWMALELAHLKGFVS---ALPDKLNHECAEGGEnLSVGQRQLVCLARALLRKTKILVLDEATAA 1457
Cdd:PRK15056 100 VVMM-----GRYGHMG-WLRRAKKRDRQIVTaalARVDMVEFRHRQIGE-LSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 1458 VDLETDDLIQSTIRT-QFEDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGaPSE 1511
Cdd:PRK15056 173 VDVKTEARIISLLRElRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG-PTE 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1306-1505 |
5.83e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.01 E-value: 5.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1306 LVLKHINVTIEGGEKVGIVGRTGAGKSSltlgLFRI----NESAEGEIiidginiaKIGlHNLrfKITIIPQDPVLFSGS 1381
Cdd:COG0488 329 TLLDDLSLRIDRGDRIGLIGPNGAGKST----LLKLlageLEPDSGTV--------KLG-ETV--KIGYFDQHQEELDPD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1382 LRMnLDPFSQYSDEevwmaLELAHLKGFVSAL---PDKLNHECaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAV 1458
Cdd:COG0488 394 KTV-LDELRDGAPG-----GTEQEVRGYLGRFlfsGDDAFKPV----GVLSGGEKARLALAKLLLSPPNVLLLDEPTNHL 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 1459 DLETddliqstiRTQFEDS------TVLTIAH-R--LNTIMDytRVIVLDKGEIRE 1505
Cdd:COG0488 464 DIET--------LEALEEAlddfpgTVLLVSHdRyfLDRVAT--RILEFEDGGVRE 509
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
662-859 |
6.18e-11 |
|
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: 67.02 E-value: 6.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAeMDKVEGHVTLKGsvayvpqQAWiqnDSLRENILfgRPLQEHC---- 737
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDG-------QDL---DGLSRRAL--RPLRRRMqvvf 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 738 ---YKA----------VMEACALLpdlEILPSGD---------LTEIG-----------EkgvnLSGGQKQRVSLARAVY 784
Cdd:COG4172 369 qdpFGSlsprmtvgqiIAEGLRVH---GPGLSAAerrarvaeaLEEVGldpaarhryphE----FSGGQRQRIAIARALI 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 785 CNSDIYLLDDPLSAVDAHVGKHIFEkvvgpmgLLKnktRILVTHGISYL-----PQV-----DVIIVMSGGKISEMGSYQ 854
Cdd:COG4172 442 LEPKLLVLDEPTSALDVSVQAQILD-------LLR---DLQREHGLAYLfishdLAVvralaHRVMVMKDGKVVEQGPTE 511
|
....*
gi 1958656469 855 ELLDR 859
Cdd:COG4172 512 QVFDA 516
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1307-1498 |
6.37e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 63.02 E-value: 6.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGIniAKIGLhnLRFKITIIPQDPVLFSGSLRMNL 1386
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG--ARVAY--VPQRSEVPDSLPLTVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1387 ----DPFSQYSDE---EVWMALELAHLKGFvsalpdkLNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1459
Cdd:NF040873 83 warrGLWRRLTRDdraAVDDALERVGLADL-------AGRQLGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958656469 1460 LETDDLIQSTIRTQFEDS-TVLTIAHRLNTIMDYTRVIVL 1498
Cdd:NF040873 152 AESRERIIALLAEEHARGaTVVVVTHDLELVRRADPCVLL 191
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
643-856 |
7.74e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 64.72 E-value: 7.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 643 NSITVKNATFTWARDE----PPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAW- 717
Cdd:PRK13633 3 EMIKCKNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 718 IQNdslRENILFGRPLQEHCYKAVMEACALLPD-LEILPSGDLTEIGE--KGVN-----------LSGGQKQRVSLARAV 783
Cdd:PRK13633 83 IRN---KAGMVFQNPDNQIVATIVEEDVAFGPEnLGIPPEEIRERVDEslKKVGmyeyrrhaphlLSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 784 YCNSDIYLLDDPLSAVDAhVGKhifEKVVGPMGLLKNK---TRILVTHGISYLPQVDVIIVMSGGKISEMGSYQEL 856
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDP-SGR---REVVNTIKELNKKygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1306-1514 |
7.86e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 64.66 E-value: 7.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1306 LVLKHINVTIEGGEKVGIVGRTGAGKSSL----------TLGLFRINEsaegEIIIDGINIAKigLHNLRFKITIIPQDP 1375
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLlqhlngllqpTSGTVTIGE----RVITAGKKNKK--LKPLRKKVGIVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1376 --VLFSGSLR-------MNldpFSQYSDEEVWMALELAHLKGFVSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKT 1446
Cdd:PRK13634 95 ehQLFEETVEkdicfgpMN---FGVSEEDAKQKAREMIELVGLPEELLARSPFE-------LSGGQMRRVAIAGVLAMEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958656469 1447 KILVLDEATAAVD----LETDDLIQSTIRTQfeDSTVLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSELLQ 1514
Cdd:PRK13634 165 EVLVLDEPTAGLDpkgrKEMMEMFYKLHKEK--GLTTVLVTHSMEDAARYAdQIVVMHKGTVFLQGTPREIFA 235
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
665-800 |
8.23e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 64.24 E-value: 8.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 665 ITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS-------------VAYVPQQAWIQND-SLRENILFG 730
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiqhyaskevarrIGLLAQNATTPGDiTVQELVARG 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 731 R----PLQEHCYKAVMEACAllpdlEILPSGDLTEIGEKGVN-LSGGQKQRVSLARAVYCNSDIYLLDDPLSAVD 800
Cdd:PRK10253 106 RyphqPLFTRWRKEDEEAVT-----KAMQATGITHLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1307-1514 |
8.42e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 64.09 E-value: 8.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLG---LFRINESA--EGEIIIDGINI--AKIGLHNLRFKITIIPQDPVLF- 1378
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEArvEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1379 --------SGSLRMN-LDPFSQYSDEEVWMALELAhlkgfvsALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKIL 1449
Cdd:PRK14267 99 hltiydnvAIGVKLNgLVKSKKELDERVEWALKKA-------ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 1450 VLDEATAAVDLETDDLIQSTIRTQFEDSTVLTIAH---RLNTIMDYTRVIVLdkGEIRECGAPSELLQ 1514
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHspaQAARVSDYVAFLYL--GKLIEVGPTRKVFE 237
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
659-871 |
1.11e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.81 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 659 PPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS--------------VAYVP----QQAWIQN 720
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVPedrkGEGLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 721 DSLRENILFGRpLQEHC------YKAVMEACA-LLPDLEILPSGDLTEIGekgvNLSGGQKQRVSLARAVYCNSDIYLLD 793
Cdd:COG1129 345 LSIRENITLAS-LDRLSrgglldRRRERALAEeYIKRLRIKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 794 DPLSAVDahVG-KH-IFEKVvgpMGLLKNKTRILVthgIS-YLPQV----DVIIVMSGGKISEMgsyqelLDRDGAFAEF 866
Cdd:COG1129 420 EPTRGID--VGaKAeIYRLI---RELAAEGKAVIV---ISsELPELlglsDRILVMREGRIVGE------LDREEATEEA 485
|
....*
gi 1958656469 867 VRTYA 871
Cdd:COG1129 486 IMAAA 490
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
644-851 |
1.11e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 63.49 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 644 SITVKNATFTWARDEppTLNGITFAIPDGALVAVVGQVGCGKSSLLSAL-LAEMDKvEGHVTLKGS---VAYVPQQAWIQ 719
Cdd:PRK11124 2 SIQLNGINCFYGAHQ--ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPR-SGTLNIAGNhfdFSKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 720 ndSLRENIlfGRPLQEHC---YKAVME--------------ACALLPDLEILPSGDLTEIGEK-GVNLSGGQKQRVSLAR 781
Cdd:PRK11124 79 --ELRRNV--GMVFQQYNlwpHLTVQQnlieapcrvlglskDQALARAEKLLERLRLKPYADRfPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 782 AVYCNSDIYLLDDPLSAVD----AHVGKHIFEkvVGPMGLlknkTRILVTHgisylpQVDV-------IIVMSGGKISEM 850
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDpeitAQIVSIIRE--LAETGI----TQVIVTH------EVEVarktasrVVYMENGHIVEQ 222
|
.
gi 1958656469 851 G 851
Cdd:PRK11124 223 G 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
657-857 |
1.25e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.91 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 657 DEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSAL--LAEMD----KVEGHV-------------TLKGSVAYVPQQA- 716
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrLIEIYdskiKVDGKVlyfgkdifqidaiKLRKEVGMVFQQPn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 717 WIQNDSLRENILFgrPLQEHCYKAVMEACALLPDlEILPSGDLTEIGEK----GVNLSGGQKQRVSLARAVYCNSDIYLL 792
Cdd:PRK14246 101 PFPHLSIYDNIAY--PLKSHGIKEKREIKKIVEE-CLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 793 DDPLSAVDAhVGKHIFEKVVGPmgLLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELL 857
Cdd:PRK14246 178 DEPTSMIDI-VNSQAIEKLITE--LKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1297-1499 |
1.31e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.51 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1297 CLRyreDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSL--TL-GLFRineSAEGEIIIDGINIAK-----------IG-- 1360
Cdd:PRK13538 9 CER---DERILFSGLSFTLNAGELVQIEGPNGAGKTSLlrILaGLAR---PDAGEVLWQGEPIRRqrdeyhqdllyLGhq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1361 ---------LHNLRFkitiipqdpvlfsgSLRMNldpfSQYSDEEVWMALELAHLKGFVSALpdklnheCAeggeNLSVG 1431
Cdd:PRK13538 83 pgikteltaLENLRF--------------YQRLH----GPGDDEALWEALAQVGLAGFEDVP-------VR----QLSAG 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1432 QRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDS--TVLTIAHRLNTIMDYTRVIVLD 1499
Cdd:PRK13538 134 QQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGgmVILTTHQDLPVASDKVRKLRLG 203
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
660-878 |
2.11e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.02 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 660 PTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS--VAYVPQQ------AWIQNDSLRENILFGR 731
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHevVTRSPQDglangiVYISEDRKRDGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 732 PLQEHcykavMEACAL------------------LPDLEIL-----PSGDLTeIGekgvNLSGGQKQRVSLARAVYCNSD 788
Cdd:PRK10762 346 SVKEN-----MSLTALryfsraggslkhadeqqaVSDFIRLfniktPSMEQA-IG----LLSGGNQQKVAIARGLMTRPK 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 789 IYLLDDPLSAVDAHVGKHIFEkvvgpmglLKNKTR------ILVThgiSYLPQV----DVIIVMSGGKISemgsyqelld 858
Cdd:PRK10762 416 VLILDEPTRGVDVGAKKEIYQ--------LINQFKaeglsiILVS---SEMPEVlgmsDRILVMHEGRIS---------- 474
|
250 260
....*....|....*....|
gi 1958656469 859 rdgafAEFVRTYANTEQDLA 878
Cdd:PRK10762 475 -----GEFTREQATQEKLMA 489
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1307-1514 |
2.23e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.27 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITIIPQD-PVLFSGSLRM- 1384
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlPAAEGMTVREl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1385 ----------NLDPFSQYSDEEVWMALELAHLKGFVSALPDklnhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEA 1454
Cdd:PRK10575 106 vaigrypwhgALGRFGAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 1455 TAAVDL----ETDDLIQSTirTQFEDSTVLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSELLQ 1514
Cdd:PRK10575 175 TSALDIahqvDVLALVHRL--SQERGLTVIAVLHDINMAARYCdYLVALRGGEMIAQGTPAELMR 237
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1311-1515 |
2.46e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 63.22 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1311 INVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG----LHNLRFKITIIPQDP--VLFSGSLRM 1384
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQIRKKVGLVFQFPesQLFEETVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1385 NL----DPFSQYSDEEVWMALELAHLKGFVSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1460
Cdd:PRK13649 106 DVafgpQNFGVSQEEAEALAREKLALVGISESLFEKNPFE-------LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656469 1461 ETDDLIQSTIRTQFEDS-TVLTIAHRLNTIMDY-TRVIVLDKGEIRECGAPSELLQQ 1515
Cdd:PRK13649 179 KGRKELMTLFKKLHQSGmTIVLVTHLMDDVANYaDFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1307-1503 |
2.52e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 62.35 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGI--------NIAKIGLHnLRFKITIIPQDPVLf 1378
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvpwkrrkkFLRRIGVV-FGQKTQLWWDLPVI- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1379 sGSLRMNLD----PFSQYSdeevwmalelAHLKGFVSALpdKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEA 1454
Cdd:cd03267 114 -DSFYLLAAiydlPPARFK----------KRLDELSELL--DLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958656469 1455 TAAVDLETDDLIQSTIRTQFED--STVLTIAHRLNTIMDY-TRVIVLDKGEI 1503
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRErgTTVLLTSHYMKDIEALaRRVLVIDKGRL 232
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1308-1490 |
2.63e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.95 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1308 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRI--NESAEGEIIIDGiniAKIGLHNLR----FKITIIPQDPVL---- 1377
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEG---EELQASNIRdterAGIAIIHQELALvkel 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1378 ------FSGSL-----RMNLDpfSQYSDEEVWMAlELahlkgfvsalpdKLNHECAEGGENLSVGQRQLVCLARALLRKT 1446
Cdd:PRK13549 98 svleniFLGNEitpggIMDYD--AMYLRAQKLLA-QL------------KLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958656469 1447 KILVLDEATAAV-DLETDDLIqSTIRT-QFEDSTVLTIAHRLNTIM 1490
Cdd:PRK13549 163 RLLILDEPTASLtESETAVLL-DIIRDlKAHGIACIYISHKLNEVK 207
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1318-1519 |
2.87e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.88 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1318 GEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG---LHNLRFKITIIPQDPVlfsgslrMNLDPFSQ--Y 1392
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY-------ASLDPRQTvgD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1393 SDEEVWM----------ALELAHLKGFVSALPD---KLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1459
Cdd:PRK10261 423 SIMEPLRvhgllpgkaaAARVAWLLERVGLLPEhawRYPHE-------FSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958656469 1460 LETDDLIQSTIRTQFEDSTV--LTIAHRLNTIMDYT-RVIVLDKGEIRECGApsellqQRGVF 1519
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDFGIayLFISHDMAVVERIShRVAVMYLGQIVEIGP------RRAVF 552
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1307-1515 |
3.05e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 62.41 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSL--TLGlfRINESAEGEIIIDGiNIAKI-----GLH-------NLRFKITII- 1371
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLlkLIA--GILEPTSGRVEVNG-RVSALlelgaGFHpeltgreNIYLNGRLLg 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1372 --PQDP-------VLFSGsLRMNLD-PFSQYSDEevwMALELA-----HLKgfvsalPDklnhecaeggenlsvgqrqlv 1436
Cdd:COG1134 118 lsRKEIdekfdeiVEFAE-LGDFIDqPVKTYSSG---MRARLAfavatAVD------PD--------------------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1437 clarallrktkILVLDEATAAVDLE----TDDLIQSTIRtqfEDSTVLTIAHRLNTIMDY-TRVIVLDKGEIRECGAPSE 1511
Cdd:COG1134 167 -----------ILLVDEVLAVGDAAfqkkCLARIRELRE---SGRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDPEE 232
|
....
gi 1958656469 1512 LLQQ 1515
Cdd:COG1134 233 VIAA 236
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
662-877 |
3.08e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 62.81 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHvTLKGSVAYVPQQAWIQNDSL----RENILFGRP----- 732
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGY-RYSGDVLLGGRSIFNYRDVLefrrRVGMLFQRPnpfpm 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 733 -LQEHCYKAVmEACALLPDLEI--LPSGDLTEIG----------EKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAV 799
Cdd:PRK14271 116 sIMDNVLAGV-RAHKLVPRKEFrgVAQARLTEVGlwdavkdrlsDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656469 800 DAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLDRDgAFAEFVRTYANTEQDL 877
Cdd:PRK14271 195 DPTTTEKIEEFI---RSLADRLTVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQLFSSP-KHAETARYVAGLSGDV 269
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
666-870 |
3.20e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 63.90 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 666 TFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSvayvpQQAWIQNDSLREnilfgrpLQEHCYKAVMEAC 745
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGV-----DIAKISDAELRE-------VRRKKIAMVFQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 746 ALLPDLEILpsgDLTEIG------------EKGVN-----------------LSGGQKQRVSLARAVYCNSDIYLLDDPL 796
Cdd:PRK10070 116 ALMPHMTVL---DNTAFGmelaginaeerrEKALDalrqvglenyahsypdeLSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 797 SAVDAHVGKHIFEKVVgPMGLLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLDRDGafAEFVRTY 870
Cdd:PRK10070 193 SALDPLIRTEMQDELV-KLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNPA--NDYVRTF 264
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1311-1520 |
3.22e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.59 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1311 INVTIEGGEKVGIVGRTGAGKSSLT---LGLFRINESAEGEIIIDG---INIAKIGLHNLRF-KITIIPQDPVlfsgslr 1383
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSQTAfalMGLLAANGRIGGSATFNGreiLNLPEKELNKLRAeQISMIFQDPM------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1384 MNLDPFSQYSDE--EVWM-------------------ALELAHLKGFVSALPdklnHEcaeggenLSVGQRQLVCLARAL 1442
Cdd:PRK09473 108 TSLNPYMRVGEQlmEVLMlhkgmskaeafeesvrmldAVKMPEARKRMKMYP----HE-------FSGGMRQRVMIAMAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1443 LRKTKILVLDEATAAVDLEtddlIQSTIRTQFED------STVLTIAHRLNT---IMDytRVIVLDKGEIRECGapsell 1513
Cdd:PRK09473 177 LCRPKLLIADEPTTALDVT----VQAQIMTLLNElkrefnTAIIMITHDLGVvagICD--KVLVMYAGRTMEYG------ 244
|
....*..
