|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
8-1537 |
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: 1621.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 8 STFWNSSF-LDSPEADLPLCFEQTVLVWIPLGYLWLLAPWQLLhvYKSRTKRSSTTKLYLAK-QVFVGFLL-ILAAIELA 84
Cdd:TIGR00957 7 DPLWDWNVtWHTSNPDFTKCFQNTVLAWVPCFYLWVCFPCYFL--YLSRHDRGYIQMTHLNKtKTALGFLLwIVCWADLF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 85 LVLTEDS-GQATVPaVRYTNPSLYLGTWLL-VLLIQYSRQWCVQkNSWFLSLFWILSILCGTFQFQTLIRTLL-QGDNSN 161
Cdd:TIGR00957 85 YSFWERShGRAPAP-VFLVSPTLLGITMLLaTFLIQLERRKGVQ-SSGIMLTFWLVALVCALAILRSKILLALkEDAIVD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 162 LAYSCLFFISYGFQILILIFSAFSENNESSNNPS--------SIASFLSSITYSWYDSIILKGYKRPLTLEDVWEVDEEM 233
Cdd:TIGR00957 163 PFRDTTFYIYFALVLSQLVLSCFSDKSPLFSETNhdpnpcpeSSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKED 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 234 KTKTLVSKFETHMKRELQKARRalqrrqeKSSQQNSGARLPGLNKNQSQSQdalVLEDVEKKKKKSGTKKDVPKswLMKA 313
Cdd:TIGR00957 243 TSEMVVPVLVENWKKECKKTRK-------QPVSAVYGKKDPSKPKGSSQLD---ANEEVEALIVKSPHKPRKPS--LFKV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 314 LFKTFYMVLLKSFLLKLVNDIFTFVSPQLLKLLISFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVR 393
Cdd:TIGR00957 311 LYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 394 TAIMASVYKKALTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLV 473
Cdd:TIGR00957 391 TAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLM 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 474 IPINAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLT 553
Cdd:TIGR00957 471 VPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCT 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 554 PVLVSVVTFSVYVLVDSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERLEKYLGGDDLDTSAIRHDCNF 633
Cdd:TIGR00957 551 PFLVALITFAVYVTVDENNILDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIK 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 634 D---KAMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWI 710
Cdd:TIGR00957 631 PgegNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWI 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 711 QNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSA 790
Cdd:TIGR00957 711 QNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 791 VDAHVGKHIFNKVLGPNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAKnlktFLRHTGPEE 870
Cdd:TIGR00957 791 VDAHVGKHIFEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAE----FLRTYAPDE 866
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 871 EatvhDGSEEEDDDYGLISSVEE--IPEDAASITMRRENSFRRTLSRSSRSNGRHLKSLRNSLKTRNVNSLKEDEELVKG 948
Cdd:TIGR00957 867 Q----QGHLEDSWTALVSGEGKEakLIENGMLVTDVVGKQLQRQLSASSSDSGDQSRHHGSSAELQKAEAKEETWKLMEA 942
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 949 QKlikkefIETGKVKFSIYLEYLQAIGLFSIFFIILAFVMNSVAFIGSNLWLSAWTSDSkIFNSTDypaSQRDMRVGVYG 1028
Cdd:TIGR00957 943 DK------AQTGQVELSVYWDYMKAIGLFITFLSIFLFVCNHVSALASNYWLSLWTDDP-MVNGTQ---NNTSLRLSVYG 1012
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1029 ALGLAQGIFVFIAHFWSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLG 1108
Cdd:TIGR00957 1013 ALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFN 1092
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1109 IISTLVMICMATPVFTIIVIPLGIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEV 1188
Cdd:TIGR00957 1093 VIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDL 1172
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1189 RIDTNQKCVFSWITSNRWLAIRLELVGNLTVFFSALMMVIYRDTLSGDTVGFVLSNALNITQTLNWLVRMTSEIETNIVA 1268
Cdd:TIGR00957 1173 KVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVA 1252
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1269 VERITEYTKVENEAPW-VTDKRPPPDWPSKGKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCL 1347
Cdd:TIGR00957 1253 VERLKEYSETEKEAPWqIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGL 1332
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1348 FRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLS 1427
Cdd:TIGR00957 1333 FRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLD 1412
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1428 HEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVL 1507
Cdd:TIGR00957 1413 HECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVL 1492
|
1530 1540 1550
....*....|....*....|....*....|
gi 1388169353 1508 DNGKIIECGSPEELLQIPGPFYFMAKEAGI 1537
Cdd:TIGR00957 1493 DKGEVAEFGAPSNLLQQRGIFYSMAKDAGL 1522
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
198-1523 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 1065.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 198 ASFLSSITYSWYDSIILKGYKRPLTLEDVWEVDEEMKTKTLVSKFETHMKRELQKarralqrrqekssqqnsgarlpgln 277
Cdd:PLN03130 232 ANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKK------------------------- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 278 knqsqsqdalvledvekkkkksgtkkdvPKSWLMKALFKTFYMVLLKSFLLKLVNDIFTFVSPQLLKLLISFASDRDTyL 357
Cdd:PLN03130 287 ----------------------------PKPWLLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQNGEP-A 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 358 WIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKKALTLSNLARKEYTVGETVNLMSVDAQKLMDVTNF 437
Cdd:PLN03130 338 WIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQ 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 438 MHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAW 517
Cdd:PLN03130 418 LHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAW 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 518 EPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFSVYVLVDSNniLDAQKAFTSITLFNILRFPLSMLP 597
Cdd:PLN03130 498 ENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNSIPVLVTVVSFGVFTLLGGD--LTPARAFTSLSLFAVLRFPLFMLP 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 598 MMISSMLQASVSTERLEKYLGGDD---LDTSAIRHDCnfdKAMQFSEASFTWEHDSE-ATVRDVNLDIMAGQLVAVIGPV 673
Cdd:PLN03130 576 NLITQAVNANVSLKRLEELLLAEErvlLPNPPLEPGL---PAISIKNGYFSWDSKAErPTLSNINLDVPVGSLVAIVGST 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 674 GSGKSSLISAMLGEMENV-HGHITIKGTTAYVPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLA 752
Cdd:PLN03130 653 GEGKTSLISAMLGELPPRsDASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLT 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 753 EIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIV 832
Cdd:PLN03130 733 EIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCI--KDELRGKTRVLVTNQLHFLSQVDRII 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 833 VLGNGTIVEKGSYSALLAKKGEFAKnlktFLRHTGPEEEaTVHDGSEEEDDDyglissveeipedaasitmrrensfrrt 912
Cdd:PLN03130 811 LVHEGMIKEEGTYEELSNNGPLFQK----LMENAGKMEE-YVEENGEEEDDQ---------------------------- 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 913 lsrssrSNGRHLKSLRNSLKTRNVNSLKEDEElvKGQKLIKKEFIETGKVKFSIYLEYLQAI-GLFSIFFIILAFVMNSV 991
Cdd:PLN03130 858 ------TSSKPVANGNANNLKKDSSSKKKSKE--GKSVLIKQEERETGVVSWKVLERYKNALgGAWVVMILFLCYVLTEV 929
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 992 AFIGSNLWLSAWT--SDSKIFNSTDYpasqrdmrVGVYGALGLAQGIFVFIAHFWSAFGFVHASNILHKQLLNNILRAPM 1069
Cdd:PLN03130 930 FRVSSSTWLSEWTdqGTPKTHGPLFY--------NLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPM 1001
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1070 RFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIYVSVQMFYVSTSRQLR 1149
Cdd:PLN03130 1002 SFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVK 1081
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1150 RLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNRWLAIRLELVGNLTVFFSALMMVIY 1229
Cdd:PLN03130 1082 RLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQ 1161
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1230 RDTLS-----GDTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYTKVENEAPWVT-DKRPPPDWPSKGKIQFN 1303
Cdd:PLN03130 1162 NGRAEnqaafASTMGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPSEAPLVIeNNRPPPGWPSSGSIKFE 1241
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1304 NYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQD 1383
Cdd:PLN03130 1242 DVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQA 1321
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1384 PILFSGSLRMNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEA 1463
Cdd:PLN03130 1322 PVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEA 1401
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1464 TAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQ 1523
Cdd:PLN03130 1402 TAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLS 1461
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-1539 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 982.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 23 LPLCFEQTVLVWIPLGYLWLLAPWQLLHVYKSRTKRSSTTKLYLAKQVFVGFLLILAaieLALVLTEDSGQATVPAVRYT 102
Cdd:PLN03232 37 LVMIVSHSVLLGLCFYRIWIILDNAKAQIYVLRKKYYNCVLGILACYCVVEPVLRLV---MGISLFDMDEETDLPPFEVA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 103 NPSLYLGTW--LLVLLIQYSRQWcVQKNSWFLSlFWILSILCGTFQFQTLIRTLLQGDNSNLAYSCLFF----ISYGFQI 176
Cdd:PLN03232 114 SLMVEAFAWfsMLVLIGLETKQY-VKEFRWYVR-FGVVYVLVADAVLLDLVLPLKNSINRTALYLCISSrccqALFGILL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 177 LILI-----FSAFSENNESSNNPSSI--------------ASFLSSITYSWYDSIILKGYKRPLTLEDVWEVDEEMKTKT 237
Cdd:PLN03232 192 LVYIpeldpYPGYHILNNESLDNVEYdalrggenicperyASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTET 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 238 LVSKFETHMKRELQKarralqrrqekssqqnsgarlpglnknqsqsqdalvledvekkkkksgtkkdvPKSWLMKALFKT 317
Cdd:PLN03232 272 LIKRFQRCWTEESRR-----------------------------------------------------PKPWLLRALNNS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 318 FYMVLLKSFLLKLVNDIFTFVSPQLLKLLISFASDRDTyLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIM 397
Cdd:PLN03232 299 LGGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMQEGDP-AWVGYVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLV 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 398 ASVYKKALTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPIN 477
Cdd:PLN03232 378 AAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQ 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 478 AILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLV 557
Cdd:PLN03232 458 TLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVV 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 558 SVVTFSVYVLVDSNniLDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERLEKYLGGDD--------LDTSAirh 629
Cdd:PLN03232 538 TLVSFGVFVLLGGD--LTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEErilaqnppLQPGA--- 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 630 dcnfdKAMQFSEASFTWEHDSE-ATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVH-GHITIKGTTAYVPQQ 707
Cdd:PLN03232 613 -----PAISIKNGYFSWDSKTSkPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtSSVVIRGSVAYVPQV 687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 708 SWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDP 787
Cdd:PLN03232 688 SWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDP 767
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 788 LSAVDAHVGKHIFNKVLGPNglLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYsALLAKKGEFAKNLKtflrhtg 867
Cdd:PLN03232 768 LSALDAHVAHQVFDSCMKDE--LKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTF-AELSKSGSLFKKLM------- 837
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 868 peEEATVHDGSEEEDddygliSSVEEIPEDAASITMRRENsfrrtlsrssrsngRHLKSLRNSLKTRNVnslkedeelvk 947
Cdd:PLN03232 838 --ENAGKMDATQEVN------TNDENILKLGPTVTIDVSE--------------RNLGSTKQGKRGRSV----------- 884
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 948 gqkLIKKEFIETGKVKFSIYLEYLQAIG-LFSIFFIILAFVMNSVAFIGSNLWLSAWTSDSKIFNSTdyPAsqrdMRVGV 1026
Cdd:PLN03232 885 ---LVKQEERETGIISWNVLMRYNKAVGgLWVVMILLVCYLTTEVLRVSSSTWLSIWTDQSTPKSYS--PG----FYIVV 955
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1027 YGALGLAQGIFVFIAHFWSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCF 1106
Cdd:PLN03232 956 YALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQL 1035
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1107 LGIISTLVMICMATPVFTIIVIPLGIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHN 1186
Cdd:PLN03232 1036 WQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKIN 1115
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1187 EVRIDTNQKCVFSWITSNRWLAIRLELVGNLTVFFSALMMVIYRDTLS-----GDTVGFVLSNALNITQTLNWLVRMTSE 1261
Cdd:PLN03232 1116 GKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLRNGNAEnqagfASTMGLLLSYTLNITTLLSGVLRQASK 1195
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1262 IETNIVAVERITEYTKVENEAPWV-TDKRPPPDWPSKGKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGK 1340
Cdd:PLN03232 1196 AENSLNSVERVGNYIDLPSEATAIiENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGK 1275
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1341 SSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNLDPFNNYSDEEIWKALELAHLKSFVA 1420
Cdd:PLN03232 1276 SSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVID 1355
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1421 SLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMD 1500
Cdd:PLN03232 1356 RNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIID 1435
|
1530 1540 1550 1560
....*....|....*....|....*....|....*....|
gi 1388169353 1501 SDKVMVLDNGKIIECGSPEELLQIPGPFYF-MAKEAGIEN 1539
Cdd:PLN03232 1436 CDKILVLSSGQVLEYDSPQELLSRDTSAFFrMVHSTGPAN 1475
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
310-1521 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 826.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 310 LMKALFKTFYMVLLKSFLLKLVNDIFTFVSPQLLKLLISFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLG 389
Cdd:PTZ00243 234 LLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRFYYISIRCG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 390 VKVRTAIMASVYKKALTLSN--LARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGV 467
Cdd:PTZ00243 314 LQYRSALNALIFEKCFTISSksLAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALMAV 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 468 GVMVLVIPINAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVI 547
Cdd:PTZ00243 394 AVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVATS 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 548 FVFQLTPVLVSVVTFSVYVLvdSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERLEKYLGGDDLDTSAI 627
Cdd:PTZ00243 474 FVNNATPTLMIAVVFTVYYL--LGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLECDNATCSTV 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 628 R-----------HDCNFDKAMQFSEASFT--------------------------------------------------- 645
Cdd:PTZ00243 552 QdmeeywreqreHSTACQLAAVLENVDVTafvpvklprapkvktsllsralrmlcceqcrptkrhpspsvvvedtdygsp 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 646 ------------------------------------WEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEME 689
Cdd:PTZ00243 632 ssasrhiveggtgggheatptsersaktpkmktddfFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFE 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 690 NVHGHITIKGTTAYVPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRI 769
Cdd:PTZ00243 712 ISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARV 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 770 SLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALL 849
Cdd:PTZ00243 792 SLARAVYANRDVYLLDDPLSALDAHVGERVVEECF--LGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM 869
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 850 AKkgefakNLKTFLRHTGPEEEATVHDGSEEEDDDyglISSVEEIPEDAAsitmrrensfrrtlsrssrsngrhlkslRN 929
Cdd:PTZ00243 870 RT------SLYATLAAELKENKDSKEGDADAEVAE---VDAAPGGAVDHE----------------------------PP 912
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 930 SLKTRNVNslkEDEELVKGQ----KLIKKEFIETGKVKFSIYLEYLQAIG-LFSIFFIILAFVMNSVAFIGSNLWLSAWT 1004
Cdd:PTZ00243 913 VAKQEGNA---EGGDGAALDaaagRLMTREEKASGSVPWSTYVAYLRFCGgLHAAGFVLATFAVTELVTVSSGVWLSMWS 989
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1005 SDSKIFNSTDYpasqrdmrVGVYGALGLAQGIFVFIAHFWSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRF 1084
Cdd:PTZ00243 990 TRSFKLSAATY--------LYVYLGIVLLGTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRF 1061
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1085 AGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFS 1164
Cdd:PTZ00243 1062 SRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLE 1141
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1165 ETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNRWLAIRLELVGNLTVFFSALMMVIYR-DTLSGDTVGFV-- 1241
Cdd:PTZ00243 1142 EALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGVIGTmLRATSQEIGLVsl 1221
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1242 -LSNALNITQTLNWLVRMTSEIETNIVAVERITEYT-KVENEA-PWVTD------KR-----------------PPPDWP 1295
Cdd:PTZ00243 1222 sLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTdEVPHEDmPELDEevdaleRRtgmaadvtgtvviepasPTSAAP 1301
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1296 ---SKGKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHD 1372
Cdd:PTZ00243 1302 hpvQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRE 1381
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1373 LREKLTIIPQDPILFSGSLRMNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALL 1452
Cdd:PTZ00243 1382 LRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALL 1461
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1453 RK-SKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEEL 1521
Cdd:PTZ00243 1462 KKgSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
198-1522 |
1.53e-165 |
|
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: 539.50 E-value: 1.53e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 198 ASFLSSITYSWYDSIILKGYKRPLTLEDVWEVDEEMKTKTLVSKFETHMKRELQKARralqrrqekssqqnsgarlpgln 277
Cdd:TIGR01271 9 ANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAK----------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 278 KNqsqsqdalvledvekkkkksgtkkdvPKswLMKALFKTFYMVLLKSFLLKLVNDIFTFVSPQLLKLLI-SFASDRDTY 356
Cdd:TIGR01271 66 KN--------------------------PK--LLNALRRCFFWRFVFYGILLYFGEATKAVQPLLLGRIIaSYDPFNAPE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 357 LWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKKALTLSNLARKEYTVGETVNLMSVDAQKLMDVTN 436
Cdd:TIGR01271 118 REIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 437 FMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFA 516
Cdd:TIGR01271 198 LAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYC 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 517 WEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFSVYVLVDSnniLDAQKAFTSITLFNILRFPLS-M 595
Cdd:TIGR01271 278 WEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVVFLSVVPYALIKG---IILRRIFTTISYCIVLRMTVTrQ 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 596 LPMMISSMLQASVSTERLEKYLGGDD-------LDTSAI--------------------------RHDCNFDKAMQFSEA 642
Cdd:TIGR01271 355 FPGAIQTWYDSLGAITKIQDFLCKEEyktleynLTTTEVemvnvtaswdegigelfekikqnnkaRKQPNGDDGLFFSNF 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 643 SFTwehdSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQNGTIKDNILFG 722
Cdd:TIGR01271 435 SLY----VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFG 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 723 TEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNK 802
Cdd:TIGR01271 511 LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFES 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 803 VLGPngLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAKNL------------------KTFLR 864
Cdd:TIGR01271 591 CLCK--LMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLlgleafdnfsaerrnsilTETLR 668
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 865 HTGPEEEATVHDGSEE-------------EDDDYGLI----------SSVEEIPEDAASITM------------------ 903
Cdd:TIGR01271 669 RVSIDGDSTVFSGPETikqsfkqpppefaEKRKQSIIlnpiasarkfSFVQMGPQKAQATTIedavrepserkfslvped 748
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 904 ----------------------RRENSFRRTLSRSSRSNGRHLK--SLRNSLKTRNVNSLKE------------------ 941
Cdd:TIGR01271 749 eqgeeslprgnqyhhglqhqaqRRQSVLQLMTHSNRGENRREQLqtSFRKKSSITQQNELASeldiysrrlskdsvyeis 828
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 942 ---DEELVKgQKLIKKEFIETGKVKFSIYLEYLqAIGLFSIFFIILAFVMNSVAFIGS--NLWLSAWTSDSKIFNSTDYP 1016
Cdd:TIGR01271 829 eeiNEEDLK-ECFADERENVFETTTWNTYLRYI-TTNRNLVFVLIFCLVIFLAEVAASllGLWLITDNPSAPNYVDQQHA 906
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1017 -ASQRDMRVGVYGALGLAQGIF---VFIAHFWSAFGF------VHA----SNILHKQLLNNILRAPMRFFDTTPTGRIVN 1082
Cdd:TIGR01271 907 nASSPDVQKPVIITPTSAYYIFyiyVGTADSVLALGFfrglplVHTlltvSKRLHEQMLHSVLQAPMAVLNTMKAGRILN 986
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1083 RFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSH 1162
Cdd:TIGR01271 987 RFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSH 1066
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1163 FSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNRWLAIRLELVgnLTVFFSALMMVIYRDTLSGD-TVGFV 1241
Cdd:TIGR01271 1067 LITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDII--FVFFFIAVTFIAIGTNQDGEgEVGII 1144
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1242 LSNALNITQTLNWLVRMTSEIETNIVAVERITEYTKVENEAPWVTDKRPPPD---------------WPSKGKIQFNNYQ 1306
Cdd:TIGR01271 1145 LTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRPSGGGGKYQlstvlvienphaqkcWPSGGQMDVQGLT 1224
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1307 VRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILeAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPIL 1386
Cdd:TIGR01271 1225 AKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFI 1303
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1387 FSGSLRMNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAA 1466
Cdd:TIGR01271 1304 FSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAH 1383
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 1467 VDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELL 1522
Cdd:TIGR01271 1384 LDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL 1439
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
979-1276 |
1.20e-158 |
|
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: 481.98 E-value: 1.20e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 979 IFFIILAFVMNSVAFIGSNLWLSAWTSDSKIFNSTDYpaSQRDMRVGVYGALGLAQGIFVFIAHFWSAFGFVHASNILHK 1058
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDT--EQRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1059 QLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIYVSVQ 1138
Cdd:cd18603 79 KLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1139 MFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNRWLAIRLELVGNLT 1218
Cdd:cd18603 159 RFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLI 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1388169353 1219 VFFSALMMVIYRDTLSGDTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYT 1276
Cdd:cd18603 239 VLFAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
324-613 |
5.15e-149 |
|
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: 456.16 E-value: 5.15e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 324 KSFLLKLVNDIFTFVSPQLLKLLISFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKK 403
Cdd:cd18595 1 LAALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 404 ALTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTK 483
Cdd:cd18595 81 ALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 484 SKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFS 563
Cdd:cd18595 161 IKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1388169353 564 VYVLVDSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 613
Cdd:cd18595 241 TYVLSDPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1298-1518 |
2.40e-134 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 413.81 E-value: 2.40e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1298 GKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKL 1377
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1378 TIIPQDPILFSGSLRMNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKI 1457
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 1458 LVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSP 1518
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1024-1529 |
4.54e-119 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 386.44 E-value: 4.54e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1024 VGVYGALGLAQGIFVFIAHFWSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWI 1103
Cdd:COG1132 64 LLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1104 TCFLGIISTLVMICMATPVFTIIVIPLGIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFL 1183
Cdd:COG1132 144 RSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREEREL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1184 KHNEVRIDTNQKCVFSWITSNRWLAIRLELVGNLT---VFFSALMMVIyRDTLS-GDTVGFVLSnALNITQTLNWLVRMT 1259
Cdd:COG1132 224 ERFREANEELRRANLRAARLSALFFPLMELLGNLGlalVLLVGGLLVL-SGSLTvGDLVAFILY-LLRLFGPLRQLANVL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1260 SEIETNIVAVERITEYTKVENEAPWVTDKRPPPdwPSKGKIQFNNYQVRYRPElDLVLRGITCDIGSMEKIGVVGRTGAG 1339
Cdd:COG1132 302 NQLQRALASAERIFELLDEPPEIPDPPGAVPLP--PVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSG 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1340 KSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNL---DPfnNYSDEEIWKALELAHLK 1416
Cdd:COG1132 379 KSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAKAAQAH 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1417 SFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLH 1496
Cdd:COG1132 457 EFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLS 536
|
490 500 510
....*....|....*....|....*....|...
gi 1388169353 1497 TIMDSDKVMVLDNGKIIECGSPEELLQIPGPFY 1529
Cdd:COG1132 537 TIRNADRILVLDDGRIVEQGTHEELLARGGLYA 569
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
325-613 |
1.87e-114 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 362.57 E-value: 1.87e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 325 SFLLKLVNDIFTFVSPQLLKLLISFASDRDTY-LWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKK 403
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEpLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 404 ALTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTK 483
Cdd:cd18579 82 ALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 484 SKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFS 563
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1388169353 564 VYVLVDsnNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 613
Cdd:cd18579 242 TYVLLG--NPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
637-838 |
3.80e-114 |
|
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: 357.93 E-value: 3.80e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 637 MQFSEASFTW---EHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQNG 713
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 714 TIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 793
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1388169353 794 HVGKHIFNKVLGPNgLLKGKTRLLVTHSMHFLPQVDEIVVLGNGT 838
Cdd:cd03250 161 HVGRHIFENCILGL-LLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
979-1276 |
7.74e-111 |
|
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: 352.58 E-value: 7.74e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 979 IFFIILAFVMNSVAFIGSNLWLSAWTSDSkifnsTDYPASQRDMRVGVYGALGL-AQGIFVFIAHFWSAFGFVHASNILH 1057
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDW-----SSSPNSSSGYYLGVYAALLVlASVLLVLLRWLLFVLAGLRASRRLH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1058 KQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIYVSV 1137
Cdd:cd18580 76 DKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1138 QMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNRWLAIRLELVGNL 1217
Cdd:cd18580 156 QRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGAL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 1218 TVFFSALMMVIYRDTLSGDTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYT 1276
Cdd:cd18580 236 LALVVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
979-1276 |
1.55e-103 |
|
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: 332.13 E-value: 1.55e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 979 IFFIILAFVMNSVAFIGSNLWLSAWTSDSKIFNSTDYpasqrdmrVGVYGALGLAQGIFVFIAHFWSAFGFVHASNILHK 1058
Cdd:cd18606 1 LPLLLLLLILSQFAQVFTNLWLSFWTEDFFGLSQGFY--------IGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1059 QLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIYVSVQ 1138
Cdd:cd18606 73 KALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1139 MFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNRWLAIRLELVGNLT 1218
Cdd:cd18606 153 NYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1388169353 1219 VFFSALMMVIYRDTLSGDTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYT 1276
Cdd:cd18606 233 VLIVALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
979-1276 |
6.35e-97 |
|
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: 314.02 E-value: 6.35e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 979 IFFIILAFVMNSVAFIGSNLWLSAWTSDSKifNSTDYPASQRDMR--VGVYGALGLAQGIFVFIAHFWSAFGFVHASNIL 1056
Cdd:cd18604 1 WALLLLLFVLSQLLSVGQSWWLGIWASAYE--TSSALPPSEVSVLyyLGIYALISLLSVLLGTLRYLLFFFGSLRASRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1057 HKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIYVS 1136
Cdd:cd18604 79 HERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1137 VQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNRWLAIRLELVGN 1216
Cdd:cd18604 159 IGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGA 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1217 LTVFFSALMMVIYRDTLSGdTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYT 1276
Cdd:cd18604 239 LFSFATAALLVYGPGIDAG-LAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1294-1518 |
2.91e-96 |
|
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: 308.57 E-value: 2.91e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1294 WPSKGKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDL 1373
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1374 REKLTIIPQDPILFSGSLRMNLDPFNNYSDEEIWKALelahlksfvaslqlglshEVTEAGGNLSIGQRQLLCLGRALLR 1453
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 1454 KSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSP 1518
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1029-1534 |
2.30e-91 |
|
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: 312.92 E-value: 2.30e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1029 ALGLAQGIFVFiahFWSAFGFV------HASN----ILHKQLLNNILRAPMRFFDTTPTGRIVNRFaGDISTVDDTLP-Q 1097
Cdd:COG2274 197 VLAIGLLLALL---FEGLLRLLrsylllRLGQridlRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTgS 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1098 SLRSWITCFLGIISTLVMICMAtPVFTIIVIPLGIIYVSVQMFyvsTSRQLRRLD---SVTRSPIYSHFSETVSGLPVIR 1174
Cdd:COG2274 273 LLTALLDLLFVLIFLIVLFFYS-PPLALVVLLLIPLYVLLGLL---FQPRLRRLSreeSEASAKRQSLLVETLRGIETIK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1175 AFEHQQRFLKHNEVR----IDTNQKcVFSWITSNRWLAIRLELVGNLTVFFSALMMVIyrdtlSGD-TVG-FVLSNALnI 1248
Cdd:COG2274 349 ALGAESRFRRRWENLlakyLNARFK-LRRLSNLLSTLSGLLQQLATVALLWLGAYLVI-----DGQlTLGqLIAFNIL-S 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1249 TQTLNWLVRMTS---EIETNIVAVERITEYTKVENEAPWVTDKRPPPdwPSKGKIQFNNYQVRYRPELDLVLRGITCDIG 1325
Cdd:COG2274 422 GRFLAPVAQLIGllqRFQDAKIALERLDDILDLPPEREEGRSKLSLP--RLKGDIELENVSFRYPGDSPPVLDNISLTIK 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1326 SMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNL---DPfnNYS 1402
Cdd:COG2274 500 PGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDP--DAT 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1403 DEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNE 1482
Cdd:COG2274 578 DEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL 657
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 1483 FAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFYFMAKE 1534
Cdd:COG2274 658 LKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
979-1276 |
4.05e-85 |
|
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: 281.03 E-value: 4.05e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 979 IFFIILAFVMNSVAFIGSNLWLSAWTS-----DSKIFNSTDYPASQRDMR--VGVYGALGLAQGIFVFIAHFWSAFGFVH 1051
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWTEanhdvASVVFNITSSSLEDDEVSyyISVYAGLSLGAVILSLVTNLAGELAGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1052 ASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLG 1131
Cdd:cd18602 81 AARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1132 IIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNRWLAIRL 1211
Cdd:cd18602 161 IVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388169353 1212 ELVGNLTVFFSAL--MMVIYRDTLSGDTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYT 1276
Cdd:cd18602 241 DYLGAVIVFLAALssLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
980-1276 |
3.32e-84 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 278.26 E-value: 3.32e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 980 FFIILAFVMNSVAFIGSNLWLSAWTSDSKIFNSTDYPASQRDMRVgVYGALGLAQGIFVFIAHFWSAFGFVHASNILHKQ 1059
Cdd:cd18605 2 ILILLSLILMQASRNLIDFWLSYWVSHSNNSFFNFINDSFNFFLT-VYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1060 LLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIYVSVQM 1139
Cdd:cd18605 81 LLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1140 FYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNRWLAIRLELVGNLTV 1219
Cdd:cd18605 161 YYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVLIV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1220 FF---SALMMVIYRDTLSGDTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYT 1276
Cdd:cd18605 241 TFvalTAVVQHFFGLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
326-613 |
6.82e-83 |
|
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: 274.76 E-value: 6.82e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 326 FLLKLVNDIFTFVSPQLLK-LLISFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKKA 404
Cdd:cd18596 3 ALLAVLSSVLSFAPPFFLNrLLRYLEDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 405 LTLSNLA-------------------RKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLA 465
Cdd:cd18596 83 LRRRDKSgssksseskkkdkeededeKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 466 GVGVMVLVIPINAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCV 545
Cdd:cd18596 163 GLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388169353 546 VIFVFQLTPVLVSVVTFSVYVLVdSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 613
Cdd:cd18596 243 LSLLWFLIPILVTVVTFATYTLV-MGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
325-613 |
6.91e-83 |
|
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: 273.95 E-value: 6.91e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 325 SFLLKLVNDIFTFVSPQLLKLLISFASDR-----DTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMAS 399
Cdd:cd18597 2 AGLLKLLADVLQVLSPLLLKYLINFVEDAylggpPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 400 VYKKALTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAI 479
Cdd:cd18597 82 IYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 480 LSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSV 559
Cdd:cd18597 162 LMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASM 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 560 VTFSVYVLVdsNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 613
Cdd:cd18597 242 LSFITYYAT--GHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1298-1528 |
9.72e-78 |
|
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: 257.91 E-value: 9.72e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1298 GKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKL 1377
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1378 TIIPQDPILFSGSLRMNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKI 1457
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 1458 LVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELL-QIPGPF 1528
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVF 249
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
325-613 |
1.84e-76 |
|
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: 255.60 E-value: 1.84e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 325 SFLLKLVNDIFTFVSPQLLKLLISFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKKA 404
Cdd:cd18559 2 FLLIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 405 LTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTKS 484
Cdd:cd18559 82 LRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 485 KTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFSV 564
Cdd:cd18559 162 RQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1388169353 565 YVLVDSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 613
Cdd:cd18559 242 YVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
309-857 |
3.87e-76 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 264.72 E-value: 3.87e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 309 WLMKALFKTFYMVLLKSFLLKLVNDIFTFVSPQLLKLLISFASDRDTYLWIGYLCAILLFtAALIQSFCLQCYFQLCFKL 388
Cdd:COG1132 10 RRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLG-LALLRALLSYLQRYLLARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 389 GVKVRTAIMASVYKKALTLSNLARKEYTVGETVNLMSVDAQKLMD-VTNFMHMLWSSVLQIVLSI---FFLWRELGPSVL 464
Cdd:COG1132 89 AQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQfLAHGLPQLVRSVVTLIGALvvlFVIDWRLALIVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 465 AGVGVMVLVIpinAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPS----FRDQVQNLRKKELKNLLAFS 540
Cdd:COG1132 169 LVLPLLLLVL---RLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERelerFREANEELRRANLRAARLSA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 541 QLQCVVIFVFQLTPVLVsvVTFSVYvLVdSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERLEKYL--G 618
Cdd:COG1132 246 LFFPLMELLGNLGLALV--LLVGGL-LV-LSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLdeP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 619 GDDLDTSAIRHDCNFDKAMQFSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIK 698
Cdd:COG1132 322 PEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPV-LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 699 GT-------------TAYVPQQSWIQNGTIKDNILFG-TEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGG 764
Cdd:COG1132 401 GVdirdltleslrrqIGVVPQDTFLFSGTIRENIRYGrPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 765 QKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGS 844
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL---ERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
570
....*....|...
gi 1388169353 845 YSALLAKKGEFAK 857
Cdd:COG1132 558 HEELLARGGLYAR 570
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
327-613 |
4.41e-76 |
|
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: 254.40 E-value: 4.41e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 327 LLKLVNDIFTFVSPQLLKLLISFASDRDTYLWIGYLCAILLFTAALIQSFC-LQCYFQLCfKLGVKVRTAIMASVYKKAL 405
Cdd:cd18598 4 LLKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLsSHYNFQMN-KVSLKVRAALVTAVYRKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 406 TLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTKSK 485
Cdd:cd18598 83 RVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 486 TIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFSVY 565
Cdd:cd18598 163 ALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPVLISILTFATY 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1388169353 566 VLVdsNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 613
Cdd:cd18598 243 VLM--GNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
973-1526 |
3.18e-74 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 258.92 E-value: 3.18e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 973 AIGLFSIFFIILAFVMnsVAFIGSNLWLSAWTSDSkifnstdypasqrdmrvgVYGALGLAQGIFVF---IAHFWSAFGF 1049
Cdd:COG4988 24 LLGLLSGLLIIAQAWL--LASLLAGLIIGGAPLSA------------------LLPLLGLLLAVLLLralLAWLRERAAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1050 VHASNI---LHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDD----TLPQSLRSWITC--------FLGIISTLV 1114
Cdd:COG4988 84 RAAARVkrrLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGyfarYLPQLFLAALVPllilvavfPLDWLSGLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1115 MICmatpvfTIIVIPLGIIyvsvqMFYVSTSRQLRR-LDSVTR-SpiySHFSETVSGLPVIRAF----EHQQRFLKHNE- 1187
Cdd:COG4988 164 LLV------TAPLIPLFMI-----LVGKGAAKASRRqWRALARlS---GHFLDRLRGLTTLKLFgrakAEAERIAEASEd 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1188 VRIDT--------NQKCVFSWITSnrwLAI---------RLeLVGNLTvFFSALMMVI-----Y---RDtlsgdtvgfvL 1242
Cdd:COG4988 230 FRKRTmkvlrvafLSSAVLEFFAS---LSIalvavyigfRL-LGGSLT-LFAALFVLLlapefFlplRD----------L 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1243 SNAlnitqtlnWLVRMTseietNIVAVERITEYtkVENEAPWVTDKRPPPDWPSKGKIQFNNYQVRYrPELDLVLRGITC 1322
Cdd:COG4988 295 GSF--------YHARAN-----GIAAAEKIFAL--LDAPEPAAPAGTAPLPAAGPPSIELEDVSFSY-PGGRPALDGLSL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1323 DIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNLDPFN-NY 1401
Cdd:COG4988 359 TIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRpDA 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1402 SDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQN 1481
Cdd:COG4988 439 SDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR 518
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1388169353 1482 EFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPG 1526
Cdd:COG4988 519 LAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1298-1526 |
2.49e-73 |
|
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: 244.06 E-value: 2.49e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1298 GKIQFNNYQVRYRPElDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKL 1377
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1378 TIIPQDPILFSGSLRMNLDPFNNYS-DEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSK 1456
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNAtDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1457 ILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPG 1526
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
975-1276 |
4.57e-73 |
|
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: 246.71 E-value: 4.57e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 975 GLFSIFFIILAFVMNSVAFIGSNLWLSAW------TSDSKIFNSTDYPASQRD-----MRVGVYGALGLAQGIFVFIAHF 1043
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWlkqgsgNTTNNVDNSTVDSGNISDnpdlnFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1044 WSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVF 1123
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1124 TIIVIPLGIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITS 1203
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 1204 NRWLAIRLELVGNLTVFFSALMMVIYRDTLSGDTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYT 1276
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
975-1276 |
5.44e-71 |
|
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: 240.69 E-value: 5.44e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 975 GLFSIFFIILAFVMNSVAFIGSNLWLSAW----------TSDSKIFNST--DYPASQRDMRVGVYGALGLAQGIFVFIAH 1042
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWanleeklndtTDRVQGENSTnvDIEDLDRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1043 FWSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPV 1122
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1123 FTIIVIPLGIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWIT 1202
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 1203 SNRWLAIRLELVGNLTVFFSALMMVIYRDTLSGDTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYT 1276
Cdd:cd18601 241 TSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEYS 314
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
306-857 |
2.41e-70 |
|
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: 251.68 E-value: 2.41e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 306 PKSWLMKALF---KTFYMVLLKSFLLKLvndiFTFVSPQLLKLLISF---ASDRDTyLWIgylCAILLFTAALIQSF--C 377
Cdd:COG2274 143 GLRWFLRLLRryrRLLLQVLLASLLINL----LALATPLFTQVVIDRvlpNQDLST-LWV---LAIGLLLALLFEGLlrL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 378 LQCYFQLcfKLGVKVRTAIMASVYKKALTLSNLARKEYTVGETVNLMSvDAQKLMD-VTNFMHMLWSSVLQIVLSIFFLW 456
Cdd:COG2274 215 LRSYLLL--RLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREfLTGSLLTALLDLLFVLIFLIVLF 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 457 RELGPSVLAGVGVMVLVIPINAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKK----- 531
Cdd:COG2274 292 FYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKylnar 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 532 -ELKNLLAFSQLqcVVIFVFQLTPVLVsvVTFSVYvLVDSNNIldaqkaftsiTL-----FNIL--RF--PLSMLPMMIS 601
Cdd:COG2274 372 fKLRRLSNLLST--LSGLLQQLATVAL--LWLGAY-LVIDGQL----------TLgqliaFNILsgRFlaPVAQLIGLLQ 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 602 SMLQASVSTERLEKYLGGD---DLDTSAIRHDcNFDKAMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKS 678
Cdd:COG2274 437 RFQDAKIALERLDDILDLPperEEGRSKLSLP-RLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKS 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 679 SLISAMLGEMENVHGHITIKGT-------------TAYVPQQSWIQNGTIKDNILFG-TEFNEKRYQQVLEACALLPDLE 744
Cdd:COG2274 516 TLLKLLLGLYEPTSGRILIDGIdlrqidpaslrrqIGVVLQDVFLFSGTIRENITLGdPDATDEEIIEAARLAGLHDFIE 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 745 MLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHF 824
Cdd:COG2274 596 ALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENL---RRLLKGRTVIIIAHRLST 672
|
570 580 590
....*....|....*....|....*....|...
gi 1388169353 825 LPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAK 857
Cdd:COG2274 673 IRLADRIIVLDKGRIVEDGTHEELLARKGLYAE 705
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
327-613 |
3.33e-68 |
|
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 1 (TMD1) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and they belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350035 [Multi-domain] Cd Length: 309 Bit Score: 232.51 E-value: 3.33e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 327 LLKLVNDIFTFVSPQLLKLLISFASDR------------------DTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKL 388
Cdd:cd18591 4 ILKLLGDLLGFVGPLCISGIVDYVEENtysssnstdklsvsyvtvEEFFSNGYVLAVILFLALLLQATFSQASYHIVIRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 389 GVKVRTAIMASVYKKALTLS--NLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAG 466
Cdd:cd18591 84 GIRLKTALQAMIYEKALRLSswNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 467 VGVMVLVIPINAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVV 546
Cdd:cd18591 164 AALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSLM 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388169353 547 IFVFQLTPVLVSVVTFSVYVLVDSNNiLDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 613
Cdd:cd18591 244 TFLTQASPILVTLVTFGLYPYLEGEP-LTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1030-1522 |
4.80e-68 |
|
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: 241.16 E-value: 4.80e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1030 LGLAQGIFVFIAHF---WSAFGFVHAsniLHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCF 1106
Cdd:TIGR02203 63 LAVLRGICSFVSTYllsWVSNKVVRD---IRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRET 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1107 LGIIS-TLVMICMATPVFTIIVIPLGIIYVSVQMFyvstSRQLRRLDS---VTRSPIYSHFSETVSGLPVIRAFEHQ--- 1179
Cdd:TIGR02203 140 LTVIGlFIVLLYYSWQLTLIVVVMLPVLSILMRRV----SKRLRRISKeiqNSMGQVTTVAEETLQGYRVVKLFGGQaye 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1180 -QRFLKHNEvridtnqkcvfswitSNRWLAIRLELVGNLT------VFFSALMMVIY-------RDTLS-GDTVGFVLSn 1244
Cdd:TIGR02203 216 tRRFDAVSN---------------RNRRLAMKMTSAGSISspitqlIASLALAVVLFialfqaqAGSLTaGDFTAFITA- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1245 ALNITQTLNWLVRMTSEIETNIVAVERITEYTKVENEAPwvTDKRPPPDwpSKGKIQFNNYQVRYRPELDLVLRGITCDI 1324
Cdd:TIGR02203 280 MIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKD--TGTRAIER--ARGDVEFRNVTFRYPGRDRPALDSISLVI 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1325 GSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNL---DPfNNY 1401
Cdd:TIGR02203 356 EPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT-EQA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1402 SDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQN 1481
Cdd:TIGR02203 435 DRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALER 514
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1388169353 1482 EFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELL 1522
Cdd:TIGR02203 515 LMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELL 555
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1077-1529 |
2.43e-67 |
|
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: 238.90 E-value: 2.43e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1077 TGRIVNRFAGDISTVDDTLpqsLRSW------------ITCFLGIIS-TLVMICMATPVFTIIVIPLgiiyvsvqMFYVS 1143
Cdd:COG4987 111 SGDLLNRLVADVDALDNLY---LRVLlpllvallvilaAVAFLAFFSpALALVLALGLLLAGLLLPL--------LAARL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1144 TSRQLRRLdSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKH---NEVRIDTNQKcvfswiTSNRWLAIR---LELVGNL 1217
Cdd:COG4987 180 GRRAGRRL-AAARAALRARLTDLLQGAAELAAYGALDRALARldaAEARLAAAQR------RLARLSALAqalLQLAAGL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1218 TVFFSALMMV--IYRDTLSG-DTVGFVLSnALNITQTLNWLVRMTSEIETNIVAVERITEytkVENEAPWVTDKRPPPDW 1294
Cdd:COG4987 253 AVVAVLWLAAplVAAGALSGpLLALLVLA-ALALFEALAPLPAAAQHLGRVRAAARRLNE---LLDAPPAVTEPAEPAPA 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1295 PSKGKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLR 1374
Cdd:COG4987 329 PGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLR 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1375 EKLTIIPQDPILFSGSLRMNL---DPfnNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRAL 1451
Cdd:COG4987 409 RRIAVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARAL 486
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388169353 1452 LRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFY 1529
Cdd:COG4987 487 LRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYR 564
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1300-1522 |
4.95e-64 |
|
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: 217.48 E-value: 4.95e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTI 1379
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1380 IPQDPILFSGSLRMNL---DPfnNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSK 1456
Cdd:cd03251 81 VSQDVFLFNDTVAENIaygRP--GATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 1457 ILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELL 1522
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELL 224
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1029-1531 |
1.04e-61 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 223.06 E-value: 1.04e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1029 ALGLAQGIFV--FIA---HFWSAFGFVHASNILHKQL----LNNILRAPMRFFDTTPTGRIVNRFAGDISTVDD----TL 1095
Cdd:PRK10790 64 VAGLAAAYVGlqLLAaglHYAQSLLFNRAAVGVVQQLrtdvMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDlyvtVV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1096 PQSLRS--WITCFLGIISTL--VMICMATPVFTIIVIPLgIIYvsvQMFYVSTSRQLRRLdsvtRSPIYSHFSETVSGLP 1171
Cdd:PRK10790 144 ATVLRSaaLIGAMLVAMFSLdwRMALVAIMIFPAVLVVM-VIY---QRYSTPIVRRVRAY----LADINDGFNEVINGMS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1172 VIRAFEHQQRFLK--------HNEVRIDTnqkcvfswitsnrwlaIRLE--LVGNLTVFFSAL----MMVIYRDTLSGdT 1237
Cdd:PRK10790 216 VIQQFRQQARFGErmgeasrsHYMARMQT----------------LRLDgfLLRPLLSLFSALilcgLLMLFGFSASG-T 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1238 VGF-VLSNALNITQTLNW-LVRMTSE---IETNIVAVERITEYTKVENEaPWVTDKRPPpdwpSKGKIQFNNYQVRYRPE 1312
Cdd:PRK10790 279 IEVgVLYAFISYLGRLNEpLIELTTQqsmLQQAVVAGERVFELMDGPRQ-QYGNDDRPL----QSGRIDIDNVSFAYRDD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1313 lDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLR 1392
Cdd:PRK10790 354 -NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFL 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1393 MNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETD 1472
Cdd:PRK10790 433 ANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTE 512
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 1473 NLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFYFM 1531
Cdd:PRK10790 513 QAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQM 571
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
327-614 |
4.31e-60 |
|
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: 208.64 E-value: 4.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 327 LLKLVNDIFTFVSPQLLKLLI-SFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKKAL 405
Cdd:cd18594 4 ILLFLEESLKIVQPLLLGRLVaYFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 406 TLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTKSK 485
Cdd:cd18594 84 KLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 486 TIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFSVY 565
Cdd:cd18594 164 KYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPY 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1388169353 566 VLvdSNNILDAQKAFTSITLFNILRFPLSM-LPMMISSMLQASVSTERLE 614
Cdd:cd18594 244 VL--TGNTLTARKVFTVISLLNALRMTITRfFPESIQTLSESRVSLKRIQ 291
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1300-1531 |
1.46e-59 |
|
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: 204.77 E-value: 1.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELDlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTI 1379
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1380 IPQDPILFSGSLRMNL---DPfnNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSK 1456
Cdd:cd03253 80 VPQDTVLFNDTIGYNIrygRP--DATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 1457 ILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFYFM 1531
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
637-838 |
2.24e-59 |
|
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: 203.72 E-value: 2.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 637 MQFSEASFTWEHDSeATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHI-----------------TIKG 699
Cdd:cd03290 1 VQVTNGYFSWGSGL-ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 700 TTAYVPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNL 779
Cdd:cd03290 80 SVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 780 DIYLLDDPLSAVDAHVGKHIFNKvlgpnGLLK-----GKTRLLVTHSMHFLPQVDEIVVLGNGT 838
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQE-----GILKflqddKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1031-1531 |
2.07e-58 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 215.74 E-value: 2.07e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1031 GLAQGIFVFiahfwsAFGFVHASniLHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGII 1110
Cdd:TIGR00958 219 GLRGGSFNY------TMARINLR--IREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1111 STLVMICMATPVFTII-VIPLGIIYVSVQMF---YVSTSRQLRrlDSVTRSPIYSHfsETVSGLPVIRAF--EHQ--QRF 1182
Cdd:TIGR00958 291 GLLGFMLWLSPRLTMVtLINLPLVFLAEKVFgkrYQLLSEELQ--EAVAKANQVAE--EALSGMRTVRSFaaEEGeaSRF 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1183 LKHNEVRIDTNQK-----CVFSWITSNRWLAIRLelvgnlTVFFSALMMVIYRDTLSGDTVGFVLSNaLNITQTLNWLVR 1257
Cdd:TIGR00958 367 KEALEETLQLNKRkalayAGYLWTTSVLGMLIQV------LVLYYGGQLVLTGKVSSGNLVSFLLYQ-EQLGEAVRVLSY 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1258 MTSEIETNIVAVERITEYTKVENEAPWVTDKRPPPDwpsKGKIQFNNYQVRY--RPELdLVLRGITCDIGSMEKIGVVGR 1335
Cdd:TIGR00958 440 VYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNL---EGLIEFQDVSFSYpnRPDV-PVLKGLTFTLHPGEVVALVGP 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1336 TGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNLD-PFNNYSDEEIWKALELAH 1414
Cdd:TIGR00958 516 SGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPDEEIMAAAKAAN 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1415 LKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTiqNEFAHCTVITIAHR 1494
Cdd:TIGR00958 596 AHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHR 673
|
490 500 510
....*....|....*....|....*....|....*..
gi 1388169353 1495 LHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFYFM 1531
Cdd:TIGR00958 674 LSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1223-1523 |
9.94e-58 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 211.60 E-value: 9.94e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1223 ALMMVIYRDTLSGD-TVG-FVLSNA--LNITQTLNWLVRMTSEIETNIVAVERITEYTKVENEapwVTDKRPPPDWPSK- 1297
Cdd:COG5265 279 AMMLMAAQGVVAGTmTVGdFVLVNAylIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPE---VADAPDAPPLVVGg 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1298 GKIQFNNYQVRYRPElDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKL 1377
Cdd:COG5265 356 GEVRFENVSFGYDPE-RPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAI 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1378 TIIPQDPILFSGSLRMNLdpfnNY-----SDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALL 1452
Cdd:COG5265 435 GIVPQDTVLFNDTIAYNI----AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLL 510
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 1453 RKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQ 1523
Cdd:COG5265 511 KNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLA 581
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1300-1511 |
1.35e-57 |
|
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: 196.45 E-value: 1.35e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTI 1379
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1380 IPQDPILFSGSLRMNLdpfnnysdeeiwkalelahlksfvaslqlglshevteaggnLSIGQRQLLCLGRALLRKSKILV 1459
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 1460 LDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGK 1511
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1300-1535 |
1.36e-57 |
|
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: 199.30 E-value: 1.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRY--RPELdLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKL 1377
Cdd:cd03249 1 IEFKNVSFRYpsRPDV-PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1378 TIIPQDPILFSGSLRMNL---DpfNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRK 1454
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIrygK--PDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1455 SKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFYFMAKE 1534
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
.
gi 1388169353 1535 A 1535
Cdd:cd03249 238 Q 238
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
325-613 |
4.83e-56 |
|
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: 196.63 E-value: 4.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 325 SFLLKLVNDIFTFVSPQ-LLKLLISFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKK 403
Cdd:cd18592 2 SILLLLISLIFGFIGPTiLIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 404 ALTLSNLarKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTK 483
Cdd:cd18592 82 ILRLRSL--GDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 484 SKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFS 563
Cdd:cd18592 160 TGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1388169353 564 VYVLvdSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 613
Cdd:cd18592 240 AHVA--LGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1300-1531 |
2.39e-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: 190.00 E-value: 2.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTI 1379
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1380 IPQDPILFSGSLRMNL---DPfnNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSK 1456
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 1457 ILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFYFM 1531
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
636-853 |
1.95e-53 |
|
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: 197.67 E-value: 1.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 636 AMQFSEASFTWEhDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-------------TA 702
Cdd:COG4988 336 SIELEDVSFSYP-GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpaswrrqIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 703 YVPQQSWIQNGTIKDNILFGT-EFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDI 781
Cdd:COG4988 415 WVPQNPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPL 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 782 YLLDDPLSAVDAHVGKHIFNKVLgpnGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKG 853
Cdd:COG4988 495 LLLDEPTAHLDAETEAEILQALR---RLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
334-613 |
2.87e-53 |
|
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: 188.97 E-value: 2.87e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 334 IFTF-------VSPQLLKLLIS-FASDRDTY-LWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKKA 404
Cdd:cd18593 4 IFLFleeairvVQPIFLGKLIRyFEGNGSSIsLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIYRKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 405 LTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTKS 484
Cdd:cd18593 84 LRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFGKLF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 485 KTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFSV 564
Cdd:cd18593 164 SKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTFLA 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1388169353 565 YVLVDsnNILDAQKAFTSITLFNILRFPLSM-LPMMISSMLQASVSTERL 613
Cdd:cd18593 244 YILLG--NILTAERVFVTMALYNAVRLTMTLfFPFAIQFGSELSVSIRRI 291
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
654-862 |
3.50e-52 |
|
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: 185.45 E-value: 3.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQNGTIKDNILFGTEFNEKRYQQV 733
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 734 LEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLGPngLLKGK 813
Cdd:cd03291 133 VKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCK--LMANK 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1388169353 814 TRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAKNLKTF 862
Cdd:cd03291 211 TRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGY 259
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
386-857 |
4.76e-52 |
|
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: 193.83 E-value: 4.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 386 FKLGVKVRTaimaSVYKKALTLSNLARKEYTVGETVNLMSVDAQKLMDVtnFMHML---WSSVLQIVLSIFFLWR---EL 459
Cdd:COG4987 84 LRLLADLRV----RLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNL--YLRVLlplLVALLVILAAVAFLAFfspAL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 460 GPSVLAGVGVMVLVIPINAILSTKSKTIQVKNMKNkDKRLKIMnEILSGIKILKYFAWEPSFRDQVQNL------RKKEL 533
Cdd:COG4987 158 ALVLALGLLLAGLLLPLLAARLGRRAGRRLAAARA-ALRARLT-DLLQGAAELAAYGALDRALARLDAAearlaaAQRRL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 534 KNLLAFSQLqcVVIFVFQLTpvLVSVVTFSVYvLVDSNNILDAQKA---FTSITLFNILrfplSMLPMMISSMLQASVST 610
Cdd:COG4987 236 ARLSALAQA--LLQLAAGLA--VVAVLWLAAP-LVAAGALSGPLLAllvLAALALFEAL----APLPAAAQHLGRVRAAA 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 611 ERLEKyLGGDDLDTSAIRHDCNFDK--AMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEM 688
Cdd:COG4987 307 RRLNE-LLDAPPAVTEPAEPAPAPGgpSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 689 ENVHGHITIKGT-------------TAYVPQQSWIQNGTIKDNILFGT-EFNEKRYQQVLEACALLPDLEMLPGGDLAEI 754
Cdd:COG4987 386 DPQSGSITLGGVdlrdldeddlrrrIAVVPQRPHLFDTTLRENLRLARpDATDEELWAALERVGLGDWLAALPDGLDTWL 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 755 GEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLgpnGLLKGKTRLLVTHSMHFLPQVDEIVVL 834
Cdd:COG4987 466 GEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLL---EALAGRTVLLITHRLAGLERMDRILVL 542
|
490 500
....*....|....*....|...
gi 1388169353 835 GNGTIVEKGSYSALLAKKGEFAK 857
Cdd:COG4987 543 EDGRIVEQGTHEELLAQNGRYRQ 565
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
980-1275 |
6.45e-52 |
|
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: 185.11 E-value: 6.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 980 FFIILAFVMNSVAFIGSNLWLSAWTSDSKifnstDYPASQRDMRVGVYGALGLAQGIFVFIAHFWSAFGFVHASNILHKQ 1059
Cdd:cd18559 2 FLLIKLVLCNHVFSGPSNLWLLLWFDDPV-----NGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1060 LLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIvIPLGIIYVSVQM 1139
Cdd:cd18559 77 LYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVG-IPLGLLYVPVNR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1140 FYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDtNQKCVFSWITSNRWLAIRLELVGNLTV 1219
Cdd:cd18559 156 VYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIV 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 1220 FFSALMMVIYRDTLSGdTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEY 1275
Cdd:cd18559 235 LFASFFAYVSRHSLAG-LVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLER 289
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1298-1513 |
9.61e-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: 181.63 E-value: 9.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1298 GKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKL 1377
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1378 TIIPQDPILFSGSLRMNLDPFNNY-SDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSK 1456
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1388169353 1457 ILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKII 1513
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1106-1537 |
1.27e-50 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 189.79 E-value: 1.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1106 FLGIISTLVMICMATPV---FTIIVIPLGIIYVSVQMFYVSTSRQLRRldSVTR--SPIYSHFSETVSGLPVIRAF---E 1177
Cdd:PRK13657 138 LATLVALVVLLPLALFMnwrLSLVLVVLGIVYTLITTLVMRKTKDGQA--AVEEhyHDLFAHVSDAIGNVSVVQSYnriE 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1178 HQQRFLKHNEVRIDTNQKCVFSWitsnrWlairlELVGNLTVFFSAL-MMVIY--------RDTLS-GDTVGFVLSNALN 1247
Cdd:PRK13657 216 AETQALRDIADNLLAAQMPVLSW-----W-----ALASVLNRAASTItMLAILvlgaalvqKGQLRvGEVVAFVGFATLL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1248 ITQtlnwLVRMTSEIETNIVAVERITEYTKVENEAPWVTDkrpPPDWPS----KGKIQFNNYQVRY---RPELDlvlrGI 1320
Cdd:PRK13657 286 IGR----LDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRD---PPGAIDlgrvKGAVEFDDVSFSYdnsRQGVE----DV 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1321 TCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNL---DP 1397
Cdd:PRK13657 355 SFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIrvgRP 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1398 fnNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQT 1477
Cdd:PRK13657 435 --DATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKA 512
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1478 TIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFYFMAKEAGI 1537
Cdd:PRK13657 513 ALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQGM 572
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1065-1533 |
3.59e-48 |
|
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: 184.39 E-value: 3.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1065 LRAPMRFFDTTPTGRIVNRFAGdISTVDDTLPQS-LRSWITCFLGIISTLVMIC----MATPVFTIIVIPLGIIYVSvQM 1139
Cdd:TIGR03797 220 LRLPVSFFRQYSTGDLASRAMG-ISQIRRILSGStLTTLLSGIFALLNLGLMFYyswkLALVAVALALVAIAVTLVL-GL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1140 FYVSTSRQLRRLDSvtrsPIYSHFSETVSGLPVIRAFEHQQRFLkhnevridtnqkcvFSW---ITSNRWLAIRLELVGN 1216
Cdd:TIGR03797 298 LQVRKERRLLELSG----KISGLTVQLINGISKLRVAGAENRAF--------------ARWaklFSRQRKLELSAQRIEN 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1217 -LTVFFSAL----MMVIY--------RDTLS-GDTVGF------VLSNALNITQTLnwlvrmtseieTNIVAVERITEYT 1276
Cdd:TIGR03797 360 lLTVFNAVLpvltSAALFaaaisllgGAGLSlGSFLAFntafgsFSGAVTQLSNTL-----------ISILAVIPLWERA 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1277 K-VENEAPWVTDKRPPPDWPSkGKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLtnclFRIL---E 1352
Cdd:TIGR03797 429 KpILEALPEVDEAKTDPGKLS-GAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTL----LRLLlgfE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1353 AAG-GQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVT 1431
Cdd:TIGR03797 504 TPEsGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVIS 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1432 EAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETdnliQTTIQNEFA--HCTVITIAHRLHTIMDSDKVMVLDN 1509
Cdd:TIGR03797 584 EGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRT----QAIVSESLErlKVTRIVIAHRLSTIRNADRIYVLDA 659
|
490 500
....*....|....*....|....
gi 1388169353 1510 GKIIECGSPEELLQIPGPFYFMAK 1533
Cdd:TIGR03797 660 GRVVQQGTYDELMAREGLFAQLAR 683
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1061-1529 |
1.72e-47 |
|
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: 183.02 E-value: 1.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1061 LNNILRAPMRFFDTTPTGRIVNRFAgDISTVDDTLPQSLRS-----WITCFLGIIstLVMICMATPVFTIIVIPlgiIYV 1135
Cdd:TIGR01193 236 IKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTILSlfldmWILVIVGLF--LVRQNMLLFLLSLLSIP---VYA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1136 SVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNR-WLAIR--LE 1212
Cdd:TIGR01193 310 VIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQgQQAIKavTK 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1213 LVGNLTVFFSALMMVIYRDTLSGDTVGFvlsNAL--NITQTLNWLVRMTSEIETNIVAVERITEYTKVENEapWVTDKRP 1290
Cdd:TIGR01193 390 LILNVVILWTGAYLVMRGKLTLGQLITF---NALlsYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSE--FINKKKR 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1291 PPDWPSKGKIQFNNYQVRYRPElDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGL 1370
Cdd:TIGR01193 465 TELNNLNGDIVINDVSYSYGYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDR 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1371 HDLREKLTIIPQDPILFSGSLRMNLDPFN--NYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLG 1448
Cdd:TIGR01193 544 HTLRQFINYLPQEPYIFSGSILENLLLGAkeNVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALA 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1449 RALLRKSKILVLDEATAAVDLETDNLIQTTIQNeFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPF 1528
Cdd:TIGR01193 624 RALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFY 702
|
.
gi 1388169353 1529 Y 1529
Cdd:TIGR01193 703 A 703
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1056-1522 |
2.49e-47 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 179.83 E-value: 2.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1056 LHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIyV 1135
Cdd:PRK11176 100 MRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVIAPI-V 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1136 SVQMFYVSTS-RQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQ----RFlkhNEVRIDTNQ---KCVFSWITSNrwl 1207
Cdd:PRK11176 179 SIAIRVVSKRfRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEvetkRF---DKVSNRMRQqgmKMVSASSISD--- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1208 aIRLELVGNLtvffsALMMVIY-------RDTLSGDTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYTKVEN 1280
Cdd:PRK11176 253 -PIIQLIASL-----ALAFVLYaasfpsvMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQ 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1281 EAPwvTDKRPPPdwPSKGKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIII 1360
Cdd:PRK11176 327 EKD--EGKRVIE--RAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILL 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1361 DGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNLD--PFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLS 1438
Cdd:PRK11176 403 DGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAyaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLS 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1439 IGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSP 1518
Cdd:PRK11176 483 GGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTH 562
|
....
gi 1388169353 1519 EELL 1522
Cdd:PRK11176 563 AELL 566
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1298-1522 |
5.89e-46 |
|
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: 167.34 E-value: 5.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1298 GKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGgQIIIDGVDIASIGLHDLREKL 1377
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEG-DIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1378 TIIPQDPILFSGSLRMNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKI 1457
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 1458 LVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELL 1522
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1328-1531 |
1.13e-44 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 171.95 E-value: 1.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1328 EKIGVVGRTGAGKSSLTNCLFRILeAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNL---DPfnNYSDE 1404
Cdd:PRK11174 377 QRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllgNP--DASDE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1405 EIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFA 1484
Cdd:PRK11174 454 QLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR 533
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1388169353 1485 HCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFYFM 1531
Cdd:PRK11174 534 RQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1297-1512 |
2.18e-43 |
|
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: 158.02 E-value: 2.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1297 KGKIQFNNYQVRYRPELD-LVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLRE 1375
Cdd:cd03248 9 KGIVKFQNVTFAYPTRPDtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1376 KLTIIPQDPILFSGSLRMNLD-PFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRK 1454
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1388169353 1455 SKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKI 1512
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
639-857 |
6.28e-42 |
|
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: 153.93 E-value: 6.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 639 FSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-------------TAYVP 705
Cdd:cd03251 3 FKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqIGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 706 QQSWIQNGTIKDNILFGTEfNEKRyQQVLEAC--ALLPDLEM-LPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIY 782
Cdd:cd03251 83 QDVFLFNDTVAENIAYGRP-GATR-EEVEEAAraANAHEFIMeLPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 783 LLDDPLSAVDAhVGKHIFNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAK 857
Cdd:cd03251 161 ILDEATSALDT-ESERLVQAAL--ERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
638-853 |
2.62e-41 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 151.99 E-value: 2.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 638 QFSEASFTWEHDsEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYV 704
Cdd:cd03254 4 EFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDirdisrkslrsmiGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 705 PQQSWIQNGTIKDNILFGTEFN-EKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYL 783
Cdd:cd03254 83 LQDTFLFSGTIMENIRLGRPNAtDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 784 LDDPLSAVDAHVGKHIFNKVLgpnGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKG 853
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALE---KLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
637-837 |
1.97e-40 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 147.53 E-value: 1.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 637 MQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-------------TAY 703
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdlrdldleslrknIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 704 VPQQSWIQNGTIKDNILfgtefnekryqqvleacallpdlemlpggdlaeigekginlSGGQKQRISLARATYQNLDIYL 783
Cdd:cd03228 81 VPQDPFLFSGTIRENIL-----------------------------------------SGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 784 LDDPLSAVDAHVGKHIFNKVLgpnGLLKGKTRLLVTHSMHFLPQVDEIVVLGNG 837
Cdd:cd03228 120 LDEATSALDPETEALILEALR---ALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1285-1507 |
2.85e-40 |
|
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: 157.83 E-value: 2.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1285 VTDKRPPPDWPSKGK-------IQFNNYQVRYrPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQ 1357
Cdd:TIGR02857 300 VLDAAPRPLAGKAPVtaapassLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGS 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1358 IIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNLDPFNNY-SDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGN 1436
Cdd:TIGR02857 379 IAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAG 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 1437 LSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVL 1507
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
638-857 |
3.08e-40 |
|
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: 149.30 E-value: 3.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 638 QFSEASFTWeHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAYV 704
Cdd:cd03253 2 EFENVTFAY-DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 705 PQQSWIQNGTIKDNILFG----TEfnekryQQVLEAC--ALLPDLEM-LPGGDLAEIGEKGINLSGGQKQRISLARATYQ 777
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGrpdaTD------EEVIEAAkaAQIHDKIMrFPDGYDTIVGERGLKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 778 NLDIYLLDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAK 857
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAAL---RDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAE 231
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
638-843 |
5.11e-40 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 148.12 E-value: 5.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 638 QFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTA-------------YV 704
Cdd:cd03245 4 EFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIrqldpadlrrnigYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 705 PQQSWIQNGTIKDNILFG-TEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYL 783
Cdd:cd03245 84 PQDVTLFYGTLRDNITLGaPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 784 LDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKG 843
Cdd:cd03245 164 LDEPTSAMDMNSEERLKERL---RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1077-1495 |
1.33e-39 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 155.60 E-value: 1.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1077 TGRIVNRFAGDISTVDDTLPQSLRSWITCFL-GIISTLVMICMATPVFTIIVIPLGIIYVSVQMFYVSTSRQLRRLDSVT 1155
Cdd:TIGR02868 109 RGDLLGRLGADVDALQDLYVRVIVPAGVALVvGAAAVAAIAVLSVPAALILAAGLLLAGFVAPLVSLRAARAAEQALARL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1156 RSPIYSHFSETVSGLPVIRAFEHQQRFLK------HNEVRIDTNQKCVFSWITSNRWLAIRLELVGNLTVFFSALMmviy 1229
Cdd:TIGR02868 189 RGELAAQLTDALDGAAELVASGALPAALAqveeadRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVA---- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1230 RDTLSGDTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYTKVENEAPWVTDKRPPPDWPSKGKIQFNNYQVRY 1309
Cdd:TIGR02868 265 DGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGY 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1310 rPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSG 1389
Cdd:TIGR02868 345 -PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDT 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1390 SLRMNL---DPfnNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAA 1466
Cdd:TIGR02868 424 TVRENLrlaRP--DATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEH 501
|
410 420
....*....|....*....|....*....
gi 1388169353 1467 VDLETDNLIQTTIQNEFAHCTVITIAHRL 1495
Cdd:TIGR02868 502 LDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
657-869 |
1.33e-38 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 153.85 E-value: 1.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 657 VNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMeNVHGHITIKGT-------TAYVPQQSWI-QN-----GTIKDNILFG- 722
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIelreldpESWRKHLSWVgQNpqlphGTLRDNVLLGn 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 723 TEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNK 802
Cdd:PRK11174 448 PDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388169353 803 VlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAknlkTFLRHTGPE 869
Cdd:PRK11174 528 L---NAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFA----TLLAHRQEE 587
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1266-1529 |
2.12e-38 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 153.06 E-value: 2.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1266 IVAVERITEYTKVENEAPWVTDKRPPPDwpsKGKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTN 1345
Cdd:PRK11160 308 IASARRINEITEQKPEVTFPTTSTAAAD---QVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1346 CLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNL---DPfnNYSDEEIWKALELAHLKSFVASL 1422
Cdd:PRK11160 385 LLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKLLEDD 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1423 QlGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSD 1502
Cdd:PRK11160 463 K-GLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFD 541
|
250 260
....*....|....*....|....*..
gi 1388169353 1503 KVMVLDNGKIIECGSPEELLQIPGPFY 1529
Cdd:PRK11160 542 RICVMDNGQIIEQGTHQELLAQQGRYY 568
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
979-1249 |
2.30e-38 |
|
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: 145.09 E-value: 2.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 979 IFFIILAFVMNSVAFIGSNLWLSAWTSDskIFNSTDYPASQRDMRVGVYGALGLAQGIFVFIAHFWSAFGFVHASNILHK 1058
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDV--LLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1059 QLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIYVSVQ 1138
Cdd:pfam00664 79 KLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1139 MFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNRWLAIRLELVGNLT 1218
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLS 238
|
250 260 270
....*....|....*....|....*....|....
gi 1388169353 1219 VFFSALM---MVIYRDTLSGDTVGFVLSNALNIT 1249
Cdd:pfam00664 239 YALALWFgayLVISGELSVGDLVAFLSLFAQLFG 272
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
636-834 |
4.39e-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: 148.20 E-value: 4.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 636 AMQFSEASFTWEhDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------A 702
Cdd:TIGR02857 321 SLEFSGVSVAYP-GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPladadadswrdqiA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 703 YVPQQSWIQNGTIKDNILFGT-EFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDI 781
Cdd:TIGR02857 400 WVPQHPFLFAGTIAENIRLARpDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 782 YLLDDPLSAVDAHVGKHIFNKVLgpnGLLKGKTRLLVTHSMHFLPQVDEIVVL 834
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALR---ALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
655-860 |
8.10e-37 |
|
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: 139.60 E-value: 8.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYVPQQSWIQNGTIKDNILF 721
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDirdlnlrwlrsqiGLVSQEPVLFDGTIAENIRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 722 GTefNEKRYQQVLEAC--ALLPD-LEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKH 798
Cdd:cd03249 100 GK--PDATDEEVEEAAkkANIHDfIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 799 IFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAKNLK 860
Cdd:cd03249 178 VQEAL---DRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVK 236
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
963-1272 |
9.96e-37 |
|
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350044 [Multi-domain] Cd Length: 324 Bit Score: 142.25 E-value: 9.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 963 KFSIYLEYLQA-----IGLFSIFFIILAFVMNSVA---FIGSNLWLSAWTSDSKIFNSTDYPASQRDMRVGVYGALGLAQ 1034
Cdd:cd18600 2 TWNTYLRYITShksliFVLILCLVIFAIEVAASLVglwLLRSQADRVNTTRPESSSNTYAVIVTFTSSYYVFYIYVGVAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1035 GIFVFiaHFWSAFGFVHA----SNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGII 1110
Cdd:cd18600 82 SLLAM--GFFRGLPLVHTlitvSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1111 STLVMICMATPVFTIIVIPLGIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRI 1190
Cdd:cd18600 160 GAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1191 DTNQKCVFSWITSNRWLAIRLELVgnLTVFFSALMMVIYRDTLSGD-TVGFVLSNALNITQTLNWLVRMTSEIETNIVAV 1269
Cdd:cd18600 240 NLHTANWFLYLSTLRWFQMRIEMI--FVIFFTAVTFISIGTTGDGEgRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSV 317
|
...
gi 1388169353 1270 ERI 1272
Cdd:cd18600 318 SRI 320
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1300-1512 |
5.46e-35 |
|
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: 131.95 E-value: 5.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTI 1379
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1380 IPQDPILFSGSLRMNLdpfnnysdeeiwkalelahlksfvaslqlglshevteaggnLSIGQRQLLCLGRALLRKSKILV 1459
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 1460 LDEATAAVDLETDNLIQTTIQN-EFAHCTVITIAHRLHTIMDSDKVMVLDNGKI 1512
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
634-844 |
1.38e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 130.59 E-value: 1.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 634 DKAMQFSEASFTWehDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--------AYVP 705
Cdd:COG1121 4 MPAIELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPprrarrriGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 706 QQSWIQNG---TIKDNILFGT--------EFNEKRYQQVLEAcallpdLEMLPGGDLAE--IGEkginLSGGQKQRISLA 772
Cdd:COG1121 82 QRAEVDWDfpiTVRDVVLMGRygrrglfrRPSRADREAVDEA------LERVGLEDLADrpIGE----LSGGQQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388169353 773 RATYQNLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK-----GKTRLLVTHSMHFLPQ-VDEIVVLgNGTIVEKGS 844
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYE-------LLRelrreGKTILVVTHDLGAVREyFDRVLLL-NRGLVAHGP 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1300-1522 |
7.65e-33 |
|
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: 127.83 E-value: 7.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPElDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTI 1379
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1380 IPQDPI--LFSGSLR-------MNLdpfnNYSDEEIWK----ALELahlksfvaslqLGLSHEVTEAGGNLSIGQRQLLC 1446
Cdd:COG1122 80 VFQNPDdqLFAPTVEedvafgpENL----GLPREEIRErveeALEL-----------VGLEHLADRPPHELSGGQKQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1447 LGRALLRKSKILVLDEATAAVDLE-TDNLIQT--TIQNEfaHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELL 1522
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRgRRELLELlkRLNKE--GKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVF 222
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
504-857 |
1.08e-32 |
|
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: 137.18 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 504 EILSGIKILKYFAWEPSFRDQVQ----NLRKKELKNLLAfSQLQCVVIFVFQLTpvLVSVVTFSVYVLVDSNNILDAQka 579
Cdd:TIGR01193 339 EDLNGIETIKSLTSEAERYSKIDsefgDYLNKSFKYQKA-DQGQQAIKAVTKLI--LNVVILWTGAYLVMRGKLTLGQ-- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 580 ftSITLFNILRFPLSMLPMMIS---SMLQASVSTERL-EKYL-GGDDLDTSAIRHDCNFDKAMQFSEASFTWEHDSEAtV 654
Cdd:TIGR01193 414 --LITFNALLSYFLTPLENIINlqpKLQAARVANNRLnEVYLvDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNI-L 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYVPQQSWIQNGTIKDNILF 721
Cdd:TIGR01193 491 SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlkdidrhtlrqfiNYLPQEPYIFSGSILENLLL 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 722 GTEFNEKRyQQVLEACALLP---DLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKH 798
Cdd:TIGR01193 571 GAKENVSQ-DEIWAACEIAEikdDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKK 649
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 799 IFNKVLGpnglLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAK 857
Cdd:TIGR01193 650 IVNNLLN----LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYAS 704
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
636-857 |
1.47e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 135.34 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 636 AMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TAY---------- 703
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiADYseaalrqais 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 704 -VPQQSWIQNGTIKDNILFGT-EFNEKRYQQVLEACALLPDLEMLPGGDlAEIGEKGINLSGGQKQRISLARATYQNLDI 781
Cdd:PRK11160 418 vVSQRVHLFSATLRDNLLLAApNASDEALIEVLQQVGLEKLLEDDKGLN-AWLGEGGRQLSGGEQRRLGIARALLHDAPL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 782 YLLDDPLSAVDAHVGKHIFNkvlgpngLL----KGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAK 857
Cdd:PRK11160 497 LLLDEPTEGLDAETERQILE-------LLaehaQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQ 569
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
322-593 |
6.14e-32 |
|
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: 126.60 E-value: 6.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 322 LLKSFLLKLVNDIFTFVSPQLLKLLI-SFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASV 400
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILdVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 401 YKKALTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSV-LAGVGVMVLVIPINAI 479
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLtLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 480 LSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSV 559
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 1388169353 560 VTFSVYVLVDSNNILDAQKAFTSITLFNILRFPL 593
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1300-1516 |
1.34e-31 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 122.42 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGlHDLREKLTI 1379
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1380 IPQDPILFSGSLRMNLdpfnnysdeeiwkalelahlksfvaslqlglshevteaGGNLSIGQRQLLCLGRALLRKSKILV 1459
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1388169353 1460 LDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECG 1516
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1305-1523 |
1.40e-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: 131.18 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1305 YQVRYRPELDlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIG---LHDLREKLTIIP 1381
Cdd:COG1123 270 YPVRGKGGVR-AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQMVF 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1382 QDPilfSGSL--RMNLdpfnnysDEEIWKALELAHLKSF------VASL--QLGLSHEVTEA-GGNLSIGQRQLLCLGRA 1450
Cdd:COG1123 349 QDP---YSSLnpRMTV-------GDIIAEPLRLHGLLSRaerrerVAELleRVGLPPDLADRyPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1451 LLRKSKILVLDEATAAVDLetdnLIQTTI-------QNEFaHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELL 1522
Cdd:COG1123 419 LALEPKLLILDEPTSALDV----SVQAQIlnllrdlQREL-GLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVF 493
|
.
gi 1388169353 1523 Q 1523
Cdd:COG1123 494 A 494
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
654-857 |
4.38e-31 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 130.59 E-value: 4.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYVPQQSWIQNGTIKDNIL 720
Cdd:TIGR02204 356 LDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDlrqldpaelrarmALVPQDPVLFAASVMENIR 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 721 FGTEfnEKRYQQVLEACALLPDLEM---LPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHvGK 797
Cdd:TIGR02204 436 YGRP--DATDEEVEAAARAAHAHEFisaLPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAE-SE 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 798 HIFNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAK 857
Cdd:TIGR02204 513 QLVQQAL--ETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYAR 570
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1290-1523 |
6.80e-31 |
|
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: 129.87 E-value: 6.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1290 PPPdwpsKGKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIG 1369
Cdd:COG4618 325 PRP----KGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1370 LHDLREKLTIIPQDPILFSGSLRMNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGR 1449
Cdd:COG4618 401 REELGRHIGYLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLAR 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 1450 ALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAH-CTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQ 1523
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
637-844 |
1.83e-30 |
|
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: 120.68 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 637 MQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG---TT----------AY 703
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiSKiglhdlrsriSI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 704 VPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYL 783
Cdd:cd03244 83 IPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 784 LDDPLSAVDAHVGKHIfNKVLGPNglLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGS 844
Cdd:cd03244 163 LDEATASVDPETDALI-QKTIREA--FKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
417-857 |
2.34e-30 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 129.48 E-value: 2.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 417 VGETVNLMsvdaQKLMDVTNFmhmLWSSVLQIVLSIFFLWRELG------PSVlagVGVMVLVIPINAILSTKSKTIQVK 490
Cdd:TIGR01846 235 VGDTVARV----RELEQIRNF---LTGSALTVVLDLLFVVVFLAvmffysPTL---TGVVIGSLVCYALLSVFVGPILRK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 491 NMKNKDKR----LKIMNEILSGIKILKYFAWEPsfrdQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFSVYV 566
Cdd:TIGR01846 305 RVEDKFERsaaaTSFLVESVTGIETIKATATEP----QFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILL 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 567 LVDSNNILDAQKAFTSITLFNIL----RFPLSMLPMMISSMLQASVSTERLekylgGDDLDT-SAIRHD-----CNFDKA 636
Cdd:TIGR01846 381 WFGAHLVIGGALSPGQLVAFNMLagrvTQPVLRLAQLWQDFQQTGIALERL-----GDILNSpTEPRSAglaalPELRGA 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 637 MQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAY 703
Cdd:TIGR01846 456 ITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGvdlaiadpawlrrQMGV 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 704 VPQQSWIQNGTIKDNILFGTEfnEKRYQQVLEACALLPDLEM---LPGGDLAEIGEKGINLSGGQKQRISLARATYQNLD 780
Cdd:TIGR01846 536 VLQENVLFSRSIRDNIALCNP--GAPFEHVIHAAKLAGAHDFiseLPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPR 613
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388169353 781 IYLLDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAK 857
Cdd:TIGR01846 614 ILIFDEATSALDYESEALIMRNM---REICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYAR 687
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
754-1529 |
4.02e-30 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 130.53 E-value: 4.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 754 IGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDaHVGKHIFNKVLgpNGLLKGKTRL--LVTHSMHFLPQVDEI 831
Cdd:PTZ00265 573 VGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTI--NNLKGNENRItiIIAHRLSTIRYANTI 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 832 VVLGN-----------------------------------------------GTIVEKGSYSALLAKKG----EFAKNLK 860
Cdd:PTZ00265 650 FVLSNrergstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnagSYIIEQGTHDALMKNKNgiyyTMINNQK 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 861 TFLRHT-------GPEEEATVHDGSE---EEDDDYGLISSVEEIPEDAASITMRRENSFRRTLsrssrsnGRHLKSLRNS 930
Cdd:PTZ00265 730 VSSKKSsnndndkDSDMKSSAYKDSErgyDPDEMNGNSKHENESASNKKSCKMSDENASENNA-------GGKLPFLRNL 802
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 931 LKTRNvnslKEDEELvkgqKLIKKEFIETGKVKFSIYLEYLQAIGLFSIFFIILAFVMNSVaFIGSNLWlsawtsdskiF 1010
Cdd:PTZ00265 803 FKRKP----KAPNNL----RIVYREIFSYKKDVTIIALSILVAGGLYPVFALLYAKYVSTL-FDFANLE----------A 863
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1011 NSTDYpasqrdmrvGVYgALGLAQGIFV--FIAHFWSAFGFVHASNILHKQLLNNILRAPMRFFDT---TPtGRIVNRFA 1085
Cdd:PTZ00265 864 NSNKY---------SLY-ILVIAIAMFIseTLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHIN 932
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1086 GDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIplGIIYVSVQMFYV----STSRQLRRL---------- 1151
Cdd:PTZ00265 933 RDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVAAVLT--GTYFIFMRVFAIrarlTANKDVEKKeinqpgtvfa 1010
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1152 ----DSVTRSPIYShFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNRWL-----AIRLeLVGNLTVFFS 1222
Cdd:PTZ00265 1011 ynsdDEIFKDPSFL-IQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLwgfsqSAQL-FINSFAYWFG 1088
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1223 ALMmvIYRDTLSGDTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVER----ITEYTKVEneapwVTDK---RPPPDWP 1295
Cdd:PTZ00265 1089 SFL--IRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKyyplIIRKSNID-----VRDNggiRIKNKND 1161
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1296 SKGKIQFNNYQVRY--RPELDlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAA------------------- 1354
Cdd:PTZ00265 1162 IKGKIEIMDVNFRYisRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtndmtneq 1240
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1355 -----------------------------------GGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNLDpF- 1398
Cdd:PTZ00265 1241 dyqgdeeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-Fg 1319
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1399 -NNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQT 1477
Cdd:PTZ00265 1320 kEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1399
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 1478 TIQN--EFAHCTVITIAHRLHTIMDSDKVMVLDN----GKIIEC-GSPEELLQIPGPFY 1529
Cdd:PTZ00265 1400 TIVDikDKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAhGTHEELLSVQDGVY 1458
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
654-840 |
4.42e-30 |
|
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: 119.18 E-value: 4.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--------AYVPQQS---WIQNGTIKDNIL-- 720
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPlekerkriGYVPQRRsidRDFPISVRDVVLmg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 721 ------FGTEFNEKRYQQVLEAcallpdLEMLPGGDLAE--IGEkginLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 792
Cdd:cd03235 95 lyghkgLFRRLSKADKAKVDEA------LERVGLSELADrqIGE----LSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1388169353 793 AHvGKHIFNKVLgpNGL-LKGKTRLLVTHSMH-FLPQVDEIVVLgNGTIV 840
Cdd:cd03235 165 PK-TQEDIYELL--RELrREGMTILVVTHDLGlVLEYFDRVLLL-NRTVV 210
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
639-856 |
1.60e-29 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 118.36 E-value: 1.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 639 FSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAYVP 705
Cdd:cd03252 3 FEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 706 QQSWIQNGTIKDNILFGTEFNEKRyqQVLEACALLPDLEM---LPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIY 782
Cdd:cd03252 83 QENVLFNRSIRDNIALADPGMSME--RVIEAAKLAGAHDFiseLPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 783 LLDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFA 856
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNM---HDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
643-839 |
2.09e-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: 115.78 E-value: 2.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 643 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYVPQQSW 709
Cdd:cd03246 7 SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADisqwdpnelgdhvGYLPQDDE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 710 IQNGTIKDNILfgtefnekryqqvleacallpdlemlpggdlaeigekginlSGGQKQRISLARATYQNLDIYLLDDPLS 789
Cdd:cd03246 87 LFSGSIAENIL-----------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNS 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1388169353 790 AVDaHVGKHIFNKVLGpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTI 839
Cdd:cd03246 126 HLD-VEGERALNQAIA-ALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1265-1526 |
3.71e-29 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 124.82 E-value: 3.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1265 NIVavERITE-YTKVE---NEAPWVTD-KRPPPDwpSKGKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAG 1339
Cdd:PRK10789 278 NIV--ERGSAaYSRIRamlAEAPVVKDgSEPVPE--GRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSG 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1340 KSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNL---DPfnNYSDEEIWKALELAHLK 1416
Cdd:PRK10789 354 KSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIalgRP--DATQQEIEHVARLASVH 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1417 SFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLH 1496
Cdd:PRK10789 432 DDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLS 511
|
250 260 270
....*....|....*....|....*....|
gi 1388169353 1497 TIMDSDKVMVLDNGKIIECGSPEELLQIPG 1526
Cdd:PRK10789 512 ALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
652-840 |
1.21e-28 |
|
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: 122.93 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 652 ATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTA-------------YVPQQSWIQNGTIKDN 718
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLsqwdreelgrhigYLPQDVELFDGTIAEN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 719 IlfgTEFNEKRYQQVLEAcALLPDL-EM---LPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAh 794
Cdd:COG4618 426 I---ARFGDADPEKVVAA-AKLAGVhEMilrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD- 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1388169353 795 VGKHIFNKVLgpnGLLK--GKTRLLVTHSMHFLPQVDEIVVLGNGTIV 840
Cdd:COG4618 501 EGEAALAAAI---RALKarGATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1300-1522 |
1.30e-28 |
|
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: 116.30 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELdlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTI 1379
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1380 IPQDPIL-FSGSLR----M----NLDPFNNYSDEE---IWKALElahlksfvaslQLGLSH----EVTEaggnLSIGQRQ 1443
Cdd:COG1120 80 VPQEPPApFGLTVRelvaLgrypHLGLFGRPSAEDreaVEEALE-----------RTGLEHladrPVDE----LSGGERQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1444 LLCLGRALLRKSKILVLDEATAAVDL----ETDNLIQTtiQNEFAHCTVITIAHRL-HTIMDSDKVMVLDNGKIIECGSP 1518
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRR--LARERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPP 222
|
....
gi 1388169353 1519 EELL 1522
Cdd:COG1120 223 EEVL 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1317-1465 |
1.56e-28 |
|
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: 112.74 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1317 LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSG-SLRMNL 1395
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1396 -------DPFNNYSDEEIWKALElahlksfvaslQLGLSHE----VTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEAT 1464
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALE-----------KLGLGDLadrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 1388169353 1465 A 1465
Cdd:pfam00005 150 A 150
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
622-878 |
2.81e-28 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 121.99 E-value: 2.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 622 LDTSAIRHD-------CNFDKAMQFSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGH 694
Cdd:PRK13657 313 EDAVPDVRDppgaidlGRVKGAVEFDDVSFSYDNSRQG-VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 695 ITIKGTT-------------AYVPQQSWIQNGTIKDNILFGTE-FNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGIN 760
Cdd:PRK13657 392 ILIDGTDirtvtraslrrniAVVFQDAGLFNRSIEDNIRVGRPdATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQ 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 761 LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIV 840
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAAL---DELMKGRTTFIIAHRLSTVRNADRILVFDNGRVV 548
|
250 260 270
....*....|....*....|....*....|....*....
gi 1388169353 841 EKGSYSALLAKKGEFAKNLKT-FLRHTGPEEEATVHDGS 878
Cdd:PRK13657 549 ESGSFDELVARGGRFAALLRAqGMLQEDERRKQPAAEGA 587
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
653-851 |
3.00e-28 |
|
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: 121.69 E-value: 3.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 653 TVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAYVPQQSWIQNGTIKDNI 719
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGadlkqwdretfgkHIGYLPQDVELFPGTVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 720 L-FGTEFNEkryQQVLEACALLPDLEM---LPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAhV 795
Cdd:TIGR01842 413 ArFGENADP---EKIIEAAKLAGVHELilrLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDE-E 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 796 GKHIFNKVLGpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAK 851
Cdd:TIGR01842 489 GEQALANAIK-ALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
637-857 |
3.37e-28 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 121.66 E-value: 3.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 637 MQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSlISAMLGEMENV-HGHITIKGTT-------------A 702
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKST-IANLLTRFYDIdEGEILLDGHDlrdytlaslrnqvA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 703 YVPQQSWIQNGTIKDNILFGTEFNEKRYQqvLEACALLPD----LEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQN 778
Cdd:PRK11176 421 LVSQNVHLFNDTIANNIAYARTEQYSREQ--IEEAARMAYamdfINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRD 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 779 LDIYLLDDPLSAVDAHvGKHIFNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAK 857
Cdd:PRK11176 499 SPILILDEATSALDTE-SERAIQAAL--DELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQ 574
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
643-853 |
8.23e-28 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 120.59 E-value: 8.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 643 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITI-------------KGTTAYVPQQSW 709
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFhdipltklqldswRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 710 IQNGTIKDNILFGtefNEKRYQQVLEACALLP----DLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLD 785
Cdd:PRK10789 400 LFSDTVANNIALG---RPDATQQEIEHVARLAsvhdDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388169353 786 DPLSAVDAHVGKHIFNKvLGPNGllKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKG 853
Cdd:PRK10789 477 DALSAVDGRTEHQILHN-LRQWG--EGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
637-841 |
8.83e-28 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 112.95 E-value: 8.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 637 MQFSEASFTWEHDSEAT--VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--------TAYVPQ 706
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgpdRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 707 QS----WIqngTIKDNILFGTEFN----EKRYQQVLEAcallpdlemlpggdLAEIGEKGI------NLSGGQKQRISLA 772
Cdd:cd03293 81 QDallpWL---TVLDNVALGLELQgvpkAEARERAEEL--------------LELVGLSGFenayphQLSGGMRQRVALA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 773 RATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLgpnGLLK--GKTRLLVTHSMH---FLPqvDEIVVLGN--GTIVE 841
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELL---DIWRetGKTVLLVTHDIDeavFLA--DRVVVLSArpGRIVA 214
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
639-821 |
9.69e-28 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 119.77 E-value: 9.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 639 FSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAYVP 705
Cdd:TIGR02868 337 LRDLSAGYPGAPPV-LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssldqdevrrRVSVCA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 706 QQSWIQNGTIKDNILFGT-EFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLL 784
Cdd:TIGR02868 416 QDAHLFDTTVRENLRLARpDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....*..
gi 1388169353 785 DDPLSAVDAHVGKHIFNKVLGPnglLKGKTRLLVTHS 821
Cdd:TIGR02868 496 DEPTEHLDAETADELLEDLLAA---LSGRTVVLITHH 529
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1300-1516 |
1.10e-27 |
|
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: 112.98 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELDLV--LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLRE-- 1375
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1376 -KLTIIPQDPIlfsGSL--RMN-----LDPFNNYSDEEIWKALELAHLKSFVaslQLGLS--------HEvteaggnLSI 1439
Cdd:cd03257 82 kEIQMVFQDPM---SSLnpRMTigeqiAEPLRIHGKLSKKEARKEAVLLLLV---GVGLPeevlnrypHE-------LSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1440 GQRQLLCLGRALLRKSKILVLDEATAAVDLETD----NLIQtTIQNEFAhCTVITIAHRLHTI-MDSDKVMVLDNGKIIE 1514
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQaqilDLLK-KLQEELG-LTLLFITHDLGVVaKIADRVAVMYAGKIVE 226
|
..
gi 1388169353 1515 CG 1516
Cdd:cd03257 227 EG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1300-1525 |
1.11e-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: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELDL--VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKL 1377
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1378 TIIPQDPIlfsGSL--RMNLD-----PFNNY----SDEEIWKALELAHLKSFVASLqlgLSHEvteaggnLSIGQRQLLC 1446
Cdd:COG1124 82 QMVFQDPY---ASLhpRHTVDrilaePLRIHglpdREERIAELLEQVGLPPSFLDR---YPHQ-------LSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1447 LGRALLRKSKILVLDEATAAVDL----ETDNLIQtTIQNEFaHCTVITIAHRLHTI--MdSDKVMVLDNGKIIECGSPEE 1520
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVsvqaEILNLLK-DLREER-GLTYLFVSHDLAVVahL-CDRVAVMQNGRIVEELTVAD 225
|
....*
gi 1388169353 1521 LLQIP 1525
Cdd:COG1124 226 LLAGP 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1300-1525 |
1.52e-27 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 118.85 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAG---GQIIIDGVDIASIGLHDLREK 1376
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1377 LTIIPQDPilfsgslRMNLDPFNnySDEEIWKALEL-----AHLKSFVASL--QLGLSHEVTEAGGNLSIGQRQLLCLGR 1449
Cdd:COG1123 85 IGMVFQDP-------MTQLNPVT--VGDQIAEALENlglsrAEARARVLELleAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 1450 ALLRKSKILVLDEATAAVDLETDNLIQTTIQ--NEFAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1525
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAAP 234
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1316-1523 |
1.59e-27 |
|
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: 119.37 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNL 1395
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1396 DPF-NNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDN- 1473
Cdd:TIGR01842 413 ARFgENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQa 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1474 LIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQ 1523
Cdd:TIGR01842 493 LANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
333-856 |
1.61e-27 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 120.60 E-value: 1.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 333 DIFTFVSPQLLKLLISFASdrdtYLWIGYLCAILLFTAALIQSfclqcyfqlcfklgvKVRTAIMASVYKKALTLSNlar 412
Cdd:TIGR00958 196 GPPALASAIFFMCLLSIAS----SVSAGLRGGSFNYTMARINL---------------RIREDLFRSLLRQDLGFFD--- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 413 kEYTVGETVNLMSVDAQKLMDV--TNFMHMLWSSVLQIVLSIFFLWreLGPSvLAGVGV--MVLVIPINAILSTKSKTIQ 488
Cdd:TIGR00958 254 -ENKTGELTSRLSSDTQTMSRSlsLNVNVLLRNLVMLLGLLGFMLW--LSPR-LTMVTLinLPLVFLAEKVFGKRYQLLS 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 489 VKNMKNKDKRLKIMNEILSGIKILKYFAWE----PSFRDQVQNLRKKELKNLLAFSqLQCVVIFVFQLTpVLVSVVTFSV 564
Cdd:TIGR00958 330 EELQEAVAKANQVAEEALSGMRTVRSFAAEegeaSRFKEALEETLQLNKRKALAYA-GYLWTTSVLGML-IQVLVLYYGG 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 565 YVLVDSnnildaqkAFTSITLFNILRFPLSM------LPMMISSMLQASVSTERLEKYLGGD-DLDTSAIRHDCNFDKAM 637
Cdd:TIGR00958 408 QLVLTG--------KVSSGNLVSFLLYQEQLgeavrvLSYVYSGMMQAVGASEKVFEYLDRKpNIPLTGTLAPLNLEGLI 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 638 QFSEASFTWEHDSEATV-RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-------------TAY 703
Cdd:TIGR00958 480 EFQDVSFSYPNRPDVPVlKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplvqydhhylhrqVAL 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 704 VPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEM-LPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIY 782
Cdd:TIGR00958 560 VGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMeFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVL 639
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 783 LLDDPLSAVDAHVgkhifNKVLGPNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFA 856
Cdd:TIGR00958 640 ILDEATSALDAEC-----EQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYK 708
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1316-1528 |
1.68e-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: 112.60 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIAS---IGLHDLREKLTIIPQDPILFSG--- 1389
Cdd:cd03261 15 VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseAELYRLRRRMGMLFQSGALFDSltv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1390 ------SLRMNLdpfnNYSDEEIwkaLELAHLKsfvasLQL-GLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDE 1462
Cdd:cd03261 95 fenvafPLREHT----RLSEEEI---REIVLEK-----LEAvGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 1463 ATAAVD----LETDNLIQTTiqNEFAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIPGPF 1528
Cdd:cd03261 163 PTAGLDpiasGVIDDLIRSL--KKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRASDDPL 231
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1316-1523 |
3.64e-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: 111.87 E-value: 3.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHdLREKLTIIPQDPILFSG-SLRMN 1394
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLPDERGLYDRlTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1395 LD---PFNNYSDEEIWKALE-LAHLksfvaslqLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLE 1470
Cdd:COG4555 95 IRyfaELYGLFDEELKKRIEeLIEL--------LGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 1471 TdnliQTTIQNEFAHC-----TVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQ 1523
Cdd:COG4555 167 A----RRLLREILRALkkegkTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1301-1511 |
1.17e-26 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 109.48 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1301 QFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTII 1380
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1381 PQDP------------ILFsgSLRmNLdpfnNYSDEEIWKALELAhLKsfvaslQLGLSHEVTEAGGNLSIGQRQLLCLG 1448
Cdd:cd03225 81 FQNPddqffgptveeeVAF--GLE-NL----GLPEEEIEERVEEA-LE------LVGLEGLRDRSPFTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388169353 1449 RALLRKSKILVLDEATAAVDLE-TDNLIQT--TIQNEFAhcTVITIAHRLHTIMD-SDKVMVLDNGK 1511
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAgRRELLELlkKLKAEGK--TIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1306-1511 |
2.06e-26 |
|
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: 106.56 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1306 QVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQdpi 1385
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1386 lfsgslrmnldpfnnysdeeiwkalelahlksfvaslqlglshevteaggnLSIGQRQLLCLGRALLRKSKILVLDEATA 1465
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1388169353 1466 AVDLETDNLIQTTIQNEFAH-CTVITIAHRLHTIMD-SDKVMVLDNGK 1511
Cdd:cd00267 110 GLDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
503-855 |
4.70e-26 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 115.20 E-value: 4.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 503 NEILSGIKILKYFAWEPSF--------------RDQVQNLRKKELKNLLA-FSQL-QCVVIFVFQLTPVlvsvVTFSVYV 566
Cdd:PRK10790 208 NEVINGMSVIQQFRQQARFgermgeasrshymaRMQTLRLDGFLLRPLLSlFSALiLCGLLMLFGFSAS----GTIEVGV 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 567 LVdsnnildaqkAFtsITLFNILRFPLSMLPMMISSMLQASVSTERL--------EKYlGGDDLDTSAIRHDCNfdkamq 638
Cdd:PRK10790 284 LY----------AF--ISYLGRLNEPLIELTTQQSMLQQAVVAGERVfelmdgprQQY-GNDDRPLQSGRIDID------ 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 639 fsEASFTWEHDsEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAYVP 705
Cdd:PRK10790 345 --NVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsslshsvlrqGVAMVQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 706 QQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLD 785
Cdd:PRK10790 422 QDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILD 501
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 786 DPLSAVDAHVGKHIfNKVLgpnGLLKGKTRLLV-THSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEF 855
Cdd:PRK10790 502 EATANIDSGTEQAI-QQAL---AAVREHTTLVViAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRY 568
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
654-841 |
4.75e-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: 109.02 E-value: 4.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--------AYVPQQS----WIqngTIKDNILF 721
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPvtgpgpdrGVVFQEPallpWL---TVLDNVAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 722 GTEFN----EKRYQQVLEAcallpdlemlpggdLAEIGEKGI------NLSGGQKQRISLARATYQNLDIYLLDDPLSAV 791
Cdd:COG1116 104 GLELRgvpkAERRERAREL--------------LELVGLAGFedayphQLSGGMRQRVAIARALANDPEVLLMDEPFGAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 792 DAHVGKHIfnkvlgpNGLL------KGKTRLLVTHSmhflpqVDE-------IVVLGN--GTIVE 841
Cdd:COG1116 170 DALTRERL-------QDELlrlwqeTGKTVLFVTHD------VDEavfladrVVVLSArpGRIVE 221
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
655-839 |
5.01e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 107.59 E-value: 5.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-------------TAYVPQQSWIQNGTIKDNILF 721
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKplsampppewrrqVAYVPQEPALWGGTVRDNLPF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 722 GTEFNEKRYQQVlEACALLPDLEmLPGGDLaeigEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHvGKHIF 800
Cdd:COG4619 97 PFQLRERKFDRE-RALELLERLG-LPPDIL----DKPVeRLSGGERQRLALIRALLLQPDVLLLDEPTSALDPE-NTRRV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1388169353 801 NKVLGPNGLLKGKTRLLVTHSMHFLPQV-DEIVVLGNGTI 839
Cdd:COG4619 170 EELLREYLAEEGRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1316-1516 |
6.24e-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: 105.98 E-value: 6.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQdpilfsgslrmnl 1395
Cdd:cd03214 14 VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1396 dpfnnysdeeiwkALELahlksfvaslqLGLSH----EVTEaggnLSIGQRQLLCLGRALLRKSKILVLDEATAAVDL-- 1469
Cdd:cd03214 81 -------------ALEL-----------LGLAHladrPFNE----LSGGERQRVLLARALAQEPPILLLDEPTSHLDIah 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1470 --ETDNLIQTTIQNEfaHCTVITIAHRL-HTIMDSDKVMVLDNGKIIECG 1516
Cdd:cd03214 133 qiELLELLRRLARER--GKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
638-838 |
1.43e-25 |
|
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: 106.01 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 638 QFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-------------TAYV 704
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKdltklslkelrrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 705 PQ--QSWIQNGTIKDNILFGTEF----NEKRYQQVLEACALLpdlemlpggDLAEIGEKGI-NLSGGQKQRISLARATYQ 777
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGLENlglpEEEIEERVEEALELV---------GLEGLRDRSPfTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 778 NLDIYLLDDPLSAVDAHVGKHIFNKVLGPNGllKGKTRLLVTHSMHFLPQV-DEIVVLGNGT 838
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLKA--EGKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1314-1540 |
1.80e-25 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 106.65 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1314 DLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIAsiGLHDLREKLTIIPQDPILFSgslrm 1393
Cdd:cd03299 12 EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFP----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1394 NLDPFNN---------YSDEEI-WKALELAHLksfvaslqLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEA 1463
Cdd:cd03299 85 HMTVYKNiayglkkrkVDKKEIeRKVLEIAEM--------LGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1464 TAAVDLET-DNLIQ--TTIQNEFAhCTVITIAHRLHTI-MDSDKVMVLDNGKIIECGSPEELLQIPGPfYFMAKEAGIEN 1539
Cdd:cd03299 157 FSALDVRTkEKLREelKKIRKEFG-VTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKKPKN-EFVAEFLGFNN 234
|
.