gi 1958656469 1514 QQRGVFY 1520
Cdd:PRK09473 245 NARDVFY 251
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
660-828 |
3.25e-10 |
|
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: 61.65 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 660 PTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-SVAYVPQQA----------------WIQNDS 722
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqDVSDLRGRAipylrrkigvvfqdfrLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 723 LRENILF-----GRPLQEhCYKAVMEACALLpDLE----ILPSGdlteigekgvnLSGGQKQRVSLARAVYCNSDIYLLD 793
Cdd:cd03292 95 VYENVAFalevtGVPPRE-IRKRVPAALELV-GLShkhrALPAE-----------LSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958656469 794 DPLSAVDAHVGKHIfekvvgpMGLLK--NK---TRILVTH 828
Cdd:cd03292 162 EPTGNLDPDTTWEI-------MNLLKkiNKagtTVVVATH 194
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1301-1529 |
3.39e-10 |
|
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: 63.58 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1301 REDLDLvlkHINVTIEGGEKVGIVGRTGAGKSSLtL----GLFRineSAEGEIIIDG---------INIA----KIGLhn 1363
Cdd:COG4148 11 RGGFTL---DVDFTLPGRGVTALFGPSGSGKTTL-LraiaGLER---PDSGRIRLGGevlqdsargIFLPphrrRIGY-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1364 lrfkitiIPQDPVLFSG-SLRMNLD--------PFSQYSDEEVWMALELAHLkgfvsalpdkLNHecaeGGENLSVGQRQ 1434
Cdd:COG4148 82 -------VFQEARLFPHlSVRGNLLygrkraprAERRISFDEVVELLGIGHL----------LDR----RPATLSGGERQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1435 LVCLARALLRKTKILVLDEATAAVDLETDDLIQ---STIRTQFeDSTVLTIAHRLNTIM---DytRVIVLDKGEIRECGA 1508
Cdd:COG4148 141 RVAIGRALLSSPRLLLMDEPLAALDLARKAEILpylERLRDEL-DIPILYVSHSLDEVArlaD--HVVLLEQGRVVASGP 217
|
250 260
....*....|....*....|..
gi 1958656469 1509 PSELLQQRGVF-YSMAKDAGLV 1529
Cdd:COG4148 218 LAEVLSRPDLLpLAGGEEAGSV 239
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
647-867 |
3.74e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 63.70 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 647 VKNATFTWarDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-SVAYVP-----------Q 714
Cdd:PRK11607 22 IRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvDLSHVPpyqrpinmmfqS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 715 QAWIQNDSLRENILFGRPlQEHCYKA-----VMEACALLPDLEIlpsgdlteIGEKGVNLSGGQKQRVSLARAVYCNSDI 789
Cdd:PRK11607 100 YALFPHMTVEQNIAFGLK-QDKLPKAeiasrVNEMLGLVHMQEF--------AKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 790 YLLDDPLSAVDAHVGKHIFEKVVGPMGLLkNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQELLDRDGA--FAEF 866
Cdd:PRK11607 171 LLLDEPMGALDKKLRDRMQLEVVDILERV-GVTCVMVTHDQeEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTrySAEF 249
|
.
gi 1958656469 867 V 867
Cdd:PRK11607 250 I 250
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1307-1515 |
3.97e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 62.29 E-value: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIA-------------KIGLHNLRFKITIIPQ 1373
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1374 DPVLFSgslRMNLDPFSQYSDEEVwMALELAHLKGFVSALPDKLNHECAEGGE---NLSVGQRQLVCLARALLRKTKILV 1450
Cdd:PRK10619 100 HFNLWS---HMTVLENVMEAPIQV-LGLSKQEARERAVKYLAKVGIDERAQGKypvHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958656469 1451 LDEATAAVDLE-TDDLIQSTIRTQFEDSTVLTIAHRlntiMDYTR-----VIVLDKGEIRECGAPSELLQQ 1515
Cdd:PRK10619 176 FDEPTSALDPElVGEVLRIMQQLAEEGKTMVVVTHE----MGFARhvsshVIFLHQGKIEEEGAPEQLFGN 242
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1019-1262 |
3.98e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 62.91 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1019 ALGILQGVAVFG--YSMAvSIGGIFASRrLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSL 1096
Cdd:cd18564 62 GIALLRGLASYAgtYLTA-LVGQRVVLD-LRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1097 FSVIGAVIIIL-----LATpIAAVIIPPLGLVYFFVQRFYVASSRQLKRLESVsrspVYSHFNETLLGVSVIRAF----E 1167
Cdd:cd18564 140 LTLVGMLGVMFwldwqLAL-IALAVAPLLLLAARRFSRRIKEASREQRRREGA----LASVAQESLSAIRVVQAFgreeH 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1168 EQERFIRQSDLKVDENQKAYYPSIVANRWLAVrLECVGNCIVLFAALFAVIsRHSLSAGlvGLSVsyslqITAYLNWL-- 1245
Cdd:cd18564 215 EERRFARENRKSLRAGLRAARLQALLSPVVDV-LVAVGTALVLWFGAWLVL-AGRLTPG--DLLV-----FLAYLKNLyk 285
|
250 260
....*....|....*....|..
gi 1958656469 1246 -VRMSSEMETNI----VAVERL 1262
Cdd:cd18564 286 pVRDLAKLTGRIakasASAERV 307
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
662-847 |
4.29e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 64.36 E-value: 4.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSaLLAEMDKVeghvtlKGSVAYVPQQ--AWIQNDSL----RENilFGRPLQE 735
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKP------TSGTYRVAGQdvATLDADALaqlrREH--FGFIFQR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 736 H----------------CYKAVMEACALLPDLEILPSGDLTE-IGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSA 798
Cdd:PRK10535 95 YhllshltaaqnvevpaVYAGLERKQRLLRAQELLQRLGLEDrVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958656469 799 VDAHVGKHIfekvvgpMGLLKN-----KTRILVTHGISYLPQVDVIIVMSGGKI 847
Cdd:PRK10535 175 LDSHSGEEV-------MAILHQlrdrgHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
645-856 |
4.71e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 62.34 E-value: 4.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDEP---PTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLkGSVAYVPQQAWIQND 721
Cdd:PRK13634 3 ITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 722 SLREN--ILFGRPlqEH-----------CYK----AVMEACALLPDLEILPSGDLTE-IGEKG-VNLSGGQKQRVSLARA 782
Cdd:PRK13634 82 PLRKKvgIVFQFP--EHqlfeetvekdiCFGpmnfGVSEEDAKQKAREMIELVGLPEeLLARSpFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 783 VYCNSDIYLLDDPLSAVDAHVGKHIfekvvgpMGLL------KNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQE 855
Cdd:PRK13634 160 LAMEPEVLVLDEPTAGLDPKGRKEM-------MEMFyklhkeKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPRE 232
|
.
gi 1958656469 856 L 856
Cdd:PRK13634 233 I 233
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
1016-1226 |
5.46e-10 |
|
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: 62.12 E-value: 5.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1016 VYGALGILQGVAVFGYSMAVSIggifASRRLHLDL----LQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKM 1091
Cdd:cd18546 44 AYLAVVLAGWVAQRAQTRLTGR----TGERLLYDLrlrvFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1092 FMGSLFSVIGAVIIILLATP----IAAVIIPPLGLVYFFVQRfyvASSRQLKRL-ESVSRspVYSHFNETLLGVSVIRAF 1166
Cdd:cd18546 120 LVVSLLTLVGIAVVLLVLDPrlalVALAALPPLALATRWFRR---RSSRAYRRArERIAA--VNADLQETLAGIRVVQAF 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1167 ----EEQERFIRQSDLKVDENQKA------YYPSIvanRWLAVrlecVGNCIVLFAALFAVIsRHSLSAG 1226
Cdd:cd18546 195 rrerRNAERFAELSDDYRDARLRAqrlvaiYFPGV---ELLGN----LATAAVLLVGAWRVA-AGTLTVG 256
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1305-1472 |
6.36e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 60.66 E-value: 6.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1305 DLVLKHINVTIEGGEKVGIVGRTGAGKSSL--TL-GLFRInesAEGEIIIDGiniAKIGLHNLRFKITII-PQD---PVL 1377
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLlrLIaGLLPP---AAGTIKLDG---GDIDDPDVAEACHYLgHRNamkPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1378 fsgSLRMNLDPFSQY---SDEEVWMALE------LAHLKgfvsalpdklnhecaegGENLSVGQRQLVCLARALLRKTKI 1448
Cdd:PRK13539 89 ---TVAENLEFWAAFlggEELDIAAALEavglapLAHLP-----------------FGYLSAGQKRRVALARLLVSNRPI 148
|
170 180
....*....|....*....|....
gi 1958656469 1449 LVLDEATAAVDLETDDLIQSTIRT 1472
Cdd:PRK13539 149 WILDEPTAALDAAAVALFAELIRA 172
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1261-1515 |
6.60e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 62.54 E-value: 6.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1261 RLKEYSETEKEASWQIQETAPPSTWPHSGRVEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFR 1340
Cdd:PRK13536 12 RRLELSPIERKHQGISEAKASIPGSMSTVAIDLAGVSKSYGDKA--VVNGLSFTVASGECFGLLGPNGAGKSTIARMILG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1341 INESAEGEIIIDGINI-AKIGLhnLRFKITIIPQ-DPVLFSGSLRMNLDPFSQY-------SDEEVWMALELAHLKgfvs 1411
Cdd:PRK13536 90 MTSPDAGKITVLGVPVpARARL--ARARIGVVPQfDNLDLEFTVRENLLVFGRYfgmstreIEAVIPSLLEFARLE---- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1412 alpDKLNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQF-EDSTVLTIAHrlntIM 1490
Cdd:PRK13536 164 ---SKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTH----FM 232
|
250 260 270
....*....|....*....|....*....|.
gi 1958656469 1491 DYT-----RVIVLDKG-EIREcGAPSELLQQ 1515
Cdd:PRK13536 233 EEAerlcdRLCVLEAGrKIAE-GRPHALIDE 262
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1308-1516 |
7.82e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 61.57 E-value: 7.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1308 LKHINVTIEGGEKVGIVGRTGAGKSSLTL---GLFRINESAEGEIIIDGINIAKIG------------------LHNLRF 1366
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsGLITGDKSAGSHIELLGRTVQREGrlardirksrantgyifqQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1367 KITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVsalpdklnHECAEGGENLSVGQRQLVCLARALLRKT 1446
Cdd:PRK09984 100 RLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMV--------HFAHQRVSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958656469 1447 KILVLDEATAAVDLETDDLIQSTIR--TQFEDSTVLTIAHRLNTIMDY-TRVIVLDKGEIRECGAPSELLQQR 1516
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDYALRYcERIVALRQGHVFYDGSSQQFDNER 244
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1291-1507 |
8.22e-10 |
|
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: 60.35 E-value: 8.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGI----------NIAKI- 1359
Cdd:cd03301 1 VELENVTKRFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlppkdrDIAMVf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1360 ----------GLHNLRF--KITIIPQDPVlfsgslrmnldpfsqysDEEVWMALELAHLKGFVSALPDKlnhecaeggen 1427
Cdd:cd03301 79 qnyalyphmtVYDNIAFglKLRKVPKDEI-----------------DERVREVAELLQIEHLLDRKPKQ----------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1428 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLetddLIQSTIRTQFE------DSTVLTIAHrlntimDYT-------R 1494
Cdd:cd03301 131 LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA----KLRVQMRAELKrlqqrlGTTTIYVTH------DQVeamtmadR 200
|
250
....*....|...
gi 1958656469 1495 VIVLDKGEIRECG 1507
Cdd:cd03301 201 IAVMNDGQIQQIG 213
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1307-1522 |
8.28e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.28 E-value: 8.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIidginiakiglHNLRFKITIIPQ----DPVL-FSGS 1381
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLRIGYVPQklylDTTLpLTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1382 LRMNLDPFSQYSDeeVWMALELAHLKGFVSALPDKLNhecaeGGENlsvgqrQLVCLARALLRKTKILVLDEATAAVD-- 1459
Cdd:PRK09544 88 RFLRLRPGTKKED--ILPALKRVQAGHLIDAPMQKLS-----GGET------QRVLLARALLNRPQLLVLDEPTQGVDvn 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 1460 --LETDDLIQStIRTQFeDSTVLTIAHRLNTIMDYTRVIVLDKGEIRECGAPsELLQQRGVFYSM 1522
Cdd:PRK09544 155 gqVALYDLIDQ-LRREL-DCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGTP-EVVSLHPEFISM 216
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
644-860 |
9.82e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 61.33 E-value: 9.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 644 SITVKNATFTWARDEP---PTLNGITFAIPDGALVAVVGQVGCGKSSL---LSALLA------EMDKVEGHVTLK----- 706
Cdd:PRK13646 2 TIRFDNVSYTYQKGTPyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLiqnINALLKpttgtvTVDDITITHKTKdkyir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 707 ------GSVAYVPQQAWIQnDSLRENILFG-RPLQEHCYKAVMEACALLPDLEIlpSGDLTEigEKGVNLSGGQKQRVSL 779
Cdd:PRK13646 82 pvrkriGMVFQFPESQLFE-DTVEREIIFGpKNFKMNLDEVKNYAHRLLMDLGF--SRDVMS--QSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 780 ARAVYCNSDIYLLDDPLSAVDAHvGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELLD 858
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQ-SKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFK 235
|
..
gi 1958656469 859 RD 860
Cdd:PRK13646 236 DK 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
645-795 |
9.86e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.77 E-value: 9.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWarDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLkGS---VAYVPQqawiQND 721
Cdd:COG0488 316 LELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GEtvkIGYFDQ----HQE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 722 SLRENIlfgRPLQEhcykaVMEACALLPDLEI-------LPSGD--LTEIGekgvNLSGGQKQRVSLARAVYCNSDIYLL 792
Cdd:COG0488 389 ELDPDK---TVLDE-----LRDGAPGGTEQEVrgylgrfLFSGDdaFKPVG----VLSGGEKARLALAKLLLSPPNVLLL 456
|
...
gi 1958656469 793 DDP 795
Cdd:COG0488 457 DEP 459
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
662-856 |
1.04e-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: 60.08 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSAL--LAEMDKVEGHV----------TLKGSVAYVPQQAWIQND-SLRENI- 727
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLttLLKPTSGRATVaghdvvreprEVRRRIGIVFQDLSVDDElTGWENLy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 728 ----LFGRPLQEHCYKAvmeacallpdLEILPSGDLTEIGEKGV-NLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAH 802
Cdd:cd03265 96 iharLYGVPGAERRERI----------DELLDFVGLLEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 803 VGKHIFEkVVGPMGLLKNKTRILVTHgisYLPQV----DVIIVMSGGKISEMGSYQEL 856
Cdd:cd03265 166 TRAHVWE-YIEKLKEEFGMTILLTTH---YMEEAeqlcDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1307-1498 |
1.08e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 59.81 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL 1386
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1387 DPFSQY-SDEEVWMALELAHLKGFVSALpdklnheCAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDL 1465
Cdd:cd03231 95 RFWHADhSDEQVEEALARVGLNGFEDRP-------VAQ----LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180 190
....*....|....*....|....*....|....*
gi 1958656469 1466 IQSTIRTQFED--STVLTIAHRLNTIMDYTRVIVL 1498
Cdd:cd03231 164 FAEAMAGHCARggMVVLTTHQDLGLSEAGARELDL 198
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1307-1511 |
1.09e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 62.27 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLtLGLFRINESA-EGEIIIDGINIAKIGLH----NLRFK-------ITIIpqD 1374
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTV-LRLIAGFETPdSGRIMLDGQDITHVPAEnrhvNTVFQsyalfphMTVF--E 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1375 PVLFSgsLRMNLDPFSQYsDEEVWMALELAHLKGFVSALPdklnhecaeggENLSVGQRQLVCLARALLRKTKILVLDEA 1454
Cdd:PRK09452 106 NVAFG--LRMQKTPAAEI-TPRVMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958656469 1455 TAAVDLETDDLIQSTIRtQFEDSTVLT---IAHRLN---TIMDytRVIVLDKGEIRECGAPSE 1511
Cdd:PRK09452 172 LSALDYKLRKQMQNELK-ALQRKLGITfvfVTHDQEealTMSD--RIVVMRDGRIEQDGTPRE 231
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1308-1516 |
1.12e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 61.38 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1308 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINI----AKIGLHNLRFKITIIPQDP--VLFSGS 1381
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKKLRKKVSLVFQFPeaQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1382 LRMNLD--P--FSQYSDEEVWMALELAHLKGFVSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAA 1457
Cdd:PRK13641 103 VLKDVEfgPknFGFSEDEAKEKALKWLKKVGLSEDLISKSPFE-------LSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958656469 1458 VDLET-DDLIQSTIRTQFEDSTVLTIAHRLNTIMDYTR-VIVLDKGEIRECGAPSELLQQR 1516
Cdd:PRK13641 176 LDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADdVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1291-1514 |
1.21e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 61.36 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGlHNLRFKITI 1370
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-RHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1371 IPQ----DPVLfsgSLRMNLDPFSQY-------SDEEVWMALELAHLKgfvsalpdklNHECAEGGEnLSVGQRQLVCLA 1439
Cdd:PRK13537 85 VPQfdnlDPDF---TVRENLLVFGRYfglsaaaARALVPPLLEFAKLE----------NKADAKVGE-LSGGMKRRLTLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1440 RALLRKTKILVLDEATAAVDLETDDLIQSTIRTQF-EDSTVLTIAH------RLntimdYTRVIVLDKGEIRECGAPSEL 1512
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHAL 225
|
..
gi 1958656469 1513 LQ 1514
Cdd:PRK13537 226 IE 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
645-857 |
1.36e-09 |
|
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: 60.48 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATftWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEG-HVT-------------LKGSVA 710
Cdd:COG1119 4 LELRNVT--VRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRlfgerrggedvweLRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 711 YV-P--QQAWIQNDSLRENIL------FGRPLQehcYKAVME--ACALLPDLEIlpsGDLTE--IGEkgvnLSGGQKQRV 777
Cdd:COG1119 82 LVsPalQLRFPRDETVLDVVLsgffdsIGLYRE---PTDEQRerARELLELLGL---AHLADrpFGT----LSQGEQRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 778 SLARAVYCNSDIYLLDDPLSAVDAHvGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQEL 856
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLG-ARELLLALLDKLAAEGAPTLVLVTHHVEEIPPgITHVLLLKDGRVVAAGPKEEV 230
|
.
gi 1958656469 857 L 857
Cdd:COG1119 231 L 231
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1306-1493 |
1.86e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 60.18 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1306 LVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGINI--AKIGLHNLRFKITIIPQDPVLF 1378
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1379 SGSLRMNL------DPFSQYSDEEVWMALELAHLKGFVSalpDKLNhecaEGGENLSVGQRQLVCLARALLRKTKILVLD 1452
Cdd:PRK14243 104 PKSIYDNIaygariNGYKGDMDELVERSLRQAALWDEVK---DKLK----QSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958656469 1453 EATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRLNT---IMDYT 1493
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQaarVSDMT 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
668-851 |
1.86e-09 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 59.43 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 668 AIPDGALVAVVGQVGCGKSSLLSaLLAEMDKVE-GHVTLKG-SVAYVPQQAWIQNDSLRENILFGrplqeHCYKAVMEAC 745
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLN-LIAGFETPQsGRVLINGvDVTAAPPADRPVSMLFQENNLFA-----HLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 746 ALLPDLEILP------SGDLTEIGEKGV------NLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIFEKVVG 813
Cdd:cd03298 94 GLSPGLKLTAedrqaiEVALARVGLAGLekrlpgELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958656469 814 PMGLLKNkTRILVTHGISYLPQV-DVIIVMSGGKISEMG 851
Cdd:cd03298 174 LHAETKM-TVLMVTHQPEDAKRLaQRVVFLDNGRIAAQG 211
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
645-800 |
1.86e-09 |
|
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: 58.32 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTwARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSAlLAEMDKV-EGHVTL--KGSVAYVPQQAWIQND 721
Cdd:cd03223 1 IELENLSLA-TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRA-LAGLWPWgSGRIGMpeGEDLLFLPQRPYLPLG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656469 722 SLRENIlfgrplqehCYkavmeacallpdleilPSGDlteigekgvNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVD 800
Cdd:cd03223 79 TLREQL---------IY----------------PWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1304-1503 |
2.07e-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: 58.60 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1304 LDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHN-LRFKITIIPQDPvlfsgsL 1382
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDR------K 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1383 RMNLdpFSQYSdeeVWMALELAHLkgfvsalpdklnhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 1462
Cdd:cd03215 86 REGL--VLDLS---VAENIALSSL---------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958656469 1463 DDLIQSTIRTQFED-STVLTIAHRLNTIM---DytRVIVLDKGEI 1503
Cdd:cd03215 140 KAEIYRLIRELADAgKAVLLISSELDELLglcD--RILVMYEGRI 182
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
656-802 |
2.16e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.05 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 656 RDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG------------SVAYVPQQAWIQND-S 722
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepirrqrdeyhqDLLYLGHQPGIKTElT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 723 LRENILFGRPLQeHCYKAvmEAC--AL----LPDLEILPSGdlteigekgvNLSGGQKQRVSLARAVYCNSDIYLLDDPL 796
Cdd:PRK13538 91 ALENLRFYQRLH-GPGDD--EALweALaqvgLAGFEDVPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
....*.
gi 1958656469 797 SAVDAH 802
Cdd:PRK13538 158 TAIDKQ 163
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
662-795 |
2.19e-09 |
|
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: 59.61 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS--------------VAYVPQQAWI-QNDSLREN 726
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarlgIGYVPEGRRIfPSLTVEEN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958656469 727 IL---FGRPLQEHCYKAVMEACALLPDLEilpsgdltE-IGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDP 795
Cdd:COG0410 99 LLlgaYARRDRAEVRADLERVYELFPRLK--------ErRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEP 163
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
662-859 |
2.55e-09 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 60.52 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-SVAYVPQQAW----------IQN--DSL--R-- 724
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGqDITGLSGRELrplrrrmqmvFQDpyASLnpRmt 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 725 -ENILfGRPLQEHcykavmeacallpdlEILPSGDLTEIGEK-----GVN----------LSGGQKQRVSLARAVYCNSD 788
Cdd:COG4608 114 vGDII-AEPLRIH---------------GLASKAERRERVAEllelvGLRpehadrypheFSGGQRQRIGIARALALNPK 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 789 IYLLDDPLSAVDAHVGKHI---FEKVVGPMGLlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLDR 859
Cdd:COG4608 178 LIVCDEPVSALDVSIQAQVlnlLEDLQDELGL----TYLFISHDLSVVRHIsDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
662-859 |
2.62e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 60.75 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIQNDSLRENILFGRP--------- 732
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNPygslnprkk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 733 ----LQEhcykavmeacallPdLEILPSGDLTEIGEKG------VNL------------SGGQKQRVSLARAVYCNSDIY 790
Cdd:PRK11308 111 vgqiLEE-------------P-LLINTSLSAAERREKAlammakVGLrpehydryphmfSGGQRQRIAIARALMLDPDVV 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958656469 791 LLDDPLSAVDAHVGKHI---FEKVVGPMGLlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLDR 859
Cdd:PRK11308 177 VADEPVSALDVSVQAQVlnlMMDLQQELGL----SYVFISHDLSVVEHIaDEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1309-1503 |
2.82e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.61 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1309 KHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHN-LRFKITIIPQD---PVLF-SGSLR 1383
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDrqsSGLYlDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1384 MNLDPFSqYSDEEVWM--ALELAHLKGFVSALPDKLNHECAEGGeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1461
Cdd:PRK15439 360 WNVCALT-HNRRGFWIkpARENAVLERYRRALNIKFNHAEQAAR-TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958656469 1462 TDDLIQSTIRTQFEDST-VLTIAHRLNTIMDYT-RVIVLDKGEI 1503
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVaVLFISSDLEEIEQMAdRVLVMHQGEI 481
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
768-852 |
2.95e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 60.58 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 768 NLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIFEkvvgpmgLLK--NK----TRILVTHgisylpQVDVI-- 839
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILE-------LLKdiNRelglTIVLITH------EMDVVkr 206
|
90
....*....|....*...
gi 1958656469 840 -----IVMSGGKISEMGS 852
Cdd:PRK11153 207 icdrvAVIDAGRLVEQGT 224
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
665-857 |
3.03e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 59.47 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 665 ITFAIPDGALVAVVGQVGCGKSSLlSALLAEMDK-------VEGHVTLKGSVAYVPQQawIQ------NDSLRENILFGR 731
Cdd:COG4167 32 VSFTLEAGQTLAIIGENGSGKSTL-AKMLAGIIEptsgeilINGHKLEYGDYKYRCKH--IRmifqdpNTSLNPRLNIGQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 732 ----PL----------QEHCYKAVMEACALLPD-LEILPSgdlteigekgvNLSGGQKQRVSLARAVYCNSDIYLLDDPL 796
Cdd:COG4167 109 ileePLrlntdltaeeREERIFATLRLVGLLPEhANFYPH-----------MLSSGQKQRVALARALILQPKIIIADEAL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958656469 797 SAVDAHVGKHIF-------EKvvgpMGLlknkTRILVTHG------ISylpqvDVIIVMSGGKISEMGSYQELL 857
Cdd:COG4167 178 AALDMSVRSQIInlmlelqEK----LGI----SYIYVSQHlgivkhIS-----DKVLVMHQGEVVEYGKTAEVF 238
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1311-1515 |
3.56e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 61.36 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1311 INVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII----DGINIAKIGLHNL-RFK--ITIIPQDPVLFSGslR 1383
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDGRgRAKryIGILHQEYDLYPH--R 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1384 MNLDPFSQYSDEEvwMALELAHLK--------GF-----VSALpDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILV 1450
Cdd:TIGR03269 381 TVLDNLTEAIGLE--LPDELARMKavitlkmvGFdeekaEEIL-DKYPDE-------LSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656469 1451 LDEATAAVDLETDDLIQSTI---RTQFEDsTVLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSELLQQ 1515
Cdd:TIGR03269 451 LDEPTGTMDPITKVDVTHSIlkaREEMEQ-TFIIVSHDMDFVLDVCdRAALMRDGKIVKIGDPEEIVEE 518
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
1019-1226 |
3.70e-09 |
|
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: 59.75 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1019 ALGILQGVAVFGYSMAVSIGGIFASRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFS 1098
Cdd:cd18551 44 ALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1099 VIGAVI-----------IILLATPIAAVIIPPLGlvyffvQRFYVASSRQLKRLESVSrspvySHFNETLLGVSVIRAFE 1167
Cdd:cd18551 124 VVGAVVlmflldwvltlVTLAVVPLAFLIILPLG------RRIRKASKRAQDALGELS-----AALERALSAIRTVKASN 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 1168 EQERFIRQSDlkvDENQKAYYPSIVANRWLAVrLECVGNcIVLFAALFAVI-------SRHSLSAG 1226
Cdd:cd18551 193 AEERETKRGG---EAAERLYRAGLKAAKIEAL-IGPLMG-LAVQLALLVVLgvggarvASGALTVG 253
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
767-857 |
3.74e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.21 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 767 VNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAH-VGK--HIFEKVVGpmgllKNKTRILVTHGISYLPQVDV-IIVM 842
Cdd:PRK10619 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElVGEvlRIMQQLAE-----EGKTMVVVTHEMGFARHVSShVIFL 225
|
90
....*....|....*
gi 1958656469 843 SGGKISEMGSYQELL 857
Cdd:PRK10619 226 HQGKIEEEGAPEQLF 240
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
1020-1246 |
3.83e-09 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 59.73 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1020 LGILQGVAVFGYSMAVSIGGifASRR----LHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGS 1095
Cdd:cd18541 47 LLLALLIGIFRFLWRYLIFG--ASRRieydLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1096 LFSVIGAVIIILLATP---IAAVIIPPL--GLVYFFVQRFYVASSRQLKRLESVSrspvySHFNETLLGVSVIRAF---- 1166
Cdd:cd18541 125 LFLGVLVLVMMFTISPkltLIALLPLPLlaLLVYRLGKKIHKRFRKVQEAFSDLS-----DRVQESFSGIRVIKAFvqee 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1167 EEQERFIRQSDLKVDENQK------AYYPSIVanrwLAVRLecvGNCIVLFAALFAVIsRHSLSAG-LVglsvsyslQIT 1239
Cdd:cd18541 200 AEIERFDKLNEEYVEKNLRlarvdaLFFPLIG----LLIGL---SFLIVLWYGGRLVI-RGTITLGdLV--------AFN 263
|
....*..
gi 1958656469 1240 AYLNWLV 1246
Cdd:cd18541 264 SYLGMLI 270
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
656-847 |
4.15e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 58.04 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 656 RDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSAL---LAEMDKVEGHVTLKG------------SVAYVPQQAW-IQ 719
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGipykefaekypgEIIYVSEEDVhFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 720 NDSLRENILFGRPLQEHcykavmeacallpdlEILpsgdlteigeKGVnlSGGQKQRVSLARAVYCNSDIYLLDDPLSAV 799
Cdd:cd03233 97 TLTVRETLDFALRCKGN---------------EFV----------RGI--SGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 800 DAHVGKHIFEKvvgpmglLKNKTRILVTHGISYLPQ--------VDVIIVMSGGKI 847
Cdd:cd03233 150 DSSTALEILKC-------IRTMADVLKTTTFVSLYQasdeiydlFDKVLVLYEGRQ 198
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1307-1514 |
4.45e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.46 E-value: 4.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLtLGLF--RINESAE-------GEIIIDGINIAKIGLHNLRFKITIIPQ--DP 1375
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTL-LKALagDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaaQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1376 VL-FSGSLRMNLDPF---------SQYSDEEVWMALELAHLKGFVsalpdklnhecAEGGENLSVGQRQLVCLARAL--- 1442
Cdd:PRK13547 95 AFaFSAREIVLLGRYpharragalTHRDGEIAWQALALAGATALV-----------GRDVTTLSGGELARVQFARVLaql 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1443 ------LRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDST--VLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSELL 1513
Cdd:PRK13547 164 wpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlgVLAIVHDPNLAARHAdRIAMLADGAIVAHGAPADVL 243
|
.
gi 1958656469 1514 Q 1514
Cdd:PRK13547 244 T 244
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
642-860 |
5.18e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.03 E-value: 5.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 642 MNSITVKNATFTwardepptLNGITFAIPD-------------GALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS 708
Cdd:PRK10575 2 QEYTNHSDTTFA--------LRNVSFRVPGrtllhplsltfpaGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 709 -------------VAYVPQQ-AWIQNDSLRENILFGR-P-------LQEHCYKAVMEACALLpdleilpsgDLTEIGEKG 766
Cdd:PRK10575 74 pleswsskafarkVAYLPQQlPAAEGMTVRELVAIGRyPwhgalgrFGAADREKVEEAISLV---------GLKPLAHRL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 767 VN-LSGGQKQRVSLARAVYCNSDIYLLDDPLSAVD-AHVGKHIfeKVVGPMGLLKNKTRILVTHGISYLPQ-VDVIIVMS 843
Cdd:PRK10575 145 VDsLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiAHQVDVL--ALVHRLSQERGLTVIAVLHDINMAARyCDYLVALR 222
|
250
....*....|....*..
gi 1958656469 844 GGKISEMGSYQELLDRD 860
Cdd:PRK10575 223 GGEMIAQGTPAELMRGE 239
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
645-866 |
5.77e-09 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 58.23 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDeppTLNgITFAIPDGALVAVVGQVGCGKSSLLSaLLAEMDKVE-GHVTLKG-SVAYVP--------- 713
Cdd:COG3840 2 LRLDDLTYRYGDF---PLR-FDLTIAAGERVAILGPSGAGKSTLLN-LIAGFLPPDsGRILWNGqDLTALPpaerpvsml 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 714 -QQawiqND-----SLRENILFG-RP---LQEHCYKAVMEACA---LLPDLEILPSgdlteigekgvNLSGGQKQRVSLA 780
Cdd:COG3840 77 fQE----NNlfphlTVAQNIGLGlRPglkLTAEQRAQVEQALErvgLAGLLDRLPG-----------QLSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 781 RAVYCNSDIYLLDDPLSAVDahvgkhifekvvgP------MGLLK------NKTRILVTHGIS-YLPQVDVIIVMSGGKI 847
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALD-------------PalrqemLDLVDelcrerGLTVLMVTHDPEdAARIADRVLLVADGRI 208
|
250 260
....*....|....*....|.
gi 1958656469 848 SEMGSYQELLDRDG--AFAEF 866
Cdd:COG3840 209 AADGPTAALLDGEPppALAAY 229
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1298-1512 |
5.96e-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: 58.15 E-value: 5.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1298 LRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKiGLHNLRFKITIIPQDPVL 1377
Cdd:cd03265 6 LVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1378 fsgslrmnldpfsqysDEEV--WMALEL-AHLKGFVSALPDKLNHECAEGGE----------NLSVGQRQLVCLARALLR 1444
Cdd:cd03265 85 ----------------DDELtgWENLYIhARLYGVPGAERRERIDELLDFVGlleaadrlvkTYSGGMRRRLEIARSLVH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958656469 1445 KTKILVLDEATAAVDLETDDLIQSTIRTQFE--DSTVLTIAHRL---NTIMDytRVIVLDKGEIRECGAPSEL 1512
Cdd:cd03265 149 RPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMeeaEQLCD--RVAIIDHGRIIAEGTPEEL 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
662-849 |
6.13e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 58.93 E-value: 6.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSAL-----------------LAEMDKvEGHVTLKGSVAYVPQQA-------- 716
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLvglespsqgnvswrgepLAKLNR-AQRKAFRRDIQMVFQDSisavnprk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 717 ---WIQNDSLRENILFGRPLQEHCYKAVMEACALLP-DLEILPSgdlteigekgvNLSGGQKQRVSLARAVYCNSDIYLL 792
Cdd:PRK10419 107 tvrEIIREPLRHLLSLDKAERLARASEMLRAVDLDDsVLDKRPP-----------QLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958656469 793 DDPLSAVDAHVGKHIfekvvgpMGLLKNKTR------ILVTHGISYLPQ-VDVIIVMSGGKISE 849
Cdd:PRK10419 176 DEAVSNLDLVLQAGV-------IRLLKKLQQqfgtacLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1314-1491 |
6.37e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 59.59 E-value: 6.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1314 TIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIA---KIGLHNLRFKITIIPQDPVlfsGS--------- 1381
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNPY---GSlnprkkvgq 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1382 -----LRMNLDPFSQYSDEEVWMALELAHLKgfvsalP---DKLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLDE 1453
Cdd:PRK11308 114 ileepLLINTSLSAAERREKALAMMAKVGLR------PehyDRYPHM-------FSGGQRQRIAIARALMLDPDVVVADE 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958656469 1454 ATAAVDLetddliqsTIRTQFedstvltiahrLNTIMD 1491
Cdd:PRK11308 181 PVSALDV--------SVQAQV-----------LNLMMD 199
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
644-856 |
6.60e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 59.07 E-value: 6.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 644 SITVKNATFTWARDEP---PTLNGITFAIPDGALVAVVGQVGCGKSSLL---SALL----AEMDKVEGHVT--------- 704
Cdd:PRK13641 2 SIKFENVDYIYSPGTPmekKGLDNISFELEEGSFVALVGHTGSGKSTLMqhfNALLkpssGTITIAGYHITpetgnknlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 705 -LKGSVAYVPQ--QAWIQNDSLRENILFGrPL------QEHCYKAV--MEACALLPDLeilpsgdlteIGEKGVNLSGGQ 773
Cdd:PRK13641 82 kLRKKVSLVFQfpEAQLFENTVLKDVEFG-PKnfgfseDEAKEKALkwLKKVGLSEDL----------ISKSPFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 774 KQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIFEkvvgpmgLLKN-----KTRILVTHGISYLPQ-VDVIIVMSGGKI 847
Cdd:PRK13641 151 MRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQ-------LFKDyqkagHTVILVTHNMDDVAEyADDVLVLEHGKL 223
|
....*....