gi 1388169353 1540 V 1540
Cdd:cd03299 235 I 235
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
654-789 |
2.34e-25 |
|
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: 103.50 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYVPQQSWIQNG-TIKDNI 719
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltdderkslrkeiGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 720 LFGTEF----NEKRYQQVLEAcallpdLEMLPGGDLAE--IGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLS 789
Cdd:pfam00005 81 RLGLLLkglsKREKDARAEEA------LEKLGLGDLADrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
637-843 |
2.79e-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: 104.32 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 637 MQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT------------TAYV 704
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 705 PQQSWIQNGTIKDNIlfgtefnekryqqvleacallpdlemlpggdlaeigekGINLSGGQKQRISLARATYQNLDIYLL 784
Cdd:cd03247 81 NQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 785 DDPLSAVDAHVGKHIFNKVLgpnGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKG 843
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIF---EVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
638-857 |
2.86e-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: 105.88 E-value: 2.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 638 QFSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYV 704
Cdd:COG1122 2 ELENLSFSYPGGTPA-LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDitkknlrelrrkvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 705 PQQSWIQ--NGTIKDNILFGTEfN-----EKRYQQVLEAcallpdLEMLpggDLAEIGEKGI-NLSGGQKQRISLARATY 776
Cdd:COG1122 81 FQNPDDQlfAPTVEEDVAFGPE-NlglprEEIRERVEEA------LELV---GLEHLADRPPhELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 777 QNLDIYLLDDPLSAVDAHvGKHIFNKVLgpNGLLK-GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLAKKGE 854
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPR-GRRELLELL--KRLNKeGKTVIIVTHDLDLVAELaDRVIVLDDGRIVADGTPREVFSDYEL 227
|
...
gi 1388169353 855 FAK 857
Cdd:COG1122 228 LEE 230
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
649-863 |
5.20e-25 |
|
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: 105.71 E-value: 5.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 649 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTA------------YVPQQSWI-QNGTI 715
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVrkeprearrqigVLPDERGLyDRLTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 716 KDNILFGTEFNEKRYQQVLEACALLpdLEMLpggDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAh 794
Cdd:COG4555 92 RENIRYFAELYGLFDEELKKRIEEL--IELL---GLEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV- 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 795 VGKHIFNKVLgpnGLLK--GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLAKKGEfaKNLKTFL 863
Cdd:COG4555 166 MARRLLREIL---RALKkeGKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIGE--ENLEDAF 232
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
654-843 |
6.26e-25 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 103.28 E-value: 6.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYVPQqswiqngtikdnil 720
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDlaslspkelarkiAYVPQ-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 721 fgtefnekryqqVLEACallpdlemlpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHI 799
Cdd:cd03214 81 ------------ALELL------------GLAHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 800 FNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 843
Cdd:cd03214 137 LE-------LLRrlarerGKTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1316-1520 |
9.36e-25 |
|
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: 104.44 E-value: 9.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDlREKLTIIP--QDPILFSG---- 1389
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE-IARLGIGRtfQIPRLFPEltvl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1390 -----------SLRMNLDPFNNYSDEEIWKALELAHlksfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKIL 1458
Cdd:cd03219 94 envmvaaqartGSGLLLARARREEREARERAEELLE--------RVGLADLADRPAGELSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 1459 VLDEATAAVDL-ETDNLIQTTIQNEFAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEE 1520
Cdd:cd03219 166 LLDEPAAGLNPeETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDE 229
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
636-856 |
1.46e-24 |
|
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: 110.68 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 636 AMQFSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG------TTAY------ 703
Cdd:COG5265 357 EVRFENVSFGYDPERPI-LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdirdvTQASlraaig 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 704 -VPQQSWIQNGTIKDNILFG-TEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDI 781
Cdd:COG5265 436 iVPQDTVLFNDTIAYNIAYGrPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPI 515
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 782 YLLDDPLSAVDAHVGKHIfNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFA 856
Cdd:COG5265 516 LIFDEATSALDSRTERAI-QAAL--REVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYA 587
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1316-1528 |
1.84e-24 |
|
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: 103.91 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIG---LHDLREKLTIIPQDPILFSG--- 1389
Cdd:COG1127 20 VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRIGMLFQGGALFDSltv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1390 ------SLRMNLDpfnnYSDEEIwkaLELAHLKsfvasLQL-GLSHevteAG----GNLSIGQRQLLCLGRALLRKSKIL 1458
Cdd:COG1127 100 fenvafPLREHTD----LSEAEI---RELVLEK-----LELvGLPG----AAdkmpSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 1459 VLDEATAAVD----LETDNLIQtTIQNEFaHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIPGPF 1528
Cdd:COG1127 164 LYDEPTAGLDpitsAVIDELIR-ELRDEL-GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLASDDPW 236
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1316-1526 |
2.17e-24 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 103.43 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLfRILEA-AGGQIIIDGVDIASI---GLHDLREKLTIIPQDPILFSgsl 1391
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI-NGLERpTSGSVLVDGTDLTLLsgkELRKARRRIGMIFQHFNLLS--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1392 rmNLDPFNNysdeeIWKALELAHL-KSFVAS-----LQL-GLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEAT 1464
Cdd:cd03258 96 --SRTVFEN-----VALPLEIAGVpKAEIEErvlelLELvGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 1465 AAVDLE-TDNLIQ--TTIQNEFAhCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIPG 1526
Cdd:cd03258 169 SALDPEtTQSILAllRDINRELG-LTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
645-844 |
2.72e-24 |
|
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: 103.58 E-value: 2.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 645 TWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYVPQQSWIQ 711
Cdd:COG1120 8 SVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlaslsrrelarriAYVPQEPPAP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 712 NG-TIKDNILFG--------TEFNEKRYQQVLEAcallpdLEMLpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDI 781
Cdd:COG1120 88 FGlTVRELVALGryphlglfGRPSAEDREAVEEA------LERT---GLEHLADRPVDeLSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 782 YLLDDPLSAVDAHvgkHIFnKVLgpnGLLK------GKTRLLVThsmHFLPQV----DEIVVLGNGTIVEKGS 844
Cdd:COG1120 159 LLLDEPTSHLDLA---HQL-EVL---ELLRrlarerGRTVVMVL---HDLNLAaryaDRLVLLKDGRIVAQGP 221
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1316-1520 |
3.44e-24 |
|
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: 103.58 E-value: 3.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDlREKLTI-----IPQdpiLFSG- 1389
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHR-IARLGIartfqNPR---LFPEl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1390 ----------------SLRMNLDPFNNYSDEEIW---KALELAHlksfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGRA 1450
Cdd:COG0411 95 tvlenvlvaaharlgrGLLAALLRLPRARREEREareRAEELLE--------RVGLADRADEPAGNLSYGQQRRLEIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 1451 LLRKSKILVLDEATAAVDL-ETDNLIQTTIQ-NEFAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEE 1520
Cdd:COG0411 167 LATEPKLLLLDEPAAGLNPeETEELAELIRRlRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAE 239
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
654-871 |
3.92e-24 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 102.83 E-value: 3.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT------------TAYVPQQSWIQNG-TIKDNIL 720
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvardpaevrrrIGYVPQEPALYPDlTVRENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 721 F-------GTEFNEKRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 793
Cdd:COG1131 96 FfarlyglPRKEARERIDELLELFGLTDAADRKVG-----------TLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 794 hVGKHIFNKVLgpNGLLK-GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLAKKGEFAknlktFLRHTGPEEE 871
Cdd:COG1131 165 -EARRELWELL--RELAAeGKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKARLLEDV-----FLELTGEEAR 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
643-850 |
1.49e-23 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 106.53 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 643 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMEN---VHGHITIKGTT-------------AYVPQ 706
Cdd:COG1123 11 SVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDllelsealrgrriGMVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 707 QSWIQ-NG-TIKDNILFGTEfNEKRYQQVLEACAllpdLEMLPGGDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYL 783
Cdd:COG1123 91 DPMTQlNPvTVGDQIAEALE-NLGLSRAEARARV----LELLEAVGLERRLDRYPHqLSGGQRQRVAIAMALALDPDLLI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 784 LDDPLSAVDAHVGKHIFnkvlgpnGLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 850
Cdd:COG1123 166 ADEPTTALDVTTQAEIL-------DLLRelqrerGTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1316-1521 |
1.50e-23 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 100.72 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEA-----AGGQIIIDGVDIASIGLHD--LREKLTIIPQDPILFS 1388
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVleLRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1389 GSLRMNLD--------PFNNYSDEEIWKALELAHLKSFVASLQLGLShevteaggnLSIGQRQLLCLGRALLRKSKILVL 1460
Cdd:cd03260 95 GSIYDNVAyglrlhgiKLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQRLCLARALANEPEVLLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 1461 DEATAAVDLETDNLIQTTIQnEFAH-CTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEEL 1521
Cdd:cd03260 166 DEPTSALDPISTAKIEELIA-ELKKeYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1198-1494 |
1.54e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 107.20 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1198 FSWITSNRWLAIRLELvgNLTVF---FSALMMVI--------YrdtLSGD-TVGFV--LSNALNITQT-LNWLVRMTSEI 1262
Cdd:COG4178 251 FDAVIANWRRLIRRQR--NLTFFttgYGQLAVIFpilvaaprY---FAGEiTLGGLmqAASAFGQVQGaLSWFVDNYQSL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1263 eTNIVA-VERITEYTKVENEAPWVTDKRPPPDWPSKGKIQFNNYQVRyRPELDLVLRGITCDIGSMEKIGVVGRTGAGKS 1341
Cdd:COG4178 326 -AEWRAtVDRLAGFEEALEAADALPEAASRIETSEDGALALEDLTLR-TPDGRPLLEDLSLSLKPGERLLITGPSGSGKS 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1342 SLtnclFRILeaAG------GQIII-DGVDIAsiglhdlrekltIIPQDPILFSGSLRMNL---DPFNNYSDEEIWKALE 1411
Cdd:COG4178 404 TL----LRAI--AGlwpygsGRIARpAGARVL------------FLPQRPYLPLGTLREALlypATAEAFSDAELREALE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1412 LAHLKSFVASLqlglsHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITI 1491
Cdd:COG4178 466 AVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISV 540
|
...
gi 1388169353 1492 AHR 1494
Cdd:COG4178 541 GHR 543
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
649-843 |
1.58e-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: 100.29 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 649 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-----------TAYVPQQ-SWIQNGTIK 716
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvpperrnIGMVFQDyALFPHLTVA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 717 DNILFGTEFNEKRYQQVLEACALLpdLEMLpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHV 795
Cdd:cd03259 91 ENIAFGLKLRGVPKAEIRARVREL--LELV---GLEGLLNRYPHeLSGGQQQRVALARALAREPSLLLLDEPLSALDAKL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 796 GKHIFNKVLgpnGLLK--GKTRLLVTHSM-HFLPQVDEIVVLGNGTIVEKG 843
Cdd:cd03259 166 REELREELK---ELQRelGITTIYVTHDQeEALALADRIAVMNEGRIVQVG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
654-850 |
1.90e-23 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 106.53 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT----------------AYVPQ---QSWIQNGT 714
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltklsrrslrelrrrvQMVFQdpySSLNPRMT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 715 IKDNILFGTEFN--------EKRYQQVLEACALLPD-LEMLPGGdlaeigekginLSGGQKQRISLARATYQNLDIYLLD 785
Cdd:COG1123 361 VGDIIAEPLRLHgllsraerRERVAELLERVGLPPDlADRYPHE-----------LSGGQRQRVAIARALALEPKLLILD 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 786 DPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 850
Cdd:COG1123 430 EPTSALDVSVQAQILN-------LLRdlqrelGLTYLFISHDLAVVRYIaDRVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1300-1511 |
2.40e-23 |
|
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: 99.47 E-value: 2.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRP---ELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGvdiaSIGLhdlrek 1376
Cdd:cd03250 1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG----SIAY------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1377 ltiIPQDPILFSGSLRMNL---DPFNNysdEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLR 1453
Cdd:cd03250 71 ---VSQEPWIQNGTIRENIlfgKPFDE---ERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1454 KSKILVLDEATAAVDLET-DNLIQTTIQNEFAHC-TVITIAHRLHTIMDSDKVMVLDNGK 1511
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1300-1521 |
2.97e-23 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 100.34 E-value: 2.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYrPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIG---LHDLREK 1376
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1377 LTIIPQDPIL----------FSGSL-RMNLDP--FNNYSDEEIWKALELahLKsfvaslQLGLSHEVTEAGGNLSIGQRQ 1443
Cdd:cd03256 80 IGMIFQQFNLierlsvlenvLSGRLgRRSTWRslFGLFPKEEKQRALAA--LE------RVGLLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1444 LLCLGRALLRKSKILVLDEATAAVDLETDNLIQ---TTIQNEFAHCTVITIaHRLHTIMD-SDKVMVLDNGKIIECGSPE 1519
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMdllKRINREEGITVIVSL-HQVDLAREyADRIVGLKDGRIVFDGPPA 230
|
..
gi 1388169353 1520 EL 1521
Cdd:cd03256 231 EL 232
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1300-1523 |
4.80e-23 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 99.78 E-value: 4.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELdlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIAsiglhdlREKLTI 1379
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR-------RARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1380 --IPQD-------PILFSGSLRMNLDP----FNNYSDEE---IWKALELAHLKSFvASLQLGlshevteaggNLSIGQRQ 1443
Cdd:COG1121 78 gyVPQRaevdwdfPITVRDVVLMGRYGrrglFRRPSRADreaVDEALERVGLEDL-ADRPIG----------ELSGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1444 LLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQnEFAH--CTVITIAHRLHTIMD-SDKVMVLdNGKIIECGSPEE 1520
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLR-ELRRegKTILVVTHDLGAVREyFDRVLLL-NRGLVAHGPPEE 224
|
...
gi 1388169353 1521 LLQ 1523
Cdd:COG1121 225 VLT 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1316-1511 |
5.11e-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: 97.64 E-value: 5.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLH--DLREKLTIIPQDPILFSgslrm 1393
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRIGMVFQDFALFP----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1394 NLDPFNNysdeeiwkalelahlksfvasLQLGLShevteaGgnlsiGQRQLLCLGRALLRKSKILVLDEATAAVDLETDN 1473
Cdd:cd03229 90 HLTVLEN---------------------IALGLS------G-----GQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1388169353 1474 LIQTTIQNEFAH--CTVITIAHRLHTIMD-SDKVMVLDNGK 1511
Cdd:cd03229 138 EVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
642-850 |
5.18e-23 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 99.88 E-value: 5.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 642 ASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSW----IQ------ 711
Cdd:COG1124 9 VSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrrrVQmvfqdp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 712 ------NGTIKDNI-----LFGTEFNEKRYQQVLEACALLPD-LEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNL 779
Cdd:COG1124 89 yaslhpRHTVDRILaeplrIHGLPDREERIAELLEQVGLPPSfLDRYPH-----------QLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 780 DIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSM----HFlpqVDEIVVLGNGTIVEKGSYSALL 849
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILN-------LLKdlreerGLTYLFVSHDLavvaHL---CDRVAVMQNGRIVEELTVADLL 227
|
.
gi 1388169353 850 A 850
Cdd:COG1124 228 A 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1300-1543 |
7.18e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 100.07 E-value: 7.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTI 1379
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1380 IPQDP------------ILFSGSLRMnLDPfnnysdEEIWKALELAHLKSFVASLqlgLSHEVTeaggNLSIGQRQLLCL 1447
Cdd:PRK13632 88 IFQNPdnqfigatveddIAFGLENKK-VPP------KKMKDIIDDLAKKVGMEDY---LDKEPQ----NLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1448 GRALLRKSKILVLDEATAAVDLETDNLIQTTIQN--EFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELL--- 1522
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILnnk 233
|
250 260
....*....|....*....|....*...
gi 1388169353 1523 ------QIPGPF-YFMAKEagIENVNST 1543
Cdd:PRK13632 234 eilekaKIDSPFiYKLSKK--LKGIDPT 259
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
654-843 |
8.45e-23 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 98.73 E-value: 8.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT----------------TAYVPQQSwiqNG---- 713
Cdd:cd03257 21 LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllklsrrlrkirrkeIQMVFQDP---MSslnp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 714 --TIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSA 790
Cdd:cd03257 98 rmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVG--LPEEVLNRYPHeLSGGQRQRVAIARALALNPKLLIADEPTSA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 791 VDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 843
Cdd:cd03257 176 LDVSVQAQILD-------LLKklqeelGLTLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
643-839 |
2.29e-22 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 97.18 E-value: 2.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 643 SFTWEHDSEAT--VRDVNLDIMAGQLVAVIGPVGSGKSSLISaMLGEMENV-HGHITIKGTTA----------------- 702
Cdd:cd03255 7 SKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVRVDGTDIsklsekelaafrrrhig 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 703 YVPQQ-SWIQNGTIKDNILFGTEFNEKRYQQVLEACALLpdLEMLpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLD 780
Cdd:cd03255 86 FVFQSfNLLPDLTALENVELPLLLAGVPKKERRERAEEL--LERV---GLGDRLNHYPSeLSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 781 IYLLDDPLSAVDAHVGKHIFNKVLGPNGlLKGKTRLLVTHSMHFLPQVDEIVVLGNGTI 839
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNK-EAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
322-613 |
2.45e-22 |
|
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: 99.16 E-value: 2.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 322 LLKSFLLKLVNDIFTFVSPQLLKLLISFASDRDTYLWIGYLCAILLFtAALIQSFCLQCYFQLCFKLGVKVRTAIMASVY 401
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLL-LALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 402 KKALTLSNLARKEYTVGETVNLMSVDAQKLMD-VTNFMHMLWSSVLQIVLSIFFL----WRelgpSVLAGVGVMVLVIPI 476
Cdd:cd07346 80 RHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNlVSSGLLQLLSDVLTLIGALVILfylnWK----LTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 477 NAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPS----FRDQVQNLRKKELKNLLAFSQLQCVVIFVFQL 552
Cdd:cd07346 156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEReierFREANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 553 TPVLVSVvtFSVYvLVdSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 613
Cdd:cd07346 236 GTALVLL--YGGY-LV-LQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1316-1516 |
2.59e-22 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 96.82 E-value: 2.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHdlREKLTIIPQDPILF-------- 1387
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFphltvaen 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1388 --SGsLRMNLDPfnnySDEEIWKALELAhlksfvasLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATA 1465
Cdd:cd03259 93 iaFG-LKLRGVP----KAEIRARVRELL--------ELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 1466 AVDLETDNLIQTTIQN--EFAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECG 1516
Cdd:cd03259 160 ALDAKLREELREELKElqRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
638-838 |
3.40e-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: 94.62 E-value: 3.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 638 QFSEASFTweHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIkgttayvpqqswiqngtikd 717
Cdd:cd00267 1 EIENLSFR--YGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI-------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 718 nilFGTEFNEKRYQQVLEACALLPDLemlpggdlaeigekginlSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGK 797
Cdd:cd00267 59 ---DGKDIAKLPLEELRRRIGYVPQL------------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1388169353 798 HIFNKVLGPNglLKGKTRLLVTHSMHFLPQV-DEIVVLGNGT 838
Cdd:cd00267 118 RLLELLRELA--EEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1239-1509 |
6.11e-22 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 103.96 E-value: 6.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1239 GFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYTKVENEAPWVTDKRPPPDWPSKGKIQFNNYQVRYRPELDL-VL 1317
Cdd:PTZ00265 322 GSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYDTRKDVeIY 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1318 RGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIII-DGVDIASIGLHDLREKLTIIPQDPILFSGSLRMN-- 1394
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNik 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1395 --------LDPFNNYSDEEIWKAL---------------------------ELAHLKS---------------------F 1418
Cdd:PTZ00265 482 yslyslkdLEALSNYYNEDGNDSQenknkrnscrakcagdlndmsnttdsnELIEMRKnyqtikdsevvdvskkvlihdF 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1419 VASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVIT--IAHRLH 1496
Cdd:PTZ00265 562 VSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITiiIAHRLS 641
|
330
....*....|...
gi 1388169353 1497 TIMDSDKVMVLDN 1509
Cdd:PTZ00265 642 TIRYANTIFVLSN 654
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1316-1523 |
8.33e-22 |
|
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: 95.58 E-value: 8.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHD-LREKLTIIPQDPILFSG----- 1389
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPEltvee 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1390 SLRMNLDPFNNYSDEEIW-KALEL-AHLKSFVASLqlglshevteaGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAv 1467
Cdd:cd03224 95 NLLLGAYARRRAKRKARLeRVYELfPRLKERRKQL-----------AGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 1468 dletdnlIQTTIQNEFAHC---------TVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQ 1523
Cdd:cd03224 163 -------LAPKIVEEIFEAirelrdegvTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
655-850 |
2.93e-21 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 94.49 E-value: 2.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT----------------TAYVPQQSWIQNG-TIKD 717
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrrMGMLFQSGALFDSlTVFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 718 NILFG----TEFNEKRYQQV----LEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLS 789
Cdd:cd03261 97 NVAFPlrehTRLSEEEIREIvlekLEAVGLRGAEDLYPA-----------ELSGGMKKRVALARALALDPELLLYDEPTA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 790 AVDAhVGKHIFNK-VLGPNGLLkGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 850
Cdd:cd03261 166 GLDP-IASGVIDDlIRSLKKEL-GLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1301-1512 |
7.27e-21 |
|
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: 92.60 E-value: 7.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1301 QFNNYQVRYRPELdlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIAsiglhDLREKLTII 1380
Cdd:cd03235 1 EVEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-----KERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1381 PQD-------PILFSGSLRMNLDP----FNNYSDEEIWKALELahLKsfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGR 1449
Cdd:cd03235 74 PQRrsidrdfPISVRDVVLMGLYGhkglFRRLSKADKAKVDEA--LE------RVGLSELADRQIGELSGGQQQRVLLAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 1450 ALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAH-CTVITIAHRLHTIMDS-DKVMVLDNGKI 1512
Cdd:cd03235 146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYfDRVLLLNRTVV 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
654-839 |
8.20e-21 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 91.31 E-value: 8.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIkgttayvpqqswiqngtikdnilFGTEFNEKRyQQV 733
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV-----------------------LGKDIKKEP-EEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 734 LEACALLPDLEMLPGgDLaeIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAhVGKHIFNKVLgpNGLLK-G 812
Cdd:cd03230 72 KRRIGYLPEEPSLYE-NL--TVRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREFWELL--RELKKeG 145
|
170 180
....*....|....*....|....*...
gi 1388169353 813 KTRLLVTHSMHFLPQV-DEIVVLGNGTI 839
Cdd:cd03230 146 KTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
654-844 |
9.85e-21 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 95.60 E-value: 9.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLG-EMENvHGHITIKGTTAYV---PQQSWI----QNG------TIKDNI 719
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGlETPD-SGRIVLNGRDLFTnlpPRERRVgfvfQHYalfphmTVAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 720 LFG----TEFNEKRYQQVLEacalLpdLEMLpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAH 794
Cdd:COG1118 97 AFGlrvrPPSKAEIRARVEE----L--LELV---QLEGLADRYPSqLSGGQRQRVALARALAVEPEVLLLDEPFGALDAK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1388169353 795 VGKHIfNKVLGpnGLLK--GKTRLLVTHSmhflpQV------DEIVVLGNGTIVEKGS 844
Cdd:COG1118 168 VRKEL-RRWLR--RLHDelGGTTVFVTHD-----QEealelaDRVVVMNQGRIEQVGT 217
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
643-844 |
1.01e-20 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 92.63 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 643 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAM-----LGEMENVHGHITIKGTTAYVPQQSWIQ------ 711
Cdd:cd03260 5 DLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLDVDVLElrrrvg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 712 ---------NGTIKDNILFG--------TEFNEKRYQQVLEACALLPDLemlpgGDLAeigeKGINLSGGQKQRISLARA 774
Cdd:cd03260 85 mvfqkpnpfPGSIYDNVAYGlrlhgiklKEELDERVEEALRKAALWDEV-----KDRL----HALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 775 TYQNLDIYLLDDPLSAVDAhVGKHIFNKVLGpnGLLKGKTRLLVTHSMHflpQV----DEIVVLGNGTIVEKGS 844
Cdd:cd03260 156 LANEPEVLLLDEPTSALDP-ISTAKIEELIA--ELKKEYTIVIVTHNMQ---QAarvaDRTAFLLNGRLVEFGP 223
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
654-838 |
1.14e-20 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 91.09 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT---------------AYVPQQ-SWIQNGTIKD 717
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDltdledelpplrrriGMVFQDfALFPHLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 718 NILFGtefnekryqqvleacallpdlemlpggdlaeigekginLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGK 797
Cdd:cd03229 96 NIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1388169353 798 HIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGT 838
Cdd:cd03229 138 EVRA-------LLKslqaqlGITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
654-841 |
1.20e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 92.41 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISaMLGEMENV-HGHITIKGTTA-----------------YVPQQS-WIQNGT 714
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVLIDGQDIsslserelarlrrrhigFVFQFFnLLPELT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 715 IKDNILFGTEFN----EKRYQQVLEAcallpdLEMLpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLS 789
Cdd:COG1136 103 ALENVALPLLLAgvsrKERRERAREL------LERV---GLGDRLDHRPSqLSGGQQQRVAIARALVNRPKLILADEPTG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1388169353 790 AVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQVDEIVVLGNGTIVE 841
Cdd:COG1136 174 NLDSKTGEEVLE-------LLRelnrelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
638-839 |
2.28e-20 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 91.76 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 638 QFSEASFTWEHDSEATV-RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TAY----------- 703
Cdd:cd03248 13 KFQNVTFAYPTRPDTLVlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpiSQYehkylhskvsl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 704 VPQQSWIQNGTIKDNILFG---TEFNE-KRYQQVLEACALLPDLEMlpgGDLAEIGEKGINLSGGQKQRISLARATYQNL 779
Cdd:cd03248 93 VGQEPVLFARSLQDNIAYGlqsCSFECvKEAAQKAHAHSFISELAS---GYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 780 DIYLLDDPLSAVDAHVGKHIFNKVLGPNgllKGKTRLLVTHSMHFLPQVDEIVVLGNGTI 839
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWP---ERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1316-1512 |
2.46e-20 |
|
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: 89.76 E-value: 2.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGlHDLREKLTIIPQDPILFSG-SLRMN 1394
Cdd:cd03230 15 ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGYLPEEPSLYENlTVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1395 LDpfnnysdeeiwkalelahlksfvaslqlglshevteaggnLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNL 1474
Cdd:cd03230 94 LK----------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRRE 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1388169353 1475 IQTTIQNEFAH-CTVITIAHRLHTIMD-SDKVMVLDNGKI 1512
Cdd:cd03230 134 FWELLRELKKEgKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
639-850 |
2.97e-20 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 91.59 E-value: 2.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 639 FSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISaMLGEM-ENVHGHITIKG-------------TTAYV 704
Cdd:cd03295 3 FENVTKRYGGGKKA-VNNLNLEIAKGEFLVLIGPSGSGKTTTMK-MINRLiEPTSGEIFIDGedireqdpvelrrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 705 PQQ-SWIQNGTIKDNI-----LFGTEfNEKRYQQVLEACALLPdlemLPGGDLAE--IGEkginLSGGQKQRISLARATY 776
Cdd:cd03295 81 IQQiGLFPHMTVEENIalvpkLLKWP-KEKIRERADELLALVG----LDPAEFADryPHE----LSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 777 QNLDIYLLDDPLSAVDAHVGKHIFNKVLGPNGLLkGKTRLLVTHSM-HFLPQVDEIVVLGNGTIVEKGSYSALLA 850
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQEL-GKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1316-1513 |
3.81e-20 |
|
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: 89.02 E-value: 3.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHD-LREKLTIIPQdpilfsgslrmn 1394
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1395 ldpfnnysdeeiwkalelahlksfvaslqlglshevteaggnLSIGQRQLLCLGRALLRKSKILVLDEATAAVDL-ETDN 1473
Cdd:cd03216 83 ------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPaEVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1388169353 1474 LIQT--TIQNEfaHCTVITIAHRLHTIMD-SDKVMVLDNGKII 1513
Cdd:cd03216 121 LFKVirRLRAQ--GVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
654-844 |
4.01e-20 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 94.01 E-value: 4.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGeMENV-HGHITIKGT-----------TAYVPQqswiqNG------TI 715
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAG-FETPdSGRILLDGRdvtglppekrnVGMVFQ-----DYalfphlTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 716 KDNILFGTEF----NEKRYQQVLEAcallpdLEMLpggDLAEIGEKGIN-LSGGQKQRISLARAtyqnL----DIYLLDD 786
Cdd:COG3842 95 AENVAFGLRMrgvpKAEIRARVAEL------LELV---GLEGLADRYPHqLSGGQQQRVALARA----LapepRVLLLDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 787 PLSAVDAHVGKH----IFNkvlgpngLLK--GKTRLLVTHSmhflpQV------DEIVVLGNGTIVEKGS 844
Cdd:COG3842 162 PLSALDAKLREEmreeLRR-------LQRelGITFIYVTHD-----QEealalaDRIAVMNDGRIEQVGT 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1316-1525 |
4.11e-20 |
|
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: 93.19 E-value: 4.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEA---AGGQIIIDGVDIASIGLHDLRE----KLTIIPQDPilfs 1388
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDP---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1389 gslrMN-LDP--------------FNNYSDEEIW-KALEL----------AHLKSFvaslqlglSHEvteaggnLSIGQR 1442
Cdd:COG0444 96 ----MTsLNPvmtvgdqiaeplriHGGLSKAEAReRAIELlervglpdpeRRLDRY--------PHE-------LSGGMR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1443 QLLCLGRALLRKSKILVLDEATAAVD-------LetdNLIQtTIQNEFaHCTVITIAHRLHTI--MdSDKVMVLDNGKII 1513
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDvtiqaqiL---NLLK-DLQREL-GLAILFITHDLGVVaeI-ADRVAVMYAGRIV 230
|
250
....*....|..
gi 1388169353 1514 ECGSPEELLQIP 1525
Cdd:COG0444 231 EEGPVEELFENP 242
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
654-844 |
7.54e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 92.83 E-value: 7.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGeMENV-HGHITIKGT-----------TAYVPQqSWI--QNGTIKDNI 719
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG-LEDPtSGEILIGGRdvtdlppkdrnIAMVFQ-SYAlyPHMTVYENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 720 LFGTEFN----EKRYQQVLEACALLpDLEML----PGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAV 791
Cdd:COG3839 97 AFPLKLRkvpkAEIDRRVREAAELL-GLEDLldrkPK-----------QLSGGQRQRVALGRALVREPKVFLLDEPLSNL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 792 DAHvgkhifnkvlgpnglLKGKTR--------------LLVTHSmhflpQV------DEIVVLGNGTIVEKGS 844
Cdd:COG3839 165 DAK---------------LRVEMRaeikrlhrrlgtttIYVTHD-----QVeamtlaDRIAVMNDGRIQQVGT 217
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
655-840 |
8.39e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 91.08 E-value: 8.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--------AYVPQQS----WIqngTIKDNILFG 722
Cdd:COG4525 24 QDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVFQKDallpWL---NVLDNVAFG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 723 TEFN----EKRYQQVLEACALLpdlemlpggDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGK 797
Cdd:COG4525 101 LRLRgvpkAERRARAEELLALV---------GLADFARRRIwQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTRE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1388169353 798 HIfnKVLgpngLLK-----GKTRLLVTHSmhflpqVDEIVVLGNGTIV 840
Cdd:COG4525 172 QM--QEL----LLDvwqrtGKGVFLITHS------VEEALFLATRLVV 207
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1328-1525 |
1.16e-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: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1328 EKIGVVGRTGAGKSSLTNCLFRiLEAAGGQIIIDGVDIASIG---LHDLREKLTIIPQDPilFsGSL--RMN-------- 1394
Cdd:COG4172 313 ETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--F-GSLspRMTvgqiiaeg 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1395 ---LDPFNNYS--DEEIWKALElahlksfvaslQLGLS--------HEvteaggnLSIGQRQLLCLGRALLRKSKILVLD 1461
Cdd:COG4172 389 lrvHGPGLSAAerRARVAEALE-----------EVGLDpaarhrypHE-------FSGGQRQRIAIARALILEPKLLVLD 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 1462 EATAAVDLetdnLIQTTI-------QNEFaHCTVITIAHRLHTI--MdSDKVMVLDNGKIIECGSPEELLQIP 1525
Cdd:COG4172 451 EPTSALDV----SVQAQIldllrdlQREH-GLAYLFISHDLAVVraL-AHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1300-1514 |
1.64e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 88.96 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELDlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASI---GLHDLREK 1376
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1377 LTIIPQDpilfsGSLRMNLDPFNN---------YSDEEIWKALELAhLKsfvaslQLGLSHEVTEAGGNLSIGQRQLLCL 1447
Cdd:COG2884 81 IGVVFQD-----FRLLPDRTVYENvalplrvtgKSRKEIRRRVREV-LD------LVGLSDKAKALPHELSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 1448 GRALLRKSKILVLDEATAAVDLET-DNLIQttIQNEFAH--CTVItIA-HRLHtIMDS--DKVMVLDNGKIIE 1514
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPETsWEIME--LLEEINRrgTTVL-IAtHDLE-LVDRmpKRVLELEDGRLVR 217
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1300-1512 |
1.69e-19 |
|
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: 88.62 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYrPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIAsiGLHD-----LR 1374
Cdd:cd03292 1 IEFINVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS--DLRGraipyLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1375 EKLTIIPQDPILFSgslrmNLDPFNN--YSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALL 1452
Cdd:cd03292 78 RKIGVVFQDFRLLP-----DRNVYENvaFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 1453 RKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMD--SDKVMVLDNGKI 1512
Cdd:cd03292 153 NSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDttRHRVIALERGKL 214
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1306-1529 |
1.81e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 92.79 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1306 QVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLRE----KLTIIP 1381
Cdd:PRK10070 33 QILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1382 QDpilFSGSLRMNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLD 1461
Cdd:PRK10070 113 QS---FALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMD 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 1462 EATAAVdletDNLIQTTIQNEFAHC------TVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIPGPFY 1529
Cdd:PRK10070 190 EAFSAL----DPLIRTEMQDELVKLqakhqrTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1300-1486 |
2.17e-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: 88.30 E-value: 2.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELdlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGlHDLREKLTI 1379
Cdd:COG4133 3 LEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1380 IPQDPILFSG-SLRMNLDpF------NNYSDEEIWKALElahlksfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGRALL 1452
Cdd:COG4133 80 LGHADGLKPElTVRENLR-FwaalygLRADREAIDEALE-----------AVGLAGLADLPVRQLSAGQKRRVALARLLL 147
|
170 180 190
....*....|....*....|....*....|....
gi 1388169353 1453 RKSKILVLDEATAAVDLETDNLIQTTIQnefAHC 1486
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIA---AHL 178
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
648-834 |
2.55e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 87.67 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 648 HDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--AYVPQQSWIQNG---TIKDNILFG 722
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGArvAYVPQRSEVPDSlplTVRDLVAMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 723 TeFNE--------KRYQQVLEACallpdLEMLPGGDLAE--IGEkginLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 792
Cdd:NF040873 82 R-WARrglwrrltRDDRAAVDDA-----LERVGLADLAGrqLGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1388169353 793 AHVGKHIfnkvlgpNGLLK-----GKTRLLVTHSMHFLPQVDEIVVL 834
Cdd:NF040873 152 AESRERI-------IALLAeeharGATVVVVTHDLELVRRADPCVLL 191
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1317-1520 |
7.04e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 88.95 E-value: 7.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1317 LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIA--SIGLHDLREKLTIIPQDP--ILFSGSLR 1392
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1393 MNLD--PFN-NYSDEEI----WKALELahlksfvaslqLGLSHEV--TEAGGNLSIGQRQLLCLGRALLRKSKILVLDEA 1463
Cdd:PRK13637 103 KDIAfgPINlGLSEEEIenrvKRAMNI-----------VGLDYEDykDKSPFELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1464 TAAVDLETDNLIQTTIQN--EFAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEE 1520
Cdd:PRK13637 172 TAGLDPKGRDEILNKIKElhKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
976-1272 |
9.18e-19 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 88.38 E-value: 9.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 976 LFSIFFIILAFVMNSVAfigsnLWLSAWTSDSKIfnstdypaSQRDMR-----VGVYGALGLAQGIFVFIAHFWSAFGFV 1050
Cdd:cd07346 2 LLALLLLLLATALGLAL-----PLLTKLLIDDVI--------PAGDLSlllwiALLLLLLALLRALLSYLRRYLAARLGQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1051 HASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPL 1130
Cdd:cd07346 69 RVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1131 GIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAF--EHQ--QRFLKHNEVRIDTNqkcvfswITSNRW 1206
Cdd:cd07346 149 LPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFaaEEReiERFREANRDLRDAN-------LRAARL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 1207 LAIRLELVGNLTVFFSALMMV-----IYRDTLS-GDTVGFVLSNALnITQTLNWLVRMTSEIETNIVAVERI 1272
Cdd:cd07346 222 SALFSPLIGLLTALGTALVLLyggylVLQGSLTiGELVAFLAYLGM-LFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
643-840 |
1.57e-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: 85.77 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 643 SFTWEHDSEaTVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG----------TTAYVPQQSWIQN 712
Cdd:cd03226 6 SFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQDVDYQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 713 G--TIKDNILFGTEFNEKRYQQVLEacaLLPDLemlpggDLAEIGEKG-INLSGGQKQRISLARATYQNLDIYLLDDPLS 789
Cdd:cd03226 85 FtdSVREELLLGLKELDAGNEQAET---VLKDL------DLYALKERHpLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 790 AVDAH----VGKhIFNKVLGpngllKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIV 840
Cdd:cd03226 156 GLDYKnmerVGE-LIRELAA-----QGKAVIVITHDYEFLAKVcDRVLLLANGAIV 205
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
655-839 |
1.60e-18 |
|
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: 85.66 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQ----------------NGTIKDN 718
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElrqkvgmvfqqfnlfpHLTVLEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 719 ILFG--TEFNEKRYQQVLEACALLPDLemlpgGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVg 796
Cdd:cd03262 97 ITLApiKVKGMSKAEAEERALELLEKV-----GLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1388169353 797 khiFNKVLgpnGLLK-----GKTRLLVTHSMHFLPQV-DEIVVLGNGTI 839
Cdd:cd03262 171 ---VGEVL---DVMKdlaeeGMTMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
656-844 |
1.60e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 88.99 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-----------TAYVPQQ-SWIQNGTIKDNILFGT 723
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHyALFRHMTVFDNIAFGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 724 EFNEKRY--------QQVLEAcallpdLEMLPGGDLAEigEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHV 795
Cdd:PRK10851 100 TVLPRRErpnaaaikAKVTQL------LEMVQLAHLAD--RYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1388169353 796 GKHIFNKVLGPNGLLKgKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 844
Cdd:PRK10851 172 RKELRRWLRQLHEELK-FTSVFVTHDQEEAMEVaDRVVVMSQGNIEQAGT 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1316-1521 |
1.62e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.85 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDG--VDIASIglHDLREK-LTIIPQDPIL------ 1386
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSP--RDAQAAgIAIIHQELNLvpnlsv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1387 ----FSGSLRMNLDPFNnysdeeiWKALE---LAHLKsfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILV 1459
Cdd:COG1129 97 aeniFLGREPRRGGLID-------WRAMRrraRELLA------RLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 1460 LDEATAAVDL-ETDNLiqttiqneFAH--------CTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEEL 1521
Cdd:COG1129 164 LDEPTASLTErEVERL--------FRIirrlkaqgVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
647-842 |
1.71e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.06 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 647 EHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--------AYVPQQS----WiQNgt 714
Cdd:PRK11248 10 DYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPvegpgaerGVVFQNEgllpW-RN-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 715 IKDNILFGTEF-NEKRYQQVLEAcallpdLEMLPGGDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 792
Cdd:PRK11248 87 VQDNVAFGLQLaGVEKMQRLEIA------HQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 793 AhvgkhiFNKVLGPNGLLK-----GKTRLLVTHSMH---FLpqVDEIVVL--GNGTIVEK 842
Cdd:PRK11248 161 A------FTREQMQTLLLKlwqetGKQVLLITHDIEeavFM--ATELVLLspGPGRVVER 212
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
654-851 |
1.92e-18 |
|
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: 86.10 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISaMLGEMEN-VHGHITIKGT----------------TAYVPQQ-SWIQNGTI 715
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIR-CINGLERpTSGSVLVDGTdltllsgkelrkarrrIGMIFQHfNLLSSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 716 KDNILFGTEF----NEKRYQQVLEACALLpDLEmlpggDLAEIGEKgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAV 791
Cdd:cd03258 100 FENVALPLEIagvpKAEIEERVLELLELV-GLE-----DKADAYPA--QLSGGQKQRVGIARALANNPKVLLCDEATSAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 792 DAHVGKHIFNKVLGPNGLLkGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLAK 851
Cdd:cd03258 172 DPETTQSILALLRDINREL-GLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1300-1517 |
2.89e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 87.93 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNN----YQVRYRPELdlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASI---GLHD 1372
Cdd:PRK11153 2 IELKNiskvFPQGGRTIH--ALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1373 LREKLTIIPQDPILFSG-------SLRMNLDpfnNYSDEEIWK-ALELahlksfvasLQL-GLSHEVTEAGGNLSIGQRQ 1443
Cdd:PRK11153 80 ARRQIGMIFQHFNLLSSrtvfdnvALPLELA---GTPKAEIKArVTEL---------LELvGLSDKADRYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1444 LLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQ--NEFAHCTVITIAHRlhtiMD-----SDKVMVLDNGKIIECG 1516
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKdiNRELGLTIVLITHE----MDvvkriCDRVAVIDAGRLVEQG 223
|
.
gi 1388169353 1517 S 1517
Cdd:PRK11153 224 T 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1300-1527 |
4.20e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 85.19 E-value: 4.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRpelDLVLRgITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDlReKLTI 1379
Cdd:COG3840 2 LRLDDLTYRYG---DFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-R-PVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1380 IPQDPILFSG-SLRMN----LDPFNNYSDEEIWKALELAHlksfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRK 1454
Cdd:COG3840 76 LFQENNLFPHlTVAQNiglgLRPGLKLTAEQRAQVEQALE--------RVGLAGLLDRLPGQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388169353 1455 SKILVLDEATAAVD----LETDNLIQTTIQNEFAhcTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIPGP 1527
Cdd:COG3840 148 RPILLLDEPFSALDpalrQEMLDLVDELCRERGL--TVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGEPP 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
650-843 |
4.65e-18 |
|
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: 85.08 E-value: 4.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 650 SEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-----------TAYVPQQ-SWIQNGTIKD 717
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 718 NILFG----TEFNEKRYQQVLEACALLPDLEMLpggdlaeiGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 793
Cdd:cd03299 91 NIAYGlkkrKVDKKEIERKVLEIAEMLGIDHLL--------NRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 794 HVGKHIFN--KVLGPNgllKGKTRLLVTHSM-HFLPQVDEIVVLGNGTIVEKG 843
Cdd:cd03299 163 RTKEKLREelKKIRKE---FGVTVLHVTHDFeEAWALADKVAIMLNGKLIQVG 212
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1300-1512 |
4.86e-18 |
|
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: 84.50 E-value: 4.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELdlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDI--ASIGLHDLREKL 1377
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1378 TIIPQDPILFSgslrmNLDPFNNYSDEEIW-------KALELA--HLKsfvaslQLGLSHEVTEAGGNLSIGQRQLLCLG 1448
Cdd:cd03262 79 GMVFQQFNLFP-----HLTVLENITLAPIKvkgmskaEAEERAleLLE------KVGLADKADAYPAQLSGGQQQRVAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 1449 RALLRKSKILVLDEATAAVDLETDNLIQTTIQNeFAH--CTVITIAHRlhtiMD-----SDKVMVLDNGKI 1512
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPELVGEVLDVMKD-LAEegMTMVVVTHE----MGfarevADRVIFMDDGRI 213
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1300-1522 |
5.53e-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: 85.14 E-value: 5.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRY--RPeldlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFR-ILEAAGGQIII-----DGVDI----AS 1367
Cdd:COG1119 4 LELRNVTVRRggKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLfgerrGGEDVwelrKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1368 IGL------HDLREKLTIIpqDPIL--FSGSLrmnlDPFNNYSDEEIWKALELAHLksfvaslqLGLSHEVTEAGGNLSI 1439
Cdd:COG1119 80 IGLvspalqLRFPRDETVL--DVVLsgFFDSI----GLYREPTDEQRERARELLEL--------LGLAHLADRPFGTLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1440 GQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIqNEFAH---CTVITIAHRLHTIMDS-DKVMVLDNGKIIEC 1515
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALL-DKLAAegaPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAA 224
|
....*..