gi 1958656469 848 SEMGSYQEL 856
Cdd:PRK13641 224 IKHASPKEI 232
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1318-1504 |
7.11e-09 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 57.69 E-value: 7.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1318 GEKVGIVGRTGAGKSSL---TLGLFRINEsaeGEIIIDGINI----AKIGLHNLRFKITIIPQDPVLFSG-SLRMNL--- 1386
Cdd:cd03297 23 EEVTGIFGASGAGKSTLlrcIAGLEKPDG---GTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFPHlNVRENLafg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1387 -----DPFSQYSDEEVWMALELAHLKGfvsALPDKLnhecaeggenlSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1461
Cdd:cd03297 100 lkrkrNREDRISVDELLDLLGLDHLLN---RYPAQL-----------SGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958656469 1462 TDDLIQSTIRTQFED--STVLTIAHRLNTIMDYT-RVIVLDKGEIR 1504
Cdd:cd03297 166 LRLQLLPELKQIKKNlnIPVIFVTHDLSEAEYLAdRIVVMEDGRLQ 211
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1307-1486 |
7.36e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 58.57 E-value: 7.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEG-----EIIIDGINIAKI-GLHNLRFKITIIPQDPVLFSG 1380
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1381 SLRMN---------LDPFSQYSDEEVWMALELahlkGFVSALPDKLnhecAEGGENLSVGQRQLVCLARALLRKTKILVL 1451
Cdd:PRK14271 116 SIMDNvlagvrahkLVPRKEFRGVAQARLTEV----GLWDAVKDRL----SDSPFRLSGGQQQLLCLARTLAVNPEVLLL 187
|
170 180 190
....*....|....*....|....*....|....*
gi 1958656469 1452 DEATAAVDLETDDLIQSTIRTQFEDSTVLTIAHRL 1486
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNL 222
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1307-1462 |
8.49e-09 |
|
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: 57.83 E-value: 8.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLtLGLFRINESA-EGEIIIDGINIAKI---GLHNLRF-KITIIPQDPVLFsGS 1381
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTL-LGLLAGLDRPtSGTVRLAGQDLFALdedARARLRArHVGFVFQSFQLL-PT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1382 LRMnLdpfsqysdEEVWMALELA-HLKGFVSA--------LPDKLNHECAEggenLSVGQRQLVCLARALLRKTKILVLD 1452
Cdd:COG4181 105 LTA-L--------ENVMLPLELAgRRDARARArallervgLGHRLDHYPAQ----LSGGEQQRVALARAFATEPAILFAD 171
|
170
....*....|
gi 1958656469 1453 EATAAVDLET 1462
Cdd:COG4181 172 EPTGNLDAAT 181
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1306-1502 |
9.53e-09 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 55.53 E-value: 9.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1306 LVLKHINVTIEGGEKVGIVGRTGAGKSSLtlglfrinesaegeiiidginiakiglhnlrfkITIIPQDPVLFSGSLRmn 1385
Cdd:cd03221 14 LLLKDISLTINPGDRIGLVGRNGAGKSTL---------------------------------LKLIAGELEPDEGIVT-- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1386 ldpfsqysdeevWMA-LELAHLkgfvsalpdklnhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDD 1464
Cdd:cd03221 59 ------------WGStVKIGYF-------------------EQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIE 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958656469 1465 LIQSTIRTQfeDSTVLTIAH-R--LNTIMdyTRVIVLDKGE 1502
Cdd:cd03221 108 ALEEALKEY--PGTVILVSHdRyfLDQVA--TKIIELEDGK 144
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
645-863 |
1.08e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 58.56 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDEP---PTLNGITFAIPDGALVAVVGQVGCGKSSL---LSALL--------------------AEMDK 698
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtelKALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALLlpdtgtiewifkdeknkkktKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 699 VEGHVTLKGS--------------VAYVPQQAWIQ--NDSLRENILFGrPLQEHCYKAvmEACALLPDLEILPSGDLTEI 762
Cdd:PRK13651 83 VLEKLVIQKTrfkkikkikeirrrVGVVFQFAEYQlfEQTIEKDIIFG-PVSMGVSKE--EAKKRAAKYIELVGLDESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 763 GEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGK---HIFEKVVgpmglLKNKTRILVTHGI-SYLPQVDV 838
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKeilEIFDNLN-----KQGKTIILVTHDLdNVLEWTKR 234
|
250 260
....*....|....*....|....*
gi 1958656469 839 IIVMSGGKISEMGSYQELLdRDGAF 863
Cdd:PRK13651 235 TIFFKDGKIIKDGDTYDIL-SDNKF 258
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1002-1171 |
1.12e-08 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 58.26 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1002 AVNGTQENRNFRLSVYGALGIL--QGVAVFGYSMAVSIGGIFASRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELD 1079
Cdd:cd18576 25 AALGGGDTASLNQIALLLLGLFllQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1080 TVDSMIPQVIKMFMGSLFSVIGAVIIILLATP----IAAVIIPPLGLVYFFVQRFYVASSRQlkRLESVSRSPVysHFNE 1155
Cdd:cd18576 105 QIQDTLTTTLAEFLRQILTLIGGVVLLFFISWkltlLMLATVPVVVLVAVLFGRRIRKLSKK--VQDELAEANT--IVEE 180
|
170
....*....|....*...
gi 1958656469 1156 TLLGVSVIRAF--EEQER 1171
Cdd:cd18576 181 TLQGIRVVKAFtrEDYEI 198
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
669-844 |
1.16e-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: 57.80 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 669 IPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-SVAYVPQQAWIQNDSLRENILFGRpLQEHCYKAVMEAcal 747
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKADYEGTVRDLLSSI-TKDFYTHPYFKT--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 748 lpdlEILPSGDLTEIGEKGVN-LSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHvGKHIFEKVVGPMGLLKNKTRILV 826
Cdd:cd03237 98 ----EIAKPLQIEQILDREVPeLSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE-QRLMASKVIRRFAENNEKTAFVV 172
|
170 180
....*....|....*....|.
gi 1958656469 827 THGI---SYLpqVDVIIVMSG 844
Cdd:cd03237 173 EHDIimiDYL--ADRLIVFEG 191
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
666-800 |
1.21e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 57.28 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 666 TFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS--VAYVPQQAWI----QNDSL------RENILFG--- 730
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhTTTPPSRRPVsmlfQENNLfshltvAQNIGLGlnp 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958656469 731 ----RPLQEHCYKAVMEACALLPDLEILPSgdlteigekgvNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVD 800
Cdd:PRK10771 99 glklNAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
1021-1248 |
1.28e-08 |
|
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: 58.18 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1021 GILQGVAVFGYSMAVsIGGIFAS-------RRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFM 1093
Cdd:cd18548 43 LLMLLLALLGLIAGI-LAGYFAAkasqgfgRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1094 GSLFSVIGAVIIILLATP----IAAVIIPPLGLVYFFVQRF-YVASSRQLKRLESVSRSpvyshFNETLLGVSVIRAF-- 1166
Cdd:cd18548 122 RAPIMLIGAIIMAFRINPklalILLVAIPILALVVFLIMKKaIPLFKKVQKKLDRLNRV-----VRENLTGIRVIRAFnr 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1167 --EEQERFIrqsdlkvDENQKAYYPSIVANRWLAVR---LECVGN----CIVLFAALFavISRHSLSAG-LVGLsVSYSL 1236
Cdd:cd18548 197 edYEEERFD-------KANDDLTDTSLKAGRLMALLnplMMLIMNlaivAILWFGGHL--INAGSLQVGdLVAF-INYLM 266
|
250
....*....|..
gi 1958656469 1237 QITAYLNWLVRM 1248
Cdd:cd18548 267 QILMSLMMLSMV 278
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1307-1513 |
1.29e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 58.17 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLT--LGLFRINESAEGEIIIDGINIAKIGLHNLRFKITIIPQDP----VLFSG 1380
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIehLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEKLVIQKTrfkkIKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1381 SLRMNLD---PFSQY--------------------SDEEvwmALELAhlKGFVS--ALPDKLnheCAEGGENLSVGQRQL 1435
Cdd:PRK13651 102 EIRRRVGvvfQFAEYqlfeqtiekdiifgpvsmgvSKEE---AKKRA--AKYIElvGLDESY---LQRSPFELSGGQKRR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1436 VCLARALLRKTKILVLDEATAAVDLE-TDDLIQSTIRTQFEDSTVLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSELL 1513
Cdd:PRK13651 174 VALAGILAMEPDFLVFDEPTAGLDPQgVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTkRTIFFKDGKIIKDGDTYDIL 253
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
662-800 |
1.38e-08 |
|
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: 57.17 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG--------------SVAYVPQQAWIQND-SLREN 726
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmhkrarlGIGYLPQEASIFRKlTVEEN 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 727 ILFGRPLQEHCYKAVME-ACALLPDLEILPSGDlteigEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVD 800
Cdd:cd03218 96 ILAVLEIRGLSKKEREEkLEELLEEFHITHLRK-----SKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1308-1501 |
1.67e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.03 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1308 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGlHNLRFK--ITIIPQD-PVLFSGSLRM 1384
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQlgIGIIYQElSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1385 NLdPFSQYSDEEVWMA--LELAHLKGFVSALPDK--LNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAV-D 1459
Cdd:PRK09700 100 NL-YIGRHLTKKVCGVniIDWREMRVRAAMMLLRvgLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtN 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958656469 1460 LETDDLIQSTIRTQFEDSTVLTIAHRLNTIMDY-TRVIVLDKG 1501
Cdd:PRK09700 179 KEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRIcDRYTVMKDG 221
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
662-876 |
1.81e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 57.33 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLL---SALLAEMDKVEGHVTLKGSV------------------AYVPQQAWIQN 720
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLrhlSGLITGDKSAGSHIELLGRTvqregrlardirksrantGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 721 D-SLRENILFG----RPLQEHCYKAvmeacaLLPDLEILPSGDLTEIG------EKGVNLSGGQKQRVSLARAVYCNSDI 789
Cdd:PRK09984 100 RlSVLENVLIGalgsTPFWRTCFSW------FTREQKQRALQALTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 790 YLLDDPLSAVDAHVGKHIFEkVVGPMGLLKNKTRILVTHGISY-LPQVDVIIVMSGGKISEMGSYQElLDRDgAFAEFVR 868
Cdd:PRK09984 174 ILADEPIASLDPESARIVMD-TLRDINQNDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQ-FDNE-RFDHLYR 250
|
....*...
gi 1958656469 869 TYANTEQD 876
Cdd:PRK09984 251 SINRVEEN 258
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
662-860 |
2.29e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 57.51 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS------------VAYVPQQAWIQND-SLRENIL 728
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharqrVGVVPQFDNLDPDfTVRENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 729 -FGRplqeHCYKAVMEACALLPDLeiLPSGDLTEIGEKGV-NLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKH 806
Cdd:PRK13537 103 vFGR----YFGLSAAAARALVPPL--LEFAKLENKADAKVgELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 807 IFEKVVGPMGllKNKTRILVTHGISYLPQV--DVIIVMSGGKISEmGSYQELLDRD 860
Cdd:PRK13537 177 MWERLRSLLA--RGKTILLTTHFMEEAERLcdRLCVIEEGRKIAE-GAPHALIESE 229
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
662-851 |
2.48e-08 |
|
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: 55.41 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEmdkvEGHVTLKGSVAYVPQQAWIQNDSLRENILFGrplqehcykav 741
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----SGKARLISFLPKFSRNKLIFIDQLQFLIDVG----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 742 meacallpdLEILPsgdlteIGEKGVNLSGGQKQRVSLARAVYCNSD--IYLLDDPLSAVDaHVGKHIFEKVVGPMGLLK 819
Cdd:cd03238 76 ---------LGYLT------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH-QQDINQLLEVIKGLIDLG 139
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958656469 820 NkTRILVTHGISYLPQVDVIIVM------SGGKISEMG 851
Cdd:cd03238 140 N-TVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
662-863 |
3.39e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.98 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSlLSALLAEMD-KVEGHVTLKGSVAYVPQQAWIQND-SLRENILFgrplqehcyK 739
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKST-LSNLIAGVTmPNKGTVDIKGSAALIAISSGLNGQlTGIENIEL---------K 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 740 AVMEACALLPDLEILPSG-DLTEIGeKGVN-----LSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIFEKvvg 813
Cdd:PRK13545 110 GLMMGLTKEKIKEIIPEIiEFADIG-KFIYqpvktYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDK--- 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 814 pMGLLKN--KTRILVTHGISylpQVDVI----IVMSGGKISEMGSYQELLDRDGAF 863
Cdd:PRK13545 186 -MNEFKEqgKTIFFISHSLS---QVKSFctkaLWLHYGQVKEYGDIKEVVDHYDEF 237
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1307-1459 |
3.66e-08 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 55.90 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIID----GINIAKIG---LHNLRfKITI--------- 1370
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASpreILALR-RRTIgyvsqflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1371 IPQ--------DPVLFSGslrmnldpfsqYSDEEvwmALE-----LAHLKgfvsaLPDKLNHecaeggenL-----SVGQ 1432
Cdd:COG4778 105 IPRvsaldvvaEPLLERG-----------VDREE---ARArarelLARLN-----LPERLWD--------LppatfSGGE 157
|
170 180
....*....|....*....|....*..
gi 1958656469 1433 RQLVCLARALLRKTKILVLDEATAAVD 1459
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLD 184
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1297-1466 |
3.88e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.98 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1297 CLRYRED--LDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG-------------- 1360
Cdd:PRK11629 12 CKRYQEGsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaakaelrnqklgf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1361 ---LHNLRFKITIIPQD--PVLFSGSLRMNldpfSQYSDEEVWMALELAHlkgfvsalpdKLNHECAEggenLSVGQRQL 1435
Cdd:PRK11629 92 iyqFHHLLPDFTALENVamPLLIGKKKPAE----INSRALEMLAAVGLEH----------RANHRPSE----LSGGERQR 153
|
170 180 190
....*....|....*....|....*....|.
gi 1958656469 1436 VCLARALLRKTKILVLDEATAAVDLETDDLI 1466
Cdd:PRK11629 154 VAIARALVNNPRLVLADEPTGNLDARNADSI 184
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
662-828 |
3.95e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.98 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVTLKGSVayVPQQAWIQNDSLRENILfGRPLQEHcyka 740
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLH-LLGGLDTpTSGDVIFNGQP--MSKLSSAAKAELRNQKL-GFIYQFH---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 741 vmeacALLPD-------------------------LEILPSGDLTEIGE-KGVNLSGGQKQRVSLARAVYCNSDIYLLDD 794
Cdd:PRK11629 97 -----HLLPDftalenvamplligkkkpaeinsraLEMLAAVGLEHRANhRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190
....*....|....*....|....*....|....
gi 1958656469 795 PLSAVDAHVGKHIFEkVVGPMGLLKNKTRILVTH 828
Cdd:PRK11629 172 PTGNLDARNADSIFQ-LLGELNRLQGTAFLVVTH 204
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1307-1503 |
4.90e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 57.81 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHNL----RFKITIIPQDPVLFSG-S 1381
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1382 LRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1461
Cdd:PRK10535 103 AAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQ----LSGGQQQRVSIARALMNGGQVILADEPTGALDSH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958656469 1462 TDDLIQSTIRtQFEDS--TVLTIAHRLNTIMDYTRVIVLDKGEI 1503
Cdd:PRK10535 179 SGEEVMAILH-QLRDRghTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
1015-1170 |
4.96e-08 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 56.37 E-value: 4.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1015 SVYGALG---ILQGVAVFGYSMAVSIGGIFASRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKM 1091
Cdd:cd18573 42 TFALALLgvfVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1092 FMGSLFSVIGAVIIILLATP----IAAVIIPPLGLVYFFVQRFYVASSRQLkrLESVSRSpvySHF-NETLLGVSVIRAF 1166
Cdd:cd18573 122 GLRSLVSGVGGIGMMLYISPkltlVMLLVVPPIAVGAVFYGRYVRKLSKQV--QDALADA---TKVaEERLSNIRTVRAF 196
|
....*.
gi 1958656469 1167 --EEQE 1170
Cdd:cd18573 197 aaERKE 202
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1016-1261 |
5.22e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 56.33 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1016 VYGALGILQGVAVFGYSMAVSIGGIFASRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGS 1095
Cdd:cd18540 47 LYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1096 LFSVIGAVIIILLATP----IAAVIIPPLGLVYFFVQRFYVASSRQLKRLESVsrspVYSHFNETLLGVSVIRAF--EEQ 1169
Cdd:cd18540 127 ITYMIGILIVMLILNWklalIVLAVVPVLAVVSIYFQKKILKAYRKVRKINSR----ITGAFNEGITGAKTTKTLvrEEK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1170 --ERFirqsdLKVDENQKAYypSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLV---GLSV--SYSLQITAYL 1242
Cdd:cd18540 203 nlREF-----KELTEEMRRA--SVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAItigTLVAfiSYATQFFEPI 275
|
250
....*....|....*....
gi 1958656469 1243 NWLVRMSSEMETNIVAVER 1261
Cdd:cd18540 276 QQLARVLAELQSAQASAER 294
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1308-1489 |
5.23e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.53 E-value: 5.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1308 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRI--NESAEGEIIIDGINIAKIGLHNLRFK-ITIIPQDPVLFSgslrm 1384
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVP----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1385 NLDPFsqysdEEVWMALELAHlKGFVSALPdKLNHECAEGGENLSV--------------GQRQLVCLARALLRKTKILV 1450
Cdd:TIGR02633 92 ELSVA-----ENIFLGNEITL-PGGRMAYN-AMYLRAKNLLRELQLdadnvtrpvgdyggGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958656469 1451 LDEATAAV-DLETDDLIQSTIRTQFEDSTVLTIAHRLNTI 1489
Cdd:TIGR02633 165 LDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEV 204
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
1014-1165 |
6.56e-08 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 56.06 E-value: 6.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1014 LSVYGAlgILQGVAVF--GYSMAVSIGGIFASRRLHLDLLQNV----LRSPMSFFERTPSGNLVNRFSkELDTV-DSMIP 1086
Cdd:cd18782 41 LYVIGV--VMLVAALLeaVLTALRTYLFTDTANRIDLELGGTIidhlLRLPLGFFDKRPVGELSTRIS-ELDTIrGFLTG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1087 QVIKMFMGSLFSVIGAVIIILLATPIAAVI---IPPLGLVYFFVQRFYvasSRQLKRLESvSRSPVYSHFNETLLGVSVI 1163
Cdd:cd18782 118 TALTTLLDVLFSVIYIAVLFSYSPLLTLVVlatVPLQLLLTFLFGPIL---RRQIRRRAE-ASAKTQSYLVESLTGIQTV 193
|
..
gi 1958656469 1164 RA 1165
Cdd:cd18782 194 KA 195
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
1022-1185 |
7.22e-08 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 56.01 E-value: 7.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1022 ILQGVAVFGYSMAVSIGGIFASRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIG 1101
Cdd:cd18574 53 LLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1102 AVIIILLATP----IAAVIIPPLGLVYFFVQRFYVASSRQLKRLESVSRspvySHFNETLLGVSVIRAF----EEQERFI 1173
Cdd:cd18574 133 CVVSLYLISPkltlLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKAT----GVADEALGNIRTVRAFamedRELELYE 208
|
170
....*....|..
gi 1958656469 1174 RQSDLKVDENQK 1185
Cdd:cd18574 209 EEVEKAAKLNEK 220
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1006-1261 |
8.53e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 55.59 E-value: 8.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1006 TQENRNFRLsVYGALGILQGVAVFGYSMAVSIGGIFA------SRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELD 1079
Cdd:cd18563 33 LGPGGNTSL-LLLLVLGLAGAYVLSALLGILRGRLLArlgeriTADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1080 TVDSMIPQVIKMFMGSLFSVIGAVIIIL-----LAtpiAAVIIP-PL--GLVYFFVQRFYVASSRQLKRlesvsRSPVYS 1151
Cdd:cd18563 112 RLQDFLSDGLPDFLTNILMIIGIGVVLFslnwkLA---LLVLIPvPLvvWGSYFFWKKIRRLFHRQWRR-----WSRLNS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1152 HFNETLLGVSVIRAF----EEQERFIRQSDLKVDENQKA------YYPSIVAnrwlavrLECVGNCIVLFAALFAVISRH 1221
Cdd:cd18563 184 VLNDTLPGIRVVKAFgqekREIKRFDEANQELLDANIRAeklwatFFPLLTF-------LTSLGTLIVWYFGGRQVLSGT 256
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1958656469 1222 sLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVER 1261
Cdd:cd18563 257 -MTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAER 295
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
643-898 |
1.02e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 55.24 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 643 NSITVKNATFTWArDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIQnds 722
Cdd:PRK13636 4 YILKVEELNYNYS-DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMK--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 723 LRENI--LFGRPLQEHCYKAVMEACAL------LPDLEI-------LPSGDLTEIGEKGVN-LSGGQKQRVSLARAVYCN 786
Cdd:PRK13636 80 LRESVgmVFQDPDNQLFSASVYQDVSFgavnlkLPEDEVrkrvdnaLKRTGIEHLKDKPTHcLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 787 SDIYLLDDPLSAVDAHVGKHIFEKVVG---PMGLlknkTRILVTHGISYLP-QVDVIIVMSGGK------ISEMGSYQEL 856
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEmqkELGL----TIIIATHDIDIVPlYCDNVFVMKEGRvilqgnPKEVFAEKEM 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1958656469 857 -------LDRDGAFAEFVRT---YANTEQDLaseddSVSGLGKESKPVENGI 898
Cdd:PRK13636 236 lrkvnlrLPRIGHLMEILKEkdgFVFDELDL-----TISQARKTLNSWKNKI 282
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1307-1512 |
1.03e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 55.86 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLtlglFRI----NESAEGEIIIDGINIA-------KIG--------------L 1361
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTL----LRIiaglEHQTSGHIRFHGTDVSrlhardrKVGfvfqhyalfrhmtvF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1362 HNLRFKITIIPQDPvlfsgslrmnlDPFSQYSDEEVWMALELAHLKGFVSALPDKLnhecaeggenlSVGQRQLVCLARA 1441
Cdd:PRK10851 93 DNIAFGLTVLPRRE-----------RPNAAAIKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958656469 1442 LLRKTKILVLDEATAAVDLETDDLIQSTIRTQFED--STVLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSEL 1512
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElkFTSVFVTHDQEEAMEVAdRVVVMSQGNIEQAGTPDQV 224
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
659-859 |
1.07e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 54.71 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 659 PPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALL----AEMDKVEGHVTLKGsVAYVPQQ------AWI-QN------- 720
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALgilpAGVRQTAGRVLLDG-KPVAPCAlrgrkiATImQNprsafnp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 721 -----DSLRENIL-FGRPLQEHCYKAVMEACALLPDLEILPSgdlteigeKGVNLSGGQKQRVSLARAVYCNSDIYLLDD 794
Cdd:PRK10418 95 lhtmhTHARETCLaLGKPADDATLTAALEAVGLENAARVLKL--------YPFEMSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958656469 795 PLSAVDAHVGKHIF---EKVV---GPmGLLknktriLVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLDR 859
Cdd:PRK10418 167 PTTDLDVVAQARILdllESIVqkrAL-GML------LVTHDMGVVARLaDDVAVMSHGRIVEQGDVETLFNA 231
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
672-844 |
1.35e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 672 GALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQqaWIQNDS-------LRENilfGRPLQEHCYKAvmea 744
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQ--YIKPDYdgtvedlLRSI---TDDLGSSYYKS---- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 745 callpdlEILPSGDLTEIGEKGVN-LSGGQKQRVSLARAVYCNSDIYLLDDPLSAVD-------AHVGKHIFEKvvgpmg 816
Cdd:PRK13409 436 -------EIIKPLQLERLLDKNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAIRRIAEE------ 502
|
170 180 190
....*....|....*....|....*....|.
gi 1958656469 817 llKNKTRILVTHGIS---YLpqVDVIIVMSG 844
Cdd:PRK13409 503 --REATALVVDHDIYmidYI--SDRLMVFEG 529
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
662-878 |
1.44e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.33 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG--SVAYVPQ------------------------- 714
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwQLAWVNQetpalpqpaleyvidgdreyrqlea 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 715 ---QAWIQNDSLRENILFGRPLQEHCYKAVMEACALLPDLeilpsGDLTEIGEKGV-NLSGGQKQRVSLARAVYCNSDIY 790
Cdd:PRK10636 97 qlhDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGL-----GFSNEQLERPVsDFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 791 LLDDPLSAVDahvgkhiFEKVVGPMGLLKN--KTRILVTHGISYL-PQVDVIIVMSGGKISE-MGSYQEL-LDRDGAFAE 865
Cdd:PRK10636 172 LLDEPTNHLD-------LDAVIWLEKWLKSyqGTLILISHDRDFLdPIVDKIIHIEQQSLFEyTGNYSSFeVQRATRLAQ 244
|
250
....*....|...
gi 1958656469 866 FVRTYANTEQDLA 878
Cdd:PRK10636 245 QQAMYESQQERVA 257
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1318-1504 |
1.83e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.71 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1318 GEKVGIVGRTGAGKSSLTLGLFRINESA-EGEIIIDGiniAKIGLHN----LRFKITIIPQD-------PVLFSG--SLR 1383
Cdd:PRK13549 288 GEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDG---KPVKIRNpqqaIAQGIAMVPEDrkrdgivPVMGVGknITL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1384 MNLDPFSQYS--DEevwmALELAHLKGFVSALPDKLNHECAEGGeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDL- 1460
Cdd:PRK13549 365 AALDRFTGGSriDD----AAELKTILESIQRLKVKTASPELAIA-RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVg 439
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958656469 1461 ---ETDDLIQSTIRtqfEDSTVLTIAHRLNTIMDYT-RVIVLDKGEIR 1504
Cdd:PRK13549 440 akyEIYKLINQLVQ---QGVAIIVISSELPEVLGLSdRVLVMHEGKLK 484
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1019-1186 |
2.03e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 54.77 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1019 ALGILQGVAVFGYSMAVSIGGIFASRRLHLDLLQNVLRSPMSFFERTP--SGNLVNRFSKELDTVDSMIPQVIKMFMGSL 1096
Cdd:cd18578 60 VLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLILQAI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1097 FSVIGAVIIILLA----TPIAAVIIPPLGLVYFFVQRFYVASSRQLKR-LESVSRspvysHFNETLLGVSVIRAFEEQER 1171
Cdd:cd18578 140 VTLVAGLIIAFVYgwklALVGLATVPLLLLAGYLRMRLLSGFEEKNKKaYEESSK-----IASEAVSNIRTVASLTLEDY 214
|
170
....*....|....*
gi 1958656469 1172 FIRQSDLKVDENQKA 1186
Cdd:cd18578 215 FLEKYEEALEEPLKK 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
662-860 |
2.41e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 54.47 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEM----------DKVEGHVTLKGSVAYVPQQAWIQN----------- 720
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIkskygtiqvgDIYIGDKKNNHELITNPYSKKIKNfkelrrrvsmv 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 721 ----------DSLRENILFGrP--LQEHCYKAVMEACALL-------PDLEILPSGdlteigekgvnLSGGQKQRVSLAR 781
Cdd:PRK13631 122 fqfpeyqlfkDTIEKDIMFG-PvaLGVKKSEAKKLAKFYLnkmglddSYLERSPFG-----------LSGGQKRRVAIAG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 782 AVYCNSDIYLLDDPLSAVDAHvGKHIFekvvgpMGLLK-----NKTRILVTHGISYLPQV-DVIIVMSGGKISEMGS-YQ 854
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPK-GEHEM------MQLILdakanNKTVFVITHTMEHVLEVaDEVIVMDKGKILKTGTpYE 262
|
....*.
gi 1958656469 855 ELLDRD 860
Cdd:PRK13631 263 IFTDQH 268
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1307-1453 |
3.15e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 53.34 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINI-----AKIglhnLRFKITIIPQDPVLFSgs 1381
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdwqtAKI----MREAVAIVPEGRRVFS-- 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 1382 lRMNLDpfsqysdEEVWMALELAHLKGF------VSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDE 1453
Cdd:PRK11614 94 -RMTVE-------ENLAMGGFFAERDQFqerikwVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
662-847 |
3.22e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 53.55 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-SVAYVPQQ---AWI----QNDSL--------RE 725
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkDVTKLPEYkraKYIgrvfQDPMMgtapsmtiEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 726 NIL----------FGRPLQEHCYKAVMEACALLpdleilpsgDL-------TEIGekgvNLSGGQKQRVSLARAVYCNSD 788
Cdd:COG1101 102 NLAlayrrgkrrgLRRGLTKKRRELFRELLATL---------GLglenrldTKVG----LLSGGQRQALSLLMATLTKPK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 789 IYLLDDPLSAVDAHVGKHIFE---KVVGPMGLlknkTRILVTH----GISYlpqVDVIIVMSGGKI 847
Cdd:COG1101 169 LLLLDEHTAALDPKTAALVLElteKIVEENNL----TTLMVTHnmeqALDY---GNRLIMMHEGRI 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1307-1459 |
3.24e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 54.64 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--INI--------AKIGL-------------HN 1363
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIrsprdairAGIAYvpedrkgeglvldLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1364 LRFKITIipqdPVLFSGSLRMNLDPfsqysdeevwmALELAHLKGFVSAL---PDKLNHECAeggeNLSVGQRQLVCLAR 1440
Cdd:COG1129 347 IRENITL----ASLDRLSRGGLLDR-----------RRERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAK 407
|
170
....*....|....*....
gi 1958656469 1441 ALLRKTKILVLDEATAAVD 1459
Cdd:COG1129 408 WLATDPKVLILDEPTRGID 426
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1308-1515 |
3.45e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 53.94 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1308 LKHINVTIEGGEKVGIVGRTGAGKSS----LTlGLfrINESAeGEIIIDGINIAKIGLHNLRfKITII------------ 1371
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTtikmLT-GI--LVPTS-GEVRVLGYVPFKRRKEFAR-RIGVVfgqrsqlwwdlp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1372 PQDpvlfsgSLRMN-----LDP--FSQYSDEEVWMaLELAH-LKGFVsalpdklnhecaeggENLSVGQRQLVCLARALL 1443
Cdd:COG4586 113 AID------SFRLLkaiyrIPDaeYKKRLDELVEL-LDLGElLDTPV---------------RQLSLGQRMRCELAAALL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 1444 RKTKILVLDEATAAVDLETDDLIQSTIRT--QFEDSTVLTIAHRLNTIMDY-TRVIVLDKGEIRECGAPSELLQQ 1515
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEALcDRVIVIDHGRIIYDGSLEELKER 245
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
654-861 |
3.83e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 53.47 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 654 WAR-DEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIqndSLRENI--LFG 730
Cdd:PRK13638 8 WFRyQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLL---ALRQQVatVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 731 RPLQEHCYKAVMEACAL------LPDLEILPSGD--LTEIGEKGVN------LSGGQKQRVSLARAVYCNSDIYLLDDPL 796
Cdd:PRK13638 85 DPEQQIFYTDIDSDIAFslrnlgVPEAEITRRVDeaLTLVDAQHFRhqpiqcLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 797 SAVDAhVGK----HIFEKVVGpmgllKNKTRILVTHGISYLPQV-DVIIVMSGGKI------SEMGSYQELLDRDG 861
Cdd:PRK13638 165 AGLDP-AGRtqmiAIIRRIVA-----QGNHVIISSHDIDLIYEIsDAVYVLRQGQIlthgapGEVFACTEAMEQAG 234
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
653-800 |
4.62e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.16 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 653 TWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS----------VAYVPQQAWIQND- 721
Cdd:PRK13543 18 AFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsrfMAYLGHLPGLKADl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 722 SLRENILFGRPLqeHCYKAvmeacallpdlEILPSGDLTEIGEKGV------NLSGGQKQRVSLARAVYCNSDIYLLDDP 795
Cdd:PRK13543 98 STLENLHFLCGL--HGRRA-----------KQMPGSALAIVGLAGYedtlvrQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
....*
gi 1958656469 796 LSAVD 800
Cdd:PRK13543 165 YANLD 169
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
647-875 |
4.77e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.41 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 647 VKNATftwaRDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS--------------VAYV 712
Cdd:PRK09700 268 VRNVT----SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprspldavkkgMAYI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 713 PQQ----AWIQNDSLRENILFGRPLQEHCYKAVM----------EACALLPDLEILPSGDLTEIGEkgvnLSGGQKQRVS 778
Cdd:PRK09700 344 TESrrdnGFFPNFSIAQNMAISRSLKDGGYKGAMglfhevdeqrTAENQRELLALKCHSVNQNITE----LSGGNQQKVL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 779 LARAVYCNSDIYLLDDPLSAVDAHVGKHIFeKVvgpMGLLKN--KTRILVThgiSYLPQV----DVIIVMSGGKISemgs 852
Cdd:PRK09700 420 ISKWLCCCPEVIIFDEPTRGIDVGAKAEIY-KV---MRQLADdgKVILMVS---SELPEIitvcDRIAVFCEGRLT---- 488
|
250 260
....*....|....*....|...
gi 1958656469 853 yQELLDRDGAFAEFVRTYANTEQ 875
Cdd:PRK09700 489 -QILTNRDDMSEEEIMAWALPQE 510
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1428-1512 |
5.50e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 53.32 E-value: 5.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1428 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD-DLIQSTIRTQFEDSTVLTIAHRLNTIMDYT-RVIVLDKGEIRE 1505
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEhEMMQLILDAKANNKTVFVITHTMEHVLEVAdEVIVMDKGKILK 256
|
....*..
gi 1958656469 1506 CGAPSEL 1512
Cdd:PRK13631 257 TGTPYEI 263
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
662-851 |
7.19e-07 |
|
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: 51.60 E-value: 7.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-SVAYVPQQAW----IQND--------SLRENIL 728
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARrrlgFVSDstglydrlTARENLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 729 -FGR--PLQEHCYKAVMEACALLPDLEILpsgdlteIGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGK 805
Cdd:cd03266 101 yFAGlyGLKGDELTARLEELADRLGMEEL-------LDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATR 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958656469 806 HIFE-----KVVGpmgllknKTRILVTHGISYLPQV-DVIIVMSGGKISEMG 851
Cdd:cd03266 174 ALREfirqlRALG-------KCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
645-875 |
7.86e-07 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 53.65 E-value: 7.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWarDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSAL--LAEMDKVEG----HVTLKGSVAYVPQQA-- 716
Cdd:TIGR03269 1 IEVKNLTKKF--DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGriiyHVALCEKCGYVERPSkv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 717 ------------------WIQNDSLRENI-------------LFG---------RPLQEHCY---KAVMEACALLPDLEI 753
Cdd:TIGR03269 79 gepcpvcggtlepeevdfWNLSDKLRRRIrkriaimlqrtfaLYGddtvldnvlEALEEIGYegkEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 754 lpSGDLTEIGEkgvNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIFEKVVGpmGLLKNKTRILVThgiSYL 833
Cdd:TIGR03269 159 --SHRITHIAR---DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEE--AVKASGISMVLT---SHW 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958656469 834 PQV-----DVIIVMSGGKISEMGSYQELLDRDGAFAEFVRTYANTEQ 875
Cdd:TIGR03269 229 PEViedlsDKAIWLENGEIKEEGTPDEVVAVFMEGVSEVEKECEVEV 275
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1286-1485 |
8.74e-07 |
|
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: 53.60 E-value: 8.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1286 PHSGRVEFRDYCLRYrEDLDLV-------LKHINVTIEGGEKVGIVGRTGAGKSSLtlglFRInesaEGEII-IDGINIA 1357
Cdd:TIGR00954 440 PGRGIVEYQDNGIKF-ENIPLVtpngdvlIESLSFEVPSGNNLLICGPNGCGKSSL----FRI----LGELWpVYGGRLT 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1358 KiglhNLRFKITIIPQDPVLFSGSLR------MNLDPFSQ--YSDEEVWMALELAHLKGFVSAlpdklnhecaEGG---- 1425
Cdd:TIGR00954 511 K----PAKGKLFYVPQRPYMTLGTLRdqiiypDSSEDMKRrgLSDKDLEQILDNVQLTHILER----------EGGwsav 576
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958656469 1426 ----ENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQfeDSTVLTIAHR 1485
Cdd:TIGR00954 577 qdwmDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHR 638
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1027-1191 |
9.53e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 52.57 E-value: 9.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1027 AVFGYSMAVSIGGiFASRRLH---LDLLQNVLRSPMSFFERTPSGNL-------VNRFSKELDTvdsMIPQVIKMFmgSL 1096
Cdd:cd18565 68 SLFQYLSGVLWRR-FAQRVQHdlrTDTYDHVQRLDMAFFEDRQTGDLmsvlnndVNQLERFLDD---GANSIIRVV--VT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1097 FSVIGAVIIIL---LATpIAAVIIPPL-GLVYFFVQRfyvASSRQLKRLESVSRspVYSHFNETLLGVSVIRAF----EE 1168
Cdd:cd18565 142 VLGIGAILFYLnwqLAL-VALLPVPLIiAGTYWFQRR---IEPRYRAVREAVGD--LNARLENNLSGIAVIKAFtaedFE 215
|
170 180
....*....|....*....|....*....