gi 1388169353 1516 GSPEELL 1522
Cdd:COG1119 225 GPKEEVL 231
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1316-1512 |
5.58e-18 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 84.46 E-value: 5.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDL----REKLTIIPQDPILFSG-- 1389
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafrRRHIGFVFQSFNLLPDlt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1390 -----SLRMNLDPFNNYSDEEiwKALELAHlksfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEAT 1464
Cdd:cd03255 99 alenvELPLLLAGVPKKERRE--RAEELLE--------RVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1465 AAVDLETDNLIQTTIQ--NEFAHCTVITIAHRLHTIMDSDKVMVLDNGKI 1512
Cdd:cd03255 169 GNLDSETGKEVMELLRelNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
654-850 |
6.28e-18 |
|
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: 84.41 E-value: 6.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--------------TAYVPQ-QSWIQNGTIKDN 718
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEgRRIFPELTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 719 ILFG--TEFNEKRYQQVLEACALLPDL-EMLpggdlaeiGEKGINLSGGQKQRISLARATYQNLDIYLLDDP---LSAVd 792
Cdd:cd03224 96 LLLGayARRRAKRKARLERVYELFPRLkERR--------KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPsegLAPK- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 793 ahVGKHIFNKVLGPNGllKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 850
Cdd:cd03224 167 --IVEEIFEAIRELRD--EGVTILLVEQNARFALEIaDRAYVLERGRVVLEGTAAELLA 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
658-863 |
8.01e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 84.42 E-value: 8.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 658 NLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TAYVPQQ---SWI-QNG------TIKDNILFG--- 722
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdlTALPPAErpvSMLfQENnlfphlTVAQNIGLGlrp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 723 ----TEFNEKRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAvdahvgkh 798
Cdd:COG3840 99 glklTAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSA-------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 799 ifnkvLGPN------GLLK------GKTRLLVTHSmhflPQ-----VDEIVVLGNGTIVEKGSYSALLAkkGEFAKNLKT 861
Cdd:COG3840 160 -----LDPAlrqemlDLVDelcrerGLTVLMVTHD----PEdaariADRVLLVADGRIAADGPTAALLD--GEPPPALAA 228
|
..
gi 1388169353 862 FL 863
Cdd:COG3840 229 YL 230
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
655-850 |
9.63e-18 |
|
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: 84.26 E-value: 9.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG---TTAYVPQQSWI--------QNG------TIKD 717
Cdd:COG1127 22 DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqdiTGLSEKELYELrrrigmlfQGGalfdslTVFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 718 NILFG----TEFNEK-RYQQVLEAcallpdLEM--LPG-GDL--AEigekginLSGGQKQRISLARATYQNLDIYLLDDP 787
Cdd:COG1127 102 NVAFPlrehTDLSEAeIRELVLEK------LELvgLPGaADKmpSE-------LSGGMRKRVALARALALDPEILLYDEP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 788 LSAVDAhVGKHIFNKvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 850
Cdd:COG1127 169 TAGLDP-ITSAVIDE------LIRelrdelGLTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEELLA 231
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
649-844 |
1.01e-17 |
|
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: 83.23 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 649 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAYVPQQSWIQNGTI 715
Cdd:cd03369 19 DLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 716 KDNIlfgTEFNEKRYQQVLEACallpdlemlpggdlaEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHV 795
Cdd:cd03369 99 RSNL---DPFDEYSDEEIYGAL---------------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1388169353 796 gKHIFNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGS 844
Cdd:cd03369 161 -DALIQKTI--REEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1332-1525 |
1.14e-17 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 85.00 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1332 VVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLRE-----------KLTIIPQDPILfsgslrmnldpfnn 1400
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkkismvfqSFALLPHRTVL-------------- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1401 ysdEEIWKALELAHL-------KSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVdletDN 1473
Cdd:cd03294 121 ---ENVAFGLEVQGVpraereeRAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL----DP 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 1474 LIQTTIQNEF------AHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1525
Cdd:cd03294 194 LIRREMQDELlrlqaeLQKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
657-850 |
1.26e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 84.42 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 657 VNLDIMAGQLVAVIGPVGSGKSSLISAM--LGEMENVH---GHITIKGTTAYVPQQSWI-----------QN------GT 714
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCInlLEQPEAGTirvGDITIDTARSLSQQKGLIrqlrqhvgfvfQNfnlfphRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 715 IKDNILFGTEFNEKRYQQvlEACALLPDLemlpggdLAEIGEKGIN------LSGGQKQRISLARATYQNLDIYLLDDPL 788
Cdd:PRK11264 102 VLENIIEGPVIVKGEPKE--EATARAREL-------LAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVILFDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 789 SAVDAHVGKHIFNKVlgpNGLLKGK-TRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 850
Cdd:PRK11264 173 SALDPELVGEVLNTI---RQLAQEKrTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKALFA 233
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1300-1521 |
1.41e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 84.78 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELD-LVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLT 1378
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1379 IIPQDPI-LFSGSLRMNLDPF--NNysdeeiwKALELAHLKSFV-ASLQL-GLSHEVTEAGGNLSIGQRQLLCLGRALLR 1453
Cdd:PRK13650 85 MVFQNPDnQFVGATVEDDVAFglEN-------KGIPHEEMKERVnEALELvGMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 1454 KSKILVLDEATAAVDLETD-NLIQT--TIQNEFaHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEEL 1521
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRlELIKTikGIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
653-843 |
1.76e-17 |
|
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: 82.69 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 653 TVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-----------TTAYVPQQ-SWIQNGTIKDNIL 720
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkdrDIAMVFQNyALYPHMTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 721 FGTEFNEKRY----QQVLEACALLpDLEMLpggdlaeIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVG 796
Cdd:cd03301 95 FGLKLRKVPKdeidERVREVAELL-QIEHL-------LDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 797 KHIFNKVlgpNGLLK--GKTRLLVTHSmhflpQV------DEIVVLGNGTIVEKG 843
Cdd:cd03301 167 VQMRAEL---KRLQQrlGTTTIYVTHD-----QVeamtmaDRIAVMNDGQIQQIG 213
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
643-844 |
1.81e-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: 84.02 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 643 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSW---------IQN- 712
Cdd:TIGR04520 7 SFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeirkkvgmvFQNp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 713 ------GTIKDNILFGTEfN--------EKRYQQVLEACALLPDLEMLPggdlaeigekgINLSGGQKQRISLARATYQN 778
Cdd:TIGR04520 87 dnqfvgATVEDDVAFGLE-NlgvpreemRKRVDEALKLVGMEDFRDREP-----------HLLSGGQKQRVAIAGVLAMR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 779 LDIYLLDDPLSAVDAhVGK-------HIFNKVlgpngllKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGS 844
Cdd:TIGR04520 155 PDIIILDEATSMLDP-KGRkevletiRKLNKE-------EGITVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
654-844 |
2.39e-17 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 83.16 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG--TTAYVPQQSWI----------QNGTIKDNILF 721
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedATDVPVQERNVgfvfqhyalfRHMTVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 722 GTEFnEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIf 800
Cdd:cd03296 98 GLRV-KPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAqLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKEL- 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 801 nkvlgpNGLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 844
Cdd:cd03296 176 ------RRWLRrlhdelHVTTVFVTHDQEEALEVaDRVVVMNKGRIEQVGT 220
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1316-1513 |
2.40e-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: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDlREKLtI--IPQDPIL-FSGSL- 1391
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK-RAKY-IgrVFQDPMMgTAPSMt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1392 -------------RMNLDPFNNYSDEEIWKALelahlksfVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKIL 1458
Cdd:COG1101 99 ieenlalayrrgkRRGLRRGLTKKRRELFREL--------LATLGLGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 1459 VLDEATAAVDLET-DNLIQTT--IQNEFaHCTVITIAHRLH--------TIMdsdkvmvLDNGKII 1513
Cdd:COG1101 171 LLDEHTAALDPKTaALVLELTekIVEEN-NLTTLMVTHNMEqaldygnrLIM-------MHEGRII 228
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1316-1522 |
3.12e-17 |
|
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: 82.72 E-value: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDL-REKLTIIPQDPILFSG-SLRM 1393
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1394 NLD--PFNNYSDEEIWKALELAH-----LKSFVASLqlglshevteaGGNLSIGQRQLLCLGRALLRKSKILVLDEATAA 1466
Cdd:COG0410 98 NLLlgAYARRDRAEVRADLERVYelfprLKERRRQR-----------AGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 1467 -----VDlETDNLIQ------TTI----QN-EFAhctvITIAHRlhtimdsdkVMVLDNGKIIECGSPEELL 1522
Cdd:COG0410 167 lapliVE-EIFEIIRrlnregVTIllveQNaRFA----LEIADR---------AYVLERGRIVLEGTAAELL 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
418-876 |
3.35e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 88.11 E-value: 3.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 418 GETVNLMSVDAQKL-MDVTNFMHMLWSSVLQIvLSIFFLWRELgpSVLAGVGVMVLVIPI-NAILSTKSKTIQVKNMKN- 494
Cdd:PLN03232 1007 GRVINRFSKDIGDIdRNVANLMNMFMNQLWQL-LSTFALIGTV--STISLWAIMPLLILFyAAYLYYQSTSREVRRLDSv 1083
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 495 -KDKRLKIMNEILSGIK-ILKYFAWepsfrDQVQNLRKKELKNLLAFSQLQC-----VVIFVFQLTPVLVSVV-TFSVYV 566
Cdd:PLN03232 1084 tRSPIYAQFGEALNGLSsIRAYKAY-----DRMAKINGKSMDNNIRFTLANTssnrwLTIRLETLGGVMIWLTaTFAVLR 1158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 567 LVDSNNildaQKAFTSiTLFNILRFPLSMLPMMISSMLQASV------STERLEKYLggdDLDTSAIRHDCN-------- 632
Cdd:PLN03232 1159 NGNAEN----QAGFAS-TMGLLLSYTLNITTLLSGVLRQASKaenslnSVERVGNYI---DLPSEATAIIENnrpvsgwp 1230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 633 FDKAMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG------------- 699
Cdd:PLN03232 1231 SRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcdvakfgltdlrr 1310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 700 TTAYVPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNL 779
Cdd:PLN03232 1311 VLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRS 1390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 780 DIYLLDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGE-FAKn 858
Cdd:PLN03232 1391 KILVLDEATASVDVRTDSLIQRTI---REEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSaFFR- 1466
|
490
....*....|....*...
gi 1388169353 859 lktFLRHTGPEEEATVHD 876
Cdd:PLN03232 1467 ---MVHSTGPANAQYLSN 1481
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1300-1516 |
3.53e-17 |
|
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: 81.86 E-value: 3.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELdlVLRGITCDIGS-MekIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIaSIGLHDLREKLT 1378
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPgM--YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1379 IIPQDpilFSGSLRMNLDPFNNY-----------SDEEIWKALELahlksfvaslqLGLSHEVTEAGGNLSIGQRQLLCL 1447
Cdd:cd03264 76 YLPQE---FGVYPNFTVREFLDYiawlkgipskeVKARVDEVLEL-----------VNLGDRAKKKIGSLSGGMRRRVGI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1448 GRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDS-DKVMVLDNGKIIECG 1516
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
656-843 |
6.41e-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: 81.19 E-value: 6.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 656 DVNLDI---MAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-----------------AYVPQQ-SWIQNGT 714
Cdd:cd03297 12 DFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrkiGLVFQQyALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 715 IKDNILFGTEFNEKRYQQVLEAcallpdlEMLPGGDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 793
Cdd:cd03297 92 VRENLAFGLKRKRNREDRISVD-------ELLDLLGLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 794 HVGKHIFNKVlgpNGLLK--GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 843
Cdd:cd03297 165 ALRLQLLPEL---KQIKKnlNIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1300-1522 |
6.46e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 83.97 E-value: 6.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELDLV--LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRiLEAA-GGQIIIDGVDIASI---GLHDL 1373
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL-LERPtSGSVLVDGVDLTALserELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1374 REKLTIIPQDPILFSgS----------LRMnldpfNNYSDEEIW-KALELahlksfvasLQL-GLSHevtEAG---GNLS 1438
Cdd:COG1135 81 RRKIGMIFQHFNLLS-SrtvaenvalpLEI-----AGVPKAEIRkRVAEL---------LELvGLSD---KADaypSQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1439 IGQRQLLCLGRALLRKSKILVLDEATAAVDLETD----NLIQtTIQNEFaHCTVITIAHRLHTIMD-SDKVMVLDNGKII 1513
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTrsilDLLK-DINREL-GLTIVLITHEMDVVRRiCDRVAVLENGRIV 220
|
....*....
gi 1388169353 1514 ECGSPEELL 1522
Cdd:COG1135 221 EQGPVLDVF 229
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
635-836 |
7.56e-17 |
|
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: 82.31 E-value: 7.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 635 KAMQFSEASFTWEHDSEAT-----VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------- 701
Cdd:cd03294 16 KAFKLLAKGKSKEEILKKTgqtvgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDiaamsrke 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 702 ----------------AYVPQQswiqngTIKDNILFGTEFN-------EKRYQQVLEACALLPDLEMLPGgdlaeigekg 758
Cdd:cd03294 96 lrelrrkkismvfqsfALLPHR------TVLENVAFGLEVQgvpraerEERAAEALELVGLEGWEHKYPD---------- 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388169353 759 iNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLGPNGLLKgKTRLLVTHSMhflpqvDEIVVLGN 836
Cdd:cd03294 160 -ELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQ-KTIVFITHDL------DEALRLGD 229
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
645-848 |
8.31e-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: 8.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 645 TWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT----------------TAYVPQQ- 707
Cdd:cd03256 9 TYPNGKKA-LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrrqIGMIFQQf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 708 SWIQNGTIKDNILFG---------TEFNEKRYQQVLEACALLPDLEMLpggDLAEIgeKGINLSGGQKQRISLARATYQN 778
Cdd:cd03256 88 NLIERLSVLENVLSGrlgrrstwrSLFGLFPKEEKQRALAALERVGLL---DKAYQ--RADQLSGGQQQRVAIARALMQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 779 LDIYLLDDPLSAVD---AHvgkhifnKVLgpnGLLK------GKTRLLVTHSMHF-LPQVDEIVVLGNGTIVEKGSYSAL 848
Cdd:cd03256 163 PKLILADEPVASLDpasSR-------QVM---DLLKrinreeGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
655-794 |
1.11e-16 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 80.22 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT------------TAYVPQQS-WIQNGTIKDNILF 721
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpirdaredyrrrLAYLGHADgLKPELTVRENLRF 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388169353 722 -----GTEFNEKRYQQVLEACALlPDLEMLPGGdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAH 794
Cdd:COG4133 99 waalyGLRADREAIDEALEAVGL-AGLADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA 165
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
1026-1272 |
1.51e-16 |
|
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: 81.84 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1026 VYGALGLAQGIFVFI-AHFWSAFGFvHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWIT 1104
Cdd:cd18557 41 ILLAIYLLQSVFTFVrYYLFNIAGE-RIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1105 CFLGIISTLVMICMATPVFTIIVIPLGIIYVSVQMFYVSTSRQLRR--LDSVTRSPiySHFSETVSGLPVIRAF---EHQ 1179
Cdd:cd18557 120 NILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKevQDALAKAG--QVAEESLSNIRTVRSFsaeEKE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1180 -QRFLKHNEVRIDTNQKCVFsWITSNRWLAIRLELVGNLTVFFSALMMVIYRDTLSGDTVGFVLSnALNITQTLNWLVRM 1258
Cdd:cd18557 198 iRRYSEALDRSYRLARKKAL-ANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILY-TIMVASSVGGLSSL 275
|
250
....*....|....
gi 1388169353 1259 TSEIETNIVAVERI 1272
Cdd:cd18557 276 LADIMKALGASERV 289
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1316-1514 |
1.84e-16 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 80.09 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDL----REKLTIIPQD-------- 1383
Cdd:COG1136 23 ALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlrRRHIGFVFQFfnllpelt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1384 -------PILFSGSLRmnldpfnNYSDEEIWKALElahlksfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSK 1456
Cdd:COG1136 103 alenvalPLLLAGVSR-------KERRERARELLE-----------RVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1457 ILVLDEATAAVDLETDNLIQTTIQ--NEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIE 1514
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRelNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
636-876 |
2.12e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.08 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 636 AMQFSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT----------TAYVP 705
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTA-LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 706 QQS---WIQNGTIKDNILFGT--------EFNEKRYQQVLEACALLPDLEMlpggDLAEIGEkginLSGGQKQRISLARA 774
Cdd:PRK15056 85 QSEevdWSFPVLVEDVVMMGRyghmgwlrRAKKRDRQIVTAALARVDMVEF----RHRQIGE----LSGGQKKRVFLARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 775 TYQNLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK-----GKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKG-SYSAL 848
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIIS-------LLRelrdeGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGpTETTF 229
|
250 260 270
....*....|....*....|....*....|.
gi 1388169353 849 LAKKGEFAknLKTFLRH---TGPEEEATVHD 876
Cdd:PRK15056 230 TAENLELA--FSGVLRHvalNGSEESIITDD 258
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1316-1525 |
2.89e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.48 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGV------DIASIGLHDLREKLTIIPQDPILFSG 1389
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1390 -SLRMNLD-PFNNY---SDEEIWKALELAHLKsfvaslqLGLSHEVTE----AGGNLSIGQRQLLCLGRALLRKSKILVL 1460
Cdd:PRK14246 105 lSIYDNIAyPLKSHgikEKREIKKIVEECLRK-------VGLWKEVYDrlnsPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 1461 DEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1525
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
638-841 |
3.50e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 79.33 E-value: 3.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 638 QFSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG------TTAYVPQ----- 706
Cdd:COG2884 3 RFENVSKRYPGGREA-LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlKRREIPYlrrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 707 ----QSW--IQNGTIKDNILFG---TEFNEKRYQQ-VLEAcallpdLEMLpggdlaEIGEKG----INLSGGQKQRISLA 772
Cdd:COG2884 82 gvvfQDFrlLPDRTVYENVALPlrvTGKSRKEIRRrVREV------LDLV------GLSDKAkalpHELSGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 773 RATYQNLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK-----GKTRLLVTHSMHFLPQVDE-IVVLGNGTIVE 841
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIME-------LLEeinrrGTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
655-844 |
5.13e-16 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 79.27 E-value: 5.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGeMENV-HGHITIKGTTAYVPQQSWIQ----------------NGTIKD 717
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKSTLLRCINL-LEEPdSGTITVDGEDLTDSKKDINKlrrkvgmvfqqfnlfpHLTVLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 718 NILFGTEFNEKRYQQVLEACAllpdLEMLpggDLAEIGEKG----INLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 793
Cdd:COG1126 97 NVTLAPIKVKKMSKAEAEERA----MELL---ERVGLADKAdaypAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1388169353 794 H-VGkhifnKVLgpnGLLK-----GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 844
Cdd:COG1126 170 ElVG-----EVL---DVMRdlakeGMTMVVVTHEMGFAREVaDRVVFMDGGRIVEEGP 219
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1300-1494 |
5.14e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 77.19 E-value: 5.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVrYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLtnclFRIL----EAAGGQIIIDGvdiasiglhdlRE 1375
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSL----FRALaglwPWGSGRIGMPE-----------GE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1376 KLTIIPQDPILFSGSLRmnldpfnnysdEEI---WKAlelahlksfvaslqlglshevteaggNLSIGQRQLLCLGRALL 1452
Cdd:cd03223 65 DLLFLPQRPYLPLGTLR-----------EQLiypWDD--------------------------VLSGGEQQRLAFARLLL 107
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1388169353 1453 RKSKILVLDEATAAVDLETDNLIQTTIQNEFAhcTVITIAHR 1494
Cdd:cd03223 108 HKPKFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
656-887 |
1.23e-15 |
|
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: 80.53 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-----------------AYVPQQSwiq-ngTIKD 717
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargiflpphrrriGYVFQEArlfphlSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 718 NILFGTEFNEK--RYQQVLEACALL---PDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 792
Cdd:COG4148 97 NLLYGRKRAPRaeRRISFDEVVELLgigHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 793 AHVGKHIfnkvlgpngL-----LKGKTR---LLVTHSMhflpqvDEI-------VVLGNGTIVEKGSYSALLAKKGefak 857
Cdd:COG4148 166 LARKAEI---------LpylerLRDELDipiLYVSHSL------DEVarladhvVLLEQGRVVASGPLAEVLSRPD---- 226
|
250 260 270
....*....|....*....|....*....|..
gi 1388169353 858 nlktfLRHTGPEEEA-TVHDGS-EEEDDDYGL 887
Cdd:COG4148 227 -----LLPLAGGEEAgSVLEATvAAHDPDYGL 253
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
653-822 |
1.25e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 78.28 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 653 TVRDVNLDIMAGQLVAVIGPVGSGKSSLISAmLGEMENVHGHITIKGTTAY---------------------VPQQSWIQ 711
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRS-INRMNDLNPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 712 NGTIKDNILFGTEFNEKRYQQVLEACALlpdlEMLPGGDLAE-----IGEKGINLSGGQKQRISLARATYQNLDIYLLDD 786
Cdd:PRK14239 99 PMSIYENVVYGLRLKGIKDKQVLDEAVE----KSLKGASIWDevkdrLHDSALGLSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1388169353 787 PLSAVDAHVGKHIFNKVLGpnglLKGK-TRLLVTHSM 822
Cdd:PRK14239 175 PTSALDPISAGKIEETLLG----LKDDyTMLLVTRSM 207
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1300-1521 |
1.38e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 78.64 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTI 1379
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1380 IPQDPI-LFSGS---------LRMNLDPFNNYSdEEIWKALElahlksfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGR 1449
Cdd:PRK13648 88 VFQNPDnQFVGSivkydvafgLENHAVPYDEMH-RRVSEALK-----------QVDMLERADYEPNALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 1450 ALLRKSKILVLDEATAAVDLETDNLIQTTIQ--NEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEEL 1521
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1317-1522 |
1.54e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 78.74 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1317 LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDG--VDIASIGLHDLREKLTIIPQDP--ILFSGSLR 1392
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGMVFQDPdnQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1393 MNLD--PFN-NYSDEEIWKALELAHLKSFVASLQlglsHEVTEAggnLSIGQRQLLCLGRALLRKSKILVLDEATAAVD- 1468
Cdd:PRK13636 102 QDVSfgAVNlKLPEDEVRKRVDNALKRTGIEHLK----DKPTHC---LSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDp 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1388169353 1469 ---LETDNLIQTTiQNEFAhCTVITIAHRLHTI-MDSDKVMVLDNGKIIECGSPEELL 1522
Cdd:PRK13636 175 mgvSEIMKLLVEM-QKELG-LTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
654-840 |
1.87e-15 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 75.54 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTayvpqqswIQNGTIKDNILFGTEFnekRYQqv 733
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE--------VSFASPRDARRAGIAM---VYQ-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 734 leacallpdlemlpggdlaeigekginLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVlgpnGLLK-- 811
Cdd:cd03216 83 ---------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVI----RRLRaq 131
|
170 180 190
....*....|....*....|....*....|
gi 1388169353 812 GKTRLLVTHSMHFLPQV-DEIVVLGNGTIV 840
Cdd:cd03216 132 GVAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
656-887 |
2.03e-15 |
|
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: 79.77 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-----------------AYVPQQ-SWIQNGTIKD 717
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlfdsrkgiflppekrriGYVFQEaRLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 718 NILFGTEF-----NEKRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 792
Cdd:TIGR02142 95 NLRYGMKRarpseRRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 793 AHVGKHIFnkvlgPngLLKGKTR------LLVTHSM-HFLPQVDEIVVLGNGTIVEKGSYSALLAKkgefaKNLKTFLRh 865
Cdd:TIGR02142 164 DPRKYEIL-----P--YLERLHAefgipiLYVSHSLqEVLRLADRVVVLEDGRVAAAGPIAEVWAS-----PDLPWLAR- 230
|
250 260
....*....|....*....|...
gi 1388169353 866 tgpEEEATVHDGS-EEEDDDYGL 887
Cdd:TIGR02142 231 ---EDQGSLIEGVvAEHDQHYGL 250
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1299-1521 |
2.57e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 77.77 E-value: 2.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1299 KIQFNNYQVRYRPELdlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILE-----AAGGQIIIDGVDI--ASIGLH 1371
Cdd:COG1117 11 KIEVRNLNVYYGDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlipgaRVEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1372 DLREKLTIIPQDPILFSGS--------LRMNLDPFNNYSDEEIWKALELAhlksfvaslqlGLSHEV----TEAGGNLSI 1439
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSiydnvaygLRLHGIKSKSELDEIVEESLRKA-----------ALWDEVkdrlKKSALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1440 GQRQLLCLGRALLRKSKILVLDEATAAVD-LETDNlIQTTIQNEFAHCTVITIAHRlhtiMD-----SDKVMVLDNGKII 1513
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDpISTAK-IEELILELKKDYTIVIVTHN----MQqaarvSDYTAFFYLGELV 232
|
....*...
gi 1388169353 1514 ECGSPEEL 1521
Cdd:COG1117 233 EFGPTEQI 240
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
654-848 |
3.59e-15 |
|
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: 76.39 E-value: 3.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT------------TAYVPQqswiqngtikDNILF 721
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsirtdrkaarqsLGYCPQ----------FDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 722 gTEFNekryqqVLEACALLPDLEMLPGGDLAEIGEKGI--------------NLSGGQKQRISLARATYQNLDIYLLDDP 787
Cdd:cd03263 88 -DELT------VREHLRFYARLKGLPKSEIKEEVELLLrvlgltdkankrarTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 788 LSAVDAHVGKHIFNKVLgpnGLLKGKTRLLVTHSMH---FLpqVDEIVVLGNGTIVEKGSYSAL 848
Cdd:cd03263 161 TSGLDPASRRAIWDLIL---EVRKGRSIILTTHSMDeaeAL--CDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
654-843 |
3.64e-15 |
|
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: 76.42 E-value: 3.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQ-QSWIQNG-TIKDNILF-GTEFN--EK 728
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGlGGGFNPElTGRENIYLnGRLLGlsRK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 729 RYQQVLEACAllpdlemlpggDLAEIGE------KgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAH----VGKH 798
Cdd:cd03220 118 EIDEKIDEII-----------EFSELGDfidlpvK--TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfqekCQRR 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1388169353 799 IFNKVlgpnglLKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 843
Cdd:cd03220 185 LRELL------KQGKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
637-861 |
3.67e-15 |
|
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: 77.26 E-value: 3.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 637 MQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-TAYVPQQSWIQNGTI 715
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIdISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 716 --KDNILFG--TEFN--------EKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYL 783
Cdd:cd03288 100 ilQDPILFSgsIRFNldpeckctDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 784 LDDPLSAVDAHVgKHIFNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKK-GEFAKNLKT 861
Cdd:cd03288 180 MDEATASIDMAT-ENILQKVV--MTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLVRT 255
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
632-852 |
3.82e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 77.34 E-value: 3.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 632 NFDKAMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQ 711
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 712 N---------------GTIKDNILFGTE---FNEKRYQQVLEACALLPDLEMLpggdlaeIGEKGINLSGGQKQRISLAR 773
Cdd:PRK13632 83 KkigiifqnpdnqfigATVEDDIAFGLEnkkVPPKKMKDIIDDLAKKVGMEDY-------LDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 774 ATYQNLDIYLLDDPLSAVDAHvGKHIFNKVLGPNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKK 852
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPK-GKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
656-848 |
4.32e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 78.61 E-value: 4.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTayVPQQSwIQNG---------------TIKDNIL 720
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED--VTHRS-IQQRdicmvfqsyalfphmSLGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 721 FGTEF----NEKRYQQVLEACALLpdlemlpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHV 795
Cdd:PRK11432 101 YGLKMlgvpKEERKQRVKEALELV---------DLAGFEDRYVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 796 GKHIFNKVLGPNGLLkGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSAL 848
Cdd:PRK11432 172 RRSMREKIRELQQQF-NITSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQEL 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1300-1525 |
5.35e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.95 E-value: 5.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYrPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIG-LHDLREKLT 1378
Cdd:PRK13644 2 IRLENVSYSY-PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1379 IIPQDP-----------ILFSGSLRMNLDPFnnysdeEIWKALELAhlksfvaSLQLGLSHEVTEAGGNLSIGQRQLLCL 1447
Cdd:PRK13644 81 IVFQNPetqfvgrtveeDLAFGPENLCLPPI------EIRKRVDRA-------LAEIGLEKYRHRSPKTLSGGQGQCVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 1448 GRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHC-TVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIP 1525
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
654-872 |
5.37e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 78.20 E-value: 5.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLI---------SAmlgemenvhGHITIKGT--TAY--------------VPQQ- 707
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIrcinllerpTS---------GSVLVDGVdlTALserelraarrkigmIFQHf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 708 SWIQNGTIKDNILFGTEFN----EKRYQQVLEacaLLpdlemlpggDLAEIGEKG----INLSGGQKQRISLARATYQNL 779
Cdd:COG1135 92 NLLSSRTVAENVALPLEIAgvpkAEIRKRVAE---LL---------ELVGLSDKAdaypSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 780 DIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS-YSALLAK 851
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILD-------LLKdinrelGLTIVLITHEMDVVRRIcDRVAVLENGRIVEQGPvLDVFANP 232
|
250 260
....*....|....*....|..
gi 1388169353 852 KGEFAKNL-KTFLRHTGPEEEA 872
Cdd:COG1135 233 QSELTRRFlPTVLNDELPEELL 254
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
655-794 |
6.87e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 75.30 E-value: 6.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG----TTAYVPQQSWI--QNG-----TIKDNILFGT 723
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdidDPDVAEACHYLghRNAmkpalTVAENLEFWA 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 724 EFNEKRYQQVLEA-CAL-LPDLEMLPGGdlaeigekgiNLSGGQKQRISLAR--ATYQNldIYLLDDPLSAVDAH 794
Cdd:PRK13539 99 AFLGGEELDIAAAlEAVgLAPLAHLPFG----------YLSAGQKRRVALARllVSNRP--IWILDEPTAALDAA 161
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1299-1525 |
7.47e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 76.10 E-value: 7.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1299 KIQFNNYQVryrpeldlvLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILE-----AAGGQIIIDGVDIASIGLHDL 1373
Cdd:PRK14247 10 KVSFGQVEV---------LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1374 REKLTIIPQDP-------ILFSGSLRMNLDPFNNYSDE---EIWKALELAHLKSFVaslqlglSHEVTEAGGNLSIGQRQ 1443
Cdd:PRK14247 81 RRRVQMVFQIPnpipnlsIFENVALGLKLNRLVKSKKElqeRVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1444 LLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAH------RLhtimdSDKVMVLDNGKIIECGS 1517
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVEWGP 228
|
....*...
gi 1388169353 1518 PEELLQIP 1525
Cdd:PRK14247 229 TREVFTNP 236
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
647-844 |
9.83e-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: 75.35 E-value: 9.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 647 EHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG--TTAYVPQQSWI----QNG------T 714
Cdd:cd03300 9 FYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkdITNLPPHKRPVntvfQNYalfphlT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 715 IKDNILFGTEFNEKRYQQVLEACAllpdlEMLPGGDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 793
Cdd:cd03300 89 VFENIAFGLRLKKLPKAEIKERVA-----EALDLVQLEGYANRKPSqLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 794 HVGKHI------FNKVLgpngllkGKTRLLVTH------SMHflpqvDEIVVLGNGTIVEKGS 844
Cdd:cd03300 164 KLRKDMqlelkrLQKEL-------GITFVFVTHdqeealTMS-----DRIAVMNKGKIQQIGT 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1322-1516 |
1.01e-14 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 74.84 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1322 CDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDlrEKLTIIPQDPILFSgslrmNLDPFNNY 1401
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFA-----HLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1402 S---------DEEIWKALElahlksfVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETD 1472
Cdd:cd03298 92 GlglspglklTAEDRQAIE-------VALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1388169353 1473 NLIQTTIqNEFAHCTVITIAHRLHTIMDS----DKVMVLDNGKIIECG 1516
Cdd:cd03298 165 AEMLDLV-LDLHAETKMTVLMVTHQPEDAkrlaQRVVFLDNGRIAAQG 211
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
649-793 |
1.14e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 79.08 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 649 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITI--KGTTAYVPQQSWIQNGTIKDNILF---GT 723
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQRPYLPLGTLREALLYpatAE 453
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 724 EFNEKRYQQVLEACAlLPDLEmlpgGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 793
Cdd:COG4178 454 AFSDAELREALEAVG-LGHLA----ERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
654-843 |
1.24e-14 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 74.56 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQNGTI------------KDNILF 721
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALieapgfypnltaRENLRL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 722 ---GTEFNEKRYQQVLEAcallpdlemlpgGDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGK 797
Cdd:cd03268 96 larLLGIRKKRIDEVLDV------------VGLKDSAKKKVkGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1388169353 798 HIFNKVLGPNGllKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 843
Cdd:cd03268 164 ELRELILSLRD--QGITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
643-867 |
1.36e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 75.82 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 643 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTaYVPQQSW---------IQN- 712
Cdd:PRK13635 12 SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV-LSEETVWdvrrqvgmvFQNp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 713 ------GTIKDNILFGTEFNE-------KRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNL 779
Cdd:PRK13635 91 dnqfvgATVQDDVAFGLENIGvpreemvERVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 780 DIYLLDDPLSAVDAhVGKHifnKVLGPNGLLKGKTRLLV---THSMHFLPQVDEIVVLGNGTIVEKG------SYSALLA 850
Cdd:PRK13635 160 DIIILDEATSMLDP-RGRR---EVLETVRQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEEGtpeeifKSGHMLQ 235
|
250 260
....*....|....*....|
gi 1388169353 851 KKG---EFAKNLKTFLRHTG 867
Cdd:PRK13635 236 EIGldvPFSVKLKELLKRNG 255
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
655-854 |
1.46e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.57 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITI-KGTT-AYVPQ-QSWIQNGTIKDNILFGtefNEKRYQ 731
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpKGLRiGYLPQePPLDDDLTVLDTVLDG---DAELRA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 732 QVLEACALLPDLEMlPGGDLAEIGEK-----------------------GI----------NLSGGQKQRISLARATYQN 778
Cdd:COG0488 92 LEAELEELEAKLAE-PDEDLERLAELqeefealggweaearaeeilsglGFpeedldrpvsELSGGWRRRVALARALLSE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 779 LDIYLLDDP-----LSAVD---AHVGKHifnkvlgPNGLlkgktrLLVTHSMHFLPQV-DEIVVLGNGTIVE-KGSYSAL 848
Cdd:COG0488 171 PDLLLLDEPtnhldLESIEwleEFLKNY-------PGTV------LVVSHDRYFLDRVaTRILELDRGKLTLyPGNYSAY 237
|
....*.
gi 1388169353 849 LAKKGE 854
Cdd:COG0488 238 LEQRAE 243
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
656-794 |
1.95e-14 |
|
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: 74.23 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 656 DVNLDIMAGQLVAVIGPVGSGKSSL---ISAMLGEMENVHGHITIKG----------TTAYVPQQS-WIQNGTIKDNILF 721
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLldaISGRVEGGGTTSGQILFNGqprkpdqfqkCVAYVRQDDiLLPGLTVRETLTY 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 722 -----GTEFNEKRYQQVLEACALLPDLEMLP-GGDLAEigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAH 794
Cdd:cd03234 105 tailrLPRKSSDAIRKKRVEDVLLRDLALTRiGGNLVK------GISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
634-844 |
1.97e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 75.61 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 634 DKAMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSS---LISAMLGEMENVHGHITIKGTTaYVPQQSW- 709
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGIT-LTAKTVWd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 710 --------IQN-------GTIKDNILFGTEFNEKRYQQVLEACA-LLPDLEMLPggdlaEIGEKGINLSGGQKQRISLAR 773
Cdd:PRK13640 82 irekvgivFQNpdnqfvgATVGDDVAFGLENRAVPRPEMIKIVRdVLADVGMLD-----YIDSEPANLSGGQKQRVAIAG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 774 ATYQNLDIYLLDDPLSAVDAHVGKHIFN---KVLGPNGLlkgkTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGS 844
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKlirKLKKKNNL----TVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1300-1527 |
2.07e-14 |
|
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: 74.64 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYrPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTI 1379
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1380 IPQDPILFSG-SLRMN--LDP-FNNYSDEEIWK----ALELAHLKSfvASLQLGLSHEvteaggnLSIGQRQLLCLGRAL 1451
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPkLLKWPKEKIREradeLLALVGLDP--AEFADRYPHE-------LSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1452 LRKSKILVLDEATAAVDLETdnliQTTIQNEFA------HCTVITIAHRL-HTIMDSDKVMVLDNGKIIECGSPEELLQI 1524
Cdd:cd03295 151 AADPPLLLMDEPFGALDPIT----RDQLQEEFKrlqqelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
...
gi 1388169353 1525 PGP 1527
Cdd:cd03295 227 PAN 229
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
654-841 |
2.09e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 75.07 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISA---MLGEMENVH--GHITIKGTTAY---------------VPQQSwiqN- 712
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRClnrMNDLIPGARveGEILLDGEDIYdpdvdvvelrrrvgmVFQKP---Np 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 713 --GTIKDNILFGtefnekryqqvleacalLPDLEMLPGGDLAEIGEK------------------GINLSGGQKQRISLA 772
Cdd:COG1117 104 fpKSIYDNVAYG-----------------LRLHGIKSKSELDEIVEEslrkaalwdevkdrlkksALGLSGGQQQRLCIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388169353 773 RATYQNLDIYLLDDPLSAVD----AHVGKHIFNkvlgpnglLKGK-TRLLVTHSMHflpQV----DEIVVLGNGTIVE 841
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDpistAKIEELILE--------LKKDyTIVIVTHNMQ---QAarvsDYTAFFYLGELVE 233
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1299-1523 |
2.10e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 75.44 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1299 KIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLT 1378
Cdd:PRK13635 5 IIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1379 IIPQDPI-LFSGSLRMNLDPF----NNYSDEEIWK----ALELAHLKSFvaslqlgLSHEVTeaggNLSIGQRQLLCLGR 1449
Cdd:PRK13635 85 MVFQNPDnQFVGATVQDDVAFglenIGVPREEMVErvdqALRQVGMEDF-------LNREPH----RLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 1450 ALLRKSKILVLDEATAAVDLETDNLIQTTIQ--NEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQ 1523
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
656-843 |
2.19e-14 |
|
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: 73.68 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG---TTAYV---PQQSWIQNG------TIKDNILFG- 722
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvTAAPPadrPVSMLFQENnlfahlTVEQNVGLGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 723 ------TEFNEKRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVG 796
Cdd:cd03298 96 spglklTAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1388169353 797 KHIFNKVLGPNGlLKGKTRLLVTHSMHFLPQVDE-IVVLGNGTIVEKG 843
Cdd:cd03298 165 AEMLDLVLDLHA-ETKMTVLMVTHQPEDAKRLAQrVVFLDNGRIAAQG 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1315-1521 |
2.42e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.12 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1315 LVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIG-LHDLREKLTIIPQDP--------- 1384
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQNPdnqivativ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1385 ---ILFsGSLRMNLDPfnnysdEEIWKALELAhLKSfvaslqLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLD 1461
Cdd:PRK13633 104 eedVAF-GPENLGIPP------EEIRERVDES-LKK------VGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 1462 EATAAVDLETDNLIQTTIQ--NEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEEL 1521
Cdd:PRK13633 170 EPTAMLDPSGRREVVNTIKelNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1316-1523 |
2.61e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 74.67 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSG-SLR-- 1392
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRel 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1393 --MNLDPFNNY----SDEE---IWKALELAHLKSFVaslqlglSHEVTEaggnLSIGQRQLLCLGRALLRKSKILVLDEA 1463
Cdd:PRK11231 97 vaYGRSPWLSLwgrlSAEDnarVNQAMEQTRINHLA-------DRRLTD----LSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 1464 TAAVDL----ETDNLIQTTIQNefaHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQ 1523
Cdd:PRK11231 166 TTYLDInhqvELMRLMRELNTQ---GKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
658-850 |
3.27e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 73.85 E-value: 3.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 658 NLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TAYVPQQSWI-----QNG-----TIKDNILFG--- 722
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhTTTPPSRRPVsmlfqENNlfshlTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 723 ----TEFNEKRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKH 798
Cdd:PRK10771 99 glklNAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 799 IFNkvlgpngLL------KGKTRLLVTHS----MHFLPQVdeiVVLGNGTIVEKGSYSALLA 850
Cdd:PRK10771 168 MLT-------LVsqvcqeRQLTLLMVSHSledaARIAPRS---LVVADGRIAWDGPTDELLS 219
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
643-850 |
3.67e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 74.49 E-value: 3.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 643 SFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT---------------------- 700
Cdd:COG4167 19 GLFRRQQFEA-VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleygdykyrckhirmifqdpn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 701 TAYVPQQswiQNGTIKDNIL-FGTEFNEK-RYQQV---LEACALLPDLemlpggdlAEIGekgIN-LSGGQKQRISLARA 774
Cdd:COG4167 98 TSLNPRL---NIGQILEEPLrLNTDLTAEeREERIfatLRLVGLLPEH--------ANFY---PHmLSSGQKQRVALARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 775 TYQNLDIYLLDDPLSAVDAHVGKHIFNKvlgpngLLKGKTRL-----LVTHSM----HFlpqVDEIVVLGNGTIVEKGSY 845
Cdd:COG4167 164 LILQPKIIIADEALAALDMSVRSQIINL------MLELQEKLgisyiYVSQHLgivkHI---SDKVLVMHQGEVVEYGKT 234
|
....*
gi 1388169353 846 SALLA 850
Cdd:COG4167 235 AEVFA 239
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1331-1520 |
4.18e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.99 E-value: 4.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1331 GVVGRTGAGKSSLTNCLFRILEAAGGQIIIDG--VDIAS--------IGLhdlrekltiIPQDPILFsgslrmnlDPFN- 1399
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSprdaialgIGM---------VHQHFMLV--------PNLTv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1400 --NY--SDEEIWKA-LELAHLKSFVASL--QLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATaAV--DLE 1470
Cdd:COG3845 98 aeNIvlGLEPTKGGrLDRKAARARIRELseRYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPT-AVltPQE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 1471 TDNLIQtTIQNeFAH--CTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEE 1520
Cdd:COG3845 177 ADELFE-ILRR-LAAegKSIIFITHKLREVMAiADRVTVLRRGKVVGTVDTAE 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1332-1538 |
4.38e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 74.45 E-value: 4.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1332 VVGRTGAGKSS---LTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPI-LFSGSlrmnldpfnNYSDEEIW 1407
Cdd:PRK13640 38 LIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREKVGIVFQNPDnQFVGA---------TVGDDVAF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1408 ----KALELAHLKSFVASL--QLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQN 1481
Cdd:PRK13640 109 glenRAVPRPEMIKIVRDVlaDVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRK 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 1482 --EFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGpfyfMAKEAGIE 1538
Cdd:PRK13640 189 lkKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVE----MLKEIGLD 243
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1316-1516 |
5.29e-14 |
|
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: 72.20 E-value: 5.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCL--FRILEAAGGQIIIDGVdiaSIGLHDLREKLTIIPQDPILFsGSLrm 1393
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGR---PLDKRSFRKIIGYVPQDDILH-PTL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1394 nldpfnnysdeEIWKALEL-AHLKSfvaslqlglshevteaggnLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETD 1472
Cdd:cd03213 98 -----------TVRETLMFaAKLRG-------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1388169353 1473 NLIQTTIQNE-FAHCTVITIAHRLHTIMDS--DKVMVLDNGKIIECG 1516
Cdd:cd03213 148 LQVMSLLRRLaDTGRTIICSIHQPSSEIFElfDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1300-1522 |
5.39e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 73.97 E-value: 5.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELDL-VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLT 1378
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1379 IIPQDPI-LFSGSLRMNLDPF----NNYSDEEIWKALELAHLKSFVASLQlglshevTEAGGNLSIGQRQLLCLGRALLR 1453
Cdd:PRK13642 85 MVFQNPDnQFVGATVEDDVAFgmenQGIPREEMIKRVDEALLAVNMLDFK-------TREPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 1454 KSKILVLDEATAAVDLETDNLIQTTIQ--NEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELL 1522
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHeiKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
654-850 |
5.66e-14 |
|
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: 73.09 E-value: 5.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--------------AYVPQqswiqnG------ 713
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDitglpphriarlgiGYVPE------Grrifps 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 714 -TIKDNILFG--TEFNEKRYQQVLE-ACALLPDL-EML--PGGdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDD 786
Cdd:COG0410 93 lTVEENLLLGayARRDRAEVRADLErVYELFPRLkERRrqRAG----------TLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388169353 787 P---LSAVdahVGKHIFNKVLGPNGllKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 850
Cdd:COG0410 163 PslgLAPL---IVEEIFEIIRRLNR--EGVTILLVEQNARFALEIaDRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1300-1514 |
5.86e-14 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 72.89 E-value: 5.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELD--LVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHdlrekL 1377
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1378 TIIPQDPILF---------SGSLRMNLDPFNNySDEEIWKALELAHLKSFVASLqlglSHEvteaggnLSIGQRQLLCLG 1448
Cdd:cd03293 76 GYVFQQDALLpwltvldnvALGLELQGVPKAE-ARERAEELLELVGLSGFENAY----PHQ-------LSGGMRQRVALA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 1449 RALLRKSKILVLDEATAAVDLETDNLIQTTIQN--EFAHCTVITIAHRLH-TIMDSDKVMVLDN--GKIIE 1514
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
654-873 |
6.02e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 73.66 E-value: 6.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAM-----LGEMENVHGHITIKGTTAYVPQQSWIQ---------------NG 713
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYAPDVDPVEvrrrigmvfqkpnpfPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 714 TIKDNILFGTEFN------EKRYQQVLEACALLPDLEmlpggdlAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDP 787
Cdd:PRK14243 106 SIYDNIAYGARINgykgdmDELVERSLRQAALWDEVK-------DKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 788 LSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLakkGEFAKNLKTFlrhTG 867
Cdd:PRK14243 179 CSALDPISTLRIEELM---HELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYL---VEFDRTEKIF---NS 249
|
....*.
gi 1388169353 868 PEEEAT 873
Cdd:PRK14243 250 PQQQAT 255
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1300-1525 |
7.30e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 72.82 E-value: 7.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELdlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDI--ASIGLHDLREKL 1377
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1378 TIIPQDPILFS----------GSLRMNldpfnNYSDEEiwkALELAhlKSFVAslQLGLSHEVTEAGGNLSIGQRQLLCL 1447
Cdd:PRK09493 80 GMVFQQFYLFPhltalenvmfGPLRVR-----GASKEE---AEKQA--RELLA--KVGLAERAHHYPSELSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1448 GRALLRKSKILVLDEATAAVDLETDNLIQTTIQ---NEFAHCTVITiahrlHTIMDSDKV----MVLDNGKIIECGSPEE 1520
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELRHEVLKVMQdlaEEGMTMVIVT-----HEIGFAEKVasrlIFIDKGRIAEDGDPQV 222
|
....*
gi 1388169353 1521 LLQIP 1525
Cdd:PRK09493 223 LIKNP 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1316-1523 |
7.46e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 73.27 E-value: 7.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPIL-FSGS---- 1390
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTveev 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1391 LRMNLDPFNNYSDEE---IWKALELAHLKSFVASLQLGLShevteagGnlsiGQRQLLCLGRALLR------KSKILVLD 1461
Cdd:PRK13548 97 VAMGRAPHGLSRAEDdalVAAALAQVDLAHLAGRDYPQLS-------G----GEQQRVQLARVLAQlwepdgPPRWLLLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388169353 1462 EATAAVDLETDnliQTTIQ--NEFAH---CTVITIAHRLH-TIMDSDKVMVLDNGKIIECGSPEELLQ 1523
Cdd:PRK13548 166 EPTSALDLAHQ---HHVLRlaRQLAHergLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
1024-1187 |
8.19e-14 |
|
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: 73.98 E-value: 8.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1024 VGVYGALGLAQGIFVFIAHFWSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWI 1103
Cdd:cd18547 48 LLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1104 TCFLGIISTLVMICMATPVFTIIVIPLGIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQ---- 1179
Cdd:cd18547 128 SSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREeeai 207
|
....*...
gi 1388169353 1180 QRFLKHNE 1187
Cdd:cd18547 208 EEFDEINE 215
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1300-1516 |
8.51e-14 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 72.40 E-value: 8.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELDLV--LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIAS--------IG 1369
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKepaearrrLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1370 LHD----LREKLTIIPQdpILFSGSLR-MNLDPFNNYSDEeiwkalelahlksfVASlQLGLSHEVTEAGGNLSIGQRQL 1444
Cdd:cd03266 82 FVSdstgLYDRLTAREN--LEYFAGLYgLKGDELTARLEE--------------LAD-RLGMEELLDRRVGGFSTGMRQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 1445 LCLGRALLRKSKILVLDEATAAVD-LETDNLIQTTIQNEFAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECG 1516
Cdd:cd03266 145 VAIARALVHDPPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
637-865 |
8.79e-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: 8.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 637 MQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLgEMENVHGHITIKGTT-------------AY 703
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGVSwnsvplqkwrkafGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 704 VPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYL 783
Cdd:cd03289 82 IPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 784 LDDPLSAVDAhVGKHIFNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEF------AK 857
Cdd:cd03289 162 LDEPSAHLDP-ITYQVIRKTL--KQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFkqaispSD 238
|
....*...
gi 1388169353 858 NLKTFLRH 865
Cdd:cd03289 239 RLKLFPRR 246
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
656-865 |
1.01e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 72.43 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAM--LGEMEN----VHGhITIKGTTA----------YVPQQSWI-QNGTIKDN 718
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITSgdliVDG-LKVNDPKVderlirqeagMVFQQFYLfPHLTALEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 719 ILFGTEFNEKRYQQVLEACALlpdlEMLPGGDLAE-IGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVgK 797
Cdd:PRK09493 98 VMFGPLRVRGASKEEAEKQAR----ELLAKVGLAErAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL-R 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 798 HIFNKV---LGPNGLlkgkTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLAKKGefAKNLKTFLRH 865
Cdd:PRK09493 173 HEVLKVmqdLAEEGM----TMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIKNPP--SQRLQEFLQH 238
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
654-844 |
1.05e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 72.88 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAYVPQQS-----WiqngTI 715
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHSslsfpF----TV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 716 KDNILFGTE---FNEKRYQQVLEACALLPDLEMLPGGDLAEigekginLSGGQKQRISLARA----TYQNLD--IYLLDD 786
Cdd:PRK13548 94 EEVVAMGRAphgLSRAEDDALVAAALAQVDLAHLAGRDYPQ-------LSGGEQQRVQLARVlaqlWEPDGPprWLLLDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 787 PLSAVD-AHvgKHIfnkVLgpnGLLKGKTR---LLVTHSMHFLPQV----DEIVVLGNGTIVEKGS 844
Cdd:PRK13548 167 PTSALDlAH--QHH---VL---RLARQLAHergLAVIVVLHDLNLAaryaDRIVLLHQGRLVADGT 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1316-1523 |
1.10e-13 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 72.19 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDlREKLTII--PQDPILFSG-SLR 1392
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIGylPQEASIFRKlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1393 MNLD---PFNNYSDEEIWKALElAHLKSFvaslqlGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDL 1469
Cdd:cd03218 94 ENILavlEIRGLSKKEREEKLE-ELLEEF------HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 1470 ETDNLIQTTIQN--EFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQ 1523
Cdd:cd03218 167 IAVQDIQKIIKIlkDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
654-850 |
1.15e-13 |
|
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: 72.08 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TAYVPQQSW-------------IQNGTIKDN 718
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEdiTGLPPHEIArlgigrtfqiprlFPELTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 719 ILFGTEFNEKRYQ-----------------QVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDI 781
Cdd:cd03219 96 VMVAAQARTGSGLllararreereareraeELLERVGLADLADRPAG-----------ELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 782 YLLDDP---LSAVDAHVGKHIFNKVLGpngllKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 850
Cdd:cd03219 165 LLLDEPaagLNPEETEELAELIRELRE-----RGITVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDEVRN 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
649-844 |
1.27e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 74.60 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 649 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-TTAYVPQ---------QSW--IQNGTIK 716
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqDITHVPAenrhvntvfQSYalFPHMTVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 717 DNILFGTEF----NEKRYQQVLEAcallpdLEMLPGGDLAEigEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 792
Cdd:PRK09452 105 ENVAFGLRMqktpAAEITPRVMEA------LRMVQLEEFAQ--RKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 793 AHVGKHIFNKvlgpnglLK------GKTRLLVTH------SMHflpqvDEIVVLGNGTIVEKGS 844
Cdd:PRK09452 177 YKLRKQMQNE-------LKalqrklGITFVFVTHdqeealTMS-----DRIVVMRDGRIEQDGT 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
632-843 |
1.51e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 72.48 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 632 NFDKAMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHI-------------TIK 698
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfeKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 699 GTTAYVPQQSWIQ--NGTIKDNILFGTEFNEKRYQQVLEACA-LLPDLEMLPGGDlaeigEKGINLSGGQKQRISLARAT 775
Cdd:PRK13648 83 KHIGIVFQNPDNQfvGSIVKYDVAFGLENHAVPYDEMHRRVSeALKQVDMLERAD-----YEPNALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388169353 776 YQNLDIYLLDDPLSAVDAHVGKHIFNKVLGPNGlLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKG 843
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKS-EHNITIISITHDLSEAMEADHVIVMNKGTVYKEG 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1316-1525 |
1.68e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.53 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDP--ILFSGSLRM 1393
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1394 NL--DPFNNYSDEEiwkalELAHLKSFVASLqLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLE- 1470
Cdd:PRK13652 99 DIafGPINLGLDEE-----TVAHRVSSALHM-LGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQg 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 1471 TDNLIQttIQNEFAH---CTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1525
Cdd:PRK13652 173 VKELID--FLNDLPEtygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
637-857 |
1.86e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 72.50 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 637 MQFSEASFTWE----HDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT----------- 701
Cdd:PRK13646 3 IRFDNVSYTYQkgtpYEHQA-IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithktkdkyir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 702 ------AYVPQ--QSWIQNGTIKDNILFGTE-FNEKRYQQVLEACALLPDLemlpgGDLAEIGEKG-INLSGGQKQRISL 771
Cdd:PRK13646 82 pvrkriGMVFQfpESQLFEDTVEREIIFGPKnFKMNLDEVKNYAHRLLMDL-----GFSRDVMSQSpFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 772 ARATYQNLDIYLLDDPLSAVDAHvGKHIFNKVLGPNGLLKGKTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGSYSALLA 850
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQ-SKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFK 235
|
....*..
gi 1388169353 851 KKGEFAK 857
Cdd:PRK13646 236 DKKKLAD 242
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1314-1486 |
2.07e-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: 70.47 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1314 DLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIAsiglhdlreKLTIIPQDPILFSG---- 1389
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA---------EQRDEPHENILYLGhlpg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1390 -----SLRMNLD---PFNNYSDEEIWKALElahlksfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLD 1461
Cdd:TIGR01189 84 lkpelSALENLHfwaAIHGGAQRTIEDALA-----------AVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILD 152
|
170 180
....*....|....*....|....*
gi 1388169353 1462 EATAAVDLETDNLIQTTIQnefAHC 1486
Cdd:TIGR01189 153 EPTTALDKAGVALLAGLLR---AHL 174
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
654-852 |
2.14e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 71.65 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTA--------YVPQQSwiqnGtiKDNILF---- 721
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSallelgagFHPELT----G--RENIYLngrl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 722 -GteFNEKRYQQVLEACAllpdlemlpggDLAEIGEKgINL-----SGGQKQRISLARATYQNLDIYLLDDPLSAVDAHV 795
Cdd:COG1134 116 lG--LSRKEIDEKFDEIV-----------EFAELGDF-IDQpvktySSGMRARLAFAVATAVDPDILLVDEVLAVGDAAF 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 796 GKHIFNKVlgpNGLLK-GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS-------YSALLAKK 852
Cdd:COG1134 182 QKKCLARI---RELREsGRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDpeeviaaYEALLAGR 244
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1319-1525 |
2.14e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.20 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1319 GITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREK---LTIIPQDPiLFSGSLRMNL 1395
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDP-LASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1396 -----DPFNNYSDEeiwkaLELAHLKSFVAS--LQLGL--------SHEvteaggnLSIGQRQLLCLGRALLRKSKILVL 1460
Cdd:PRK15079 118 geiiaEPLRTYHPK-----LSRQEVKDRVKAmmLKVGLlpnlinryPHE-------FSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1461 DEATAAVDLETD----NLIQtTIQNEFAhCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1525
Cdd:PRK15079 186 DEPVSALDVSIQaqvvNLLQ-QLQREMG-LSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1300-1498 |
2.33e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 71.99 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYrpELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAG-----GQIIIDGVDIAS--IGLHD 1372
Cdd:PRK14258 8 IKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYErrVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1373 LREKLTIIPQDPILFSGSLRMNLdpfnNYSDEEI-WK-ALEL-----AHLKSfvASLQLGLSHEVTEAGGNLSIGQRQLL 1445
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNV----AYGVKIVgWRpKLEIddiveSALKD--ADLWDEIKHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 1446 CLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEF--AHCTVITIAHRLHTI 1498
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQV 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1317-1521 |
2.62e-13 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 70.86 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1317 LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASiGLHDLREKLTIIPQDPILFSG-SLRMNL 1395
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDElTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1396 DPF-------NNYSDEEIWKALELahlksfvaslqLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVD 1468
Cdd:cd03265 95 YIHarlygvpGAERRERIDELLDF-----------VGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1469 LETDNLIQTTIQ--NEFAHCTVITIAHrlhtIMD-----SDKVMVLDNGKIIECGSPEEL 1521
Cdd:cd03265 164 PQTRAHVWEYIEklKEEFGMTILLTTH----YMEeaeqlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1317-1510 |
2.77e-13 |
|
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: 70.82 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1317 LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREK----LTIIPQDPILFSGSLR 1392
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1393 MNL---DPFNnysdEEIWKAL-ELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVD 1468
Cdd:cd03290 97 ENItfgSPFN----KQRYKAVtDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1388169353 1469 LE-TDNLIQTTIQnEFAH---CTVITIAHRLHTIMDSDKVMVLDNG 1510
Cdd:cd03290 173 IHlSDHLMQEGIL-KFLQddkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
654-851 |
2.78e-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: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIkGTT---AYVPQQswiQ-----NGTIKDNIlfgTEF 725
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETvkiGYFDQH---QeeldpDKTVLDEL---RDG 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 726 NEKRYQQvlEACALLPDLeMLPGGD-LAEIGekgiNLSGGQKQRISLARATYQNLDIYLLDDP-----LSAVDAhvgkhi 799
Cdd:COG0488 404 APGGTEQ--EVRGYLGRF-LFSGDDaFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPtnhldIETLEA------ 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1388169353 800 fnkvLgpNGLL---KGkTRLLVTHSMHFLPQV-DEIVVLGNGTIVEK-GSYSALLAK 851
Cdd:COG0488 471 ----L--EEALddfPG-TVLLVSHDRYFLDRVaTRILEFEDGGVREYpGGYDDYLEK 520
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1300-1521 |
3.28e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 71.78 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELDLVLRG---ITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDI----ASIGLHD 1372
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGldnISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1373 LREKLTIIPQDP--ILFSGSLRMNLD--PFN-NYSDEEIwKALELAHLKsfvaslQLGLSHEVTEAGG-NLSIGQRQLLC 1446
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTVLKDVEfgPKNfGFSEDEA-KEKALKWLK------KVGLSEDLISKSPfELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388169353 1447 LGRALLRKSKILVLDEATAAVDLET-DNLIQTTIQNEFAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEEL 1521
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEI 232
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1316-1522 |
4.61e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.95 E-value: 4.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPIL---FSGS-- 1390
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfeFDVRqv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1391 LRMN-------LDPFNNYSDEEIWKALELAHLKSFVAslqlglsHEVTEaggnLSIGQRQLLCLGRALLRKSKILVLDEA 1463
Cdd:PRK09536 98 VEMGrtphrsrFDTWTETDRAAVERAMERTGVAQFAD-------RPVTS----LSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 1464 TAAVDL----ETDNLIQTTIQNEFahcTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELL 1522
Cdd:PRK09536 167 TASLDInhqvRTLELVRRLVDDGK---TAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1313-1522 |
5.51e-13 |
|
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: 72.44 E-value: 5.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1313 LDLVLRGITcdigsmekiGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDG---VDIAS----------IGLhdlreklti 1379
Cdd:COG4148 20 FTLPGRGVT---------ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARgiflpphrrrIGY--------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1380 IPQDPILFSG-SLRMNLDpfnnYSDEEIWKALELAHLKSFVAslQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKIL 1458
Cdd:COG4148 82 VFQEARLFPHlSVRGNLL----YGRKRAPRAERRISFDEVVE--LLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 1459 VLDEATAAVDLETDNLIQ---TTIQNEFAhCTVITIAH------RLhtimdSDKVMVLDNGKIIECGSPEELL 1522
Cdd:COG4148 156 LMDEPLAALDLARKAEILpylERLRDELD-IPILYVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVL 222
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
649-792 |
7.54e-13 |
|
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: 67.95 E-value: 7.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 649 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITI--KGTTAYVPQQSWIQNGTIKDNILFgtefn 726
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpeGEDLLFLPQRPYLPLGTLREQLIY----- 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 727 ekryqqvleacallpdlemlPGGDlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 792
Cdd:cd03223 87 --------------------PWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
654-792 |
1.33e-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: 69.11 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--------------TAYVPQQSWI-QNGTIKDN 718
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarlgIGYLPQEASIfRKLTVEEN 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 719 ILFGTEFNEKRYQQVLE-ACALLPDLemlpggDLAEI-GEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 792
Cdd:cd03218 96 ILAVLEIRGLSKKEREEkLEELLEEF------HITHLrKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
637-820 |
1.35e-12 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 68.59 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 637 MQFSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT---------TAYVPQQ 707
Cdd:cd03292 1 IEFINVTKTYPNGTAA-LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdlrgraIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 708 --------SWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGG--DLAEigekgiNLSGGQKQRISLARATYQ 777
Cdd:cd03292 80 igvvfqdfRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKhrALPA------ELSGGEQQRVAIARAIVN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1388169353 778 NLDIYLLDDPLSAVDAHVGKHIFNKVLGPNglLKGKTRLLVTH 820
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKIN--KAGTTVVVATH 194
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
654-844 |
1.69e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 69.27 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYVPQQSWIQNG-TIKDNI 719
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPismlssrqlarrlALLPQHHLTPEGiTVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 720 LFG-----------TEFNEKRYQQVLEACallpdlemlpggDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDP 787
Cdd:PRK11231 98 AYGrspwlslwgrlSAEDNARVNQAMEQT------------RINHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 788 LSAVDahvgkhiFNKVLGPNGLL-----KGKTRLLVTHSmhfLPQV----DEIVVLGNGTIVEKGS 844
Cdd:PRK11231 166 TTYLD-------INHQVELMRLMrelntQGKTVVTVLHD---LNQAsrycDHLVVLANGHVMAQGT 221
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
976-1272 |
1.83e-12 |
|
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: 69.76 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 976 LFSIFFIILAfvmnsVAFIGSNLWLSAWTSDsKIFNstdypasQRDMRVGVYGALGLAqGIFVF--IAHFWSAFGFVHAS 1053
Cdd:cd18552 2 ALAILGMILV-----AATTAALAWLLKPLLD-DIFV-------EKDLEALLLVPLAII-GLFLLrgLASYLQTYLMAYVG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1054 N-ILH---KQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTL-VMICMATP--VFTII 1126
Cdd:cd18552 68 QrVVRdlrNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLgVLFYLDWKltLIALV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1127 VIPLGIIYVSVqmfyvsTSRQLRRL-----DSVTRspIYSHFSETVSGLPVIRAF---EHQ-QRFLKHNEvridtnqkcv 1197
Cdd:cd18552 148 VLPLAALPIRR------IGKRLRKIsrrsqESMGD--LTSVLQETLSGIRVVKAFgaeDYEiKRFRKANE---------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1198 fswitSNRWLAIRLELVGNLTV----FFSALMM--VIY---RDTLSGD-TVG-FV--LSNALNITQTLNWLVRMTSEIET 1264
Cdd:cd18552 210 -----RLRRLSMKIARARALSSplmeLLGAIAIalVLWyggYQVISGElTPGeFIsfITALLLLYQPIKRLSNVNANLQR 284
|
....*...
gi 1388169353 1265 NIVAVERI 1272
Cdd:cd18552 285 GLAAAERI 292
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
654-844 |
1.98e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 70.21 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TAYVPQQ---------------SWIQNGTIK 716
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdlTALSEKElrkarrqigmifqhfNLLSSRTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 717 DNILFGTEFN----EKRYQQVLEacaLLpdlemlpggDLAEIGEKG----INLSGGQKQRISLARATYQNLDIYLLDDPL 788
Cdd:PRK11153 101 DNVALPLELAgtpkAEIKARVTE---LL---------ELVGLSDKAdrypAQLSGGQKQRVAIARALASNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 789 SAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 844
Cdd:PRK11153 169 SALDPATTRSILE-------LLKdinrelGLTIVLITHEMDVVKRIcDRVAVIDAGRLVEQGT 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
645-845 |
2.31e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 70.63 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 645 TWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-AYVPQ---------QSW--IQN 712
Cdd:PRK11607 26 TKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDlSHVPPyqrpinmmfQSYalFPH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 713 GTIKDNILFGTEFNEKRYQQVLEACAllpdlEMLPGGDLAEI-GEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAV 791
Cdd:PRK11607 106 MTVEQNIAFGLKQDKLPKAEIASRVN-----EMLGLVHMQEFaKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 792 DAHVGKHIFNKVLgpnGLLK--GKTRLLVTHSmhflpQVDEIVVLGNGTIVEKGSY 845
Cdd:PRK11607 181 DKKLRDRMQLEVV---DILErvGVTCVMVTHD-----QEEAMTMAGRIAIMNRGKF 228
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
638-838 |
3.01e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 65.55 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 638 QFSEASFTWEhdSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--AYVPQqswiqngti 715
Cdd:cd03221 2 ELENLSKTYG--GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVkiGYFEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 716 kdnilfgtefnekryqqvleacallpdlemlpggdlaeigekginLSGGQKQRISLARATYQNLDIYLLDDPLSAVDahv 795
Cdd:cd03221 71 ---------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD--- 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1388169353 796 gkhIFNKVLGPNGLLK-GKTRLLVTHSMHFLPQV-DEIVVLGNGT 838
Cdd:cd03221 103 ---LESIEALEEALKEyPGTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
655-841 |
3.08e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.68 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKgttayVPQQSWIQNGTIKDNILFGTEFNEKRYqqVL 734
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----VPDNQFGREASLIDAIGRKGDFKDAVE--LL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 735 EACALlpdlemlpgGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVD---AHVGKHIFNKVLGPngllK 811
Cdd:COG2401 120 NAVGL---------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQKLARR----A 186
|
170 180 190
....*....|....*....|....*....|..
gi 1388169353 812 GKTRLLVTHSMHFLP--QVDEIVVLGNGTIVE 841
Cdd:COG2401 187 GITLVVATHHYDVIDdlQPDLLIFVGYGGVPE 218
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
656-858 |
3.23e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 68.89 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTayvpqqswIQNG---------------------- 713
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERV--------ITAGkknkklkplrkkvgivfqfpeh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 714 -----TIKDNILFG-------TEFNEKRYQQVLEACALLPD-LEMLPggdlaeigekgINLSGGQKQRISLARATYQNLD 780
Cdd:PRK13634 97 qlfeeTVEKDICFGpmnfgvsEEDAKQKAREMIELVGLPEElLARSP-----------FELSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 781 IYLLDDPLSAVDAHVGKHI---FNKVLGPNGLlkgkTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGSYSALLAKKGEFA 856
Cdd:PRK13634 166 VLVLDEPTAGLDPKGRKEMmemFYKLHKEKGL----TTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADPDELE 241
|
..
gi 1388169353 857 KN 858
Cdd:PRK13634 242 AI 243
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
655-793 |
4.20e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.17 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHI--------TIKGTTAYVPQQS----WiqnGTIKDNILFG 722
Cdd:PRK11247 29 NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELlagtaplaEAREDTRLMFQDArllpW---KKVIDNVGLG 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 723 TEFN-EKRYQQVLEACALlpdlemlpgGDLAeiGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 793
Cdd:PRK11247 106 LKGQwRDAALQALAAVGL---------ADRA--NEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
643-843 |
4.38e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 68.14 E-value: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 643 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAmLGEMENVHGHITIKGTTAYVPQQSWIQNGTI------- 715
Cdd:PRK14258 12 NLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNIYERRVNLnrlrrqv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 716 -----KDNIlfgteFNEKRYQQVLEACALL---PDLEM-------LPGGDL-----AEIGEKGINLSGGQKQRISLARAT 775
Cdd:PRK14258 91 smvhpKPNL-----FPMSVYDNVAYGVKIVgwrPKLEIddivesaLKDADLwdeikHKIHKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 776 YQNLDIYLLDDPLSAVDAHVGKHIfnKVLGPNGLLKGK-TRLLVTHSMHFLPQVDEIVVL--GN----GTIVEKG 843
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKV--ESLIQSLRLRSElTMVIVSHNLHQVSRLSDFTAFfkGNenriGQLVEFG 238
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
655-841 |
4.45e-12 |
|
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: 67.46 E-value: 4.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-----------------AYVpQQSW--IQNGTI 715
Cdd:COG4181 29 KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDlfaldedararlrarhvGFV-FQSFqlLPTLTA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 716 KDNI-----LFGTEFNEKRYQQVLEACALLPDLEMLPGGdlaeigekginLSGGQKQRISLARATYQNLDIYLLDDPLSA 790
Cdd:COG4181 108 LENVmlpleLAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1388169353 791 VDAHVGKHIFnkvlgpnGLL------KGKTRLLVTHSMHFLPQVDEIVVLGNGTIVE 841
Cdd:COG4181 177 LDAATGEQII-------DLLfelnreRGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1316-1521 |
4.74e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 70.60 E-value: 4.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCL--FRILEAAGGQII---------------------------------I 1360
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtlepeeV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1361 DGVDIASIGLHDLREKLTIIPQDPILFSGSLR-----MNLDPFNNYS-DEEIWKALELAHlksfvaslQLGLSHEVTEAG 1434
Cdd:TIGR03269 95 DFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTvldnvLEALEEIGYEgKEAVGRAVDLIE--------MVQLSHRITHIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1435 GNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQN--EFAHCTVITIAHRLHTIMD-SDKVMVLDNGK 1511
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIEDlSDKAIWLENGE 246
|
250
....*....|
gi 1388169353 1512 IIECGSPEEL 1521
Cdd:TIGR03269 247 IKEEGTPDEV 256
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
654-843 |
5.39e-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: 66.42 E-value: 5.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVH--GHITIKGT----------TAYVPQqswiqngtikDNILF 721
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRpldkrsfrkiIGYVPQ----------DDILH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 722 GTefnekryQQVLEAcallpdLEMlpggdLAEIgeKGInlSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFn 801
Cdd:cd03213 95 PT-------LTVRET------LMF-----AAKL--RGL--SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM- 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 802 kvlgpnGLLK-----GKTRLLVTH----SMHFLpqVDEIVVLGNGTIVEKG 843
Cdd:cd03213 152 ------SLLRrladtGRTIICSIHqpssEIFEL--FDKLLLLSQGRVIYFG 194
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1295-1514 |
5.84e-12 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 67.81 E-value: 5.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1295 PSKGKIQFNNYQVRYRPELD--LVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGlhd 1372
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1373 lrEKLTIIPQDP-----------ILFSgsLRMNLDPfNNYSDEEIWKALELAHLKSFVASLqlglSHEvteaggnLSIGQ 1441
Cdd:COG1116 80 --PDRGVVFQEPallpwltvldnVALG--LELRGVP-KAERRERARELLELVGLAGFEDAY----PHQ-------LSGGM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1442 RQLLCLGRALLRKSKILVLDEATAAVDletdnlIQT--TIQNEFA------HCTVITIAH------RLhtimdSDKVMVL 1507
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDEPFGALD------ALTreRLQDELLrlwqetGKTVLFVTHdvdeavFL-----ADRVVVL 212
|
....*....
gi 1388169353 1508 DN--GKIIE 1514
Cdd:COG1116 213 SArpGRIVE 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1316-1521 |
5.94e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.08 E-value: 5.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIG---LHDLreKLTIIPQDPILFSgslr 1392
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakAHQL--GIYLVPQEPLLFP---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1393 mNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVteAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVD-LET 1471
Cdd:PRK15439 100 -NLSVKENILFGLPKRQASMQKMKQLLAALGCQLDLDS--SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpAET 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 1472 DNL---IQTTIQNEFAhctVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEEL 1521
Cdd:PRK15439 177 ERLfsrIRELLAQGVG---IVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1316-1514 |
6.89e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 67.79 E-value: 6.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASI---GLHDLREKLTIIPQDPIlfsgslr 1392
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSI------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1393 mnlDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGG-----------NLSIGQRQLLCLGRALLRKSKILVLD 1461
Cdd:PRK10419 100 ---SAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDlddsvldkrppQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 1462 EATAAVDLetdnLIQTTI-------QNEFA-HCTVITiaHRLHTIMD-SDKVMVLDNGKIIE 1514
Cdd:PRK10419 177 EAVSNLDL----VLQAGVirllkklQQQFGtACLFIT--HDLRLVERfCQRVMVMDNGQIVE 232
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
655-843 |
7.33e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.90 E-value: 7.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTA-YVPQ---------QSWI--QNGTIKDNILFG 722
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMnDVPPaergvgmvfQSYAlyPHLSVAENMSFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 723 TEFN-------EKRYQQVLEACALLPDLEMLPGGdlaeigekginLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA-- 793
Cdd:PRK11000 100 LKLAgakkeeiNQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAal 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 794 HVGKHI----FNKVLgpngllkGKTRLLVTHSmhflpQV------DEIVVLGNGTIVEKG 843
Cdd:PRK11000 169 RVQMRIeisrLHKRL-------GRTMIYVTHD-----QVeamtlaDKIVVLDAGRVAQVG 216
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
648-844 |
7.64e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 67.03 E-value: 7.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 648 HDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG----TTAY--------VPQQSwiqNG-- 713
Cdd:COG4604 11 YGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvaTTPSrelakrlaILRQE---NHin 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 714 ---TIKDNILFGtefnekRY------------QQVLEACALLpdlemlpggDLAEIGEKGIN-LSGGQKQRISLARATYQ 777
Cdd:COG4604 88 srlTVRELVAFG------RFpyskgrltaedrEIIDEAIAYL---------DLEDLADRYLDeLSGGQRQRAFIAMVLAQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 778 NLDIYLLDDPLSAVDAHVGKHIFnkvlgpnGLLK------GKTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGS 844
Cdd:COG4604 153 DTDYVLLDEPLNNLDMKHSVQMM-------KLLRrladelGKTVVIVLHDINFASCyADHIVAMKDGRVVAQGT 219
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
1024-1184 |
8.23e-12 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 67.80 E-value: 8.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1024 VGVYGALGLAQGIFVFIAHFWSAFGfvhASNILH---KQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLR 1100
Cdd:cd18544 44 ALLYLGLLLLSFLLQYLQTYLLQKL---GQRIIYdlrRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1101 SWITCFLGIISTLVMICMATP---VFTIIVIPLgIIYVSVqmFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFE 1177
Cdd:cd18544 121 TLIGDLLLLIGILIAMFLLNWrlaLISLLVLPL-LLLATY--LFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFN 197
|
....*..
gi 1388169353 1178 HQQRFLK 1184
Cdd:cd18544 198 REKREFE 204
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1328-1513 |
8.26e-12 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 66.16 E-value: 8.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1328 EKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVdiasiglhdlrekltiipqdpILFSGSLRMNLDP--------FN 1399
Cdd:cd03297 24 EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT---------------------VLFDSRKKINLPPqqrkiglvFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1400 NYS-------DEEI---WKALELAHLKSFVASL--QLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAV 1467
Cdd:cd03297 83 QYAlfphlnvRENLafgLKRKRNREDRISVDELldLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1468 DLETDNLIQ---TTIQNEFaHCTVITIAHRLHTI-MDSDKVMVLDNGKII 1513
Cdd:cd03297 163 DRALRLQLLpelKQIKKNL-NIPVIFVTHDLSEAeYLADRIVVMEDGRLQ 211
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1316-1525 |
8.45e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 68.63 E-value: 8.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDiASIGLHDLREKLTIIPQDPILFsgslRmNL 1395
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD-LFTNLPPRERRVGFVFQHYALF----P-HM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1396 DPFNN---------YSDEEIwKA-----LELAHLKSFvaslqlglshevteAG---GNLSIGQRQLLCLGRALLRKSKIL 1458
Cdd:COG1118 91 TVAENiafglrvrpPSKAEI-RArveelLELVQLEGL--------------ADrypSQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 1459 VLDEATAAVD------LEtDNLIQttIQNEFaHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1525
Cdd:COG1118 156 LLDEPFGALDakvrkeLR-RWLRR--LHDEL-GGTTVFVTHDQEEALElADRVVVMNQGRIEQVGTPDEVYDRP 225
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1308-1522 |
9.74e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 67.34 E-value: 9.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1308 RYRPELdlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDG--VDIASIGLHDLREKLTIIPQDP- 1384
Cdd:PRK13638 10 RYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDPe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1385 --ILFSG-------SLRmNLdpfnNYSDEEIWK----ALELAHLKSFVASLQLGLSHevteaggnlsiGQRQLLCLGRAL 1451
Cdd:PRK13638 88 qqIFYTDidsdiafSLR-NL----GVPEAEITRrvdeALTLVDAQHFRHQPIQCLSH-----------GQKKRVAIAGAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 1452 LRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCT-VITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELL 1522
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNhVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
654-843 |
9.85e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 66.79 E-value: 9.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAM-----LGEMENVHGHITIKGTTAYVPQQSWIQ----------------N 712
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIEvrrevgmvfqypnpfpH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 713 GTIKDNILFGTEFN---------EKRYQQVLEACALLPDLEmlpggdlAEIGEKGINLSGGQKQRISLARATYQNLDIYL 783
Cdd:PRK14267 100 LTIYDNVAIGVKLNglvkskkelDERVEWALKKAALWDEVK-------DRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 784 LDDPLSAVDAhVGKHIFNKVLGPngLLKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 843
Cdd:PRK14267 173 MDEPTANIDP-VGTAKIEELLFE--LKKEYTIVLVTHSPAQAARVsDYVAFLYLGKLIEVG 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
656-834 |
1.02e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.28 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TAYVPQQSWIQ-----------NGTIKDNILFG 722
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdiSTLKPEIYRQQvsycaqtptlfGDTVYDNLIFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 723 TEFnekRYQQVLEAcALLPDLEM--LPggdlAEIGEKGIN-LSGGQKQRISLARatyqNLD----IYLLDDPLSAVDAHv 795
Cdd:PRK10247 105 WQI---RNQQPDPA-IFLDDLERfaLP----DTILTKNIAeLSGGEKQRISLIR----NLQfmpkVLLLDEITSALDES- 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1388169353 796 GKHIFNKVLGPNGLLKGKTRLLVTHSMHFLPQVDEIVVL 834
Cdd:PRK10247 172 NKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1316-1516 |
1.02e-11 |
|
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: 66.40 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGL-HDLREKLTIIpqDPILFSGSLrMN 1394
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLgGGFNPELTGR--ENIYLNGRL-LG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1395 LDPfnNYSDEEIWKALELAHLKSFvaslqlglsheVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNL 1474
Cdd:cd03220 114 LSR--KEIDEKIDEIIEFSELGDF-----------IDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1388169353 1475 IQTTIQNEFAHC-TVITIAHRLHTIMD-SDKVMVLDNGKIIECG 1516
Cdd:cd03220 181 CQRRLRELLKQGkTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
654-853 |
1.09e-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: 65.63 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEM--ENVHGHITIKGttayvpqqswiqngtikDNILFgTEFNEKryq 731
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKG-----------------EDITD-LPPEER--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 732 qvleacALL---------PDLEMLPGGD-LAEIGEkgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFN 801
Cdd:cd03217 75 ------ARLgiflafqypPEIPGVKNADfLRYVNE---GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1388169353 802 KVlgpNGLL-KGKTRLLVTHSMHFLPQV--DEIVVLGNGTIVEKGSYSAL--LAKKG 853
Cdd:cd03217 146 VI---NKLReEGKSVLIITHYQRLLDYIkpDRVHVLYDGRIVKSGDKELAleIEKKG 199
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
654-849 |
1.16e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 68.71 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-------------TAYVPQQSWIQ-NGTIKDNI 719
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsaraasrrVASVPQDTSLSfEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 720 LFGTEFNEKRYQQVLEACALLPDlEMLPGGDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHvgkH 798
Cdd:PRK09536 99 EMGRTPHRSRFDTWTETDRAAVE-RAMERTGVAQFADRPVtSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN---H 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 799 IFNKVLGPNGLLK-GKTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGSYSALL 849
Cdd:PRK09536 175 QVRTLELVRRLVDdGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1319-1522 |
1.23e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 69.06 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1319 GITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIII----DGVDIASIGLhDLREKLT----IIPQDPILFSGs 1390
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGP-DGRGRAKryigILHQEYDLYPH- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1391 lRMNLDPFNNYSDEEIWKalELAHLKSFVASLQLGLSHEVTEA-----GGNLSIGQRQLLCLGRALLRKSKILVLDEATA 1465
Cdd:TIGR03269 380 -RTVLDNLTEAIGLELPD--ELARMKAVITLKMVGFDEEKAEEildkyPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1466 AVDLETDNLIQTTIQN--EFAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELL 1522
Cdd:TIGR03269 457 TMDPITKVDVTHSILKarEEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
656-844 |
1.25e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 67.38 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT---------------TAYVPQQSWIQ--NGTIKDN 718
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVditdkkvklsdirkkVGLVFQYPEYQlfEETIEKD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 719 ILFGT----EFNEKRYQQVLEACALLpdlemlpGGDLAEIGEKG-INLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 793
Cdd:PRK13637 105 IAFGPinlgLSEEEIENRVKRAMNIV-------GLDYEDYKDKSpFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 794 HVGKHIFNKVlgpnGLLKGK---TRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGS 844
Cdd:PRK13637 178 KGRDEILNKI----KELHKEynmTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
642-849 |
1.60e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.55 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 642 ASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGttAYVPQQSWI----------- 710
Cdd:PRK13536 45 AGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG--VPVPARARLararigvvpqf 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 711 ----QNGTIKDNIL-FGTEFNEKRYQqvLEAcaLLPDLEmlpggDLAEIGEKG----INLSGGQKQRISLARATYQNLDI 781
Cdd:PRK13536 123 dnldLEFTVRENLLvFGRYFGMSTRE--IEA--VIPSLL-----EFARLESKAdarvSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 782 YLLDDPLSAVDAHVGKHIFNKVLGPngLLKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALL 849
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSL--LARGKTILLTTHFMEEAERLcDRLCVLEAGRKIAEGRPHALI 260
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1316-1523 |
1.70e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.07 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHD-LREKLTIIPQDPILFSgslrmN 1394
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFR-----R 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1395 LDPFNN-YSDEEIWKALELAHLKSFVASL--QLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLET 1471
Cdd:PRK10895 93 LSVYDNlMAVLQIRDDLSAEQREDRANELmeEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 1472 DNLIQTTIQN--EFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQ 1523
Cdd:PRK10895 173 VIDIKRIIEHlrDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
632-850 |
1.71e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 66.35 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 632 NFDKAMQFSEASFTWEHdSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG------------ 699
Cdd:PRK15112 9 NLSKTFRYRTGWFRRQT-VEA-VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysyrs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 700 ----------TTAYVPQQ--SWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDlemlpggdlaEIGEKGINLSGGQKQ 767
Cdd:PRK15112 87 qrirmifqdpSTSLNPRQriSQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPD----------HASYYPHMLAPGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 768 RISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLGPNGlLKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYS 846
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQE-KQGISYIYVTQHLGMMKHIsDQVLVMHQGEVVERGSTA 235
|
....
gi 1388169353 847 ALLA 850
Cdd:PRK15112 236 DVLA 239
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
976-1272 |
1.72e-11 |
|
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: 66.69 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 976 LFSIFFIILAFVMNSVafigsNLWLSAWTSDSKIfnstdypaSQRDMR-----VGVYGALGLAQGIFVFIAHFWSAFGFV 1050
Cdd:cd18542 2 LLAILALLLATALNLL-----IPLLIRRIIDSVI--------GGGLREllwllALLILGVALLRGVFRYLQGYLAEKASQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1051 HASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLpqslrSWItcFLGIISTLVMICMATPV-------- 1122
Cdd:cd18542 69 KVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFL-----AFG--LVELVRAVLLFIGALIImfsinwkl 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1123 --FTIIVIPLgIIYVSVQMF------YVSTSRQLRRLDSVTRspiyshfsETVSGLPVIRAF---EHQ-QRFLKHNEVRI 1190
Cdd:cd18542 142 tlISLAIIPF-IALFSYVFFkkvrpaFEEIREQEGELNTVLQ--------ENLTGVRVVKAFareDYEiEKFDKENEEYR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1191 DTNqkcvfswITSNRWLAIR---LELVGNLTVFFSALM---MVIyRDTLS-GDTVGFVLsnalnITQTLNWLVRM----T 1259
Cdd:cd18542 213 DLN-------IKLAKLLAKYwplMDFLSGLQIVLVLWVggyLVI-NGEITlGELVAFIS-----YLWMLIWPVRQlgrlI 279
|
330
....*....|...
gi 1388169353 1260 SEIETNIVAVERI 1272
Cdd:cd18542 280 NDMSRASASAERI 292
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
649-844 |
1.86e-11 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 65.47 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 649 DSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISaMLGEM-------ENVHGH------ITIKGTTAYVPQQSWIQNG-T 714
Cdd:cd03265 12 DFEA-VRGVSFRVRRGEIFGLLGPNGAGKTTTIK-MLTTLlkptsgrATVAGHdvvrepREVRRRIGIVFQDLSVDDElT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 715 IKDNI-----LFGTEfNEKRYQQVLEACALLpdlemlpggDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPL 788
Cdd:cd03265 90 GWENLyiharLYGVP-GAERRERIDELLDFV---------GLLEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 789 SAVDAHVGKHIFNKVlgpNGLLK--GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 844
Cdd:cd03265 160 IGLDPQTRAHVWEYI---EKLKEefGMTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGT 215
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1316-1521 |
1.87e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 67.41 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIAsiglhDLREK---LTIIPQDPILF----- 1387
Cdd:COG3839 18 ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT-----DLPPKdrnIAMVFQSYALYphmtv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1388 -----SGsLRMNldpfnNYSDEEIWKAL-ELAHLksfvaslqLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLD 1461
Cdd:COG3839 93 yeniaFP-LKLR-----KVPKAEIDRRVrEAAEL--------LGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 1462 E------ATAAVDLETDnLIQttIQNEFAHCTVI---------TIAhrlhtimdsDKVMVLDNGKIIECGSPEEL 1521
Cdd:COG3839 159 EplsnldAKLRVEMRAE-IKR--LHRRLGTTTIYvthdqveamTLA---------DRIAVMNDGRIQQVGTPEEL 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
649-850 |
2.03e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 66.55 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 649 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTA-----------------YVPQQSWIQ 711
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfsklqgirklvgivfQNPETQFVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 712 NgTIKDNILFGTEfnekryqqvlEACalLPDLEMLPGGD--LAEIG-EK-----GINLSGGQKQRISLARATYQNLDIYL 783
Cdd:PRK13644 93 R-TVEEDLAFGPE----------NLC--LPPIEIRKRVDraLAEIGlEKyrhrsPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388169353 784 LDDPLSAVDAHVGKHIFNKVLGPNGllKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLA 850
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHE--KGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
634-860 |
2.54e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.91 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 634 DKAMQFSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQN- 712
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKA-LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 713 --------------GTIKDNILFGTEFNEKRYQQVLEACAllpdlEMLPGGDLAEIGEKG-INLSGGQKQRISLARATYQ 777
Cdd:PRK13647 81 vglvfqdpddqvfsSTVWDDVAFGPVNMGLDKDEVERRVE-----EALKAVRMWDFRDKPpYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 778 NLDIYLLDDPLSAVDAHvGKHIFNKVLgpNGLLK-GKTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGSYSALLAKKGEF 855
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPR-GQETLMEIL--DRLHNqGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDEDIVE 232
|
....*
gi 1388169353 856 AKNLK 860
Cdd:PRK13647 233 QAGLR 237
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1316-1507 |
2.79e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 64.18 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVdiASIGLhdLREKLTIIPQDPILFSGSLRMNL 1395
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG--ARVAY--VPQRSEVPDSLPLTVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1396 dpfnnYSDEEIWKALELAHLKSFVASLQ-LGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNL 1474
Cdd:NF040873 83 -----WARRGLWRRLTRDDRAAVDDALErVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
|
170 180 190
....*....|....*....|....*....|....
gi 1388169353 1475 IQTTIQNEFAH-CTVITIAHRLHTIMDSDKVMVL 1507
Cdd:NF040873 158 IIALLAEEHARgATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1317-1530 |
3.04e-11 |
|
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: 65.05 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1317 LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHD-----------LREKLTIIpqDPI 1385
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQErnvgfvfqhyaLFRHMTVF--DNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1386 LFSgsLRM---NLDPFNNYSDEEIWKALELAHLKSFVASLQlglshevteagGNLSIGQRQLLCLGRALLRKSKILVLDE 1462
Cdd:cd03296 96 AFG--LRVkprSERPPEAEIRAKVHELLKLVQLDWLADRYP-----------AQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 1463 ATAAVDLETDNLIQT---TIQNEFAHCTVItIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIPG-PFYF 1530
Cdd:cd03296 163 PFGALDAKVRKELRRwlrRLHDELHVTTVF-VTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYDHPAsPFVY 234
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
704-860 |
3.43e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.52 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 704 VPQQSWIQNGTIKDNILFGTEfnEKRYQQVLEAC---ALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLD 780
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGKE--DATREDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPK 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 781 IYLLDDPLSAVDAHVGKHIFNKVLGpnglLKGK---TRLLVTHSMHFLPQVDEIVVLGN----GTIVE-KGSYSALL-AK 851
Cdd:PTZ00265 1379 ILLLDEATSSLDSNSEKLIEKTIVD----IKDKadkTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLsVQ 1454
|
....*....
gi 1388169353 852 KGEFAKNLK 860
Cdd:PTZ00265 1455 DGVYKKYVK 1463
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1314-1525 |
3.91e-11 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 64.57 E-value: 3.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1314 DLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHdlREKLTIIPQDPILFSgslrm 1393
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALFP----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1394 NLDPFNNYS-------------DEEIWKALELAHLKsfvaslqlGLSHEVTEAggnLSIGQRQLLCLGRALLRKSKILVL 1460
Cdd:cd03300 86 HLTVFENIAfglrlkklpkaeiKERVAEALDLVQLE--------GYANRKPSQ---LSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 1461 DEATAAVDLETDNLIQ---TTIQNEFAhCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1525
Cdd:cd03300 155 DEPLGALDLKLRKDMQlelKRLQKELG-ITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
654-801 |
3.95e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 67.85 E-value: 3.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISaMLGEMENVHG---HITIKGTTAYVPQQSWIQNGTIKDNILF---GTEFNE 727
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIYpdsSEDMKR 546
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388169353 728 KRY-QQVLEACALLPDLEML--PGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFN 801
Cdd:TIGR00954 547 RGLsDKDLEQILDNVQLTHIleREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYR 623
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1328-1523 |
4.22e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 64.60 E-value: 4.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1328 EKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDiasiglHDL----REKLTIIPQDPILFSG-SLRMN----LDPF 1398
Cdd:PRK10771 26 ERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD------HTTtppsRRPVSMLFQENNLFSHlTVAQNiglgLNPG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1399 NNYSDEEIWKALELAHlksfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVD----LETDNL 1474
Cdd:PRK10771 100 LKLNAAQREKLHAIAR--------QMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalrQEMLTL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1475 IQTTIQNEfaHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQ 1523
Cdd:PRK10771 172 VSQVCQER--QLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELLS 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
643-844 |
4.95e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 65.10 E-value: 4.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 643 SFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWI----------QN 712
Cdd:PRK13639 8 KYSYPDGTEA-LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevrktvgivfQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 713 G-------TIKDNILFG-------TEFNEKRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQN 778
Cdd:PRK13639 87 PddqlfapTVEEDVAFGplnlglsKEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388169353 779 LDIYLLDDPLSAVDAHVGKHIFNKVLGPNGllKGKTRLLVTHSMHFLP-QVDEIVVLGNGTIVEKGS 844
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNK--EGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGT 220
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
657-844 |
5.33e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.03 E-value: 5.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 657 VNLDIMAGQLVAVIGPVGSGKSSLI---SAMLGEMENVHGHITIKGTT------------------AYVPQQ-SWIQNGT 714
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLrhlSGLITGDKSAGSHIELLGRTvqregrlardirksrantGYIFQQfNLVNRLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 715 IKDNILFG------------TEFNEKRYQQVLEAcallpdlemLPGGDLAEIGEKGIN-LSGGQKQRISLARATYQNLDI 781
Cdd:PRK09984 103 VLENVLIGalgstpfwrtcfSWFTREQKQRALQA---------LTRVGMVHFAHQRVStLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 782 YLLDDPLSAVDAHVGKHIFNKVLGPNGlLKGKTRLLVTHSMHF-LPQVDEIVVLGNGTIVEKGS 844
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQ-NDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGS 236
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
654-850 |
5.38e-11 |
|
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: 65.84 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLG---EMENVHGHITIKGT-----------------TAYVPQQS----- 708
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEdllklsekelrkirgreIQMIFQDPmtsln 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 709 --WiqngTIKDNI-----LFGTEFNEKRYQQVLEAcallpdLEMLpggdlaeigekGIN------------LSGGQKQRI 769
Cdd:COG0444 101 pvM----TVGDQIaeplrIHGGLSKAEARERAIEL------LERV-----------GLPdperrldrypheLSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 770 SLARATYQNLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEK 842
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILN-------LLKdlqrelGLAILFITHDLGVVAEIaDRVAVMYAGRIVEE 232
|
....*...
gi 1388169353 843 GSYSALLA 850
Cdd:COG0444 233 GPVEELFE 240
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
632-864 |
6.25e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 66.21 E-value: 6.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 632 NFDKAMQFSEASFTWEHDSEAT-----VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGttayvpq 706
Cdd:PRK10070 17 HPQRAFKYIEQGLSKEQILEKTglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 707 qswIQNGTIKDNILfgTEFNEKRYQQVLEACALLPDLEMLP----GGDLAEIG-----EKGIN----------------- 760
Cdd:PRK10070 90 ---VDIAKISDAEL--REVRRKKIAMVFQSFALMPHMTVLDntafGMELAGINaeerrEKALDalrqvglenyahsypde 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 761 LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLGpnglLKGKTRLLVTHSMHFLPQV----DEIVVLGN 836
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVK----LQAKHQRTIVFISHDLDEAmrigDRIAIMQN 240
|
250 260
....*....|....*....|....*...
gi 1388169353 837 GTIVEKGSYSALLAKKGEfaKNLKTFLR 864
Cdd:PRK10070 241 GEVVQVGTPDEILNNPAN--DYVRTFFR 266
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
643-860 |
7.49e-11 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 64.44 E-value: 7.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 643 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT---------------------- 700
Cdd:TIGR02769 16 GLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQdlyqldrkqrrafrrdvqlvfq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 701 ---TAYVPQQS--WIQNGTIKDNILFGTEFNEKRYQQVLEACALLPD-LEMLPGgdlaeigekgiNLSGGQKQRISLARA 774
Cdd:TIGR02769 96 dspSAVNPRMTvrQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEdADKLPR-----------QLSGGQLQRINIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 775 TYQNLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSA 847
Cdd:TIGR02769 165 LAVKPKLIVLDEAVSNLDMVLQAVILE-------LLRklqqafGTAYLFITHDLRLVQSFcQRVAVMDKGQIVEECDVAQ 237
|
250
....*....|...