gi 1958656469 1169 QERFIRQSDLKVDENQKA------YYPSI 1191
Cdd:cd18565 216 RERVADASEEYRDANWRAirlraaFFPVI 244
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1308-1489 |
1.04e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.99 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1308 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGiniakiglHNLRFK---------ITIIPQDpvlf 1378
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG--------QEMRFAsttaalaagVAIIYQE---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1379 sgslrMNLDPfsQYSDEEVWMALELAHLKGFV--SALPDKLNHECAEGGEN---------LSVGQRQLVCLARALLRKTK 1447
Cdd:PRK11288 88 -----LHLVP--EMTVAENLYLGQLPHKGGIVnrRLLNYEAREQLEHLGVDidpdtplkyLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958656469 1448 ILVLDEATAAVDL-ETDDLIQSTIRTQFEDSTVLTIAHRLNTI 1489
Cdd:PRK11288 161 VIAFDEPTSSLSArEIEQLFRVIRELRAEGRVILYVSHRMEEI 203
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
662-859 |
1.09e-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: 50.99 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMD-KV-EGHVTLKGsvayvpqqawiqndslrENILFgRPLQEHCYK 739
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyEVtEGEILFKG-----------------EDITD-LPPEERARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 740 AVMEACALLPDLEILPSGDLteIGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIFEKVvgpMGLL- 818
Cdd:cd03217 78 GIFLAFQYPPEIPGVKNADF--LRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVI---NKLRe 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958656469 819 KNKTRILVTH--GISYLPQVDVIIVMSGGKISEMGSyQELLDR 859
Cdd:cd03217 153 EGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELALE 194
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
660-811 |
1.24e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.72 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 660 PTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS------VAYVPQQAWIQNDS-------LREN 726
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlCTYQKQLCFVGHRSginpyltLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 727 ILFgrplQEHCYKAVMEACAL-----LPDLEILPSGdlteigekgvNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDA 801
Cdd:PRK13540 95 CLY----DIHFSPGAVGITELcrlfsLEHLIDYPCG----------LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170
....*....|
gi 1958656469 802 HVGKHIFEKV 811
Cdd:PRK13540 161 LSLLTIITKI 170
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
583-860 |
1.39e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.05 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 583 AFVSLALFnILRFPL----NILPMVISsivqASVSLKRLRIFlsheELEPDSIERWSIKDGGGMNSITVKNATFTWArDE 658
Cdd:PRK10522 266 ATYSLTLL-FLRTPLlsavGALPTLLS----AQVAFNKLNKL----ALAPYKAEFPRPQAFPDWQTLELRNVTFAYQ-DN 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 659 PPTLNGITFAIPDGALVAVVGQVGCGKSSLlSALLAEMDK-VEGHVTLKGS-VAYVPQQAWIQNDS--LRENILFGRPLQ 734
Cdd:PRK10522 336 GFSVGPINLTIKRGELLFLIGGNGSGKSTL-AMLLTGLYQpQSGEILLDGKpVTAEQPEDYRKLFSavFTDFHLFDQLLG 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 735 EHCYKAVMEACALLpdLEILPSGDLTEIGEKGV---NLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVgKHIFEKV 811
Cdd:PRK10522 415 PEGKPANPALVEKW--LERLKMAHKLELEDGRIsnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF-RREFYQV 491
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1958656469 812 VGPMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEM-GSYQELLDRD 860
Cdd:PRK10522 492 LLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSELtGEERDAASRD 541
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
672-844 |
1.41e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.86 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 672 GALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQqaWIQNDS-------LRENIlfGRPLQEHCYKAvmea 744
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQ--YISPDYdgtveefLRSAN--TDDFGSSYYKT---- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 745 callpdlEILPSGDLTEIGEKGV-NLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVD-------AHVGKHIFEKvvgpmg 816
Cdd:COG1245 438 -------EIIKPLGLEKLLDKNVkDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAIRRFAEN------ 504
|
170 180
....*....|....*....|....*....
gi 1958656469 817 llKNKTRILVTHGISYLPQV-DVIIVMSG 844
Cdd:COG1245 505 --RGKTAMVVDHDIYLIDYIsDRLMVFEG 531
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
642-860 |
1.46e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 51.73 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 642 MNSITVKNATFTWARDEPpTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS------------- 708
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 709 VAYVPQQA--WIQNDSLRENILFGrPL-----QEHCYKAVMEACALLpdleilpsgDLTEIGEKGVN-LSGGQKQRVSLA 780
Cdd:PRK13652 80 VGLVFQNPddQIFSPTVEQDIAFG-PInlgldEETVAHRVSSALHML---------GLEELRDRVPHhLSGGEKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 781 RAVYCNSDIYLLDDPLSAVDAHVGKHIFeKVVGPMGLLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLDR 859
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDPQGVKELI-DFLNDLPETYGMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEIFLQ 228
|
.
gi 1958656469 860 D 860
Cdd:PRK13652 229 P 229
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1308-1503 |
1.49e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.03 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1308 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLfrinesaEGEIIIDG--INIAKiglhnlRFKITIIPQDP------VLFS 1379
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDgrIIYEQ------DLIVARLQQDPprnvegTVYD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1380 ---------GSL-----RMNLDPFSQYSDEevwMALELAHLKGFVS-----ALPDKLNHECAEGGEN-------LSVGQR 1433
Cdd:PRK11147 86 fvaegieeqAEYlkryhDISHLVETDPSEK---NLNELAKLQEQLDhhnlwQLENRINEVLAQLGLDpdaalssLSGGWL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958656469 1434 QLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTqFEDSTVLtIAHRLNTI--MdYTRVIVLDKGEI 1503
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT-FQGSIIF-ISHDRSFIrnM-ATRIVDLDRGKL 231
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
662-828 |
1.84e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 50.55 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-----------------SVAYVPQQ-AWIQNDSL 723
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqmdeearaklrakHVGFVFQSfMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 724 RENILFGRPLQ-EHCYKAVMEACALLPDLEI------LPSgdlteigekgvNLSGGQKQRVSLARAVYCNSDIYLLDDPL 796
Cdd:PRK10584 106 LENVELPALLRgESSRQSRNGAKALLEQLGLgkrldhLPA-----------QLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180 190
....*....|....*....|....*....|..
gi 1958656469 797 SAVDAHVGKHIFEkVVGPMGLLKNKTRILVTH 828
Cdd:PRK10584 175 GNLDRQTGDKIAD-LLFSLNREHGTTLILVTH 205
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
1045-1262 |
1.87e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 51.43 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1045 RLHLDLLQNVLRSPMSFFERTPSGNLVNRFsKELDTV-DSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAViipPLGLV 1123
Cdd:cd18566 76 RLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIrEFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLV---PLVLL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1124 YFFVQRFYVASSRQLKRLESVSRSPV--YSHFNETLLGVSVIR--AFEEQ--ERFIRQSDLKVDENQKAYYPSIVANRWL 1197
Cdd:cd18566 152 GLFVLVAILLGPILRRALKERSRADErrQNFLIETLTGIHTIKamAMEPQmlRRYERLQANAAYAGFKVAKINAVAQTLG 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 1198 AVRLECVGNCIVLFAALFaVISrHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERL 1262
Cdd:cd18566 232 QLFSQVSMVAVVAFGALL-VIN-GDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQQVRVAVRRL 294
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1046-1192 |
1.97e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 51.38 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1046 LHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPI-AAVIIPPLGLVY 1124
Cdd:cd18778 75 LRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKlALLTLIPIPFLA 154
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 1125 FFVqRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAF----EEQERFIRQSDLKVDENQKA------YYPSIV 1192
Cdd:cd18778 155 LGA-WLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFgreeEEAKRFEALSRRYRKAQLRAmklwaiFHPLME 231
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
662-828 |
2.37e-06 |
|
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: 49.97 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS---------VAYVPQQAWI-QNDSLRENILF-- 729
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarnrIGYLPEERGLyPKMKVIDQLVYla 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 730 ---GRPLQEhcykavmeacALLPDLEILPSGDLTEIGEKGVN-LSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAhVGK 805
Cdd:cd03269 96 qlkGLKKEE----------ARRRIDEWLERLELSEYANKRVEeLSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNV 164
|
170 180
....*....|....*....|....
gi 1958656469 806 HIFEKVVgpMGLL-KNKTRILVTH 828
Cdd:cd03269 165 ELLKDVI--RELArAGKTVILSTH 186
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
655-802 |
2.44e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.98 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 655 ARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMD--------KVEGHVTLKGSV-------------AYVP 713
Cdd:PRK13547 10 ARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPlaaidaprlarlrAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 714 QQAwiQND---SLRENILFGRplQEHCYKAVMEA--------CAL-LPDLEILPSGDLTeigekgvNLSGGQKQRVSLAR 781
Cdd:PRK13547 90 QAA--QPAfafSAREIVLLGR--YPHARRAGALThrdgeiawQALaLAGATALVGRDVT-------TLSGGELARVQFAR 158
|
170 180 190
....*....|....*....|....*....|.
gi 1958656469 782 AV---------YCNSDIYLLDDPLSAVD-AH 802
Cdd:PRK13547 159 VLaqlwpphdaAQPPRYLLLDEPTAALDlAH 189
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
769-856 |
2.46e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 51.28 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 769 LSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIFEkvvgpmgLL------KNKTRILVTHGISYLPQV-DVIIV 841
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIE-------LLlelqqkENMALVLITHDLALVAEAaHKIIV 226
|
90
....*....|....*
gi 1958656469 842 MSGGKISEMGSYQEL 856
Cdd:PRK11022 227 MYAGQVVETGKAHDI 241
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
1017-1226 |
2.73e-06 |
|
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: 50.92 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1017 YGALGILQGVAvfgySMAVSIGGIFASRRLHLDLLQNV----LRSPMSFFERTPSGNLVNRFSkELDTVDSMIP-QVIKM 1091
Cdd:cd18567 48 FGLLLLLQALL----SALRSWLVLYLSTSLNLQWTSNLfrhlLRLPLSYFEKRHLGDIVSRFG-SLDEIQQTLTtGFVEA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1092 FMGSLFSVIGAVIIILLATPIAAVIIPPLgLVYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAF-EEQE 1170
Cdd:cd18567 123 LLDGLMAILTLVMMFLYSPKLALIVLAAV-ALYALLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFgREAE 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958656469 1171 RFIRQSDLKVDENQKayypSIVANRWLAVR------LECVGNCIVLFAALFAVISRHsLSAG 1226
Cdd:cd18567 202 REARWLNLLVDAINA----DIRLQRLQILFsaanglLFGLENILVIYLGALLVLDGE-FTVG 258
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
1043-1262 |
2.79e-06 |
|
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: 50.91 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1043 SRRLHLDLLQN----VLRSPMSFFERTPSGNLVNRFSkELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATP----IAA 1114
Cdd:cd18570 70 SQKLDIRLILGyfkhLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIISGIILFFYNWklflITL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1115 VIIPPLGLVYFFVQRFYvassRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPS---I 1191
Cdd:cd18570 149 LIIPLYILIILLFNKPF----KKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLgklS 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 1192 VANRWLAVRLECVGNCIVLFAALFAVISrHSLSaglVGLSVSYsLQITAY----LNWLVRMSSEMETNIVAVERL 1262
Cdd:cd18570 225 NLQSSIKGLISLIGSLLILWIGSYLVIK-GQLS---LGQLIAF-NALLGYflgpIENLINLQPKIQEAKVAADRL 294
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
660-802 |
3.02e-06 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 50.02 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 660 PTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGsvaYVPqqaWIQNDSLRENI--LFGRPLQEHC 737
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG---LVP---WKRRKKFLRRIgvVFGQKTQLWW 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656469 738 YKAVMEACALLPDLEILPSG-------------DLTEIGEKGV-NLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAH 802
Cdd:cd03267 109 DLPVIDSFYLLAAIYDLPPArfkkrldelsellDLEELLDTPVrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
665-856 |
3.68e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 50.88 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 665 ITFAIPDGALVAV---------------VGQVGCGKSSL---LSALLAEMDKVEGHVTLKG-SVAYVPQQ---------- 715
Cdd:PRK09473 20 VTFSTPDGDVTAVndlnfslragetlgiVGESGSGKSQTafaLMGLLAANGRIGGSATFNGrEILNLPEKelnklraeqi 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 716 AWIQND---SLRENILFGRPLQE--HCYKAVMEACALLPDLEILpsgDLTEIGE--KGVNL-----SGGQKQRVSLARAV 783
Cdd:PRK09473 100 SMIFQDpmtSLNPYMRVGEQLMEvlMLHKGMSKAEAFEESVRML---DAVKMPEarKRMKMyphefSGGMRQRVMIAMAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 784 YCNSDIYLLDDPLSAVDAHVGKHIfekvvgpMGLLK------NKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQEL 856
Cdd:PRK09473 177 LCRPKLLIADEPTTALDVTVQAQI-------MTLLNelkrefNTAIIMITHDLGVVAGIcDKVLVMYAGRTMEYGNARDV 249
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
640-847 |
3.86e-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: 51.94 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 640 GGMNSITVKNATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG------------ 707
Cdd:TIGR01257 924 GLVPGVCVKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldavrq 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 708 SVAYVPQQAWI-QNDSLRENILFGRPLQEHCY-KAVMEACALLPDleilpSGDLTEIGEKGVNLSGGQKQRVSLARAVYC 785
Cdd:TIGR01257 1004 SLGMCPQHNILfHHLTVAEHILFYAQLKGRSWeEAQLEMEAMLED-----TGLHHKRNEEAQDLSGGMQRKLSVAIAFVG 1078
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656469 786 NSDIYLLDDPLSAVDAHVGKHIFEKvvgpmgLLK---NKTRILVTHgisYLPQVDV----IIVMSGGKI 847
Cdd:TIGR01257 1079 DAKVVVLDEPTSGVDPYSRRSIWDL------LLKyrsGRTIIMSTH---HMDEADLlgdrIAIISQGRL 1138
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
648-875 |
4.47e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.20 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 648 KNATFTwardeppTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIqNDSLR--E 725
Cdd:PRK13546 33 KNKTFF-------ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGL-SGQLTgiE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 726 NILFGRPLQEHCYKavmEACALLPdlEILPSGDLTEIGEKGV-NLSGGQKQRVSLARAVYCNSDIYLLDDPLSavdahVG 804
Cdd:PRK13546 105 NIEFKMLCMGFKRK---EIKAMTP--KIIEFSELGEFIYQPVkKYSSGMRAKLGFSINITVNPDILVIDEALS-----VG 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 805 KHIF-EKVVGPMGLLK--NKTRILVTHGISYLPQVDVIIV-MSGGKISEMGSYQELLDRDGAFAEFVRTYANTEQ 875
Cdd:PRK13546 175 DQTFaQKCLDKIYEFKeqNKTIFFVSHNLGQVRQFCTKIAwIEGGKLKDYGELDDVLPKYEAFLNDFKKKSKAEQ 249
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1314-1511 |
4.65e-06 |
|
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: 49.71 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1314 TIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAkiglhnlrFKITIIPQDpvlFSGSLRMNLDPFSQYS 1393
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS--------YKPQYIKAD---YEGTVRDLLSSITKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1394 DEEVWMALELAHLKGFVSALPDKLNhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQ 1473
Cdd:cd03237 90 YTHPYFKTEIAKPLQIEQILDREVP--------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958656469 1474 FE--DSTVLTIAHrlNTIM-DYT--RVIVLDkgeirecGAPSE 1511
Cdd:cd03237 162 AEnnEKTAFVVEH--DIIMiDYLadRLIVFE-------GEPSV 195
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1308-1514 |
4.73e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.39 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1308 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEI-------------IIDGINIAKIGLHNLR-------FK 1367
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQSAAQMRHVRgadmamiFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1368 ITIIPQDPVLFSG-----SLRMNLDPFSQYSDEEVWMALELAHL---KGFVSALPdklnHEcaeggenLSVGQRQLVCLA 1439
Cdd:PRK10261 112 EPMTSLNPVFTVGeqiaeSIRLHQGASREEAMVEAKRMLDQVRIpeaQTILSRYP----HQ-------LSGGMRQRVMIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 1440 RALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDST--VLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSELLQ 1514
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIAdRVLVMYQGEAVETGSVEQIFH 258
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
662-800 |
5.41e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.28 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVT-LKGS-------------VAYVPQqawi---qndSL 723
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLS-LIAGARKIqQGRVEvLGGDmadarhrravcprIAYMPQglgknlyptlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 724 RENI-----LFGRPLQEHCYK--AVMEACALLPDLEiLPSGdlteigekgvNLSGGQKQRVSLARAVYCNSDIYLLDDPL 796
Cdd:NF033858 96 FENLdffgrLFGQDAAERRRRidELLRATGLAPFAD-RPAG----------KLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
....
gi 1958656469 797 SAVD 800
Cdd:NF033858 165 TGVD 168
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1306-1512 |
5.59e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 49.60 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1306 LVLKHINVTIEGGEKVGIVGRTGAGKSS----LTlGLFRineSAEGEIIIDGIN--------IAKIGL----HNLR-FK- 1367
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTvfncLT-GFYK---PTGGTILLRGQHieglpghqIARMGVvrtfQHVRlFRe 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1368 ITIIPQDPV---------LFSGSLRMnldPFSQYSDEEvwmALELAHLKGFVSALPDKLNHECAeggeNLSVGQRQLVCL 1438
Cdd:PRK11300 95 MTVIENLLVaqhqqlktgLFSGLLKT---PAFRRAESE---ALDRAATWLERVGLLEHANRQAG----NLAYGQQRRLEI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 1439 ARALLRKTKILVLDEATAAVD-LETDDLIQ--STIRTQFeDSTVLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSEL 1512
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNpKETKELDEliAELRNEH-NVTVLLIEHDMKLVMGISdRIYVVNQGTPLANGTPEEI 241
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
656-828 |
5.87e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 49.19 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 656 RDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGhvtlKGSVAyVPQQAWIQNDSLRENILFGRPLqe 735
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPV----AGCVD-VPDNQFGREASLIDAIGRKGDF-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 736 hcyKAVME---ACALlpdleilpsGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVD---AHVGKHIFE 809
Cdd:COG2401 113 ---KDAVEllnAVGL---------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQ 180
|
170
....*....|....*....