gi 1388169353 848 LLAKKGEFAKNLK 860
Cdd:TIGR02769 238 LLSFKHPAGRNLQ 250
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1315-1525 |
7.74e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 64.24 E-value: 7.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1315 LVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREK--------------LTII 1380
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMgvvrtfqhvrlfreMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1381 PQDPI---------LFSGSLRMnldPFNNYSDEEiwkALELAH--LKsfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGR 1449
Cdd:PRK11300 99 ENLLVaqhqqlktgLFSGLLKT---PAFRRAESE---ALDRAAtwLE------RVGLLEHANRQAGNLAYGQQRRLEIAR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1450 ALLRKSKILVLDEATAAVD-LETDNLIQTTIQ--NEFAhCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1525
Cdd:PRK11300 167 CMVTQPEILMLDEPAAGLNpKETKELDELIAElrNEHN-VTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1328-1525 |
8.25e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 65.63 E-value: 8.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1328 EKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHdlREKLTIIPQDPILFSG-SLRMNLdPFNNYSDEei 1406
Cdd:PRK11607 46 EIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPINMMFQSYALFPHmTVEQNI-AFGLKQDK-- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1407 wkaLELAHLKSFVASLqLGLSHEVTEAG---GNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQN-- 1481
Cdd:PRK11607 121 ---LPKAEIASRVNEM-LGLVHMQEFAKrkpHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDil 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1388169353 1482 EFAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1525
Cdd:PRK11607 197 ERVGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIYEHP 241
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
647-850 |
8.96e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.22 E-value: 8.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 647 EHDseaTVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAY----------VPQQSWIQNGTIK 716
Cdd:PRK10619 17 EHE---VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkVADKNQLRLLRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 717 DNILFgTEFNEKRYQQVLEACALLPdLEMLP-----------------GGDLAEIGEKGINLSGGQKQRISLARATYQNL 779
Cdd:PRK10619 94 LTMVF-QHFNLWSHMTVLENVMEAP-IQVLGlskqeareravkylakvGIDERAQGKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 780 DIYLLDDPLSAVDAH-VGK--HIFNKVLGpngllKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 850
Cdd:PRK10619 172 EVLLFDEPTSALDPElVGEvlRIMQQLAE-----EGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1330-1525 |
9.52e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.43 E-value: 9.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1330 IGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPI-----------LFSGSLRMNLDPF 1398
Cdd:PRK15112 42 LAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPStslnprqrisqILDFPLRLNTDLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1399 NNYSDEEIWKALElahlksfvaslQLGLSHE-VTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLET-DNLIQ 1476
Cdd:PRK15112 122 PEQREKQIIETLR-----------QVGLLPDhASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMrSQLIN 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 1477 TTIQNEFAH-CTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1525
Cdd:PRK15112 191 LMLELQEKQgISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLASP 241
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1030-1462 |
9.64e-11 |
|
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: 66.36 E-value: 9.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1030 LGLAqgIFVFIAHFWSAFGFVHAS-NILHK---QLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDT---LPQSLRSW 1102
Cdd:COG4615 55 AGLL--VLLLLSRLASQLLLTRLGqHAVARlrlRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAfvrLPELLQSV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1103 IT---CF--LGIISTLVMicmatpVFTIIVIPLGIIyvsvqMFYVSTSRQLRRLDSV--TRSPIYSHFSETVSG------ 1169
Cdd:COG4615 133 ALvlgCLayLAWLSPPLF------LLTLVLLGLGVA-----GYRLLVRRARRHLRRAreAEDRLFKHFRALLEGfkelkl 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1170 -------------LPVIRAFEHQQrflkhneVRIDTNQKCVFSWITSNrWLAirleLVGnLTVFFSALMMVIYRDTLSGd 1236
Cdd:COG4615 202 nrrrrraffdedlQPTAERYRDLR-------IRADTIFALANNWGNLL-FFA----LIG-LILFLLPALGWADPAVLSG- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1237 tvgFVLSnALNITQTLNWLVRMTSEIETNIVAVERITEYT-KVENEAPWVTDKRPPPDWPSKGKIQFNNYQVRYRPE--- 1312
Cdd:COG4615 268 ---FVLV-LLFLRGPLSQLVGALPTLSRANVALRKIEELElALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEdgd 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1313 -------LDLVL-RGitcdigsmEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDP 1384
Cdd:COG4615 344 egftlgpIDLTIrRG--------ELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDF 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1385 ILFSGslrmNLDPFNNYSDEEIWKALElahlksfvaslQLGLSHEVTEAGG-----NLSIGQRQLLCLGRALLRKSKILV 1459
Cdd:COG4615 416 HLFDR----LLGLDGEADPARARELLE-----------RLELDHKVSVEDGrfsttDLSQGQRKRLALLVALLEDRPILV 480
|
...
gi 1388169353 1460 LDE 1462
Cdd:COG4615 481 FDE 483
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1308-1525 |
1.10e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 66.73 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1308 RYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIiidgvdiasiglhdLREK-LTIIPQDPIL 1386
Cdd:PTZ00243 667 FFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------------WAERsIAYVPQQAWI 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1387 FSGSLRMNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAA 1466
Cdd:PTZ00243 733 MNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1467 VDLETDNLI-QTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIP 1525
Cdd:PTZ00243 813 LDAHVGERVvEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
654-792 |
1.30e-10 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.12 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TA------------YVPQQSWI-QNGTIKDN 718
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdiTHlpmhkrarlgigYLPQEASIfRKLTVEDN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388169353 719 I---LFGTEFNEKRYQQVLEAcaLLPDLemlpggDLAEIGE-KGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 792
Cdd:COG1137 99 IlavLELRKLSKKEREERLEE--LLEEF------GITHLRKsKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1316-1512 |
1.37e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 63.54 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIdgvdiASIGLHDLREKLTIIPQDPILFsgslrmnl 1395
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA-----GTAPLAEAREDTRLMFQDARLL-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1396 dPFNNYSD------EEIWKALELAHLKSfvaslqLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVD- 1468
Cdd:PRK11247 94 -PWKKVIDnvglglKGQWRDAALQALAA------VGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDa 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1388169353 1469 ---LETDNLIQTTIQNEfaHCTVITIAHRL-HTIMDSDKVMVLDNGKI 1512
Cdd:PRK11247 167 ltrIEMQDLIESLWQQH--GFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1316-1525 |
1.43e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 63.32 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILE-----AAGGQIIIDGVDIASIGLH--DLREKLTIIPQDPILFS 1388
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDpiEVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1389 gslrmNLDPFNNY-----------SDEEIWKALELAHLKsfvASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKI 1457
Cdd:PRK14267 99 -----HLTIYDNVaigvklnglvkSKKELDERVEWALKK---AALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 1458 LVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHR-LHTIMDSDKVMVLDNGKIIECGSPEELLQIP 1525
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFENP 239
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
656-865 |
1.43e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 63.11 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAM-LGEMENvHGHITIKGT-------------------TAYVPQQS--WiQNG 713
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPR-SGTLNIAGNhfdfsktpsdkairelrrnVGMVFQQYnlW-PHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 714 TIKDNIL------FGTEFNE--KRYQQVLEACALLPDLEMLPggdlaeigekgINLSGGQKQRISLARATYQNLDIYLLD 785
Cdd:PRK11124 98 TVQQNLIeapcrvLGLSKDQalARAEKLLERLRLKPYADRFP-----------LHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 786 DPLSAVDAHVGKHIFN--KVLGPNGLlkgkTRLLVTHSMHFLPQVDEIVV-LGNGTIVEKGSYSALLAKKGEfakNLKTF 862
Cdd:PRK11124 167 EPTAALDPEITAQIVSiiRELAETGI----TQVIVTHEVEVARKTASRVVyMENGHIVEQGDASCFTQPQTE---AFKNY 239
|
...
gi 1388169353 863 LRH 865
Cdd:PRK11124 240 LSH 242
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1300-1523 |
1.54e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.98 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELDLVLRG---ITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIG----LHD 1372
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRAlfdIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1373 LREKLTIIPQDP--ILFSGSLRMNL--DPFN-NYSDEEIWKalelahlksfVASLQL---GLSHEVTEAGG-NLSIGQRQ 1443
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVafGPQNfGIPKEKAEK----------IAAEKLemvGLADEFWEKSPfELSGGQMR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1444 LLCLGRALLRKSKILVLDEATAAVD----LETDNLIQTTIQNefaHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSP 1518
Cdd:PRK13643 152 RVAIAGILAMEPEVLVLDEPTAGLDpkarIEMMQLFESIHQS---GQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTP 228
|
....*
gi 1388169353 1519 EELLQ 1523
Cdd:PRK13643 229 SDVFQ 233
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
655-823 |
1.59e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 63.57 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-AYVPQQ---SWI----QN---GT-----IKDN 718
Cdd:COG1101 23 DGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvTKLPEYkraKYIgrvfQDpmmGTapsmtIEEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 719 IL----------FGTEFNEKRYQQVLEACALLpdlemlpggDL-------AEIGekgiNLSGGQKQRISLARATYQNLDI 781
Cdd:COG1101 103 LAlayrrgkrrgLRRGLTKKRRELFRELLATL---------GLglenrldTKVG----LLSGGQRQALSLLMATLTKPKL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1388169353 782 YLLDDPLSAVDAHVGKHIF---NKVLGPNGLlkgkTRLLVTHSMH 823
Cdd:COG1101 170 LLLDEHTAALDPKTAALVLeltEKIVEENNL----TTLMVTHNME 210
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1314-1480 |
1.68e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.20 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1314 DLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDiasIGLHDLREKLTII-PQDPILFSGSLR 1392
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD---IDDPDVAEACHYLgHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1393 MNLdpfnnysdeEIWKALELAHLKSFVASLQ-LGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLET 1471
Cdd:PRK13539 92 ENL---------EFWAAFLGGEELDIAAALEaVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
....*....
gi 1388169353 1472 DNLIQTTIQ 1480
Cdd:PRK13539 163 VALFAELIR 171
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
632-844 |
1.72e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 63.87 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 632 NFDKAMQFSEASFTWEHDSEATVRDVN---LDIMAGQLVAVIGPVGSGKSSLIS------------AMLGEMENVHGHIT 696
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTPFEFKALNntsLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqTIVGDYAIPANLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 697 IK---------GTTAYVPQQSWIQNgTIKDNILFGT----EFNEKRYQQVLEacalLPDLEMLPGgDLAEigEKGINLSG 763
Cdd:PRK13645 82 IKevkrlrkeiGLVFQFPEYQLFQE-TIEKDIAFGPvnlgENKQEAYKKVPE----LLKLVQLPE-DYVK--RSPFELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 764 GQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLGPNGlLKGKTRLLVTHSM-HFLPQVDEIVVLGNGTIVEK 842
Cdd:PRK13645 154 GQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNK-EYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISI 232
|
..
gi 1388169353 843 GS 844
Cdd:PRK13645 233 GS 234
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
1036-1272 |
2.04e-10 |
|
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: 63.62 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1036 IFVFIAHFWSAFGFV------HASNILHKQLL----NNILRAPMRFFDTTPTGRIVNRFaGDISTVDDTLPQ-SLRSWIT 1104
Cdd:cd18570 47 GLILLYLFQSLLSYIrsylllKLSQKLDIRLIlgyfKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISStTISLFLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1105 CFLGIISTLVMICMATPVFTIIVIPLgIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLK 1184
Cdd:cd18570 126 LLMVIISGIILFFYNWKLFLITLLII-PLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1185 HNEVRIDTNQKCVFS---WITSNRWLAIRLELVGNLTVFFSALMMVIyRDTLS-GDTVGFvlsNAL--NITQTLNWLVRM 1258
Cdd:cd18570 205 KIEKKFSKLLKKSFKlgkLSNLQSSIKGLISLIGSLLILWIGSYLVI-KGQLSlGQLIAF---NALlgYFLGPIENLINL 280
|
250
....*....|....
gi 1388169353 1259 TSEIETNIVAVERI 1272
Cdd:cd18570 281 QPKIQEAKVAADRL 294
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1320-1525 |
2.12e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 65.26 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1320 ITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIG---LHDLREKLTIIPQDPIlfsgslrMNLD 1396
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY-------ASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1397 PFNN--YSDEEIWKALELAHLKSF---VASL--QLGLSHE-VTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVD 1468
Cdd:PRK10261 416 PRQTvgDSIMEPLRVHGLLPGKAAaarVAWLleRVGLLPEhAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 1469 L----ETDNLIqTTIQNEFAhCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1525
Cdd:PRK10261 496 VsirgQIINLL-LDLQRDFG-IAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1307-1521 |
2.20e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 63.17 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1307 VRYR-PELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIA--SIGLHDLREKLTIIPQD 1383
Cdd:PRK13639 7 LKYSyPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKTVGIVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1384 P--ILFSGSLRMNL--DPFN-NYSDEEIWKALELAhLKsfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKIL 1458
Cdd:PRK13639 87 PddQLFAPTVEEDVafGPLNlGLSKEEVEKRVKEA-LK------AVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 1459 VLDEATAAVDLETDNLIQTTIQ--NEfAHCTVITIAHRLHTI-MDSDKVMVLDNGKIIECGSPEEL 1521
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYdlNK-EGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
654-843 |
2.60e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 61.91 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG---------TTAYVPQQSWI-QNGTIKDNILFgt 723
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaarnRIGYLPEERGLyPKMKVIDQLVY-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 724 eFNEKRYQQVLEACALLPD-LEMLpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVD---AHVGKH 798
Cdd:cd03269 94 -LAQLKGLKKEEARRRIDEwLERL---ELSEYANKRVEeLSKGNQQKVQFIAAVIHDPELLILDEPFSGLDpvnVELLKD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1388169353 799 IFNKVLGpngllKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 843
Cdd:cd03269 170 VIRELAR-----AGKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
654-837 |
2.63e-10 |
|
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: 62.10 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVP---QQSWIQN------GTIKDNILFGT- 723
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpdRMVVFQNysllpwLTVRENIALAVd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 724 ----EFNEKRYQQVLEAcallpDLEMLpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKH 798
Cdd:TIGR01184 81 rvlpDLSKSERRAIVEE-----HIALV---GLTEAADKRPGqLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1388169353 799 IFNKvlgpngLLK-----GKTRLLVTHSM-HFLPQVDEIVVLGNG 837
Cdd:TIGR01184 153 LQEE------LMQiweehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
654-843 |
2.66e-10 |
|
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: 61.83 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGqLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG------------TTAYVPQQ-SWIQNGTIKD--- 717
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQEfGVYPNFTVREfld 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 718 --NILFGTEFNE--KRYQQVLEACallpdlemlpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVD 792
Cdd:cd03264 95 yiAWLKGIPSKEvkARVDEVLELV------------NLGDRAKKKIGsLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 793 AhVGKHIFNKVLGpnGLLKGKTRLLVTH-----SMHflpqVDEIVVLGNGTIVEKG 843
Cdd:cd03264 163 P-EERIRFRNLLS--ELGEDRIVILSTHivedvESL----CNQVAVLNKGKLVFEG 211
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
643-840 |
2.86e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.13 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 643 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISaMLGEMEN-VHGHITIKGTTA------------------- 702
Cdd:PRK10535 13 SYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKpTSGTYRVAGQDVatldadalaqlrrehfgfi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 703 -----YVPQQSWIQNGTIKdNILFGTEFNEKRyqqvLEACALLPDLemlpggDLAE-IGEKGINLSGGQKQRISLARATY 776
Cdd:PRK10535 92 fqryhLLSHLTAAQNVEVP-AVYAGLERKQRL----LRAQELLQRL------GLEDrVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 777 QNLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK-----GKTRLLVTHSMHFLPQVDEIVVLGNGTIV 840
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMA-------ILHqlrdrGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
645-828 |
3.02e-10 |
|
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: 61.22 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 645 TWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT----TAYVPQQS--WI--QNG--- 713
Cdd:TIGR01189 7 ACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeQRDEPHENilYLghLPGlkp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 714 --TIKDNILFGTEFNEKRYQQVLEACAL--LPDLEMLPGGdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLS 789
Cdd:TIGR01189 87 elSALENLHFWAAIHGGAQRTIEDALAAvgLTGFEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 1388169353 790 AVDAHvGKHIFNKVLGPNgLLKGKTRLLVTHsmHFLPQV 828
Cdd:TIGR01189 157 ALDKA-GVALLAGLLRAH-LARGGIVLLTTH--QDLGLV 191
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1316-1513 |
3.42e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 64.75 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDL----REKLTIIPQDPILFSgsl 1391
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLS--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1392 rmNLDPFNNYSDEEIWKALEL-AHLKSFVASLQ-LGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDL 1469
Cdd:PRK10535 100 --HLTAAQNVEVPAVYAGLERkQRLLRAQELLQrLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1388169353 1470 ETDNLIQTTIQ--NEFAHcTVITIAHRLHTIMDSDKVMVLDNGKII 1513
Cdd:PRK10535 178 HSGEEVMAILHqlRDRGH-TVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
654-850 |
3.98e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 62.90 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT------------AYVPQ-QSWIQNGTIKDNIL 720
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPvpsrarharqrvGVVPQfDNLDPDFTVRENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 721 -FGTEFNEKRyQQVLEACALLPDLEMLPGGDLAEIGEkginLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHI 799
Cdd:PRK13537 103 vFGRYFGLSA-AAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 800 FNKVlgPNGLLKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 850
Cdd:PRK13537 178 WERL--RSLLARGKTILLTTHFMEEAERLcDRLCVIEEGRKIAEGAPHALIE 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
622-841 |
4.96e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.01 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 622 LDTSAIRHdcnfdkamQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT- 700
Cdd:PRK10419 4 LNVSGLSH--------HYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 701 ------------------------TAYVPQQS--WIqngtIKDNILFGTEFNEK----RYQQVLEACALLP-DLEMLPGg 749
Cdd:PRK10419 76 laklnraqrkafrrdiqmvfqdsiSAVNPRKTvrEI----IREPLRHLLSLDKAerlaRASEMLRAVDLDDsVLDKRPP- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 750 dlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSM- 822
Cdd:PRK10419 151 ----------QLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIR-------LLKklqqqfGTACLFITHDLr 213
|
250 260
....*....|....*....|..
gi 1388169353 823 ---HFLPQVdeiVVLGNGTIVE 841
Cdd:PRK10419 214 lveRFCQRV---MVMDNGQIVE 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1316-1513 |
5.05e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.93 E-value: 5.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGvdiasiglhdlREKLTIIPQDPILFSG------ 1389
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLPQEPPLDDDltvldt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1390 ---------SLRMNLDPFNNYSDEEIWKALELAHLKSFVASL--------------QLGLSHEVTEAG-GNLSIGQRQLL 1445
Cdd:COG0488 82 vldgdaelrALEAELEELEAKLAEPDEDLERLAELQEEFEALggweaearaeeilsGLGFPEEDLDRPvSELSGGWRRRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 1446 CLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEfaHCTVITIAH-R--LHTImdSDKVMVLDNGKII 1513
Cdd:COG0488 162 ALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNY--PGTVLVVSHdRyfLDRV--ATRILELDRGKLT 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
634-870 |
5.42e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 62.03 E-value: 5.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 634 DKAMQFSEASFTWEHDSEAT-VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTaYVPQQSW--- 709
Cdd:PRK13642 2 NKILEVENLVFKYEKESDVNqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEL-LTAENVWnlr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 710 ------IQN-------GTIKDNILFGTEfNE--------KRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQR 768
Cdd:PRK13642 81 rkigmvFQNpdnqfvgATVEDDVAFGME-NQgipreemiKRVDEALLAVNMLDFKTREPA-----------RLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 769 ISLARATYQNLDIYLLDDPLSAVDAhVGKHIFNKVLGPnglLKGK---TRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSY 845
Cdd:PRK13642 149 VAVAGIIALRPEIIILDESTSMLDP-TGRQEIMRVIHE---IKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAP 224
|
250 260 270
....*....|....*....|....*....|....*..
gi 1388169353 846 SALLAKKGE---------FAKNLKTFLRHTG---PEE 870
Cdd:PRK13642 225 SELFATSEDmveigldvpFSSNLMKDLRKNGfdlPEK 261
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
656-848 |
5.62e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 62.41 E-value: 5.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAM-----------------------LGEMENVHGHITIKGTT----------- 701
Cdd:PRK13651 25 NVSVEINQGEFIAIIGQTGSGKTTFIEHLnalllpdtgtiewifkdeknkkkTKEKEKVLEKLVIQKTRfkkikkikeir 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 702 ---AYVPQQSWIQ--NGTIKDNILFG-------TEFNEKRYQQVLEACALlpDLEMLPggdlaeigEKGINLSGGQKQRI 769
Cdd:PRK13651 105 rrvGVVFQFAEYQlfEQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGL--DESYLQ--------RSPFELSGGQKRRV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 770 SLARATYQNLDIYLLDDPLSAVDAHVGKHIFNkvLGPNGLLKGKTRLLVTHSM-HFLPQVDEIVVLGNGTIVEKG-SYSA 847
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLdNVLEWTKRTIFFKDGKIIKDGdTYDI 252
|
.
gi 1388169353 848 L 848
Cdd:PRK13651 253 L 253
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1274-1494 |
6.08e-10 |
|
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: 64.00 E-value: 6.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1274 EYTKVENEAPWVTDKRPPPDWPSKGKIQFNNYQVRYR------PELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLtncl 1347
Cdd:TIGR00954 419 KRPRVEEIESGREGGRNSNLVPGRGIVEYQDNGIKFEniplvtPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSL---- 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1348 FRIL----EAAGGQIIIDGvdiasiglhdlREKLTIIPQDPILFSGSLR------MNLDPF--NNYSDEEIWKALELAHL 1415
Cdd:TIGR00954 495 FRILgelwPVYGGRLTKPA-----------KGKLFYVPQRPYMTLGTLRdqiiypDSSEDMkrRGLSDKDLEQILDNVQL 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1416 ksfvaslqlglSHEVTEAGG---------NLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNefAHC 1486
Cdd:TIGR00954 564 -----------THILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGI 630
|
....*...
gi 1388169353 1487 TVITIAHR 1494
Cdd:TIGR00954 631 TLFSVSHR 638
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1328-1512 |
6.35e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 63.69 E-value: 6.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1328 EKIGVVGRTGAGKSSLTNCLFRILEAA-GGQIIIDG--VDIASIgLHDLREKLTIIPQD-------PILFSGSlRMNLDP 1397
Cdd:TIGR02633 287 EILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNP-AQAIRAGIAMVPEDrkrhgivPILGVGK-NITLSV 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1398 FNNYSDE-EIWKALELAHLKSFVASLQLGLSHEVTEAGGnLSIGQRQLLCLGRALLRKSKILVLDEATAAVDL----ETD 1472
Cdd:TIGR02633 365 LKSFCFKmRIDAAAELQIIGSAIQRLKVKTASPFLPIGR-LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVgakyEIY 443
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1388169353 1473 NLIQTTIQNEFAhctVITIAHRLHTIMD-SDKVMVLDNGKI 1512
Cdd:TIGR02633 444 KLINQLAQEGVA---IIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
654-849 |
6.56e-10 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 61.25 E-value: 6.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHG-HITIKGTT-------------AYV-P--QQSWIQNGTIK 716
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERrggedvwelrkriGLVsPalQLRFPRDETVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 717 DNIL---FGT-----EFNEkryQQVLEACALLPDLEMlpgGDLAE--IGEkginLSGGQKQRISLARATYQNLDIYLLDD 786
Cdd:COG1119 99 DVVLsgfFDSiglyrEPTD---EQRERARELLELLGL---AHLADrpFGT----LSQGEQRRVLIARALVKDPELLILDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 787 PLSAVDAHvGKHIFNKVLgpNGLLK--GKTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGSYSALL 849
Cdd:COG1119 169 PTAGLDLG-ARELLLALL--DKLAAegAPTLVLVTHHVEEIPPgITHVLLLKDGRVVAAGPKEEVL 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1333-1513 |
7.22e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.48 E-value: 7.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1333 VGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDI----------ASIGLhdLREKLTIIPQDPI---LFSGslRMNLDPFN 1399
Cdd:PRK10762 36 VGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpkssqeAGIGI--IHQELNLIPQLTIaenIFLG--REFVNRFG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1400 NYSdeeiWKAL--ELAHLKSfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAV-DLETDNLIQ 1476
Cdd:PRK10762 112 RID----WKKMyaEADKLLA-----RLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFR 182
|
170 180 190
....*....|....*....|....*....|....*...
gi 1388169353 1477 TTIQNEFAHCTVITIAHRLHTIMD-SDKVMVLDNGKII 1513
Cdd:PRK10762 183 VIRELKSQGRGIVYISHRLKEIFEiCDDVTVFRDGQFI 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1317-1525 |
8.69e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.94 E-value: 8.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1317 LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILE-----AAGGQIIIDGVDIAS--IGLHDLREKLTIIPQDPILFSG 1389
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSprTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1390 SLRMNLD---PFNNYSDEEIwkaLELAHLKSFV-ASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATA 1465
Cdd:PRK14239 101 SIYENVVyglRLKGIKDKQV---LDEAVEKSLKgASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 1466 AVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1525
Cdd:PRK14239 178 ALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQMFMNP 238
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1332-1525 |
9.61e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 61.27 E-value: 9.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1332 VVGRTGAGKSSLTNCLFRILEAAGG-----QIIIDGVDIASI-GLHDLREKLTIIPQDPILFSGSLRMNLdpfnnysdEE 1405
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPMSIMDNV--------LA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1406 IWKALELAHLKSFVASLQLGLSH---------EVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQ 1476
Cdd:PRK14271 124 GVRAHKLVPRKEFRGVAQARLTEvglwdavkdRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1477 TTIQNEFAHCTVITIAHRL-HTIMDSDKVMVLDNGKIIECGSPEELLQIP 1525
Cdd:PRK14271 204 EFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSSP 253
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1300-1523 |
9.76e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 61.74 E-value: 9.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELdlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHdLREKLTI 1379
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1380 IPQ----DPILfsgSLRMNLDPFNNY-------SDEEIWKALELAHLKSfVASLQLGlshevteaggNLSIGQRQLLCLG 1448
Cdd:PRK13537 85 VPQfdnlDPDF---TVRENLLVFGRYfglsaaaARALVPPLLEFAKLEN-KADAKVG----------ELSGGMKRRLTLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1449 RALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITI-------AHRLhtimdSDKVMVLDNGKIIECGSPEEL 1521
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVIEEGRKIAEGAPHAL 225
|
..
gi 1388169353 1522 LQ 1523
Cdd:PRK13537 226 IE 227
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
1024-1272 |
1.08e-09 |
|
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: 61.33 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1024 VGVYGALGLAQGIFVFIAHFWSAfgfVHASNILH---KQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLR 1100
Cdd:cd18545 43 ALLFLALNLVNWVASRLRIYLMA---KVGQRILYdlrQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1101 SWITCFLGIISTLVM----------ICMAT-PVFTIIVIPLGIIyvsvqmfyvstSRQLRRLDSVTRSPIYSHFSETVSG 1169
Cdd:cd18545 120 NLIPDLLTLVGIVIImfslnvrlalVTLAVlPLLVLVVFLLRRR-----------ARKAWQRVRKKISNLNAYLHESISG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1170 LPVIRAFEHQQRFLKHNEvriDTNQKCVFSWITSNRWLAIRLELVGNLTVFFSALMMVI-YRDTLSGD-TVGFVLSNALN 1247
Cdd:cd18545 189 IRVIQSFAREDENEEIFD---ELNRENRKANMRAVRLNALFWPLVELISALGTALVYWYgGKLVLGGAiTVGVLVAFIGY 265
|
250 260
....*....|....*....|....*...
gi 1388169353 1248 IT---QTLNWLVRMTSEIETNIVAVERI 1272
Cdd:cd18545 266 VGrfwQPIRNLSNFYNQLQSAMASAERI 293
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1316-1523 |
1.12e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.48 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGvDIASI-----GLH-DL--REKltiipqdpILF 1387
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-RVSALlelgaGFHpELtgREN--------IYL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1388 SGSLrmnldpfNNYSDEEIwKAL-----ELAHLKSFvaslqlgLSHEVteagGNLSIGQRQLLCLGRALLRKSKILVLDE 1462
Cdd:COG1134 112 NGRL-------LGLSRKEI-DEKfdeivEFAELGDF-------IDQPV----KTYSSGMRARLAFAVATAVDPDILLVDE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 1463 ATAAVDLE----TDNLIQTTIQNefaHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQ 1523
Cdd:COG1134 173 VLAVGDAAfqkkCLARIRELRES---GRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
654-823 |
1.25e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.21 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTayVPQQSWIQNGTIKDNIL-FGTEFNEkryqq 732
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQP--MSKLSSAAKAELRNQKLgFIYQFHH----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 733 vleacaLLPD---LE-----MLPGGD------------LAEIG-EKGIN-----LSGGQKQRISLARATYQNLDIYLLDD 786
Cdd:PRK11629 98 ------LLPDftaLEnvampLLIGKKkpaeinsralemLAAVGlEHRANhrpseLSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 1388169353 787 PLSAVDAHVGKHIFNkVLGPNGLLKGKTRLLVTHSMH 823
Cdd:PRK11629 172 PTGNLDARNADSIFQ-LLGELNRLQGTAFLVVTHDLQ 207
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1305-1525 |
1.28e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 61.52 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1305 YQVR---YRPElDLV--LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIAS---IGLHDLREK 1376
Cdd:PRK11308 15 YPVKrglFKPE-RLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1377 LTIIPQDPIlfsGSLrmnlDPFNNYSD--EE---IWKALELAHLKSFVASL--QLGLSHEVTEAGGNL-SIGQRQLLCLG 1448
Cdd:PRK11308 94 IQIVFQNPY---GSL----NPRKKVGQilEEpllINTSLSAAERREKALAMmaKVGLRPEHYDRYPHMfSGGQRQRIAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1449 RALLRKSKILVLDEATAAVDLEtdnlIQTTIQNEFA------HCTVITIAHRL----HTimdSDKVMVLDNGKIIECGSP 1518
Cdd:PRK11308 167 RALMLDPDVVVADEPVSALDVS----VQAQVLNLMMdlqqelGLSYVFISHDLsvveHI---ADEVMVMYLGRCVEKGTK 239
|
....*..
gi 1388169353 1519 EELLQIP 1525
Cdd:PRK11308 240 EQIFNNP 246
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1316-1522 |
1.31e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 61.77 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGlHDLREKLTIIPQ-DPILFSGSLRMN 1394
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA-RLARARIGVVPQfDNLDLEFTVREN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1395 LDPFNNY-------SDEEIWKALELAHLKSFVASlqlglshEVTEaggnLSIGQRQLLCLGRALLRKSKILVLDEATAAV 1467
Cdd:PRK13536 135 LLVFGRYfgmstreIEAVIPSLLEFARLESKADA-------RVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 1468 DLETDNLIQTTIQNEFAHC-TVITIAHrlhtIMDS-----DKVMVLDNGKIIECGSPEELL 1522
Cdd:PRK13536 204 DPHARHLIWERLRSLLARGkTILLTTH----FMEEaerlcDRLCVLEAGRKIAEGRPHALI 260
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1316-1513 |
1.34e-09 |
|
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: 60.42 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVD--------IASIGLHdLREKLTIIPQDPILf 1387
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrrkkfLRRIGVV-FGQKTQLWWDLPVI- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1388 sGSLRMNLDPFNnysdeeiwkaLELAHLKSFVASLQ--LGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATA 1465
Cdd:cd03267 114 -DSFYLLAAIYD----------LPPARFKKRLDELSelLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 1466 AVDLETDNLIQTTIQ--NEFAHCTVITIAHRLHTIMD-SDKVMVLDNGKII 1513
Cdd:cd03267 183 GLDVVAQENIRNFLKeyNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
657-850 |
1.43e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 60.28 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 657 VNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG--------------TTAYVPQQSWI-QNGTIKDNILF 721
Cdd:PRK11614 24 VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditdwqtakimreAVAIVPEGRRVfSRMTVEENLAM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 722 GTEFNEK-RYQQVLEAC-ALLPDLemlpggdLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHI 799
Cdd:PRK11614 104 GGFFAERdQFQERIKWVyELFPRL-------HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 800 FNKVLGPNGllKGKTRLLVTHSMH-FLPQVDEIVVLGNGTIVEKGSYSALLA 850
Cdd:PRK11614 177 FDTIEQLRE--QGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
654-843 |
1.43e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 60.31 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAM-----LGEMENVHGHITIKGTTAY----------------VPQQswIQN 712
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQDIFkmdvielrrrvqmvfqIPNP--IPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 713 GTIKDNILFGTEFN---------EKRYQQVLEACALLPDLEmlpggdlAEIGEKGINLSGGQKQRISLARATYQNLDIYL 783
Cdd:PRK14247 97 LSIFENVALGLKLNrlvkskkelQERVRWALEKAQLWDEVK-------DRLDAPAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 784 LDDPLSAVDAHVGKHIFNKVLgpnGLLKGKTRLLVThsmHFLPQV----DEIVVLGNGTIVEKG 843
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFL---ELKKDMTIVLVT---HFPQQAarisDYVAFLYKGQIVEWG 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
643-844 |
1.72e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 60.49 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 643 SFTWEHDSEAT----VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSW-IQNgtiKD 717
Cdd:PRK13633 11 SYKYESNEESTeklaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIRN---KA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 718 NILFGTEFNEKRYQQVLEACALLPdlEMLpGGDLAEIGE------KGIN-----------LSGGQKQRISLARATYQNLD 780
Cdd:PRK13633 88 GMVFQNPDNQIVATIVEEDVAFGP--ENL-GIPPEEIRErvdeslKKVGmyeyrrhaphlLSGGQKQRVAIAGILAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 781 IYLLDDPLSAVDAHVGKHIFNKVLGPNGLlKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGS 844
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNTIKELNKK-YGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1328-1512 |
2.30e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.87 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1328 EKIGVVGRTGAGKSSLTNCLFRILEAA-GGQIIIDG--VDIASIgLHDLREKLTIIPQD-------PILFSG--SLRMNL 1395
Cdd:PRK13549 289 EILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGkpVKIRNP-QQAIAQGIAMVPEDrkrdgivPVMGVGknITLAAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1396 DPFNNYSdeEIWKALELAHLKSFVASLQLGLSHeVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDL----ET 1471
Cdd:PRK13549 368 DRFTGGS--RIDDAAELKTILESIQRLKVKTAS-PELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVgakyEI 444
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1388169353 1472 DNLIQTTIQNEFAhctVITIAHRLHTIMD-SDKVMVLDNGKI 1512
Cdd:PRK13549 445 YKLINQLVQQGVA---IIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
655-852 |
2.34e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.87 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITI-KGTTA-YVPQQSWI-QNGTIKDNILFG--------T 723
Cdd:TIGR03719 22 KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIKVgYLPQEPQLdPTKTVRENVEEGvaeikdalD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 724 EFNE-------------------KRYQQVLEACA---LLPDLEM------LPGGDlAEIGekgiNLSGGQKQRISLARAT 775
Cdd:TIGR03719 102 RFNEisakyaepdadfdklaaeqAELQEIIDAADawdLDSQLEIamdalrCPPWD-ADVT----KLSGGERRRVALCRLL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 776 YQNLDIYLLDDPLSAVDAH----VGKHIFNkvlgpnglLKGkTRLLVTHSMHFLPQVDE-IVVLGNGT-IVEKGSYSALL 849
Cdd:TIGR03719 177 LSKPDMLLLDEPTNHLDAEsvawLERHLQE--------YPG-TVVAVTHDRYFLDNVAGwILELDRGRgIPWEGNYSSWL 247
|
...
gi 1388169353 850 AKK 852
Cdd:TIGR03719 248 EQK 250
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
654-850 |
2.73e-09 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 59.67 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TAYVPQQswI---------QNG------TIK 716
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRdiTGLPPHR--IarlgiartfQNPrlfpelTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 717 DNIL-----------FGTEFNEKRYQ-----------QVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARA 774
Cdd:COG0411 98 ENVLvaaharlgrglLAALLRLPRARreereareraeELLERVGLADRADEPAG-----------NLSYGQQRRLEIARA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 775 tyqnL----DIYLLDDP---LSAVDAHVGKHIFNKVLGPNGLlkgkTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYS 846
Cdd:COG0411 167 ----LatepKLLLLDEPaagLNPEETEELAELIRRLRDERGI----TILLIEHDMDLVMGLaDRIVVLDFGRVIAEGTPA 238
|
....
gi 1388169353 847 ALLA 850
Cdd:COG0411 239 EVRA 242
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
645-793 |
2.75e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 58.66 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 645 TWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWI--------QNG--- 713
Cdd:cd03231 7 TCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIArgllylghAPGikt 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 714 --TIKDNILFGTEFNEKryQQVLEAcallpdlemlpggdLAEIGEKGI------NLSGGQKQRISLARATYQNLDIYLLD 785
Cdd:cd03231 87 tlSVLENLRFWHADHSD--EQVEEA--------------LARVGLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWILD 150
|
....*...
gi 1388169353 786 DPLSAVDA 793
Cdd:cd03231 151 EPTTALDK 158
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
654-850 |
3.04e-09 |
|
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: 61.62 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGeMENVHGHITIKGT-------TAYVPQQSWIQ------NG------T 714
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQdldglsrRALRPLRRRMQvvfqdpFGslsprmT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 715 IKDNI-----LFGTEFNEK-RYQQVLEAcallpdlemlpggdLAEIG-----------EkginLSGGQKQRISLARATYQ 777
Cdd:COG4172 381 VGQIIaeglrVHGPGLSAAeRRARVAEA--------------LEEVGldpaarhryphE----FSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 778 NLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 850
Cdd:COG4172 443 EPKLLVLDEPTSALDVSVQAQILD-------LLRdlqrehGLAYLFISHDLAVVRALaHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
655-841 |
3.18e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 61.19 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGemenVH----GHITIKGTT--------------AYVPQQ-SWIQNGTI 715
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSG----VYqpdsGEILLDGEPvrfrsprdaqaagiAIIHQElNLVPNLSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 716 KDNILFGTE------FNEKR-YQQVLEACALLpDLEMLPGgdlAEIGEkginLSGGQKQRISLARATYQNLDIYLLDDPL 788
Cdd:COG1129 97 AENIFLGREprrgglIDWRAmRRRARELLARL-GLDIDPD---TPVGD----LSVAQQQLVEIARALSRDARVLILDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 789 SAVDAHVGKHIFNKVLGpnglLK--GKTRLLVThsmHFLPQV----DEIVVLGNGTIVE 841
Cdd:COG1129 169 ASLTEREVERLFRIIRR----LKaqGVAIIYIS---HRLDEVfeiaDRVTVLRDGRLVG 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1317-1510 |
3.29e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.34 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1317 LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDI--------ASIGLHDLREKLTIIPQDPI--- 1385
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnkldhklaAQLGIGIIYQELSVIDELTVlen 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1386 LFSGSLRMNLDPFNNYSDeeiWKALELahlKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATA 1465
Cdd:PRK09700 101 LYIGRHLTKKVCGVNIID---WREMRV---RAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1388169353 1466 AV-DLETDNL--IQTTIQNEFAhcTVITIAHRLHTIMD-SDKVMVLDNG 1510
Cdd:PRK09700 175 SLtNKEVDYLflIMNQLRKEGT--AIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1316-1525 |
3.55e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 59.38 E-value: 3.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDI-ASIGL-------HDLREKLTIIPQDPILF 1387
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLsqqkgliRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1388 ----------SGSLRMNLDPfnnySDEEIWKALELAhlksfvasLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKI 1457
Cdd:PRK11264 98 phrtvleniiEGPVIVKGEP----KEEATARARELL--------AKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 1458 LVLDEATAAVDLETDNLIQTTIQnEFAH--CTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1525
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNTIR-QLAQekRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1316-1524 |
3.59e-09 |
|
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: 58.31 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCL--FRILEAAGGQIIIDGVDIASIGLHD-LREKLTIIPQDPILFSGslr 1392
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEErARLGIFLAFQYPPEIPG--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1393 mnldpfnnysdeeiwkalelAHLKSFVASLQLGLShevteagGnlsiGQRQLLCLGRALLRKSKILVLDEATAAVDLETD 1472
Cdd:cd03217 92 --------------------VKNADFLRYVNEGFS-------G----GEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 1473 NLIQTTIqNEFA--HCTVITIAH--RLHTIMDSDKVMVLDNGKIIECGSPEELLQI 1524
Cdd:cd03217 141 RLVAEVI-NKLReeGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKELALEI 195
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1316-1521 |
3.88e-09 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 60.11 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCL--FriLEAAGGQIIIDGVDIASIGLHdlREKLTIIPQDPILFS----- 1388
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIagF--ETPDSGRILLDGRDVTGLPPE--KRNVGMVFQDYALFPhltva 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1389 -----GsLRMNldpfnNYSDEEIWK----ALELAHLKSFvaslqlgLSHEVTEaggnLSIGQRQLLCLGRALLRKSKILV 1459
Cdd:COG3842 96 envafG-LRMR-----GVPKAEIRArvaeLLELVGLEGL-------ADRYPHQ----LSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 1460 LDEATAAVDLET-----DNLIQttIQNEFaHCTVITIAHrlhtimD-------SDKVMVLDNGKIIECGSPEEL 1521
Cdd:COG3842 159 LDEPLSALDAKLreemrEELRR--LQREL-GITFIYVTH------DqeealalADRIAVMNDGRIEQVGTPEEI 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1317-1513 |
4.06e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1317 LRGITCDIGSMEKIGVVGRTGAGKSSLtnclFRILEAA------GGQIIIDGVDIASIGLHDLREK--------LTIIPQ 1382
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTL----MKVLSGVyphgtyEGEIIFEGEELQASNIRDTERAgiaiihqeLALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1383 DPIL---FSGSL-----RMNLDPFnnYSDEEIWKAlelahlksfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRK 1454
Cdd:PRK13549 97 LSVLeniFLGNEitpggIMDYDAM--YLRAQKLLA-------------QLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 1455 SKILVLDEATAAV-DLETDNLIqTTIQNEFAH-CTVITIAHRLHTIMD-SDKVMVLDNGKII 1513
Cdd:PRK13549 162 ARLLILDEPTASLtESETAVLL-DIIRDLKAHgIACIYISHKLNEVKAiSDTICVIRDGRHI 222
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1318-1512 |
4.35e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.83 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1318 RGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHD-LREKLTIIPQDP----ILFSGSLR 1392
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDRqssgLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1393 MNLDPFnNYSDEEIW--KALELAHLKSFVASLQLGLSHEVTEAGGnLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLE 1470
Cdd:PRK15439 360 WNVCAL-THNRRGFWikPARENAVLERYRRALNIKFNHAEQAART-LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1388169353 1471 TDNLIQTTIQNEFA-HCTVITIAHRLHTIMD-SDKVMVLDNGKI 1512
Cdd:PRK15439 438 ARNDIYQLIRSIAAqNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
644-843 |
4.93e-09 |
|
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: 58.50 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 644 FTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGttaYVPqqsWIQNGTIKDNI--LF 721
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG---LVP---WKRRKKFLRRIgvVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 722 GT---------------------EFNEKRYQQVLEACAllpdlEMLpggDLAEIGEKGI-NLSGGQKQRISLARATYQNL 779
Cdd:cd03267 101 GQktqlwwdlpvidsfyllaaiyDLPPARFKKRLDELS-----ELL---DLEELLDTPVrQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 780 DIYLLDDPLSAVDAHVGKHIFNKVLGPNGlLKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 843
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYNR-ERGTTVLLTSHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1328-1525 |
8.21e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 58.97 E-value: 8.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1328 EKIGVVGRTGAGKSSLTNCLFRILEAAG---GQIIIDGVDIASIGLHDLR----EKLTIIPQDPIlfsgslrMNLDPFNN 1400
Cdd:PRK09473 43 ETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPEKELNklraEQISMIFQDPM-------TSLNPYMR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1401 YSdEEIWKALEL----AHLKSFVASLQLGLSHEVTEAGGNL-------SIGQRQLLCLGRALLRKSKILVLDEATAAVDL 1469
Cdd:PRK09473 116 VG-EQLMEVLMLhkgmSKAEAFEESVRMLDAVKMPEARKRMkmyphefSGGMRQRVMIAMALLCRPKLLIADEPTTALDV 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1470 ETDNLIQT---TIQNEFaHCTVITIAHRLHTIMDS-DKVMVLDNGKIIECGSPEELLQIP 1525
Cdd:PRK09473 195 TVQAQIMTllnELKREF-NTAIIMITHDLGVVAGIcDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
654-843 |
8.45e-09 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 57.38 E-value: 8.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-TTAYVPQQSWIQNG------------TIKDNIL 720
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARRRLGfvsdstglydrlTARENLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 721 -FGTEFNEKRYQQVLEACALLPDLEMlpgGDLAEIGEKGinLSGGQKQRISLARATYQNLDIYLLDDPLSAVDahvgkhi 799
Cdd:cd03266 101 yFAGLYGLKGDELTARLEELADRLGM---EELLDRRVGG--FSTGMRQKVAIARALVHDPPVLLLDEPTTGLD------- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 800 fnkVLGPNGLLK--------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 843
Cdd:cd03266 169 ---VMATRALREfirqlralGKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1316-1519 |
9.26e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.82 E-value: 9.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIidgvdiasiglHDLREKLTIIPQ----DPIL-FSGS 1390
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLRIGYVPQklylDTTLpLTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1391 LRMNLDPfnNYSDEEIWKALE---LAHLKSfvASLQlglshevteaggNLSIGQRQLLCLGRALLRKSKILVLDEATAAV 1467
Cdd:PRK09544 88 RFLRLRP--GTKKEDILPALKrvqAGHLID--APMQ------------KLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1388169353 1468 D----LETDNLIQtTIQNEFaHCTVITIAHRLHTIM-DSDKVMVLdNGKIIECGSPE 1519
Cdd:PRK09544 152 DvngqVALYDLID-QLRREL-DCAVLMVSHDLHLVMaKTDEVLCL-NHHICCSGTPE 205
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
654-792 |
9.90e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 57.60 E-value: 9.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITI--------------KGTTAYVPQQSWI-QNGTIKDN 718
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllplharaRRGIGYLPQEASIfRRLSVYDN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 719 ILFGTEFNE--KRYQQVLEACALLPDLEMLPGGDlaeigEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 792
Cdd:PRK10895 99 LMAVLQIRDdlSAEQREDRANELMEEFHIEHLRD-----SMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1316-1516 |
9.92e-09 |
|
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: 57.26 E-value: 9.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIAsiglhDLREK---LTIIPQDPILFSgslR 1392
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT-----DLPPKdrdIAMVFQNYALYP---H 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1393 MNLdpFNNysdeeIWKALELAHLK--------SFVASLqLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEAT 1464
Cdd:cd03301 87 MTV--YDN-----IAFGLKLRKVPkdeidervREVAEL-LQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 1465 AAVD--------LETDNLIQ----TTI-----QNEfahctVITIAhrlhtimdsDKVMVLDNGKIIECG 1516
Cdd:cd03301 159 SNLDaklrvqmrAELKRLQQrlgtTTIyvthdQVE-----AMTMA---------DRIAVMNDGQIQQIG 213
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1300-1513 |
1.00e-08 |
|
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: 57.29 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELdlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHD------- 1372
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRigylpee 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1373 --LREKLTIIPQdpILFSGSLR-MNLDPFNNYSDEeiW-KALELAHLKSfvaslqlglshEVTEaggNLSIGQRQLLCLG 1448
Cdd:cd03269 79 rgLYPKMKVIDQ--LVYLAQLKgLKKEEARRRIDE--WlERLELSEYAN-----------KRVE---ELSKGNQQKVQFI 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388169353 1449 RALLRKSKILVLDEATAAVDLETDNLIQTTIqNEFAH--CTVITIAHRLHTIMD-SDKVMVLDNGKII 1513
Cdd:cd03269 141 AAVIHDPELLILDEPFSGLDPVNVELLKDVI-RELARagKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
637-846 |
1.00e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.59 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 637 MQFSEASFTWEHDSEATVR---DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-TTAYVPQQSWIQN 712
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRalfDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDiVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 713 GTIKDNILFgtEFNEKRY--QQVLEACALLPD----------------LEMLpgGDLAEIGEKG-INLSGGQKQRISLAR 773
Cdd:PRK13643 82 VRKKVGVVF--QFPESQLfeETVLKDVAFGPQnfgipkekaekiaaekLEMV--GLADEFWEKSpFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 774 ATYQNLDIYLLDDPLSAVDAHVGKHIFNkvLGPNGLLKGKTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGSYS 846
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQ--LFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPS 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1316-1529 |
1.12e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.72 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILeAAGGQIIIDGVDIASIG---LHDLREKLTIIPQDPilfSGSL- 1391
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP---NSSLn 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1392 -RMNLDpfnnysdEEIWKALELAHLKSFVASLQLGLSHEVTEAG----------GNLSIGQRQLLCLGRALLRKSKILVL 1460
Cdd:PRK15134 377 pRLNVL-------QIIEEGLRVHQPTLSAAQREQQVIAVMEEVGldpetrhrypAEFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 1461 DEATAAVDLETDNLIQT---TIQNEFaHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIPGPFY 1529
Cdd:PRK15134 450 DEPTSSLDKTVQAQILAllkSLQQKH-QLAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1332-1507 |
1.24e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.03 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1332 VVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNLD-PF---NNYSDEeiw 1407
Cdd:PRK10247 38 ITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNLIfPWqirNQQPDP--- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1408 kalelahlKSFVASL-QLGLSHEVTEAGGN-LSIGQRQLLCLGRALLRKSKILVLDEATAAVDleTDNliqTTIQNEFAH 1485
Cdd:PRK10247 115 --------AIFLDDLeRFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALD--ESN---KHNVNEIIH 181
|
170 180
....*....|....*....|....*....