gi 1958656469 810 KVVGPMGllknKTRILVTH 828
Cdd:COG2401 181 KLARRAG----ITLVVATH 195
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
1016-1166 |
5.91e-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: 49.82 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1016 VYGALGILQG--VAVFGYSMAVSIGGIFASRRLHLdllqnvlrsPMSFFERTPSGNLVNRFSkELDTVDSMIP-QVIKMF 1092
Cdd:cd18555 54 LYGLFSFLRGyiIIKLQTKLDKSLMSDFFEHLLKL---------PYSFFENRSSGDLLFRAN-SNVYIRQILSnQVISLI 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656469 1093 MGSLFSVIGAVIIILLATPIAAVIIpPLGLVYFFvqrFYVASSRQLKRL---ESVSRSPVYSHFNETLLGVSVIRAF 1166
Cdd:cd18555 124 IDLLLLVIYLIYMLYYSPLLTLIVL-LLGLLIVL---LLLLTRKKIKKLnqeEIVAQTKVQSYLTETLYGIETIKSL 196
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
662-855 |
6.65e-06 |
|
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: 48.97 E-value: 6.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-SVAYVPQQAWI--------QNDSL------REN 726
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeDITGLPPHEIArlgigrtfQIPRLfpeltvLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 727 ILFGRPLQEHCYKAVMEACALLPDL-----EILpsgDLTEIGEKG----VNLSGGQKQRVSLARAVYCNSDIYLLDDP-- 795
Cdd:cd03219 96 VMVAAQARTGSGLLLARARREEREAreraeELL---ERVGLADLAdrpaGELSYGQQRRLEIARALATDPKLLLLDEPaa 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958656469 796 -LSAVDAHVGKHIFEKVVGpmgllKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQE 855
Cdd:cd03219 173 gLNPEETEELAELIRELRE-----RGITVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDE 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
660-859 |
6.96e-06 |
|
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: 50.45 E-value: 6.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 660 PTLNGITFAIPDGALVAVVGQVGCGKS----SLLSALLAEMDKVEGHVTLKG-SVAYVPQQAWIQ---ND---------- 721
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGqDLLGLSERELRRirgNRiamifqepmt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 722 SLreNILF--GR----PLQEHcyKAVMEACALLPDLEILpsgDLTEI--GEKGVN-----LSGGQKQRVSLARAVYCNSD 788
Cdd:COG4172 104 SL--NPLHtiGKqiaeVLRLH--RGLSGAAARARALELL---ERVGIpdPERRLDayphqLSGGQRQRVMIAMALANEPD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 789 IYLLDDPLSAVDAHVGKHIFEkvvgpmgLLKNKTR------ILVTH--GIsylpqV----DVIIVMSGGKISEMGSYQEL 856
Cdd:COG4172 177 LLIADEPTTALDVTVQAQILD-------LLKDLQRelgmalLLITHdlGV-----VrrfaDRVAVMRQGEIVEQGPTAEL 244
|
...
gi 1958656469 857 LDR 859
Cdd:COG4172 245 FAA 247
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
660-802 |
7.65e-06 |
|
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: 48.97 E-value: 7.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 660 PTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAemdkveGHVTLKGSVAYVPQQAWIqnD----------SLRENIL- 728
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG------NYLPDSGSILVRHDGGWV--DlaqaspreilALRRRTIg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 729 ----FGR-------------PLQEHCY---KAVMEACALLPDLEI------LPSGdlteigekgvNLSGGQKQRVSLARA 782
Cdd:COG4778 97 yvsqFLRviprvsaldvvaePLLERGVdreEARARARELLARLNLperlwdLPPA----------TFSGGEQQRVNIARG 166
|
170 180
....*....|....*....|
gi 1958656469 783 VYCNSDIYLLDDPLSAVDAH 802
Cdd:COG4778 167 FIADPPLLLLDEPTASLDAA 186
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1291-1512 |
1.06e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 49.64 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINI-----AKIGLHNLR 1365
Cdd:PRK11000 4 VTLRNVTKAYGDVV--ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMndvppAERGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1366 FKITIIPQDPVLFSGSLRMNLDPFS----QYSDEEVWMALELAHLkgfVSALPdklnhecaeggENLSVGQRQLVCLARA 1441
Cdd:PRK11000 82 QSYALYPHLSVAENMSFGLKLAGAKkeeiNQRVNQVAEVLQLAHL---LDRKP-----------KALSGGQRQRVAIGRT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1442 LLRKTKILVLDEATAAVDletddliqSTIRTQFEdSTVLTIAHRLNTIMDYT------------RVIVLDKGEIRECGAP 1509
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLD--------AALRVQMR-IEISRLHKRLGRTMIYVthdqveamtladKIVVLDAGRVAQVGKP 218
|
...
gi 1958656469 1510 SEL 1512
Cdd:PRK11000 219 LEL 221
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1308-1513 |
1.90e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 48.47 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1308 LKHINVTIEGGEKVGIVGRTGAGKSS---LTLGLFrINESAE---GEIIIDGiNIAKIG-LHNLRFKITIIPQDP--VLF 1378
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTmiqLTNGLI-ISETGQtivGDYAIPA-NLKKIKeVKRLRKEIGLVFQFPeyQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1379 SGSLRMNL--DPFSQYSD-EEVWMalELAHLKGFVSALPDKLNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEAT 1455
Cdd:PRK13645 105 QETIEKDIafGPVNLGENkQEAYK--KVPELLKLVQLPEDYVKRSPFE----LSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958656469 1456 AAVDLE-TDDLIQSTIRTQFEDST-VLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSELL 1513
Cdd:PRK13645 179 GGLDPKgEEDFINLFERLNKEYKKrIIMVTHNMDQVLRIAdEVIVMHEGKVISIGSPFEIF 239
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
658-872 |
1.96e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 49.11 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 658 EPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAemdKVEGHvTLKGSV---------AYVPQQAWIQNDSL----- 723
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG---RIQGN-NFTGTIlannrkptkQILKRTGFVTQDDIlyphl 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 724 --RENILF------GRPLQEHCYKAVMEAcaLLPDLEILPSGDlTEIGEKGVN-LSGGQKQRVSLARAVYCNSDIYLLDD 794
Cdd:PLN03211 156 tvRETLVFcsllrlPKSLTKQEKILVAES--VISELGLTKCEN-TIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 795 PLSAVDAHVGKhifeKVVGPMGLLKNKTRILVT--HGIS--YLPQVDVIIVMSGG------KISEMGSYQELLDRDGAF- 863
Cdd:PLN03211 233 PTSGLDATAAY----RLVLTLGSLAQKGKTIVTsmHQPSsrVYQMFDSVLVLSEGrclffgKGSDAMAYFESVGFSPSFp 308
|
250
....*....|..
gi 1958656469 864 ---AEFVRTYAN 872
Cdd:PLN03211 309 mnpADFLLDLAN 320
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1003-1171 |
2.00e-05 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 48.25 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1003 VNGTQENRNFRLSVYGALGILQGVAVFGYSMAVSIGGIFASRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVD 1082
Cdd:cd18575 28 AAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1083 SMIPQVIKMFMGSLFSVIGAVI-----------IILLATPIaaVIIPplglVYFFVQRFYVASSRQLKRLESVSrspvyS 1151
Cdd:cd18575 108 TVVGSSLSIALRNLLLLIGGLVmlfitspkltlLVLLVIPL--VVLP----IILFGRRVRRLSRASQDRLADLS-----A 176
|
170 180
....*....|....*....|..
gi 1958656469 1152 HFNETLLGVSVIRAF--EEQER 1171
Cdd:cd18575 177 FAEETLSAIKTVQAFtrEDAER 198
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
660-860 |
2.07e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.89 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 660 PTLNGITFAIPDGALVAVVGQVGCGKSSLLS--ALLAEMD----KVEGHVTLKGSVA-------Y-VPQQAWI-QNDSLR 724
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKiiAGIVPPDsgtlEIGGNPCARLTPAkahqlgiYlVPQEPLLfPNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 725 ENILFGRPLQEHCYKAVMEACALLP---DLEIlPSGDLtEIGEkgvnlsggqKQRVSLARAVYCNSDIYLLDDPLSAVDA 801
Cdd:PRK15439 105 ENILFGLPKRQASMQKMKQLLAALGcqlDLDS-SAGSL-EVAD---------RQIVEILRGLMRDSRILILDEPTASLTP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958656469 802 HVGKHIFEKVvgpMGLLKNKTRIL-VTHGISYLPQV-DVIIVMSGGKISEMGSYQELLDRD 860
Cdd:PRK15439 174 AETERLFSRI---RELLAQGVGIVfISHKLPEIRQLaDRISVMRDGTIALSGKTADLSTDD 231
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
1040-1262 |
2.08e-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: 48.33 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1040 IFASRRLHLDLL----QNVLRSPMSFFERTPSGNLVNRFsKELDTVDSMI-PQVIKMFMGSLFSVIgaVIIILLA----- 1109
Cdd:cd18568 67 DYFANRIDLSLLsdfyKHLLSLPLSFFASRKVGDIITRF-QENQKIRRFLtRSALTTILDLLMVFI--YLGLMFYynlql 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1110 TPIAAVIIPPLGLvyffvqrFYVASSRQLKRLES---VSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKA 1186
Cdd:cd18568 144 TLIVLAFIPLYVL-------LTLLSSPKLKRNSReifQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1187 YYPSIVanrwLAVRLECV-------GNCIVLFAALFAVISrHSLSAG-LVGLSVSYSLQITAYLNwLVRMSSEMETNIVA 1258
Cdd:cd18568 217 RFRGQK----LSIVLQLIsslinhlGTIAVLWYGAYLVIS-GQLTIGqLVAFNMLFGSVINPLLA-LVGLWDELQETRIS 290
|
....
gi 1958656469 1259 VERL 1262
Cdd:cd18568 291 VERL 294
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1318-1502 |
3.84e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.44 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1318 GEKVGIVGRTGAGKSSLTLGLFR-INESAEGEIIIDGINIAKIGLHNLRFKITiipqdpvlfsgslrmnldpfsqysdee 1396
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQLLLIIV--------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1397 vwmalelahlkgfvsalpdklnhecAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQF-- 1474
Cdd:smart00382 55 -------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLll 109
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958656469 1475 -----EDSTVLTIAHRLNTIMD------YTRVIVLDKGE 1502
Cdd:smart00382 110 llkseKNLTVILTTNDEKDLGPallrrrFDRRIVLLLIL 148
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
645-856 |
4.34e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 47.04 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 645 ITVKNATFTWARDEP---PTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-SVAYVPQQAWIQN 720
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDiVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 721 DSLRENILFGRPLQEHCYKAVMEACALLP--------DLEILPSGDLTEIG------EKG-VNLSGGQKQRVSLARAVYC 785
Cdd:PRK13643 82 VRKKVGVVFQFPESQLFEETVLKDVAFGPqnfgipkeKAEKIAAEKLEMVGladefwEKSpFELSGGQMRRVAIAGILAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656469 786 NSDIYLLDDPLSAVDAHVG---KHIFEKVVGpmgllKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGS----YQEL 856
Cdd:PRK13643 162 EPEVLVLDEPTAGLDPKARiemMQLFESIHQ-----SGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTpsdvFQEV 235
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
662-847 |
4.48e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 47.71 E-value: 4.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSAL--LAEMDkvEGHVTLKGS--------------VAYVPQQ-AWIQNDSLR 724
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILsgVYQPD--SGEILLDGEpvrfrsprdaqaagIAIIHQElNLVPNLSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 725 ENILFGRPLQEH-------CYKAVMEACALLpDLEILPSgdlTEIGEkgvnLSGGQKQRVSLARAVYCNSDIYLLDDPLS 797
Cdd:COG1129 98 ENIFLGREPRRGglidwraMRRRARELLARL-GLDIDPD---TPVGD----LSVAQQQLVEIARALSRDARVLILDEPTA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 798 AVDAHVGKHIFEKvvgpMGLLKNK--TRILVTHgisYLPQV----DVIIVMSGGKI 847
Cdd:COG1129 170 SLTEREVERLFRI----IRRLKAQgvAIIYISH---RLDEVfeiaDRVTVLRDGRL 218
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1314-1502 |
4.62e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.88 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1314 TIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDgINIAkiglhnlrFK---ITIIPQDPVlfSGSLRMNLDPF- 1389
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKIS--------YKpqyIKPDYDGTV--EDLLRSITDDLg 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1390 SQYSDEEVWMALELAHLkgfvsaLPDKLNhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQST 1469
Cdd:PRK13409 430 SSYYKSEIIKPLQLERL------LDKNVK--------DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKA 495
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958656469 1470 IRTQFE--DSTVLTIAHRLnTIMDY--TRVIVLDkGE 1502
Cdd:PRK13409 496 IRRIAEerEATALVVDHDI-YMIDYisDRLMVFE-GE 530
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
638-855 |
4.66e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 638 DGGGMNSITVKNATFTWArDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV--TLKGSVAyVPQQ 715
Cdd:PLN03073 502 DRPGPPIISFSDASFGYP-GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrSAKVRMA-VFSQ 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 716 AWIQNDSLRENILFgrpLQEHCYKAVMEAC--ALLPDLEIlpSGDLTEigEKGVNLSGGQKQRVSLARAVYCNSDIYLLD 793
Cdd:PLN03073 580 HHVDGLDLSSNPLL---YMMRCFPGVPEQKlrAHLGSFGV--TGNLAL--QPMYTLSGGQKSRVAFAKITFKKPHILLLD 652
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958656469 794 DP-----LSAVDAHV-GKHIFEKVVgpmgllknktrILVTHG---ISylPQVDVIIVMSGGKISEM-GSYQE 855
Cdd:PLN03073 653 EPsnhldLDAVEALIqGLVLFQGGV-----------LMVSHDehlIS--GSVDELWVVSEGKVTPFhGTFHD 711
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
669-800 |
4.86e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.56 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 669 IPDGALVAVVGQVGCGKSSLLSAL--LAEMDkvEGHVTLKGSV-----------------AYVPQQAWI-QNDSLRENIL 728
Cdd:PRK11144 21 LPAQGITAIFGRSGAGKTSLINAIsgLTRPQ--KGRIVLNGRVlfdaekgiclppekrriGYVFQDARLfPHYKVRGNLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 729 FGrplqehcYKAVMEA-----CALL---PDLEILPSgdlteigekgvNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVD 800
Cdd:PRK11144 99 YG-------MAKSMVAqfdkiVALLgiePLLDRYPG-----------SLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1307-1513 |
5.37e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.78 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESA-----EGEIIIDGINIAKIGLHNLRF----KITIIPQDPVL 1377
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1378 fsgslrmNLDPFSQYSDE--EVW-----MALELAhlKGFVSALPDKLNHECAEGGEN-----LSVGQRQLVCLARALLRK 1445
Cdd:PRK15134 104 -------SLNPLHTLEKQlyEVLslhrgMRREAA--RGEILNCLDRVGIRQAAKRLTdyphqLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958656469 1446 TKILVLDEATAAVDLETDDLIQSTIR--TQFEDSTVLTIAHRLNTIMDYT-RVIVLDKGEIRECGAPSELL 1513
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKLAdRVAVMQNGRCVEQNRAATLF 245
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
662-808 |
6.38e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 46.02 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG---------SVAYVPQQ-AWIQNDslrENILFGR 731
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlknrEVPFLRRQiGMIFQD---HHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 732 PLQEHCYKAVMEACALLPDLEILPSGDLTEIG--EKGVN----LSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGK 805
Cdd:PRK10908 95 TVYDNVAIPLIIAGASGDDIRRRVSAALDKVGllDKAKNfpiqLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
|
...
gi 1958656469 806 HIF 808
Cdd:PRK10908 175 GIL 177
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
657-856 |
6.65e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.39 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 657 DEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLaEMDKVEGHVTLKGSvayvPQQAW-----------IQ------ 719
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALL-RLINSQGEIWFDGQ----PLHNLnrrqllpvrhrIQvvfqdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 720 NDSL--RENIL--------FGRPL-----QEHCYKAVMEACALLPDLEI-LPSgdlteigekgvNLSGGQKQRVSLARAV 783
Cdd:PRK15134 372 NSSLnpRLNVLqiieeglrVHQPTlsaaqREQQVIAVMEEVGLDPETRHrYPA-----------EFSGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 784 YCNSDIYLLDDPLSAVDAHVGKHIFEkvvgpmgLLKNKTRilvTHGISYL-------------PQVdviIVMSGGKISEM 850
Cdd:PRK15134 441 ILKPSLIILDEPTSSLDKTVQAQILA-------LLKSLQQ---KHQLAYLfishdlhvvralcHQV---IVLRQGEVVEQ 507
|
....*.
gi 1958656469 851 GSYQEL 856
Cdd:PRK15134 508 GDCERV 513
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
665-857 |
6.87e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 46.32 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 665 ITFAIPDGALVAVVGQVGCGKSSL---LSALLAEMDK---VEGHVTLKGSVAYVPQQAWI--QNDS-------------- 722
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLakmLAGMIEPTSGellIDDHPLHFGDYSYRSQRIRMifQDPStslnprqrisqild 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 723 --LRENILFGRPLQEHCYKAVMEACALLPD-LEILPSGdlteigekgvnLSGGQKQRVSLARAVYCNSDIYLLDDPLSAV 799
Cdd:PRK15112 112 fpLRLNTDLEPEQREKQIIETLRQVGLLPDhASYYPHM-----------LAPGQKQRLGLARALILRPKVIIADEALASL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 800 DAHVGKHIfekvVGPMGLLKNKtrilvtHGISYLPQV----------DVIIVMSGGKISEMGSYQELL 857
Cdd:PRK15112 181 DMSMRSQL----INLMLELQEK------QGISYIYVTqhlgmmkhisDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
649-856 |
8.74e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.16 E-value: 8.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 649 NATFTWARDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG--------SVAYVPQQAWIQN 720
Cdd:PRK10261 19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrQVIELSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 721 DSLRE--------------NILF--GRPLQEHCY--------KAVMEACALLPDLEILPSGDLteIGEKGVNLSGGQKQR 776
Cdd:PRK10261 99 RHVRGadmamifqepmtslNPVFtvGEQIAESIRlhqgasreEAMVEAKRMLDQVRIPEAQTI--LSRYPHQLSGGMRQR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 777 VSLARAVYCNSDIYLLDDPLSAVDAHVGKHIFE--KVVG---PMGLlknktrILVTHGISYLPQV-DVIIVMSGGKISEM 850
Cdd:PRK10261 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQliKVLQkemSMGV------IFITHDMGVVAEIaDRVLVMYQGEAVET 250
|
....*.
gi 1958656469 851 GSYQEL 856
Cdd:PRK10261 251 GSVEQI 256
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
767-875 |
9.95e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.87 E-value: 9.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 767 VNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIfEKVVGPMGLLKNKTRILVTHGISYLPQV-DVIIVMSGg 845
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNA-ARAIRRLSEEGKKTALVVEHDLAVLDYLsDRIHVFEG- 147
|
90 100 110
....*....|....*....|....*....|...