gi 1388169353 1486 -------CTVITIAHRLHTIMDSDKVMVL 1507
Cdd:PRK10247 182 ryvreqnIAVLWVTHDKDEINHADKVITL 210
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1333-1544 |
1.27e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 60.03 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1333 VGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASiGLHDLREKLTIIPQDPILFSgslRMNLDPFNNYSDEEIWKALEL 1412
Cdd:TIGR01257 962 LGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFH---HLTVAEHILFYAQLKGRSWEE 1037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1413 AHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIA 1492
Cdd:TIGR01257 1038 AQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMST 1117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 1493 HRL-HTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFYFMAKEAGIENVNSTK 1544
Cdd:TIGR01257 1118 HHMdEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIQSQR 1170
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
575-841 |
1.43e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.22 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 575 DAQKAFT-SITLFnILRFPL-SM---LPMMISsmlqASVSTERLEKY-LGGD--DLDTSAIRHDCnfdKAMQFSEASFTW 646
Cdd:PRK10522 261 DTNVAATySLTLL-FLRTPLlSAvgaLPTLLS----AQVAFNKLNKLaLAPYkaEFPRPQAFPDW---QTLELRNVTFAY 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 647 eHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLisAML--GEMENVHGHITIKGTT-------AYVPQQSWIqngtIKD 717
Cdd:PRK10522 333 -QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTL--AMLltGLYQPQSGEILLDGKPvtaeqpeDYRKLFSAV----FTD 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 718 NILF-------GTEFNEKRYQQVLEACALLPDLEmLPGGDLAEIgekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSA 790
Cdd:PRK10522 406 FHLFdqllgpeGKPANPALVEKWLERLKMAHKLE-LEDGRISNL-----KLSKGQKKRLALLLALAEERDILLLDEWAAD 479
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 791 VDAHVgKHIFNKVLGPNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVE 841
Cdd:PRK10522 480 QDPHF-RREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
654-840 |
1.55e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.88 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--------------AYVP----QQSWIQNGTI 715
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPvrirsprdairagiAYVPedrkGEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 716 KDNIL---------FGTEFNEKRYQQVLEACALL----PDLEmlpggdlAEIGekgiNLSGGQKQRISLARATYQNLDIY 782
Cdd:COG1129 348 RENITlasldrlsrGGLLDRRRERALAEEYIKRLriktPSPE-------QPVG----NLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 783 LLDDPLSAVDahVG-KH-IFNKVlgpNGLLK-GKTRLLVTHSmhfLPQV----DEIVVLGNGTIV 840
Cdd:COG1129 417 ILDEPTRGID--VGaKAeIYRLI---RELAAeGKAVIVISSE---LPELlglsDRILVMREGRIV 473
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1316-1525 |
1.79e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 57.29 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIglHDLREKLTIIPQDPI-LFSGSLRMN 1394
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLV--RDKDGQLKVADKNQLrLLRTRLTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1395 LDPFNNYSDEEIWKALELAHLKSfvaslqLGLS-HEVTEAG------------------GNLSIGQRQLLCLGRALLRKS 1455
Cdd:PRK10619 98 FQHFNLWSHMTVLENVMEAPIQV------LGLSkQEARERAvkylakvgideraqgkypVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 1456 KILVLDEATAAVDLETDNLIQTTIQnEFAH--CTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1525
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQ-QLAEegKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
649-844 |
1.94e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.98 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 649 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYV--------------------PQQS 708
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFgkdifqidaiklrkevgmvfQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 709 WIQNGTIKDNILFGTE---FNEKR-YQQVLEACallpdleMLPGGDLAEIGEK----GINLSGGQKQRISLARATYQNLD 780
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKshgIKEKReIKKIVEEC-------LRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 781 IYLLDDPLSAVDAhVGKHIFNKVLgpNGLLKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 844
Cdd:PRK14246 174 VLLMDEPTSMIDI-VNSQAIEKLI--TELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGS 235
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1029-1272 |
2.11e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 57.52 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1029 ALGLAQGIFVFIAHFWSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLG 1108
Cdd:cd18564 62 GIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1109 IISTLVMICMATPVFTII---VIPLgiiyvsvqmFYVSTSRQLRRLDSVTR------SPIYSHFSETVSGLPVIRAF--- 1176
Cdd:cd18564 142 LVGMLGVMFWLDWQLALIalaVAPL---------LLLAARRFSRRIKEASReqrrreGALASVAQESLSAIRVVQAFgre 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1177 -EHQQRFLKHNEVRIDTNQKcvfswitSNRwLAIRLELVGNLTVFFSALMMVIY------RDTLS-GDTVGFV--LSNAL 1246
Cdd:cd18564 213 eHEERRFARENRKSLRAGLR-------AAR-LQALLSPVVDVLVAVGTALVLWFgawlvlAGRLTpGDLLVFLayLKNLY 284
|
250 260
....*....|....*....|....*.
gi 1388169353 1247 NITQTlnwLVRMTSEIETNIVAVERI 1272
Cdd:cd18564 285 KPVRD---LAKLTGRIAKASASAERV 307
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1316-1513 |
2.23e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.81 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDI-----ASIglhdLREKLTIIPQDPILFSgs 1390
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdwqtAKI----MREAVAIVPEGRRVFS-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1391 lRM----NLDPFNNYSDEEIWKalelaHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAA 1466
Cdd:PRK11614 94 -RMtveeNLAMGGFFAERDQFQ-----ERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1388169353 1467 VDLETDNLIQTTIQNEFAHCTVITIAHR--LHTIMDSDKVMVLDNGKII 1513
Cdd:PRK11614 168 LAPIIIQQIFDTIEQLREQGMTIFLVEQnaNQALKLADRGYVLENGHVV 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1328-1525 |
2.37e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.71 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1328 EKIGVVGRTGAGKSSLTNCLFRILEAAGGQI-------------IID-------------GVDIASIglhdLREKLTIIp 1381
Cdd:PRK10261 43 ETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIElseqsaaqmrhvrGADMAMI----FQEPMTSL- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1382 qDPILFSG-----SLRMNldpfNNYSDEEiwkalELAHLKSFVASLQLGLSHEV-TEAGGNLSIGQRQLLCLGRALLRKS 1455
Cdd:PRK10261 118 -NPVFTVGeqiaeSIRLH----QGASREE-----AMVEAKRMLDQVRIPEAQTIlSRYPHQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 1456 KILVLDEATAAVDLETDNLIQTTI---QNEFAhCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1525
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIkvlQKEMS-MGVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQIFHAP 260
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1331-1523 |
2.70e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 56.72 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1331 GVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQD-PILFSGSLRM-----------NLDPF 1398
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlPAAEGMTVRElvaigrypwhgALGRF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1399 NNYSDEEIWKALELAHLKSFvaslqlglSHEVTEAggnLSIGQRQLLCLGRALLRKSKILVLDEATAAVDL----ETDNL 1474
Cdd:PRK10575 121 GAADREKVEEAISLVGLKPL--------AHRLVDS---LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIahqvDVLAL 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 1475 IQTTIQNEfaHCTVITIahrLHTI-MDS---DKVMVLDNGKIIECGSPEELLQ 1523
Cdd:PRK10575 190 VHRLSQER--GLTVIAV---LHDInMAArycDYLVALRGGEMIAQGTPAELMR 237
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
1056-1128 |
2.92e-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: 57.14 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1056 LHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQS----LRSWITCFLGI-----IS---TLVMICMATPVF 1123
Cdd:cd18573 76 LRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNlsdgLRSLVSGVGGIgmmlyISpklTLVMLLVVPPIA 155
|
....*
gi 1388169353 1124 TIIVI 1128
Cdd:cd18573 156 VGAVF 160
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1271-1514 |
2.96e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 58.15 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1271 RITEYTKVENEAPWVTDKRP----PPDWPSkGK--IQFNNYQVRY--RPeldlVLRGITCDIGSMEKIGVVGRTGAGKSS 1342
Cdd:COG0488 282 RIKALEKLEREEPPRRDKTVeirfPPPERL-GKkvLELEGLSKSYgdKT----LLDDLSLRIDRGDRIGLIGPNGAGKST 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1343 LTNCLFRILEAAGGQIII-DGVDIA--SIGLHDLREKLTIIpqdpilfsgslrmnldpfnnysdEEIWKALELA---HLK 1416
Cdd:COG0488 357 LLKLLAGELEPDSGTVKLgETVKIGyfDQHQEELDPDKTVL-----------------------DELRDGAPGGteqEVR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1417 SFVASlqLGLS-HEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNeFAHcTVITIAH-R 1494
Cdd:COG0488 414 GYLGR--FLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD-FPG-TVLLVSHdR 489
|
250 260
....*....|....*....|..
gi 1388169353 1495 --LHTImdSDKVMVLDNGKIIE 1514
Cdd:COG0488 490 yfLDRV--ATRILEFEDGGVRE 509
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1056-1272 |
3.50e-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: 56.75 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1056 LHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIV-IPLGIIY 1134
Cdd:cd18563 78 LRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVlIPVPLVV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1135 VSVQMFYVSTSRQLRRLDSVtRSPIYSHFSETVSGLPVIRAF--EH--QQRFLKHNevridtnqkcvfswitsNRWLAIR 1210
Cdd:cd18563 158 WGSYFFWKKIRRLFHRQWRR-WSRLNSVLNDTLPGIRVVKAFgqEKreIKRFDEAN-----------------QELLDAN 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388169353 1211 LELVGNLTVFFSALMMVIY-----------RDTLSGD-TVGFVLSNALNITQ---TLNWLVRMTSEIETNIVAVERI 1272
Cdd:cd18563 220 IRAEKLWATFFPLLTFLTSlgtlivwyfggRQVLSGTmTLGTLVAFLSYLGMfygPLQWLSRLNNWITRALTSAERI 296
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
654-836 |
3.94e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.49 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG------------TTAYVPQQSWI-QNGTIKDNIL 720
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldavrqSLGMCPQHNILfHHLTVAEHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 721 FGTEFNEKRYQQV-LEACALLPDLemlpgGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHI 799
Cdd:TIGR01257 1026 FYAQLKGRSWEEAqLEMEAMLEDT-----GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190
....*....|....*....|....*....|....*..
gi 1388169353 800 FNKVLgpnGLLKGKTRLLVTHSMhflpqvDEIVVLGN 836
Cdd:TIGR01257 1101 WDLLL---KYRSGRTIIMSTHHM------DEADLLGD 1128
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1331-1521 |
4.41e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 57.72 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1331 GVVGRTGAGKSSLTNCLFRILEAAGGQIIIDG--VDIAS--------IGL-------------HDLREKLTIipqdPILF 1387
Cdd:COG1129 282 GIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSprdairagIAYvpedrkgeglvldLSIRENITL----ASLD 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1388 SGSLRMNLDPfnnysdeeiwkALELAHLKSFVASLQL---GLSHEVteagGNLSIGQRQLLCLGRALLRKSKILVLDEAT 1464
Cdd:COG1129 358 RLSRGGLLDR-----------RRERALAEEYIKRLRIktpSPEQPV----GNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1465 AAVDLETDNLIQTTIqNEFAH--CTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEEL 1521
Cdd:COG1129 423 RGIDVGAKAEIYRLI-RELAAegKAVIVISSELPELLGlSDRILVMREGRIVGELDREEA 481
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
643-889 |
4.76e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 56.28 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 643 SFTWEHDSEA-TVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTtAYVPQQSW---------IQN 712
Cdd:PRK13650 11 TFKYKEDQEKyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-LLTEENVWdirhkigmvFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 713 -------GTIKDNILFGTEFNEKRYQQ----VLEAcallpdLEMLPGGDLAEigEKGINLSGGQKQRISLARATYQNLDI 781
Cdd:PRK13650 90 pdnqfvgATVEDDVAFGLENKGIPHEEmkerVNEA------LELVGMQDFKE--REPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 782 YLLDDPLSAVDahvgkhifnkvlgPNGLLK------------GKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALL 849
Cdd:PRK13650 162 IILDEATSMLD-------------PEGRLEliktikgirddyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELF 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1388169353 850 AKKGE---------FAKNLKTFLRHTGPEEEATVHDGSEEEDDDYGLIS 889
Cdd:PRK13650 229 SRGNDllqlgldipFTTSLVQSLRQNGYDLPEGYLTEKELEEQLWELIS 277
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1316-1468 |
5.22e-08 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 55.52 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIID----GVDIASIG---LHDLREK--------LTII 1380
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASpreILALRRRtigyvsqfLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1381 PQDPilfsgslrmnldpfnnysdeeiwkALELahlksfVAS--LQLGLSHEVTEAGG-------NL------------SI 1439
Cdd:COG4778 106 PRVS------------------------ALDV------VAEplLERGVDREEARARArellarlNLperlwdlppatfSG 155
|
170 180
....*....|....*....|....*....
gi 1388169353 1440 GQRQLLCLGRALLRKSKILVLDEATAAVD 1468
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLD 184
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1316-1525 |
5.44e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 56.63 E-value: 5.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLtnclFRI---LEA-AGGQIIIDGVDIAsiGLHDLREKLTIIPQDPILFSgsl 1391
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTL----LRIiagLEHqTSGHIRFHGTDVS--RLHARDRKVGFVFQHYALFR--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1392 RMNLdpFNNysdeeIWKALEL---------AHLKSFVASL--QLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVL 1460
Cdd:PRK10851 88 HMTV--FDN-----IAFGLTVlprrerpnaAAIKAKVTQLleMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 1461 DEATAAVDLETDNLIQTTIQN---EFAHCTVItIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1525
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQlheELKFTSVF-VTHDQEEAMEvADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
664-844 |
5.67e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 57.36 E-value: 5.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 664 GQLVAVIGPVGSGKSSLISAMLGEMEN---VHGHITIKGT----------TAYVPQQS-WIQNGTIKDNILFGTEFNEKR 729
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMpidakemraiSAYVQQDDlFIPTLTVREHLMFQAHLRMPR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 730 Y----QQVLEACALLPDLEMLPGGDLAeIGEKGI--NLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFnKV 803
Cdd:TIGR00955 131 RvtkkEKRERVDEVLQALGLRKCANTR-IGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVV-QV 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1388169353 804 LgpNGL-LKGKTRLLVTH--SMHFLPQVDEIVVLGNGTIVEKGS 844
Cdd:TIGR00955 209 L--KGLaQKGKTIICTIHqpSSELFELFDKIILMAEGRVAYLGS 250
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1300-1525 |
5.71e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 56.18 E-value: 5.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELDLVLRGITcDIGSMEKIG----VVGRTGAGKSSLTNCLFRILEAAGGQIIIdGVDIASIG-----L 1370
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFERRALY-DVNVSIPSGsyvaIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGkknkkL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1371 HDLREKLTIIPQDP--ILFSGSLRMNL--DPFN-NYSDEEiwkALELAHlksfvASLQL-GLSHEV-TEAGGNLSIGQRQ 1443
Cdd:PRK13634 81 KPLRKKVGIVFQFPehQLFEETVEKDIcfGPMNfGVSEED---AKQKAR-----EMIELvGLPEELlARSPFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1444 LLCLGRALLRKSKILVLDEATAAVDLETdnliQTTIQNEFA--H----CTVITIAHRlhtiMD-----SDKVMVLDNGKI 1512
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKG----RKEMMEMFYklHkekgLTTVLVTHS----MEdaaryADQIVVMHKGTV 224
|
250
....*....|...
gi 1388169353 1513 IECGSPEELLQIP 1525
Cdd:PRK13634 225 FLQGTPREIFADP 237
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1032-1272 |
6.94e-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: 55.95 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1032 LAQGIFVFIAHFWsaFGFV--HASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDD----TLPQSLRSWITC 1105
Cdd:cd18576 47 LLQAVFSFFRIYL--FARVgeRVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDtlttTLAEFLRQILTL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1106 FLGIIS--------TLVMICMAtPVFTIIVIPLGiiyvsvqmfyvstsRQLRRL-----DSVTRSpiYSHFSETVSGLPV 1172
Cdd:cd18576 125 IGGVVLlffiswklTLLMLATV-PVVVLVAVLFG--------------RRIRKLskkvqDELAEA--NTIVEETLQGIRV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1173 IRAFEHQQRFLKHNEVRIDTnqkcVFS-WITSNRWLAIRLELVGnlTVFFSALMMVIY-------RDTLS-GDTVGFVLS 1243
Cdd:cd18576 188 VKAFTREDYEIERYRKALER----VVKlALKRARIRALFSSFII--FLLFGAIVAVLWyggrlvlAGELTaGDLVAFLLY 261
|
250 260
....*....|....*....|....*....
gi 1388169353 1244 nALNITQTLNWLVRMTSEIETNIVAVERI 1272
Cdd:cd18576 262 -TLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1332-1541 |
7.58e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 55.78 E-value: 7.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1332 VVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDI-ASIG----LHDLREKLTIIPQDP--ILFSGSLRMNL--DPFNNYS 1402
Cdd:PRK13645 42 VIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKkikeVKRLRKEIGLVFQFPeyQLFQETIEKDIafGPVNLGE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1403 D-EEIWKAL-ELAHLKSfvaslqlgLSHE-VTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDL--ETD--NLI 1475
Cdd:PRK13645 122 NkQEAYKKVpELLKLVQ--------LPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPkgEEDfiNLF 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1476 QTTIQNEFAHctVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEEL---------LQIPGP----FYFMAKEAGIENVN 1541
Cdd:PRK13645 194 ERLNKEYKKR--IIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEIfsnqelltkIEIDPPklyqLMYKLKNKGIDLLN 271
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1289-1514 |
7.96e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.90 E-value: 7.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1289 RPPPDWPskgKIQFNNYQVRYrPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASI 1368
Cdd:PRK10522 315 QAFPDWQ---TLELRNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1369 GLHDLREKLTIIPQDPILFSgslRMnLDPFNNYSDEEI---WkaleLAHLKsfvaslqlgLSHEVTEAGG-----NLSIG 1440
Cdd:PRK10522 391 QPEDYRKLFSAVFTDFHLFD---QL-LGPEGKPANPALvekW----LERLK---------MAHKLELEDGrisnlKLSKG 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1441 QRQLLCLGRALLRKSKILVLDEATAAVD--------LETDNLIQTTIQnefahcTVITIAHRLHTIMDSDKVMVLDNGKI 1512
Cdd:PRK10522 454 QKKRLALLLALAEERDILLLDEWAADQDphfrrefyQVLLPLLQEMGK------TIFAISHDDHYFIHADRLLEMRNGQL 527
|
..
gi 1388169353 1513 IE 1514
Cdd:PRK10522 528 SE 529
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1056-1272 |
9.48e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 55.57 E-value: 9.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1056 LHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDI----STVDDTLPQSLRSWITcflgIISTLV-MICMATP--VFTIIVI 1128
Cdd:cd18550 74 LRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVggaqSVVTGTLTSVVSNVVT----LVATLVaMLALDWRlaLLSLVLL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1129 PLGII---YVSvQMFYVSTSRQLRRLDSVTrspiySHFSET--VSGLPVIRAF----EHQQRFLKHNEVRIDtnqkcvfs 1199
Cdd:cd18550 150 PLFVLptrRVG-RRRRKLTREQQEKLAELN-----SIMQETlsVSGALLVKLFgredDEAARFARRSRELRD-------- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1200 witsnrwLAIRLELVG-----NLTVFFSALMMVIY--------RDTLS-GDTVGFVlsnAL--NITQTLNWLVRMTSEIE 1263
Cdd:cd18550 216 -------LGVRQALAGrwffaALGLFTAIGPALVYwvggllviGGGLTiGTLVAFT---ALlgRLYGPLTQLLNIQVDLM 285
|
....*....
gi 1388169353 1264 TNIVAVERI 1272
Cdd:cd18550 286 TSLALFERI 294
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1325-1545 |
9.51e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.88 E-value: 9.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1325 GSMekIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIA--SIGLHDLreklTIIPQDPILFSG---------SLRM 1393
Cdd:PRK11432 32 GTM--VTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVThrSIQQRDI----CMVFQSYALFPHmslgenvgyGLKM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1394 NldpfnNYSDEEIWK----ALELAHLKSFVASLqlglsheVTEAGGnlsiGQRQLLCLGRALLRKSKILVLDEATAAVDL 1469
Cdd:PRK11432 106 L-----GVPKEERKQrvkeALELVDLAGFEDRY-------VDQISG----GQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1470 ETDNLIQTTI---QNEFAhctvITIAHRLHTIMD----SDKVMVLDNGKIIECGSPEELLQIPGPFyFMAKEAGIENVNS 1542
Cdd:PRK11432 170 NLRRSMREKIrelQQQFN----ITSLYVTHDQSEafavSDTVIVMNKGKIMQIGSPQELYRQPASR-FMASFMGDANIFP 244
|
...
gi 1388169353 1543 TKF 1545
Cdd:PRK11432 245 ATL 247
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1302-1521 |
9.52e-08 |
|
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: 55.25 E-value: 9.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1302 FNNYQVRYRPeldlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGvdiasiglhdlreKLTIIP 1381
Cdd:cd03291 42 FSNLCLVGAP----VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1382 QDPILFSGSLRMNLdPFNNYSDEEIWKALELA-HLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVL 1460
Cdd:cd03291 105 QFSWIMPGTIKENI-IFGVSYDEYRYKSVVKAcQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 1461 DEATAAVDLETDNLI-QTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEEL 1521
Cdd:cd03291 184 DSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1299-1521 |
1.21e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 55.17 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1299 KIQFNNYQVRYR---PELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIG----LH 1371
Cdd:PRK13646 2 TIRFDNVSYTYQkgtPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1372 DLREKLTIIPQDP------------ILFS-GSLRMNLDPFNNYsdeeiwkalelahlkSFVASLQLGLSHEVTEAGG-NL 1437
Cdd:PRK13646 82 PVRKRIGMVFQFPesqlfedtvereIIFGpKNFKMNLDEVKNY---------------AHRLLMDLGFSRDVMSQSPfQM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1438 SIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTI------QNEfahcTVITIAHRLHTIMD-SDKVMVLDNG 1510
Cdd:PRK13646 147 SGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLkslqtdENK----TIILVSHDMNEVARyADEVIVMKEG 222
|
250
....*....|.
gi 1388169353 1511 KIIECGSPEEL 1521
Cdd:PRK13646 223 SIVSQTSPKEL 233
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1316-1523 |
1.27e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 54.26 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHdLREKLTI--IPQDPILFSG-SLR 1392
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMH-KRARLGIgyLPQEASIFRKlTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1393 MNldpfnnysdeeIWKALELAHL-----KSFVASL--QLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATA 1465
Cdd:COG1137 97 DN-----------ILAVLELRKLskkerEERLEELleEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 1466 AVD----LEtdnliqttIQNEFAHCT------VITiAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQ 1523
Cdd:COG1137 166 GVDpiavAD--------IQKIIRHLKergigvLIT-DHNVRETLGiCDRAYIISEGKVLAEGTPEEILN 225
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
656-792 |
1.33e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 55.65 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-----------------AYVPQQSWI-QNGTIKD 717
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgiclppekrriGYVFQDARLfPHYKVRG 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 718 NILFG-TEFNEKRYQQVLEACALLPDLEMLPggdlaeigekgINLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 792
Cdd:PRK11144 96 NLRYGmAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1313-1520 |
1.65e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 55.27 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1313 LDLVLRGITcdigsmekiGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDG---VDIAS-IGLHDLREKLTIIPQDPILF- 1387
Cdd:PRK11144 19 LTLPAQGIT---------AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgICLPPEKRRIGYVFQDARLFp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1388 ----SGSLRMNLDPFNNysdeeiwkalelAHLKSFVAslQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEA 1463
Cdd:PRK11144 90 hykvRGNLRYGMAKSMV------------AQFDKIVA--LLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 1464 TAAVDL----ETDNLIQTTIQNefAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEE 1520
Cdd:PRK11144 156 LASLDLprkrELLPYLERLARE--INIPILYVSHSLDEILRlADRVVVLEQGKVKAFGPLEE 215
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
661-790 |
1.75e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 661 IMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQqsWI---QNGTIKDNILF-GTEFNEKRYQQvlea 736
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQ--YIkpdYDGTVEDLLRSiTDDLGSSYYKS---- 435
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 737 callpdlEMLPGGDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPlSA 790
Cdd:PRK13409 436 -------EIIKPLQLERLLDKNVKdLSGGELQRVAIAACLSRDADLYLLDEP-SA 482
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
645-862 |
2.10e-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: 55.58 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 645 TWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLG--EMENVHG----HITIKGTTAYVPQQS---------- 708
Cdd:TIGR03269 7 TKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGriiyHVALCEKCGYVERPSkvgepcpvcg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 709 ----------WIQNGTIKDN------ILFGTEF----NEKRYQQVLEAcalLPDLE------MLPGGDLAE-------IG 755
Cdd:TIGR03269 87 gtlepeevdfWNLSDKLRRRirkriaIMLQRTFalygDDTVLDNVLEA---LEEIGyegkeaVGRAVDLIEmvqlshrIT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 756 EKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLgpNGLLKGKTRLLVTHsmHFlPQV-----DE 830
Cdd:TIGR03269 164 HIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALE--EAVKASGISMVLTS--HW-PEViedlsDK 238
|
250 260 270
....*....|....*....|....*....|..
gi 1388169353 831 IVVLGNGTIVEKGSYSALLAKKGEFAKNLKTF 862
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEVVAVFMEGVSEVEKE 270
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
655-794 |
2.25e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.88 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT------AYVPQQSWI--QNGtIKD------NIL 720
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPirrqrdEYHQDLLYLghQPG-IKTeltaleNLR 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388169353 721 F----GTEFNEKRYQQVLEACALLpDLEMLPGGdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAH 794
Cdd:PRK13538 97 FyqrlHGPGDDEALWEALAQVGLA-GFEDVPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
657-844 |
2.30e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.44 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 657 VNLDIMAGQLVAVIGPVGSGKSSLISAML-------GEMEnVHGHITIKGTTA-------Y-VPQQSWI-QNGTIKDNIL 720
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAgivppdsGTLE-IGGNPCARLTPAkahqlgiYlVPQEPLLfPNLSVKENIL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 721 FG---TEFNEKRYQQVLEA--CALlpDLEMLPGgdLAEIGEkginlsggqKQRISLARATYQNLDIYLLDDPLSAVDAHV 795
Cdd:PRK15439 109 FGlpkRQASMQKMKQLLAAlgCQL--DLDSSAG--SLEVAD---------RQIVEILRGLMRDSRILILDEPTASLTPAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 796 GKHIFNKVlgpNGLL-KGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 844
Cdd:PRK15439 176 TERLFSRI---RELLaQGVGIVFISHKLPEIRQLaDRISVMRDGTIALSGK 223
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
643-844 |
2.64e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.84 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 643 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG--TTAYVPQQS------WIQNGT 714
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehIQHYASKEVarriglLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 715 IKDNILFGTEFNEKRY-QQVLEACALLPDLEMLPGG----DLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPL 788
Cdd:PRK10253 92 TPGDITVQELVARGRYpHQPLFTRWRKEDEEAVTKAmqatGITHLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1388169353 789 SAVDahVGKHI-FNKVLGPNGLLKGKTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGS 844
Cdd:PRK10253 172 TWLD--ISHQIdLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGA 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1315-1513 |
3.28e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 54.83 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1315 LVLRGITCDIGSM-------------EKIGVVGRTGAGKSSLTNCLFRILEAAG--GQIIIDGVDIASIGLHDLREK-LT 1378
Cdd:TIGR02633 2 LEMKGIVKTFGGVkaldgidlevrpgECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAgIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1379 IIPQDPILFSgslrmNLDPFNNysdeeIWKALELAH-------------LKSFVASLQLGLSHeVTEAGGNLSIGQRQLL 1445
Cdd:TIGR02633 82 IIHQELTLVP-----ELSVAEN-----IFLGNEITLpggrmaynamylrAKNLLRELQLDADN-VTRPVGDYGGGQQQLV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1446 CLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAH-CTVITIAHRLHTIMD-SDKVMVLDNGKII 1513
Cdd:TIGR02633 151 EIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHgVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1315-1525 |
3.45e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 53.25 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1315 LVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILE-----AAGGQIIIDGVDI--ASIGLHDLREKLTIIPQDPILF 1387
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1388 SGSLRMNLD---PFNNYS---DEEIWKALELAHLKSFVASlqlglshEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLD 1461
Cdd:PRK14243 104 PKSIYDNIAygaRINGYKgdmDELVERSLRQAALWDEVKD-------KLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388169353 1462 EATAAVD----LETDNLIQTTIQNEfahcTVITIAHRLHTIMD-SDKVMVLD---------NGKIIECGSPEELLQIP 1525
Cdd:PRK14243 177 EPCSALDpistLRIEELMHELKEQY----TIIIVTHNMQQAARvSDMTAFFNveltegggrYGYLVEFDRTEKIFNSP 250
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1024-1242 |
4.00e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 53.69 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1024 VGVYGALGLAQGIFVFIAHFwSAFGFVHAsniLHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWI 1103
Cdd:cd18778 47 LGAYLLRALLNFLRIYLNHV-AEQKVVAD---LRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1104 TCFLGIISTLVMICMATPVFTIIV-IPLGIIYVSVqMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQ-- 1180
Cdd:cd18778 123 TNVLTLVGVAIILFSINPKLALLTlIPIPFLALGA-WLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEee 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 1181 --RFLKHNEVRIDTNQKCVFSWitsnrwlairlELVGNLTVFFSALMMVI---------YRDTLS-GDTVGFVL 1242
Cdd:cd18778 202 akRFEALSRRYRKAQLRAMKLW-----------AIFHPLMEFLTSLGTVLvlgfggrlvLAGELTiGDLVAFLL 264
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
655-792 |
4.34e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.75 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--------------TAYVPQqswiqnG------- 713
Cdd:NF033858 18 DDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGdmadarhrravcprIAYMPQ------Glgknlyp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 714 --TIKDNI-----LFG---TEfNEKRYQQVLEACALLPDLEMlPGGdlaeigekgiNLSGGQKQRISLARATYQNLDIYL 783
Cdd:NF033858 92 tlSVFENLdffgrLFGqdaAE-RRRRIDELLRATGLAPFADR-PAG----------KLSGGMKQKLGLCCALIHDPDLLI 159
|
....*....
gi 1388169353 784 LDDPLSAVD 792
Cdd:NF033858 160 LDEPTTGVD 168
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
645-793 |
5.03e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 53.69 E-value: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 645 TWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISaMLGEMENV-HGHITIKGTT-----------AYV-------P 705
Cdd:PRK11650 12 SYDGKTQV-IKGIDLDVADGEFIVLVGPSGCGKSTLLR-MVAGLERItSGEIWIGGRVvnelepadrdiAMVfqnyalyP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 706 QQSWIQN--------GTIKDNIlfgtefnEKRyqqVLEACALLpdlemlpggdlaEIGE----KGINLSGGQKQRISLAR 773
Cdd:PRK11650 90 HMSVRENmayglkirGMPKAEI-------EER---VAEAARIL------------ELEPlldrKPRELSGGQRQRVAMGR 147
|
170 180
....*....|....*....|
gi 1388169353 774 ATYQNLDIYLLDDPLSAVDA 793
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDA 167
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1332-1522 |
5.41e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.68 E-value: 5.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1332 VVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNLDPFNNYSDEEI---W- 1407
Cdd:PRK10253 38 IIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQELVARGRYPHQPLftrWr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1408 KALELAHLKSFVASlqlGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDL--ETDNLIQTTIQNEFAH 1485
Cdd:PRK10253 118 KEDEEAVTKAMQAT---GITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIshQIDLLELLSELNREKG 194
|
170 180 190
....*....|....*....|....*....|....*...
gi 1388169353 1486 CTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELL 1522
Cdd:PRK10253 195 YTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
1024-1195 |
5.46e-07 |
|
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: 53.18 E-value: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1024 VGVYGALGLAQGIFVFiahFWSAFGFVHASNI---LHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLR 1100
Cdd:cd18541 43 ALLILLLALLIGIFRF---LWRYLIFGASRRIeydLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGIL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1101 SWI-TCFLGIISTLVMICMaTPVFTII------VIPLGIIYVSVQMFYVSTSRQ--LRRLDSVTRspiyshfsETVSGLP 1171
Cdd:cd18541 120 YLVdALFLGVLVLVMMFTI-SPKLTLIallplpLLALLVYRLGKKIHKRFRKVQeaFSDLSDRVQ--------ESFSGIR 190
|
170 180
....*....|....*....|....*...
gi 1388169353 1172 VIRAF----EHQQRFLKHNEVRIDTNQK 1195
Cdd:cd18541 191 VIKAFvqeeAEIERFDKLNEEYVEKNLR 218
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
654-844 |
5.73e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 52.62 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAML---------GEMENVHGHITIKGTTAY----VPQQSWIQNGT------ 714
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLypalarrlhLKKEQPGNHDRIEGLEHIdkviVIDQSPIGRTPrsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 715 ---IKDNI--LF-----GTEFN----EKRYQ-----QVL-----EACALLPD-------LEMLP--GGDLAEIGEKGINL 761
Cdd:cd03271 91 ytgVFDEIreLFcevckGKRYNretlEVRYKgksiaDVLdmtveEALEFFENipkiarkLQTLCdvGLGYIKLGQPATTL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 762 SGGQKQRISLA-----RATYQNLdiYLLDDPLSAVDAHVGKHIFNkVLgpNGLL-KGKTRLLVTHSMHFLPQVDEIVVLG 835
Cdd:cd03271 171 SGGEAQRIKLAkelskRSTGKTL--YILDEPTTGLHFHDVKKLLE-VL--QRLVdKGNTVVVIEHNLDVIKCADWIIDLG 245
|
250
....*....|....*
gi 1388169353 836 ------NGTIVEKGS 844
Cdd:cd03271 246 peggdgGGQVVASGT 260
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1007-1229 |
5.79e-07 |
|
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: 53.25 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1007 SKIFNS-TDYPASQRD---------MRVGVYGALGLAQGIFVFIAHF-WSAFGFVHASNIlHKQLLNNILRAPMRFFDTT 1075
Cdd:cd18577 23 GDLFDAfTDFGSGESSpdeflddvnKYALYFVYLGIGSFVLSYIQTAcWTITGERQARRI-RKRYLKALLRQDIAWFDKN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1076 PTGRIVNRFAGDISTVDD-------TLPQSLRSWITCFlgIIS-------TLVMICMaTPVftiIVIPLGIiyvsvqMFY 1141
Cdd:cd18577 102 GAGELTSRLTSDTNLIQDgigeklgLLIQSLSTFIAGF--IIAfiyswklTLVLLAT-LPL---IAIVGGI------MGK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1142 VSTSRQLRRLDSVTRSpiYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKcvfswitsnrwLAIRLELVgnLTVFF 1221
Cdd:cd18577 170 LLSKYTKKEQEAYAKA--GSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARK-----------AGIKKGLV--SGLGL 234
|
....*...
gi 1388169353 1222 SALMMVIY 1229
Cdd:cd18577 235 GLLFFIIF 242
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
1009-1176 |
5.83e-07 |
|
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: 53.19 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1009 IFNSTDYPASQRDMRVGVygALGLAQGIFVFI---AHFWSAFgFVH--ASNILH---KQLLNNILRAPMRFFDTTPTGRI 1080
Cdd:cd18554 29 VIQGSSLTLDEKVYKLFT--IIGIMFFIFLILrppVEYYRQY-FAQwiANKILYdirKDLFDHLQKLSLRYYANNRSGEI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1081 VNRFAGDISTVDDTLPQSL-RSWITCFLGIISTLVMiCMATPVFTIIVIPLGIIYVSVQMFYVSTSRQLRRLDSVTRSPI 1159
Cdd:cd18554 106 ISRVINDVEQTKDFITTGLmNIWLDMITIIIAICIM-LVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEV 184
|
170
....*....|....*..
gi 1388169353 1160 YSHFSETVSGLPVIRAF 1176
Cdd:cd18554 185 QGFLHERIQGMSVIKSF 201
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1321-1522 |
6.35e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 52.24 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1321 TCDIGsmEKIGVVGRTGAGKSSLTNCLFRILEAAGgQIIIDGVDIASIGLHDL-REKLTIIPQDPILFSgslrMnldpfn 1399
Cdd:PRK03695 18 EVRAG--EILHLVGPNGAGKSTLLARMAGLLPGSG-SIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFA----M------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1400 nysdeEIWKALEL-----------AHLKSFVASLqLGLSHEVTEAGGNLSIGQRQLLCLGRALLR-------KSKILVLD 1461
Cdd:PRK03695 85 -----PVFQYLTLhqpdktrteavASALNEVAEA-LGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 1462 EATAAVDLETDNLIQTTIqNEFAHC--TVITIAHRL-HTIMDSDKVMVLDNGKIIECGSPEELL 1522
Cdd:PRK03695 159 EPMNSLDVAQQAALDRLL-SELCQQgiAVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
651-851 |
6.62e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 53.04 E-value: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 651 EATVR---DVNLDIMAGQLVAVIGPVGSGKSSLiSAMLGEMEN-VHGHITIKGTTAYVPQQSWIQNGTIKDNILFGTEFN 726
Cdd:PRK11308 25 ERLVKaldGVSFTLERGKTLAVVGESGCGKSTL-ARLLTMIETpTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNPYG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 727 ----EKRYQQVLEAcALLPD------------LEMLpggdlAEIGEKGIN-------LSGGQKQRISLARATYQNLDIYL 783
Cdd:PRK11308 104 slnpRKKVGQILEE-PLLINtslsaaerrekaLAMM-----AKVGLRPEHydryphmFSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 784 LDDPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLAK 851
Cdd:PRK11308 178 ADEPVSALDVSVQAQVLN-------LMMdlqqelGLSYVFISHDLSVVEHIaDEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
654-848 |
7.59e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 53.71 E-value: 7.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------TTAYVPQQSWIQ------------NGT 714
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqridtlsPGKLQALRRDIQfifqdpyasldpRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 715 IKDNI--------LFGTEFNEKRYQQVLEACALLPDLEM-LPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLD 785
Cdd:PRK10261 420 VGDSImeplrvhgLLPGKAAAARVAWLLERVGLLPEHAWrYPH-----------EFSGGQRQRICIARALALNPKVIIAD 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 786 DPLSAVDAHVGKHIFNKVLGPNGLLkGKTRLLVTHSMHFLPQVD-EIVVLGNGTIVEKGSYSAL 848
Cdd:PRK10261 489 EAVSALDVSIRGQIINLLLDLQRDF-GIAYLFISHDMAVVERIShRVAVMYLGQIVEIGPRRAV 551
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1316-1486 |
7.60e-07 |
|
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: 51.34 E-value: 7.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNL 1395
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1396 D---PFNnySDEEIWKALELAHLKsfvaslqlGLSHEvteAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETD 1472
Cdd:cd03231 95 RfwhADH--SDEQVEEALARVGLN--------GFEDR---PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170
....*....|....
gi 1388169353 1473 NLIQTTIQnefAHC 1486
Cdd:cd03231 162 ARFAEAMA---GHC 172
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1318-1525 |
7.74e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 53.11 E-value: 7.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1318 RGITCDIGSMEKIGVVGRTGAGKSSLTNClfrileaaggqiiidgvdIAsiGLHDlrekltIIPQDpiLFSGSLRMNLDP 1397
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRM------------------IA--GLED------ITSGD--LFIGEKRMNDVP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1398 ---------FNNYSdeeIWKALELAHLKSF------------------VAS-LQLGlsHEVTEAGGNLSIGQRQLLCLGR 1449
Cdd:PRK11000 72 paergvgmvFQSYA---LYPHLSVAENMSFglklagakkeeinqrvnqVAEvLQLA--HLLDRKPKALSGGQRQRVAIGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 1450 ALLRKSKILVLDEATAAVD--LETDNLIQTTIQNEFAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1525
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLDaaLRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTlADKIVVLDAGRVAQVGKPLELYHYP 225
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
645-828 |
8.01e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.77 E-value: 8.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 645 TWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWI-----------QNG 713
Cdd:PRK13543 18 AFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFmaylghlpglkADL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 714 TIKDNILFGTEFNEKRYQQvleacallpdlemLPGGDLAEIGEKGI------NLSGGQKQRISLARATYQNLDIYLLDDP 787
Cdd:PRK13543 98 STLENLHFLCGLHGRRAKQ-------------MPGSALAIVGLAGYedtlvrQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1388169353 788 LSAVDAHvGKHIFNKVLGPNgLLKGKTRLLVTHSMHFLPQV 828
Cdd:PRK13543 165 YANLDLE-GITLVNRMISAH-LRGGGAALVTTHGAYAAPPV 203
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1332-1521 |
8.53e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 52.93 E-value: 8.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1332 VVGRTGAGKSSLTNCLFRILEAAGGQIIIDgvDIAsIGLHDLREKLTIIP-QDPILFSGSLRMNLDPFNNYSDEEIWK-- 1408
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVG--DIY-IGDKKNNHELITNPySKKIKNFKELRRRVSMVFQFPEYQLFKdt 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1409 ----------AL----ELAHLKSFVASLQLGLSHEVTEAGG-NLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDN 1473
Cdd:PRK13631 134 iekdimfgpvALgvkkSEAKKLAKFYLNKMGLDDSYLERSPfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEH 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1474 LIQTTIQNEFAHC-TVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEEL 1521
Cdd:PRK13631 214 EMMQLILDAKANNkTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEI 263
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
656-844 |
9.74e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 52.55 E-value: 9.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIK----------GTTAYVPQQSWIQN------------- 712
Cdd:PRK13631 44 NISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkknnHELITNPYSKKIKNfkelrrrvsmvfq 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 713 --------GTIKDNILFG-------TEFNEKRYQQVLEACALLPD-LEMLPGGdlaeigekginLSGGQKQRISLARATY 776
Cdd:PRK13631 124 fpeyqlfkDTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSyLERSPFG-----------LSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 777 QNLDIYLLDDPLSAVDAHVGKHIFNKVLGPNGllKGKTRLLVTHSM-HFLPQVDEIVVLGNGTIVEKGS 844
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKA--NNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGT 259
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
657-792 |
1.03e-06 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 51.76 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 657 VNLDIMAGQLVAVIGPVGSGKSSLISAMLGeMENVHGHITIKGTT-------------AYVPQQS----------WIQng 713
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPlsdwsaaelarhrAYLSQQQsppfampvfqYLA-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 714 tikdniLFG-----TEFNEKRYQQVLEACALLPDLemlpggdlaeigEKGIN-LSGGQKQRISLARATYQ-----NLD-- 780
Cdd:COG4138 92 ------LHQpagasSEAVEQLLAQLAEALGLEDKL------------SRPLTqLSGGEWQRVRLAAVLLQvwptiNPEgq 153
|
170
....*....|..
gi 1388169353 781 IYLLDDPLSAVD 792
Cdd:COG4138 154 LLLLDEPMNSLD 165
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
1024-1189 |
1.13e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 52.16 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1024 VGVYGALGLAQGIFVFIAHFWSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWI 1103
Cdd:cd18572 39 VLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1104 TCFLGIISTLVMICMATPVFT----IIVIPLGIIYVSVQMFYVSTSRQLRrlDSVTRSpiYSHFSETVSGLPVIRAF--- 1176
Cdd:cd18572 119 RNLVQLVGGLAFMFSLSWRLTllafITVPVIALITKVYGRYYRKLSKEIQ--DALAEA--NQVAEEALSNIRTVRSFate 194
|
170 180
....*....|....*....|.
gi 1388169353 1177 --------EHQQRFLKHNEVR 1189
Cdd:cd18572 195 erearryeRALDKALKLSVRQ 215
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1317-1523 |
1.14e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 52.05 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1317 LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIG----LHDLREKLTIIPQDP--ILFSGS 1390
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQIRKKVGLVFQFPesQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1391 LRMNL--DPFN-NYSDEEiwkALELAHLKsfvasLQL-GLSHEVTEAGG-NLSIGQRQLLCLGRALLRKSKILVLDEATA 1465
Cdd:PRK13649 103 VLKDVafGPQNfGVSQEE---AEALAREK-----LALvGISESLFEKNPfELSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 1466 AVDLETDNLIQTTIQNefAHCTVITIAHRLHtIMD-----SDKVMVLDNGKIIECGSPEELLQ 1523
Cdd:PRK13649 175 GLDPKGRKELMTLFKK--LHQSGMTIVLVTH-LMDdvanyADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1300-1522 |
1.24e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 51.66 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYRPELDlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTI 1379
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1380 IPQDP--ILFS---------GSLRMNLDPfnNYSDEEIWKALELAHLKSFvaslqlglsheVTEAGGNLSIGQRQLLCLG 1448
Cdd:PRK13647 84 VFQDPddQVFSstvwddvafGPVNMGLDK--DEVERRVEEALKAVRMWDF-----------RDKPPYHLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388169353 1449 RALLRKSKILVLDEATAAVDLETDNLIqTTIQNEF--AHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELL 1522
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETL-MEILDRLhnQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLT 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
663-849 |
1.25e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 51.71 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 663 AGQLVAVIGPVGSGKSSLISaMLGEMEN-VHGHITIKGTT-------------AYVPQQSWIQNG-TIKDNILFGT---- 723
Cdd:PRK10575 36 AGKVTGLIGHNGSGKSTLLK-MLGRHQPpSEGEILLDAQPleswsskafarkvAYLPQQLPAAEGmTVRELVAIGRypwh 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 724 ----EFNEKRYQQVLEACALLpdlemlpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVD-AHVgk 797
Cdd:PRK10575 115 galgRFGAADREKVEEAISLV---------GLKPLAHRLVDsLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiAHQ-- 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 798 hifNKVLGPNGLL---KGKTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGSYSALL 849
Cdd:PRK10575 184 ---VDVLALVHRLsqeRGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELM 236
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1316-1540 |
1.46e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 52.26 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDlREKLTIIpQDPILF-------- 1387
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN-RHVNTVF-QSYALFphmtvfen 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1388 -SGSLRMNLDPFnnysdEEIWK----ALELAHLKSFVaslqlglSHEVTeaggNLSIGQRQLLCLGRALLRKSKILVLDE 1462
Cdd:PRK09452 107 vAFGLRMQKTPA-----AEITPrvmeALRMVQLEEFA-------QRKPH----QLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1463 ATAAVDLEtdnlIQTTIQNEFAH------CTVITIAH-RLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFyFMAKEA 1535
Cdd:PRK09452 171 SLSALDYK----LRKQMQNELKAlqrklgITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNL-FVARFI 245
|
....*
gi 1388169353 1536 GIENV 1540
Cdd:PRK09452 246 GEINI 250
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
979-1185 |
1.80e-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: 51.36 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 979 IFFIILAFVMNSVAFIGSnlWLSAWTSDSKIFnstdyPASQRDMRVGVYGALG--LAQGIFVFIAHFWSAfgfvHASNIL 1056
Cdd:cd18555 5 ISILLLSLLLQLLTLLIP--ILTQYVIDNVIV-----PGNLNLLNVLGIGILIlfLLYGLFSFLRGYIII----KLQTKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1057 HKQLLNN----ILRAPMRFFDTTPTGRIVNRfAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGI 1132
Cdd:cd18555 74 DKSLMSDffehLLKLPYSFFENRSSGDLLFR-ANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 1133 IYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKH 1185
Cdd:cd18555 153 LIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKK 205
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
1022-1242 |
1.99e-06 |
|
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: 51.34 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1022 MRVGVYGALGLAQGIFVF--IAHFWSAFGFVHASNILHKQLLNNI--------LRAPMRFFDTTPTGRIVNRFAGDISTV 1091
Cdd:cd18546 30 VRAGDLGVLLLAAAAYLAvvLAGWVAQRAQTRLTGRTGERLLYDLrlrvfahlQRLSLDFHERETSGRIMTRMTSDIDAL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1092 DDTLPQSLRSWITCFLGIISTLVMIC-----MATPVFTIIVIplgIIYVSVQmFYVSTSRQLRRldsvTR---SPIYSHF 1163
Cdd:cd18546 110 SELLQTGLVQLVVSLLTLVGIAVVLLvldprLALVALAALPP---LALATRW-FRRRSSRAYRR----AReriAAVNADL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1164 SETVSGLPVIRAF----EHQQRFLKHNEVRIDTNqkcvfswITSNRWLAIR---LELVGNLT----VFFSALMMViyRDT 1232
Cdd:cd18546 182 QETLAGIRVVQAFrrerRNAERFAELSDDYRDAR-------LRAQRLVAIYfpgVELLGNLAtaavLLVGAWRVA--AGT 252
|
250
....*....|.