gi 1958656469 846 kisEMGSYQELLDRDG---AFAEFVRTYANTEQ 875
Cdd:cd03222 148 ---EPGVYGIASQPKGtreGINRFLRGYLITFR 177
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1307-1512 |
1.11e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 46.38 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLtL----GLFRInesAEGEIIIDG--IN--------IAKI------------- 1359
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTL-LrmvaGLERI---TSGEIWIGGrvVNelepadrdIAMVfqnyalyphmsvr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1360 -----GLHNLRFKITIIPQdpvlfsgslRMnldpfsqysdEEVWMALELAHLkgfvsalpdkLNHECAEggenLSVGQRQ 1434
Cdd:PRK11650 95 enmayGLKIRGMPKAEIEE---------RV----------AEAARILELEPL----------LDRKPRE----LSGGQRQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1435 LVCLARALLRKTKILVLDEATAAVD--------LETDDLiQSTIRT--------QFEdstVLTIAHRLntimdytrvIVL 1498
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLDaklrvqmrLEIQRL-HRRLKTtslyvthdQVE---AMTLADRV---------VVM 208
|
250
....*....|....
gi 1958656469 1499 DKGEIRECGAPSEL 1512
Cdd:PRK11650 209 NGGVAEQIGTPVEV 222
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1307-1484 |
1.29e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 45.46 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1307 VLKHINVTIEGGEKVGIVGRTGAGKSSLtLGLFR-INESAEGEIIIDGINIAKIGLHNlrfkiTIIPQDPVLFsgslrmn 1385
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTL-LNLIAgFVPYQHGSITLDGKPVEGPGAER-----GVVFQNEGLL------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1386 ldPFSQYSDEeVWMALELA---HLKGFVSALpDKLNHECAEGGEN-----LSVGQRQLVCLARALLRKTKILVLDEATAA 1457
Cdd:PRK11248 83 --PWRNVQDN-VAFGLQLAgveKMQRLEIAH-QMLKKVGLEGAEKryiwqLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180
....*....|....*....|....*....
gi 1958656469 1458 VDLETDDLIQSTIRTQFEDS--TVLTIAH 1484
Cdd:PRK11248 159 LDAFTREQMQTLLLKLWQETgkQVLLITH 187
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1427-1490 |
1.94e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 1.94e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656469 1427 NLSVGQRQLVCLARALLRKTKILVLDEATAAVDlETD-----DLIQStIRTQfeDSTVLTIAHRLNTIM 1490
Cdd:NF040905 139 DIGVGKQQLVEIAKALSKDVKLLILDEPTAALN-EEDsaallDLLLE-LKAQ--GITSIIISHKLNEIR 203
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1318-1506 |
2.20e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1318 GEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGiniakiglHNLRFK---------ITIIPQDpvlfsgslrMNLDP 1388
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG--------KEVTFNgpkssqeagIGIIHQE---------LNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1389 fsQYS-DEEVWMALELAHLKGFV---------SALPDKLN--HECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1456
Cdd:PRK10762 93 --QLTiAENIFLGREFVNRFGRIdwkkmyaeaDKLLARLNlrFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958656469 1457 AV-DLETDDLIqSTIRT-QFEDSTVLTIAHRLNTIMDYT-RVIVLDKGE-IREC 1506
Cdd:PRK10762 171 ALtDTETESLF-RVIRElKSQGRGIVYISHRLKEIFEICdDVTVFRDGQfIAER 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
665-800 |
2.55e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 44.50 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 665 ITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTL--------------KGSVAYVPQQAWI-QNDSLRENILF 729
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllplharaRRGIGYLPQEASIfRRLSVYDNLMA 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958656469 730 GRPLQEHCYKAVME--ACALLPDLEILPSGDlteigEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAVD 800
Cdd:PRK10895 102 VLQIRDDLSAEQREdrANELMEEFHIEHLRD-----SMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
662-847 |
2.73e-04 |
|
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: 45.20 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALL-AEMDKVEGHVTLKG--------------SVAYVPQ----QAWIQNDS 722
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFgAYPGKFEGNVFINGkpvdirnpaqairaGIAMVPEdrkrHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 723 LRENILFGrPLQEHCYKAVMEACALL-------PDLEILPSGDLTEIGekgvNLSGGQKQRVSLARAVYCNSDIYLLDDP 795
Cdd:TIGR02633 356 VGKNITLS-VLKSFCFKMRIDAAAELqiigsaiQRLKVKTASPFLPIG----RLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 796 LSAVDAHVGKHIFeKVVGpmGLLKNKTRILVTHgiSYLPQV----DVIIVMSGGKI 847
Cdd:TIGR02633 431 TRGVDVGAKYEIY-KLIN--QLAQEGVAIIVVS--SELAEVlglsDRVLVIGEGKL 481
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
598-895 |
3.23e-04 |
|
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: 45.77 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 598 NILPMVISSIVQASVSLK-RLRIFLSHEELEP---------DSI--ERWSIKDGGGMNSITVKNA-TFTWARDEPPTLNG 664
Cdd:TIGR01257 1878 NLVAMAVEGVVYFLLTLLiQHHFFLSRWIAEPakepifdedDDVaeERQRIISGGNKTDILRLNElTKVYSGTSSPAVDR 1957
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 665 ITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG------------SVAYVPQQAWIqndslrENILFGRp 732
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGksiltnisdvhqNMGYCPQFDAI------DDLLTGR- 2030
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 733 lqEHCYkavmeacaLLPDLEILPSGDLTEIGEKGVN--------------LSGGQKQRVSLARAVYCNSDIYLLDDPLSA 798
Cdd:TIGR01257 2031 --EHLY--------LYARLRGVPAEEIEKVANWSIQslglslyadrlagtYSGGNKRKLSTAIALIGCPPLVLLDEPTTG 2100
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 799 VDAHVGKHIFEKVVGPmgLLKNKTRILVTHGISYLPQVDV-IIVMSGGKISEMGSYQELLdrdgafAEFVRTYANTEQDL 877
Cdd:TIGR01257 2101 MDPQARRMLWNTIVSI--IREGRAVVLTSHSMEECEALCTrLAIMVKGAFQCLGTIQHLK------SKFGDGYIVTMKIK 2172
|
330
....*....|....*...
gi 1958656469 878 ASEDDSVSGLGkeskPVE 895
Cdd:TIGR01257 2173 SPKDDLLPDLN----PVE 2186
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
662-845 |
3.51e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.16 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG--------------SVAYVPQQAWIQND-SLREN 726
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhklaaqlGIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 727 ILFGR-PLQEHC------YKAVMEACALLpdleILPSGDLTEIGEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPLSAV 799
Cdd:PRK09700 101 LYIGRhLTKKVCgvniidWREMRVRAAMM----LLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958656469 800 -DAHVgkhifEKVVGPMGLLKN--KTRILVTHGISYLPQV-DVIIVMSGG 845
Cdd:PRK09700 177 tNKEV-----DYLFLIMNQLRKegTAIVYISHKLAEIRRIcDRYTVMKDG 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
769-880 |
3.53e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.08 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 769 LSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIfekvvgpMGLLK------NKTRILVTHGISYLPQV-DVIIV 841
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQI-------LQLLRelqqelNMGLLFITHNLSIVRKLaDRVAV 229
|
90 100 110
....*....|....*....|....*....|....*....
gi 1958656469 842 MSGGKISEMGSYQELLDRDgafaefvrTYANTEQDLASE 880
Cdd:PRK15134 230 MQNGRCVEQNRAATLFSAP--------THPYTQKLLNSE 260
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
1022-1131 |
3.61e-04 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 44.22 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1022 ILQGVAVFGYSMAVSI-GGIF---ASR---RLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMG 1094
Cdd:cd18784 40 IIMGLLAIASSVAAGIrGGLFtlaMARlniRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLR 119
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1958656469 1095 SLFSVIGAVIIILLAT---PIAAVIIPPLGlvyFFVQRFY 1131
Cdd:cd18784 120 SLVKAIGVIVFMFKLSwqlSLVTLIGLPLI---AIVSKVY 156
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1311-1509 |
4.02e-04 |
|
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: 45.39 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1311 INVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIaKIGLHNLRFKITIIPQDPVLFSG-SLRMNLDPF 1389
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1390 SQY---SDEEVWMALElahlkgfvSALPDK-LNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDL 1465
Cdd:TIGR01257 1028 AQLkgrSWEEAQLEME--------AMLEDTgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958656469 1466 IQSTIRTQFEDSTVLTIAHRLNTI-MDYTRVIVLDKGEIRECGAP 1509
Cdd:TIGR01257 1100 IWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTP 1144
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
665-848 |
4.02e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.90 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 665 ITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG--------------SVAYVP----QQAWIQNDSLREN 726
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpidirsprdairaGIMLCPedrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 727 I------------LFGRPLQEhcykavmeacALLPDLEI------LPSGDlTEIGekgvNLSGGQKQRVSLARAVYCNSD 788
Cdd:PRK11288 352 InisarrhhlragCLINNRWE----------AENADRFIrslnikTPSRE-QLIM----NLSGGNQQKAILGRWLSEDMK 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 789 IYLLDDPLSAVDahVG-KH-----IFEkvvgpmgLLKNKTRILVTHgiSYLPQV----DVIIVMSGGKIS 848
Cdd:PRK11288 417 VILLDEPTRGID--VGaKHeiynvIYE-------LAAQGVAVLFVS--SDLPEVlgvaDRIVVMREGRIA 475
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
709-800 |
4.30e-04 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 43.48 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 709 VAYVPQQAWI-QNDSLRENIL-----FGRPLQEHcyKAVMEAcaLLPDLeilpsgDLTEIGE-KGVNLSGGQKQRVSLAR 781
Cdd:COG1137 80 IGYLPQEASIfRKLTVEDNILavlelRKLSKKER--EERLEE--LLEEF------GITHLRKsKAYSLSGGERRRVEIAR 149
|
90
....*....|....*....
gi 1958656469 782 AVYCNSDIYLLDDPLSAVD 800
Cdd:COG1137 150 ALATNPKFILLDEPFAGVD 168
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
1061-1262 |
7.04e-04 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 43.56 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1061 FFERTPSGNLVNRFskeLDTVDSMIPQVIKMFMGSLFSVIGAVIII-------LLATPIAAVIIPPLGL-VYFFVQRFyv 1132
Cdd:cd18554 96 YYANNRSGEIISRV---INDVEQTKDFITTGLMNIWLDMITIIIAIcimlvlnPKLTFVSLVIFPFYILaVKYFFGRL-- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1133 assRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDlkvDENQKAYYPSIVANRWLAVRLECV------GN 1206
Cdd:cd18554 171 ---RKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFD---KRNGHFLTRALKHTRWNAKTFSAVntitdlAP 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656469 1207 CIVLFAALFAVISrHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERL 1262
Cdd:cd18554 245 LLVIGFAAYLVIE-GNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1306-1513 |
7.67e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 43.00 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1306 LVLKHINV---------TIEGGEKVGIVGRTGAGKSSL---TLGLFrineSAEGEIIIDGINIAKIGLHNL-RFKITIIP 1372
Cdd:PRK03695 1 MQLNDVAVstrlgplsaEVRAGEILHLVGPNGAGKSTLlarMAGLL----PGSGSIQFAGQPLEAWSAAELaRHRAYLSQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1373 QDPVLFSgslrMnldPFSQYSD---------EEVWMAL-ELAHLKGfvsaLPDKLnHECAeggENLSVGQRQLVCLARAL 1442
Cdd:PRK03695 77 QQTPPFA----M---PVFQYLTlhqpdktrtEAVASALnEVAEALG----LDDKL-GRSV---NQLSGGEWQRVRLAAVV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1443 LR-------KTKILVLDEATAAVDLETDDLIQSTIRtQFEDS--TVLTIAHRLNTIMDY-TRVIVLDKGEIRECGAPSEL 1512
Cdd:PRK03695 142 LQvwpdinpAGQLLLLDEPMNSLDVAQQAALDRLLS-ELCQQgiAVVMSSHDLNHTLRHaDRVWLLKQGKLLASGRRDEV 220
|
.
gi 1958656469 1513 L 1513
Cdd:PRK03695 221 L 221
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
1027-1122 |
7.99e-04 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family 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. 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. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 43.39 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1027 AVFGYSMAVSIGGIFAS--------------RRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMF 1092
Cdd:cd18780 44 AVLILLGVVLIGSIATFlrswlftlagervvARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSML 123
|
90 100 110
....*....|....*....|....*....|....
gi 1958656469 1093 MGSLFSVIGAVIIILLA----TPIAAVIIPPLGL 1122
Cdd:cd18780 124 LRYLVQIIGGLVFMFTTswklTLVMLSVVPPLSI 157
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1323-1470 |
1.08e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.78 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1323 IVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGL-------HNLRFKITIIPQDpvlfsgslrmNLDPFSQYSDE 1395
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKpyctyigHNLGLKLEMTVFE----------NLKFWSEIYNS 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 1396 EVWMALELAHLKgfvsaLPDKLNHECAeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTI 1470
Cdd:PRK13541 101 AETLYAAIHYFK-----LHDLLDEKCY----SLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
660-848 |
1.12e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 43.48 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 660 PTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS--------------VAYVPQ----QAWIQND 721
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsprerrrlgVAYIPEdrlgRGLVPDM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 722 SLRENILFGR----PLQEHC---YKAVMEACA-LLPDLEILPSGDLTEIGekgvNLSGGQKQRVSLARAVYCNSDIYLLD 793
Cdd:COG3845 352 SVAENLILGRyrrpPFSRGGfldRKAIRAFAEeLIEEFDVRTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAA 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 794 DPLSAVD----AHVGKHIFEkvvgpmglLKNK-TRILVthgISY-LPQV----DVIIVMSGGKIS 848
Cdd:COG3845 428 QPTRGLDvgaiEFIHQRLLE--------LRDAgAAVLL---ISEdLDEIlalsDRIAVMYEGRIV 481
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
1023-1172 |
1.89e-03 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); 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: 350034 [Multi-domain] Cd Length: 289 Bit Score: 41.94 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1023 LQGVAVFGYSMAVSI-GGIFA------SRRLHLDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGS 1095
Cdd:cd18590 41 LMCLFSLGSSLSAGLrGGLFMctlsrlNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1096 LFSVIGAVIIIL-----------LATPIAAVIipplglvyffvQRFYVASSRQLKR--LESVSRSPvySHFNETLLGVSV 1162
Cdd:cd18590 121 LVKTLGMLGFMLslswqltlltlIEMPLTAIA-----------QKVYNTYHQKLSQavQDSIAKAG--ELAREAVSSIRT 187
|
170
....*....|....
gi 1958656469 1163 IRAF----EEQERF 1172
Cdd:cd18590 188 VRSFkaeeEEACRY 201
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
662-801 |
3.00e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 42.12 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSAL--------------LAEMDKVEGHV--TLKGSVAYVPQQ-AWIQNDSLR 724
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILsgvyphgtwdgeiyWSGSPLKASNIrdTERAGIVIIHQElTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 725 ENILFGR----PLQEHCYKAVMEAC-ALLPDLEILPSGDLTEIGEKGvnlsGGQKQRVSLARAVYCNSDIYLLDDPLSAV 799
Cdd:TIGR02633 97 ENIFLGNeitlPGGRMAYNAMYLRAkNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
..
gi 1958656469 800 DA 801
Cdd:TIGR02633 173 TE 174
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
662-798 |
3.92e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.45 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSL---LSA-----------LLAEMDKVEGHV--TLKGSVAYVPQQ-AWIQNDSLR 724
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLmkvLSGvyphgtyegeiIFEGEELQASNIrdTERAGIAIIHQElALVKELSVL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656469 725 ENILFGRPLQEHC---YKAVMEAC-ALLPDLEILPSGDlTEIGekgvNLSGGQKQRVSLARAVYCNSDIYLLDDPLSA 798
Cdd:PRK13549 101 ENIFLGNEITPGGimdYDAMYLRAqKLLAQLKLDINPA-TPVG----NLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
738-848 |
4.31e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 738 YKAVMEACALLPDLEILPsgdltEIGEKGVN-LSGGQKQRVSLARAVYCNSDIYLLDDPLSAVDAHVGKHIfekvvgPMG 816
Cdd:PLN03073 318 YTAEARAASILAGLSFTP-----EMQVKATKtFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWL------ETY 386
|
90 100 110
....*....|....*....|....*....|....
gi 1958656469 817 LLK-NKTRILVTHGISYLPQVDV-IIVMSGGKIS 848
Cdd:PLN03073 387 LLKwPKTFIVVSHAREFLNTVVTdILHLHGQKLV 420
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
643-714 |
4.55e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.42 E-value: 4.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958656469 643 NSITVKNATFTWarDEPPTLNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV--TLKGSVAYVPQ 714
Cdd:PRK15064 318 NALEVENLTKGF--DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwSENANIGYYAQ 389
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1291-1453 |
4.55e-03 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 40.90 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1291 VEFRDycLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLtLGLFRINESAE-GEIIIDGINIAKI---GLHNLRF 1366
Cdd:PRK11831 8 VDMRG--VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTL-LRLIGGQIAPDhGEILFDGENIPAMsrsRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 1367 KITIIPQdpvlfSGSLRMNLDPF----------SQYSDE----EVWMALELAHLKGFVSALPDKlnhecaeggenLSVGQ 1432
Cdd:PRK11831 85 RMSMLFQ-----SGALFTDMNVFdnvayplrehTQLPAPllhsTVMMKLEAVGLRGAAKLMPSE-----------LSGGM 148
|
170 180
....*....|....*....|.
gi 1958656469 1433 RQLVCLARALLRKTKILVLDE 1453
Cdd:PRK11831 149 ARRAALARAIALEPDLIMFDE 169
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1428-1484 |
7.15e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.09 E-value: 7.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656469 1428 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIrTQFEdSTVLTIAH 1484
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELL-DSYQ-GTVLLVSH 495
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
769-828 |
7.16e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.88 E-value: 7.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656469 769 LSGGQKQRVSLARAV----YCNSDIYLLDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTR-ILVTH 828
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAI---LEHLVKGAQvIVITH 139
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
662-808 |
9.18e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 9.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 662 LNGITFAIPDGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS--------------VAYVPQQA-WIQNDSLREN 726
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfksskealengISMVHQELnLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656469 727 ILFGR-PL------QEHCY---KAVMEACallpDLEILPSgdlteigEKGVNLSGGQKQRVSLARAVYCNSDIYLLDDPL 796
Cdd:PRK10982 94 MWLGRyPTkgmfvdQDKMYrdtKAIFDEL----DIDIDPR-------AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170
....*....|..
gi 1958656469 797 SAVDAHVGKHIF 808
Cdd:PRK10982 163 SSLTEKEVNHLF 174
|
|
| |