gi 1388169353 1233 LS-GDTVGFVL 1242
Cdd:cd18546 253 LTvGVLVAFLL 263
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
649-854 |
2.36e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.56 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 649 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLG--EMENVHGHITIKGT--TAYVPQ-----------QSWIQNG 713
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKdlLELSPEdragegifmafQYPVEIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 714 TIKDNILFGTEFNEKRYQQvleacallpDLEMLPGGDLAEIGEKGINL----------------SGGQKQRISLARATYQ 777
Cdd:PRK09580 92 GVSNQFFLQTALNAVRSYR---------GQEPLDRFDFQDLMEEKIALlkmpedlltrsvnvgfSGGEKKRNDILQMAVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 778 NLDIYLLDDPLSAVDAHVGKHIFNkvlGPNGLLKGK-TRLLVTHSMHFLPQV--DEIVVLGNGTIVEKGSYSalLAKKGE 854
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVAD---GVNSLRDGKrSFIIVTHYQRILDYIkpDYVHVLYQGRIVKSGDFT--LVKQLE 237
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1332-1513 |
2.43e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1332 VVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIA-SIGLHDLREKLTIIPQDpilfsgslrMNLDPFNNYSDEeIW--- 1407
Cdd:PRK10982 29 LMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQE---------LNLVLQRSVMDN-MWlgr 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1408 ---KALELAHLKSFVASL----QLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAV-DLETDNLIQTTI 1479
Cdd:PRK10982 99 yptKGMFVDQDKMYRDTKaifdELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtEKEVNHLFTIIR 178
|
170 180 190
....*....|....*....|....*....|....*
gi 1388169353 1480 QNEFAHCTVITIAHRLHTIMD-SDKVMVLDNGKII 1513
Cdd:PRK10982 179 KLKERGCGIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
325-612 |
2.68e-06 |
|
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: 50.86 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 325 SFLLKLVNDIFTFVSPQLLKLLISF---ASDRDTYLWIGYL---CAILLFTAALIQSFClqcyfqlCFKLGVKVRTAIMA 398
Cdd:cd18548 4 APLFKLLEVLLELLLPTLMADIIDEgiaNGDLSYILRTGLLmllLALLGLIAGILAGYF-------AAKASQGFGRDLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 399 SVYKKALTLSNLARKEYTVGETVNLMSVDAQKLMDVTN-FMHMLWSSVLQIVLSIFFLWR---ELGPSVLAGVGVMVLVI 474
Cdd:cd18548 77 DLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMmLLRMLVRAPIMLIGAIIMAFRinpKLALILLVAIPILALVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 475 pinAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEP----SFRDQVQNLRKKELKNLLAFSQLQCVVIFVF 550
Cdd:cd18548 157 ---FLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDyeeeRFDKANDDLTDTSLKAGRLMALLNPLMMLIM 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 551 QLTpvLVSVVTFSVYvLVDSNNILDAQ-KAFTSItLFNILrFPLSMLPMMISSMLQASVSTER 612
Cdd:cd18548 234 NLA--IVAILWFGGH-LINAGSLQVGDlVAFINY-LMQIL-MSLMMLSMVFVMLPRASASAKR 291
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
660-853 |
3.20e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 49.11 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 660 DIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-AYVPQQswiqngtikdnilfgtefnekryqqvleaca 738
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITpVYKPQY------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 739 llpdlemlpggdlaeigekgINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA----HVGKHIfnKVLGPNGllkGKT 814
Cdd:cd03222 70 --------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAARAI--RRLSEEG---KKT 124
|
170 180 190
....*....|....*....|....*....|....*....
gi 1388169353 815 RLLVTHSMHFLPQVDEIVVLGNGtivEKGSYSALLAKKG 853
Cdd:cd03222 125 ALVVEHDLAVLDYLSDRIHVFEG---EPGVYGIASQPKG 160
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
1054-1180 |
3.22e-06 |
|
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: 50.77 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1054 NI-LHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQS----LRSWITCFlGIISTLVMICMATPVFTIIVI 1128
Cdd:cd18784 68 NIrIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNlnifLRSLVKAI-GVIVFMFKLSWQLSLVTLIGL 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 1129 PLGIIYVSVQ-MFYVSTSRQLRrlDSVTRSPiySHFSETVSGLPVIRAFEHQQ 1180
Cdd:cd18784 147 PLIAIVSKVYgDYYKKLSKAVQ--DSLAKAN--EVAEETISSIRTVRSFANED 195
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
1032-1150 |
4.61e-06 |
|
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: 50.24 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1032 LAQGIFVF--IAhFWSAFGFVHASNiLHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDI----STVDDTLPQSLRSwITC 1105
Cdd:cd18574 53 LLQSLLTFayIS-LLSVVGERVAAR-LRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVqefkSSFKQCVSQGLRS-VTQ 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1388169353 1106 FLGIISTLVMICMATPVFTIIVIPLGIIyvsVQMFYVSTSRQLRR 1150
Cdd:cd18574 130 TVGCVVSLYLISPKLTLLLLVIVPVVVL---VGTLYGSFLRKLSR 171
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1316-1516 |
4.67e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 49.63 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLfRILE-AAGGQIIIDG--------VDIASIGLhdLREKLTIIPQD--- 1383
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVL-NLLEmPRSGTLNIAGnhfdfsktPSDKAIRE--LRRNVGMVFQQynl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1384 -PILfsgSLRMNL--DPFN--NYSDEE-IWKALELA---HLKSFVASLQLglshevteaggNLSIGQRQLLCLGRALLRK 1454
Cdd:PRK11124 94 wPHL---TVQQNLieAPCRvlGLSKDQaLARAEKLLerlRLKPYADRFPL-----------HLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 1455 SKILVLDEATAAVDLETDNLIQTTIQnEFAHcTVIT---------IAHRLHTimdsdKVMVLDNGKIIECG 1516
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIR-ELAE-TGITqvivtheveVARKTAS-----RVVYMENGHIVEQG 223
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
657-841 |
4.80e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 49.39 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 657 VNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAY------------------------VPQQSWIQN 712
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmdeearaklrakhvgfvfqsfmlIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 713 GTIKdNILFGTEFNEKRYQ--QVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSA 790
Cdd:PRK10584 109 VELP-ALLRGESSRQSRNGakALLEQLGLGKRLDHLPA-----------QLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1388169353 791 VDAHVGKHIFNKVLGPNGLLkGKTRLLVTHSMHFLPQVDEIVVLGNGTIVE 841
Cdd:PRK10584 177 LDRQTGDKIADLLFSLNREH-GTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1323-1508 |
5.06e-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: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1323 DIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASiglhdlrEKLTIIPQDPILFSGSLRMNLDPF--NN 1400
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY-------KPQYIKADYEGTVRDLLSSITKDFytHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1401 YSDEEIWKALELAHLksfvaslqlgLSHEVTEaggnLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLEtDNLIQTTIQ 1480
Cdd:cd03237 94 YFKTEIAKPLQIEQI----------LDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE-QRLMASKVI 158
|
170 180 190
....*....|....*....|....*....|..
gi 1388169353 1481 NEFA---HCTVITIAHRLHTI-MDSDKVMVLD 1508
Cdd:cd03237 159 RRFAennEKTAFVVEHDIIMIdYLADRLIVFE 190
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1315-1508 |
6.32e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 48.65 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1315 LVLRGITCDIGSMEKIGVVGRTGAGKSSLtnclFRIL----EAAGGQIIIDGVDIASIGlHDLREKLtiipqdpiLFSG- 1389
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSL----LRILaglaRPDAGEVLWQGEPIRRQR-DEYHQDL--------LYLGh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1390 ------------SLRMNLDPFNNYSDEEIWKALElahlksfvaslQLGLshevteAG------GNLSIGQRQLLCLGRAL 1451
Cdd:PRK13538 82 qpgikteltaleNLRFYQRLHGPGDDEALWEALA-----------QVGL------AGfedvpvRQLSAGQQRRVALARLW 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 1452 LRKSKILVLDEATAAVDLETDNLIQTTIQnefAHC-----TVITIAHRLHtiMDSDKVMVLD 1508
Cdd:PRK13538 145 LTRAPLWILDEPFTAIDKQGVARLEALLA---QHAeqggmVILTTHQDLP--VASDKVRKLR 201
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
660-833 |
6.41e-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: 50.94 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 660 DIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQ-SWIQNGTIKDNI--LFGTEFNEKRYQQvlea 736
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQYiSPDYDGTVEEFLrsANTDDFGSSYYKT---- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 737 callpdlEMLPGGDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA----HVGKHIFNKVLGpngllK 811
Cdd:COG1245 438 -------EIIKPLGLEKLLDKNVkDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAIRRFAEN-----R 505
|
170 180
....*....|....*....|...
gi 1388169353 812 GKTRLLVTHSMHFLPQV-DEIVV 833
Cdd:COG1245 506 GKTAMVVDHDIYLIDYIsDRLMV 528
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
643-844 |
6.89e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 49.42 E-value: 6.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 643 SFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAYVPQQS- 708
Cdd:PRK13652 10 CYSYSGSKEA-LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkenirevrkFVGLVFQNPd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 709 -WIQNGTIKDNILFG-------TEFNEKRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLD 780
Cdd:PRK13652 89 dQIFSPTVEQDIAFGpinlgldEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388169353 781 IYLLDDPLSAVDAHVGKHIFNKVlgpNGLLK--GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 844
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFL---NDLPEtyGMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGT 221
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1317-1521 |
7.17e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 49.24 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1317 LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRIL---EAAGGQIIIDGVDIASIG--LHDLRE---------------- 1375
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGrlARDIRKsrantgyifqqfnlvn 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1376 KLTIIPQDPILFSGSLRMNLDPFNNYSDEEIWKALElahlksfvASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKS 1455
Cdd:PRK09984 100 RLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQ--------ALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 1456 KILVLDEATAAVDLETDNLIQTTIQ--NEFAHCTVITIAHRL-HTIMDSDKVMVLDNGKIIECGSPEEL 1521
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVdYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
637-839 |
7.97e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.63 E-value: 7.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 637 MQFSEASFTWEhDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHI--TIKGTTAyVPQQSWIQNGT 714
Cdd:PLN03073 509 ISFSDASFGYP-GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrSAKVRMA-VFSQHHVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 715 IKDNILFgteFNEKRYQQVLEAC--ALLPDLEMlpGGDLAEigEKGINLSGGQKQRISLARATYQNLDIYLLDDP----- 787
Cdd:PLN03073 587 LSSNPLL---YMMRCFPGVPEQKlrAHLGSFGV--TGNLAL--QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPsnhld 659
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 788 LSAVDAhvgkHIFNKVLGPNGLlkgktrLLVTHSMHFLP-QVDEIVVLGNGTI 839
Cdd:PLN03073 660 LDAVEA----LIQGLVLFQGGV------LMVSHDEHLISgSVDELWVVSEGKV 702
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
325-613 |
8.22e-06 |
|
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: 49.35 E-value: 8.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 325 SFLLKLVNDIFTFVSPQLLKLLIS--FASDRDTYLWIgylCAILLFTAALIQSFC--LQCYF--QLCFKLGVKVRTAIma 398
Cdd:cd18542 4 AILALLLATALNLLIPLLIRRIIDsvIGGGLRELLWL---LALLILGVALLRGVFryLQGYLaeKASQKVAYDLRNDL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 399 svYKKaltLSNLARKEYTVGETVNLMS-----VDAqklmdVTNFMHM----LWSSVLQIVLSIFFL----WRelgpsvLA 465
Cdd:cd18542 79 --YDH---LQRLSFSFHDKARTGDLMSrctsdVDT-----IRRFLAFglveLVRAVLLFIGALIIMfsinWK------LT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 466 GVgvMVLVIPINAILSTK-SKTIQvKNMKNKDKRLKIMN----EILSGIKILKYFAWEPS----FRDQVQNLRKKELKNL 536
Cdd:cd18542 143 LI--SLAIIPFIALFSYVfFKKVR-PAFEEIREQEGELNtvlqENLTGVRVVKAFAREDYeiekFDKENEEYRDLNIKLA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 537 LAFSQLQCVVIFVFQLTPVLVSVV--------TFSVYVLVdsnnildaqkAFTSitLFNILRFPLSMLPMMISSMLQASV 608
Cdd:cd18542 220 KLLAKYWPLMDFLSGLQIVLVLWVggylvingEITLGELV----------AFIS--YLWMLIWPVRQLGRLINDMSRASA 287
|
....*
gi 1388169353 609 STERL 613
Cdd:cd18542 288 SAERI 292
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
1050-1183 |
9.15e-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: 49.38 E-value: 9.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1050 VHASNILHKQLLNNI----LRAPMRFFDTTPTGRIVNRFaGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTI 1125
Cdd:cd18567 67 LYLSTSLNLQWTSNLfrhlLRLPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLAL 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1388169353 1126 IVIPLGIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFL 1183
Cdd:cd18567 146 IVLAAVALYALLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAERE 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1331-1514 |
1.62e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.52 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1331 GVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDI------ASI--GLHDLREKLTIIPQDPI---LFSGSLrmnldP-- 1397
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasttAALaaGVAIIYQELHLVPEMTVaenLYLGQL-----Phk 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1398 --FNNYSDEEIWKALELAHLksfvaslqlGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDL-ETDNL 1474
Cdd:PRK11288 109 ggIVNRRLLNYEAREQLEHL---------GVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSArEIEQL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1388169353 1475 IQtTIQNEFAHCTVIT-IAHRLHTIMD-SDKVMVLDNGKIIE 1514
Cdd:PRK11288 180 FR-VIRELRAEGRVILyVSHRMEEIFAlCDAITVFKDGRYVA 220
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
649-787 |
1.63e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 649 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHI--TIKGTTAYVPQQS------------WI-QNG 713
Cdd:PRK15064 330 DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwSENANIGYYAQDHaydfendltlfdWMsQWR 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 714 TIKDNilfgtefnekryQQVLEACallpdL-EMLPGGDlaEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDP 787
Cdd:PRK15064 410 QEGDD------------EQAVRGT-----LgRLLFSQD--DIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1316-1523 |
1.77e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 48.28 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAG--------GQIIIDGVDIASIGLHDLREKLTIIPQ--DPI 1385
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaaQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1386 L-FSGSLRMNLDPF--------NNYSDEEI-WKALELAHLKSFVAslqlglsHEVTE-AGGNLSIGQ--RQLLCL--GRA 1450
Cdd:PRK13547 96 FaFSAREIVLLGRYpharragaLTHRDGEIaWQALALAGATALVG-------RDVTTlSGGELARVQfaRVLAQLwpPHD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388169353 1451 LLRKSKILVLDEATAAVDLETDN-LIQT--TIQNEFaHCTVITIAHRLH-TIMDSDKVMVLDNGKIIECGSPEELLQ 1523
Cdd:PRK13547 169 AAQPPRYLLLDEPTAALDLAHQHrLLDTvrRLARDW-NLGVLAIVHDPNlAARHADRIAMLADGAIVAHGAPADVLT 244
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
762-850 |
2.10e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.93 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 762 SGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLKG---KTRL---LVTHSMHFLPQV-DEIVVL 834
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILA-------LLKSlqqKHQLaylFISHDLHVVRALcHQVIVL 499
|
90
....*....|....*.
gi 1388169353 835 GNGTIVEKGSYSALLA 850
Cdd:PRK15134 500 RQGEVVEQGDCERVFA 515
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
608-857 |
2.12e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.17 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 608 VSTERLEKYLGGDDLDTSAirhdcnfdKAMqfSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGE 687
Cdd:PRK14271 1 MACERLGGQSGAADVDAAA--------PAM--AAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRM 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 688 MENVHGH-----ITIKGTTAY--------------VPQQSWIQNGTIKDNILFGtefnekryqqvLEACALLPDLEM--L 746
Cdd:PRK14271 71 NDKVSGYrysgdVLLGGRSIFnyrdvlefrrrvgmLFQRPNPFPMSIMDNVLAG-----------VRAHKLVPRKEFrgV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 747 PGGDLAEIG----------EKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRL 816
Cdd:PRK14271 140 AQARLTEVGlwdavkdrlsDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFI---RSLADRLTVI 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1388169353 817 LVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA--KKGEFAK 857
Cdd:PRK14271 217 IVTHNLAQAARIsDRAALFFDGRLVEEGPTEQLFSspKHAETAR 260
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1300-1511 |
2.51e-05 |
|
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: 45.90 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1300 IQFNNYQVRYrpELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDgvdiasiglhdlreklti 1379
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG------------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1380 ipqdpilfsgslrmnldpfnnysdeeiwKALELAHLKsfvaslqlglshevteaggNLSIGQRQLLCLGRALLRKSKILV 1459
Cdd:cd03221 61 ----------------------------STVKIGYFE-------------------QLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 1460 LDEATAAVDLETDNLIQTTIQNEfaHCTVITIAHRlHTIMDS--DKVMVLDNGK 1511
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEY--PGTVILVSHD-RYFLDQvaTKIIELEDGK 144
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
654-838 |
3.34e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.16 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLgemENVHGHITIKGTTAYVPQ--------QSWIQNGtikdnilfgtef 725
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL---YASGKARLISFLPKFSRNklifidqlQFLIDVG------------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 726 nekryqqvleacallpdLEMLPggdlaeIGEKGINLSGGQKQRISLARATYQNLD--IYLLDDPLSAVDAHVGKHIFNKV 803
Cdd:cd03238 76 -----------------LGYLT------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVI 132
|
170 180 190
....*....|....*....|....*....|....*.
gi 1388169353 804 lgpNGLL-KGKTRLLVTHSMHFLPQVDEIVVLGNGT 838
Cdd:cd03238 133 ---KGLIdLGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1056-1224 |
3.52e-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: 47.48 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1056 LHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDI----STVDDTLPQSLRSWITcFLGiisTLVMICMATPVFTIIV---I 1128
Cdd:cd18575 71 LRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTtliqTVVGSSLSIALRNLLL-LIG---GLVMLFITSPKLTLLVllvI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1129 PLGIIYVsvqmfyVSTSRQLRRLDSVTRSPI---YSHFSETVSGLPVIRAFEHQ----QRFLKHNEVRIDTNQK------ 1195
Cdd:cd18575 147 PLVVLPI------ILFGRRVRRLSRASQDRLadlSAFAEETLSAIKTVQAFTREdaerQRFATAVEAAFAAALRrirara 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1388169353 1196 --------CVFSWITSNRWLAIRLELVGNLT-------VFFSAL 1224
Cdd:cd18575 221 lltalvifLVFGAIVFVLWLGAHDVLAGRMSagelsqfVFYAVL 264
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
1024-1182 |
3.72e-05 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 47.48 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1024 VGVYGALGLAQGIFVFIAHFWSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVddtlpqslRSWI 1103
Cdd:cd18543 42 VLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLV--------QRFL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1104 TCFLGIISTLVMICMATPVFTIIVIPLGIIY-VSVQMFYVSTSRQLRRLDSVTRSP------IYSHFSETVSGLPVIRAF 1176
Cdd:cd18543 114 AFGPFLLGNLLTLVVGLVVMLVLSPPLALVAlASLPPLVLVARRFRRRYFPASRRAqdqagdLATVVEESVTGIRVVKAF 193
|
170
....*....|
gi 1388169353 1177 ---EHQ-QRF 1182
Cdd:cd18543 194 greRRElDRF 203
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
656-857 |
3.87e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.35 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQNG-TIKDNI-LFGTEFNEKRyQQV 733
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQlTGIENIeLKGLMMGLTK-EKI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 734 LEacaLLPDLEmlpggDLAEIGeKGIN-----LSGGQKQRISLARATYQNLDIYLLDDPLSavdahVGKHIF-NKVLGPN 807
Cdd:PRK13545 121 KE---IIPEII-----EFADIG-KFIYqpvktYSSGMKSRLGFAISVHINPDILVIDEALS-----VGDQTFtKKCLDKM 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 808 GLLK--GKTRLLVTHSmhfLPQVDEIVV----LGNGTIVEKGSYSALLAKKGEFAK 857
Cdd:PRK13545 187 NEFKeqGKTIFFISHS---LSQVKSFCTkalwLHYGQVKEYGDIKEVVDHYDEFLK 239
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
654-900 |
4.34e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 47.41 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT---------AYVPqqswiqngtikdnilfgte 724
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPldpedrrriGYLP------------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 725 fnEKR--YQQ--VLEACALLPDLEMLPGGD-------------LAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDD 786
Cdd:COG4152 78 --EERglYPKmkVGEQLVYLARLKGLSKAEakrradewlerlgLGDRANKKVeELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 787 PLSAVDAhVGKHIFNKVlgpngLL----KGKTRLLVTHSMHflpQV----DEIVVLGNGTIVEKGSYSALlakKGEFAKN 858
Cdd:COG4152 156 PFSGLDP-VNVELLKDV-----IRelaaKGTTVIFSSHQME---LVeelcDRIVIINKGRKVLSGSVDEI---RRQFGRN 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1388169353 859 lKTFLRHTGPEEEATVHDG--SEEEDDDYGLIssveEIPEDAAS 900
Cdd:COG4152 224 -TLRLEADGDAGWLRALPGvtVVEEDGDGAEL----KLEDGADA 262
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
1056-1272 |
4.59e-05 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); 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: 350033 [Multi-domain] Cd Length: 289 Bit Score: 47.08 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1056 LHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQ--SLRSW-ITCFLGIISTLVMICMATPVFTIIVIPlgI 1132
Cdd:cd18589 71 LQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSEnlSLLMWyLARGLFLFIFMLWLSPKLALLTALGLP--L 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1133 IYV---SVQMFYVSTSRQLRrlDSVTRSPIYShfSETVSGLPVIRAFEHQQRFLKHNEVRIDT----NQK-----CVFSW 1200
Cdd:cd18589 149 LLLvpkFVGKFQQSLAVQVQ--KSLARANQVA--VETFSAMKTVRSFANEEGEAQRYRQRLQKtyrlNKKeaaayAVSMW 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 1201 ITSNRWLAIRlelVGnltVFFSALMMVIYRDTLSGDTVGFVLSNaLNITQTLNWLVRMTSEIETNIVAVERI 1272
Cdd:cd18589 225 TSSFSGLALK---VG---ILYYGGQLVTAGTVSSGDLVTFVLYE-LQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
1058-1176 |
6.44e-05 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 46.66 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1058 KQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPV---FTIIVIPLG--- 1131
Cdd:cd18551 73 RRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVltlVTLAVVPLAfli 152
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1388169353 1132 IIYVSVQMFYVSTSRQlRRLDSVTrspiySHFSETVSGLPVIRAF 1176
Cdd:cd18551 153 ILPLGRRIRKASKRAQ-DALGELS-----AALERALSAIRTVKAS 191
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1308-1523 |
7.04e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 47.35 E-value: 7.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1308 RYRPELDLvLRGITCDIGSMEKIGVVGRTGAGKSSLTNCL-FRILEAA--GGQIIIDGVdiaSIGLHDLREKLTIIPQDP 1384
Cdd:TIGR00955 33 RERPRKHL-LKNVSGVAKPGELLAVMGSSGAGKTTLMNALaFRSPKGVkgSGSVLLNGM---PIDAKEMRAISAYVQQDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1385 IL-----------FSGSLRMnldPFNNYSDEEIWKALELAhlksfvasLQLGLS---HEVTEAGGN---LSIGQRQLLCL 1447
Cdd:TIGR00955 109 LFiptltvrehlmFQAHLRM---PRRVTKKEKRERVDEVL--------QALGLRkcaNTRIGVPGRvkgLSGGERKRLAF 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 1448 GRALLRKSKILVLDEATAAVD-LETDNLIQTTIQNEFAHCTVITIAHR-LHTIMDS-DKVMVLDNGKIIECGSPEELLQ 1523
Cdd:TIGR00955 178 ASELLTDPPLLFCDEPTSGLDsFMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELfDKIILMAEGRVAYLGSPDQAVP 256
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1436-1527 |
1.06e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 46.23 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1436 NLSIGQR---QLLClgrALLRKSKILVLDEATAAVDLETDNLIQTTIQ--NEFAHCTVITIAHRLHTIMD-SDKVMVLDN 1509
Cdd:COG4586 154 QLSLGQRmrcELAA---ALLHRPKILFLDEPTIGLDVVSKEAIREFLKeyNRERGTTILLTSHDMDDIEAlCDRVIVIDH 230
|
90
....*....|....*...
gi 1388169353 1510 GKIIECGSPEELLQIPGP 1527
Cdd:COG4586 231 GRIIYDGSLEELKERFGP 248
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
654-844 |
1.25e-04 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 45.88 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-TAYVPQQSW------IQ----------NG--T 714
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQdITGLSGRELrplrrrMQmvfqdpyaslNPrmT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 715 IKDNILFGTEFN--------EKRYQQVLEACALLPD-LEMLPGgdlaeigEkginLSGGQKQRISLARATYQNLDIYLLD 785
Cdd:COG4608 114 VGDIIAEPLRIHglaskaerRERVAELLELVGLRPEhADRYPH-------E----FSGGQRQRIGIARALALNPKLIVCD 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 786 DPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 844
Cdd:COG4608 183 EPVSALDVSIQAQVLN-------LLEdlqdelGLTYLFISHDLSVVRHIsDRVAVMYLGKIVEIAP 241
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
1029-1228 |
1.26e-04 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 45.85 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1029 ALGLAQGIFVFIAHFWSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLR----SWIT 1104
Cdd:cd18548 47 LLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRmlvrAPIM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1105 CFLGIISTLVM-------ICMATPVFTIIVIplGIIYVSVQMFyvstSRQLRRLDSVTRSpiyshFSETVSGLPVIRAF- 1176
Cdd:cd18548 127 LIGAIIMAFRInpklaliLLVAIPILALVVF--LIMKKAIPLF----KKVQKKLDRLNRV-----VRENLTGIRVIRAFn 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 1177 --EHQ-QRFLKHNEVRIDTNQKcvfswitsnrwlairlelVGNLTVFFSALMMVI 1228
Cdd:cd18548 196 reDYEeERFDKANDDLTDTSLK------------------AGRLMALLNPLMMLI 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1328-1514 |
1.42e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.32 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1328 EKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASiglhdlREKLTIIPQDPILFSGSLRMNlDPFNNYSDEE-- 1405
Cdd:PRK09700 290 EILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP------RSPLDAVKKGMAYITESRRDN-GFFPNFSIAQnm 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1406 -IWKALELAHLKSfvaslQLGLSHEVTEAG--------------------GNLSIGQRQLLCLGRALLRKSKILVLDEAT 1464
Cdd:PRK09700 363 aISRSLKDGGYKG-----AMGLFHEVDEQRtaenqrellalkchsvnqniTELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 1465 AAVDLETDNLIQtTIQNEFAH--CTVITIAHRLHTIMD-SDKVMVLDNGKIIE 1514
Cdd:PRK09700 438 RGIDVGAKAEIY-KVMRQLADdgKVILMVSSELPEIITvCDRIAVFCEGRLTQ 489
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
646-822 |
1.51e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 44.87 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 646 WEHDSEA------TVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG------TTAYVP-------- 705
Cdd:PRK10908 4 FEHVSKAylggrqALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlKNREVPflrrqigm 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 706 ---QQSWIQNGTIKDNILF-------GTEFNEKRYQQVLEACALLPDLEMLPggdlaeigekgINLSGGQKQRISLARAT 775
Cdd:PRK10908 84 ifqDHHLLMDRTVYDNVAIpliiagaSGDDIRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1388169353 776 YQNLDIYLLDDPLSAVDAHVGKHI------FNKVlgpngllkGKTRLLVTHSM 822
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGIlrlfeeFNRV--------GVTVLMATHDI 197
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
1062-1272 |
2.15e-04 |
|
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: 45.24 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1062 NNILRAPMRFFDTTPTGRIVNRFaGDISTVDDTL-PQSLRSWITCFLGIISTLVMICMaTPVFTIIVIPLGIIYVsvqMF 1140
Cdd:cd18568 83 KHLLSLPLSFFASRKVGDIITRF-QENQKIRRFLtRSALTTILDLLMVFIYLGLMFYY-NLQLTLIVLAFIPLYV---LL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1141 YVSTSRQLRRLDS---VTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFS-WITSNRWLAIR--LELV 1214
Cdd:cd18568 158 TLLSSPKLKRNSReifQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRgQKLSIVLQLISslINHL 237
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1215 GNLTVFFSALMMVIYRDTLSGDTVGFvlsNAL--NITQTLNWLVRMTSEIETNIVAVERI 1272
Cdd:cd18568 238 GTIAVLWYGAYLVISGQLTIGQLVAF---NMLfgSVINPLLALVGLWDELQETRISVERL 294
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
754-844 |
2.84e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.77 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 754 IGEKGINLSGGQKQRISLA-----RATYQNLdiYLLDDPLSAVDAHVGKHIFNkVLGpnGLL-KGKTRLLVTHSMHFLPQ 827
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAkelskRSTGRTL--YILDEPTTGLHFDDIKKLLE-VLQ--RLVdKGNTVVVIEHNLDVIKT 897
|
90 100
....*....|....*....|...
gi 1388169353 828 VDEIVVLG------NGTIVEKGS 844
Cdd:TIGR00630 898 ADYIIDLGpeggdgGGTVVASGT 920
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1317-1524 |
3.21e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1317 LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDL-----------REKLTIIPQDPI 1385
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAinhgfalvteeRRSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1386 LFSgSLRMNLDPFNNYsdeeiWKALELAHLKS----FVASLQLGL-SHEVTEagGNLSIGQRQLLCLGRALLRKSKILVL 1460
Cdd:PRK10982 344 GFN-SLISNIRNYKNK-----VGLLDNSRMKSdtqwVIDSMRVKTpGHRTQI--GSLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 1461 DEATAAVDL----ETDNLIQTTIQNEFAhctVITIAHRLHTIMD-SDKVMVLDNGK---IIECG--SPEELLQI 1524
Cdd:PRK10982 416 DEPTRGIDVgakfEIYQLIAELAKKDKG---IIIISSEMPELLGiTDRILVMSNGLvagIVDTKttTQNEILRL 486
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
648-834 |
3.29e-04 |
|
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: 42.73 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 648 HDSEATVRDVNLDimAGQLVAVIGPVGSGKSSLISAM----LGEMENVHGHITIKgTTAYVPQQSwiqngtikdnilfgt 723
Cdd:cd03227 7 FPSYFVPNDVTFG--EGSLTIITGPNGSGKSTILDAIglalGGAQSATRRRSGVK-AGCIVAAVS--------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 724 efnekryqqvLEACALLPdlemlpggdlaeigekgiNLSGGQKQRISLA----RATYQNLDIYLLDDPLSAVDAHVGKHI 799
Cdd:cd03227 69 ----------AELIFTRL------------------QLSGGEKELSALAlilaLASLKPRPLYILDEIDRGLDPRDGQAL 120
|
170 180 190
....*....|....*....|....*....|....*
gi 1388169353 800 FNKVLgpnGLLKGKTRLLVThsMHFLPQVDEIVVL 834
Cdd:cd03227 121 AEAIL---EHLVKGAQVIVI--THLPELAELADKL 150
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
762-858 |
3.65e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 762 SGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVgkhifnkVLG-PNGLLK-GKTRLLVTHSMHFLPQ-VDEIVVLGNGT 838
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA-------VLWlETYLLKwPKTFIVVSHAREFLNTvVTDILHLHGQK 418
|
90 100
....*....|....*....|.
gi 1388169353 839 IVE-KGSYSALLAKKGEFAKN 858
Cdd:PLN03073 419 LVTyKGDYDTFERTREEQLKN 439
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1328-1530 |
4.29e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.10 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1328 EKIGVVGRTGAGKSSL----TNCLFRILEAAGGQIIIDGvdiasIGLHDLREK-----------------LTIipQDPIL 1386
Cdd:TIGR00956 88 ELTVVLGRPGSGCSTLlktiASNTDGFHIGVEGVITYDG-----ITPEEIKKHyrgdvvynaetdvhfphLTV--GETLD 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1387 FSGSLRMNLDPFNNYSDEEIWKalelaHLKSFVASLqLGLSHEVTEAGGN-----LSIGQRQLLCLGRALLRKSKILVLD 1461
Cdd:TIGR00956 161 FAARCKTPQNRPDGVSREEYAK-----HIADVYMAT-YGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWD 234
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388169353 1462 EATAAVD----LETDNLIQTtiQNEFAHCTV-ITIAHRLHTIMDS-DKVMVLDNGKIIECGSPEELLQipgpfYF 1530
Cdd:TIGR00956 235 NATRGLDsataLEFIRALKT--SANILDTTPlVAIYQCSQDAYELfDKVIVLYEGYQIYFGPADKAKQ-----YF 302
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1328-1508 |
4.56e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.80 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1328 EKIGVVGRTGAGKSSLTNCLFRILEAAGGQIiidgvdiasiglhDLREKLTIIPQ----DpilFSGS----LRMNLDPFN 1399
Cdd:PRK13409 366 EVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-------------DPELKISYKPQyikpD---YDGTvedlLRSITDDLG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1400 -NYSDEEIWKALELAHLksfvaslqlgLSHEVTEaggnLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLE----TDNL 1474
Cdd:PRK13409 430 sSYYKSEIIKPLQLERL----------LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlaVAKA 495
|
170 180 190
....*....|....*....|....*....|....*
gi 1388169353 1475 IQTTIQNEFAhcTVITIAHRLHTI-MDSDKVMVLD 1508
Cdd:PRK13409 496 IRRIAEEREA--TALVVDHDIYMIdYISDRLMVFE 528
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1009-1185 |
4.82e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 43.98 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1009 IFNSTDYPASQRDMRV--GVYGALGLAQGIFVFIAHFwsAFGFV--HASNILHKQLLNNILRAPMRFFDTTP--TGRIVN 1082
Cdd:cd18578 38 VFSLPDDDELRSEANFwaLMFLVLAIVAGIAYFLQGY--LFGIAgeRLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1083 RFAGDISTV----DDTLPQSLRSWITCFLG-IIS-------TLVMICMAtPVFtiivipLGIIYVSVQMFYVSTSRQLRR 1150
Cdd:cd18578 116 RLSTDASDVrglvGDRLGLILQAIVTLVAGlIIAfvygwklALVGLATV-PLL------LLAGYLRMRLLSGFEEKNKKA 188
|
170 180 190
....*....|....*....|....*....|....*
gi 1388169353 1151 LDSVTRspiysHFSETVSGLPVIRAFEHQQRFLKH 1185
Cdd:cd18578 189 YEESSK-----IASEAVSNIRTVASLTLEDYFLEK 218
|
|
| PilT |
COG2805 |
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ... |
666-697 |
4.97e-04 |
|
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures];
Pssm-ID: 442056 Cd Length: 342 Bit Score: 44.31 E-value: 4.97e-04
10 20 30
....*....|....*....|....*....|....
gi 1388169353 666 LVAVIGPVGSGKSSLISAMLGEM-ENVHGHI-TI 697
Cdd:COG2805 127 LVLVTGPTGSGKSTTLAAMIDYInETRAKHIiTI 160
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
654-781 |
5.84e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 44.25 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--------------AYVPQ----QSWIQNGTI 715
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDitglsprerrrlgvAYIPEdrlgRGLVPDMSV 353
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388169353 716 KDNILFGTEFNEK-------RYQQVLEACA-LLPDLEMLPGGDLAEIGekgiNLSGGQKQRISLARATYQNLDI 781
Cdd:COG3845 354 AENLILGRYRRPPfsrggflDRKAIRAFAEeLIEEFDVRTPGPDTPAR----SLSGGNQQKVILARELSRDPKL 423
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1317-1512 |
5.85e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 42.94 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1317 LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHD---LREKLTIIPQDPILFsgslrM 1393
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLL-----M 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1394 NLDPFNNYSDEEIWKALELAHLKSFVASL--QLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLET 1471
Cdd:PRK10908 93 DRTVYDNVAIPLIIAGASGDDIRRRVSAAldKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1388169353 1472 DNLIQTTIQnEFAH--CTVITIAHRLHTIMDSD-KVMVLDNGKI 1512
Cdd:PRK10908 173 SEGILRLFE-EFNRvgVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
646-820 |
7.09e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 42.63 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 646 WEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT------------AYVPQQSWIQ-N 712
Cdd:PRK13540 9 FDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSikkdlctyqkqlCFVGHRSGINpY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 713 GTIKDNILFGTEFNEKRYQqVLEACAL--LPDLEMLPGGdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSA 790
Cdd:PRK13540 89 LTLRENCLYDIHFSPGAVG-ITELCRLfsLEHLIDYPCG----------LLSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157
|
170 180 190
....*....|....*....|....*....|
gi 1388169353 791 VDAHVGKHIFNKVLGPNGllKGKTRLLVTH 820
Cdd:PRK13540 158 LDELSLLTIITKIQEHRA--KGGAVLLTSH 185
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
1330-1349 |
7.63e-04 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 43.60 E-value: 7.63e-04
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
322-612 |
7.83e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 43.27 E-value: 7.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 322 LLKSFLLKLVNDIFTFVSPQLLKLLI---SFASDRDTYLWIGYLCAILLFTAALIQSFC--LQCYfqLCFKLGVKVRTAI 396
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIddvLIQLGPGGNTSLLLLLVLGLAGAYVLSALLgiLRGR--LLARLGERITADL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 397 MASVYKKA--LTLSNLARKEytVGETVNLMSVDAQKLMD-VTNFMHMLWSSVLQIVLSIFFL----WRelgpsvLAgvgV 469
Cdd:cd18563 79 RRDLYEHLqrLSLSFFDKRQ--TGSLMSRVTSDTDRLQDfLSDGLPDFLTNILMIIGIGVVLfslnWK------LA---L 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 470 MVLV-IPINAILSTK-SKTIQVKNMKNKDKRLK---IMNEILSGIKILKYFAWEPS----FRDQVQNLRKKELKNLLAFS 540
Cdd:cd18563 148 LVLIpVPLVVWGSYFfWKKIRRLFHRQWRRWSRlnsVLNDTLPGIRVVKAFGQEKReikrFDEANQELLDANIRAEKLWA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 541 QLQCVVIFVFQLTPVLVSVV--------TFSVYVLVdsnnildaqkAFTS-ITLFNilrFPLSMLPMMISSMLQASVSTE 611
Cdd:cd18563 228 TFFPLLTFLTSLGTLIVWYFggrqvlsgTMTLGTLV----------AFLSyLGMFY---GPLQWLSRLNNWITRALTSAE 294
|
.
gi 1388169353 612 R 612
Cdd:cd18563 295 R 295
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
975-1226 |
8.02e-04 |
|
Six-transmembrane helical domain 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: 350002 [Multi-domain] Cd Length: 312 Bit Score: 43.42 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 975 GLFSIFFIILAFVMNSVAFIGSnlwLSAWTSDSKIFNSTDYPASQRDmRVGVYGALGLAQGIFVFIAHFWSAFGFVHASN 1054
Cdd:cd18558 13 GLLPAFMVIFGDMTDSFTNGGM---TNITGNSSGLNSSAGPFEKLEE-EMTLYAYYYLIIGAIVLITAYIQGSFWGLAAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1055 ILHKQLLNNILRAPMR----FFDTTPTGRIVNRFAGDISTVD----DTLPQSLRSWITCFLGIISTLVMICMATPVFTII 1126
Cdd:cd18558 89 RQTKKIRYKFFHAIMRqeigWFDVNDTGELNTRLADDVSKINegigDKIGVIFQNIATFGTGFIIGFIRGWKLTLVILAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1127 VIPLGII-YVSVQMFYVSTSRQLRRLDSVTRSPiyshfSETVSGLPVIRAFEHQQRFLK--HNEVRIDTNqkcvfswits 1203
Cdd:cd18558 169 SPVLGLSaVVWAKILSGFTDKEKKAYAKAGAVA-----EEVLEAFRTVIAFGGQQKEETryAQNLEIAKR---------- 233
|
250 260
....*....|....*....|...
gi 1388169353 1204 nrwLAIRLELVGNLTVFFSALMM 1226
Cdd:cd18558 234 ---NGIKKAITFNISMGAAFLLI 253
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1328-1510 |
8.11e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.59 E-value: 8.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1328 EKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIdgvdiasiglhdlrekltiipqdpilfsgslrMNLDPFNNYSDEEIW 1407
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------IDGEDILEEVLDQLL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1408 KALelahlksfvaslqlglsheVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQ-------TTIQ 1480
Cdd:smart00382 51 LII-------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrlLLLL 111
|
170 180 190
....*....|....*....|....*....|....*.
gi 1388169353 1481 NEFAHCTVITIAHRLHTIMD------SDKVMVLDNG 1510
Cdd:smart00382 112 KSEKNLTVILTTNDEKDLGPallrrrFDRRIVLLLI 147
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
654-851 |
1.04e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 43.15 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGttaYVPQQSWIQNgtiKDNI--LFGT-------- 723
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG---YVPFKRRKEF---ARRIgvVFGQrsqlwwdl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 724 -------------EFNEKRYQQVLEACAllpdlEMLpggDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLS 789
Cdd:COG4586 112 paidsfrllkaiyRIPDAEYKKRLDELV-----ELL---DLGELLDTPVrQLSLGQRMRCELAAALLHRPKILFLDEPTI 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 790 AVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLAK 851
Cdd:COG4586 184 GLDVVSKEAIRE-------FLKeynrerGTTILLTSHDMDDIEALcDRVIVIDHGRIIYDGSLEELKER 245
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
321-613 |
1.10e-03 |
|
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: 42.82 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 321 VLLKSFLLKLVNDIFTFVSPQLLKLLIsfasdrDTYLWIG-----YLCAILLFTAALIQSFcLQcYFQ--LCFKLGVKVR 393
Cdd:cd18570 3 LLILILLLSLLITLLGIAGSFFFQILI------DDIIPSGdinllNIISIGLILLYLFQSL-LS-YIRsyLLLKLSQKLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 394 TAIMASVYKKALTL-----SNlaRKeytVGETVNLMSvDAQKLMD-VTNFMHMLWSSVLQIVLSIFFLWR---ELGPSVL 464
Cdd:cd18570 75 IRLILGYFKHLLKLplsffET--RK---TGEIISRFN-DANKIREaISSTTISLFLDLLMVIISGIILFFynwKLFLITL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 465 AGVGVMVLVIpinAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQC 544
Cdd:cd18570 149 LIIPLYILII---LLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSN 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 545 VVIFVFQLTPVLVSVVTF---SVYVLvdsNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 613
Cdd:cd18570 226 LQSSIKGLISLIGSLLILwigSYLVI---KGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1435-1514 |
1.22e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.24 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1435 GNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDlETD-----NLIQttiqnEFAH--CTVITIAHRLHTIMD-SDKVMV 1506
Cdd:NF040905 138 TDIGVGKQQLVEIAKALSKDVKLLILDEPTAALN-EEDsaallDLLL-----ELKAqgITSIIISHKLNEIRRvADSITV 211
|
....*...
gi 1388169353 1507 LDNGKIIE 1514
Cdd:NF040905 212 LRDGRTIE 219
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1024-1272 |
1.48e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 42.47 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1024 VGVYGALGLAQGIFVFIahfwsafgFVH-ASNI-------LHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTL 1095
Cdd:cd18540 45 ILLYLGLILIQALSVFL--------FIRlAGKIemgvsydLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEII 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1096 PQSLRSWITCFLGIISTLVMICMATP---VFTIIVIPLgIIYVSV--QMFYVSTSRQLRRLDSVtrspIYSHFSETVSGL 1170
Cdd:cd18540 117 SWGLVDLVWGITYMIGILIVMLILNWklaLIVLAVVPV-LAVVSIyfQKKILKAYRKVRKINSR----ITGAFNEGITGA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1171 PVIRAFehqqrflkhneVRIDTNQKcVFSWITSN---------RWLAIRLELVGNLTVFFSALMMV-----IYRDTLSGD 1236
Cdd:cd18540 192 KTTKTL-----------VREEKNLR-EFKELTEEmrrasvraaRLSALFLPIVLFLGSIATALVLWyggilVLAGAITIG 259
|
250 260 270
....*....|....*....|....*....|....*.
gi 1388169353 1237 TVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERI 1272
Cdd:cd18540 260 TLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
654-706 |
1.84e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.02 E-value: 1.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1388169353 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIkGT---TAYVPQ 706
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTkleVAYFDQ 389
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
761-850 |
2.22e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.38 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 761 LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFnkvlgpnGLLK------GKTRLLVTHSMHFLPQV-DEIVV 833
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQIL-------QLLRelqqelNMGLLFITHNLSIVRKLaDRVAV 229
|
90
....*....|....*..
gi 1388169353 834 LGNGTIVEKGSYSALLA 850
Cdd:PRK15134 230 MQNGRCVEQNRAATLFS 246
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1308-1525 |
2.26e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.38 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1308 RYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAA-----GGQIIIDGVDIASIGLHDLR----EKLT 1378
Cdd:PRK15134 16 RQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRgvrgNKIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1379 IIPQDPILfsgslrmNLDPFNNysdeeIWKALelahlkSFVASLQLGLSHE--------------VTEAGG-------NL 1437
Cdd:PRK15134 96 MIFQEPMV-------SLNPLHT-----LEKQL------YEVLSLHRGMRREaargeilncldrvgIRQAAKrltdyphQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1438 SIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQT---TIQNEFaHCTVITIAHRLHTIMD-SDKVMVLDNGKII 1513
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQllrELQQEL-NMGLLFITHNLSIVRKlADRVAVMQNGRCV 236
|
250
....*....|..
gi 1388169353 1514 ECGSPEELLQIP 1525
Cdd:PRK15134 237 EQNRAATLFSAP 248
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1304-1510 |
4.67e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 41.63 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1304 NYQVRYRPELDLVLRGIT--CDIGSMekIGVVGRTGAGKSSLTNCLfriLEAAGGQIIIDGVDIA-----------SIGL 1370
Cdd:TIGR00956 766 TYEVKIKKEKRVILNNVDgwVKPGTL--TALMGASGAGKTTLLNVL---AERVTTGVITGGDRLVngrpldssfqrSIGY 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1371 ---HDLR-EKLTIipQDPILFSGSLR----MNLDPFNNYSDEEIwKALELAHLKSFVaslqlglsheVTEAGGNLSIGQR 1442
Cdd:TIGR00956 841 vqqQDLHlPTSTV--RESLRFSAYLRqpksVSKSEKMEYVEEVI-KLLEMESYADAV----------VGVPGEGLNVEQR 907
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388169353 1443 QLLCLGRALLRKSKILV-LDEATAAVDLETDNLIQTTIQNEFAHCTVI--TIAHRLHTIMDS-DKVMVLDNG 1510
Cdd:TIGR00956 908 KRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAIlcTIHQPSAILFEEfDRLLLLQKG 979
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
325-613 |
4.73e-03 |
|
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: 40.87 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 325 SFLLKLVNDIFTFVSPQLLKLLI--SFASDRDTYLWigYLCAILLFTAAL------IQSFCLQcyfqlcfKLGVKVRTAI 396
Cdd:cd18552 4 AILGMILVAATTAALAWLLKPLLddIFVEKDLEALL--LVPLAIIGLFLLrglasyLQTYLMA-------YVGQRVVRDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 397 MASVYKKALTLSnLAR-KEYTVGETVNLMSVDAQKLMD-VTNFMHMLWSSVLQIVLSIFFL----WReLgpSVLAGVGVM 470
Cdd:cd18552 75 RNDLFDKLLRLP-LSFfDRNSSGDLISRITNDVNQVQNaLTSALTVLVRDPLTVIGLLGVLfyldWK-L--TLIALVVLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 471 VLVIPINAI---LSTKSKTIQVK--NMknkdkrLKIMNEILSGIKILKYFAWEPS----FRDQVQNLRKKELKnLLAFSQ 541
Cdd:cd18552 151 LAALPIRRIgkrLRKISRRSQESmgDL------TSVLQETLSGIRVVKAFGAEDYeikrFRKANERLRRLSMK-IARARA 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388169353 542 LqcvvifvfqLTPV--LVSVVTFSVYVLVDSNNILDAQK---AFTS-ITLFNILRFPLSMLPMMISSMLQASVSTERL 613
Cdd:cd18552 224 L---------SSPLmeLLGAIAIALVLWYGGYQVISGELtpgEFISfITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
1059-1181 |
4.75e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 40.65 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1059 QLLNNILRAPMRFFDTTPTGRIVNRFaGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIYVsVQ 1138
Cdd:cd18782 80 TIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQL-LL 157
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1388169353 1139 MFYVS--TSRQLRRLdSVTRSPIYSHFSETVSGLPVIRA--FEHQQR 1181
Cdd:cd18782 158 TFLFGpiLRRQIRRR-AEASAKTQSYLVESLTGIQTVKAqnAELKAR 203
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
655-696 |
5.10e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 40.68 E-value: 5.10e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1388169353 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHIT 696
Cdd:PRK11701 23 RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH 64
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
657-792 |
5.15e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 40.30 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 657 VNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENvHGHITIKGTT-------------AYVPQQSwiqngtikdnilfGT 723
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPleawsaaelarhrAYLSQQQ-------------TP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 724 EFNEKRYQ----------QVLEACALLPDL-EMLPGGDLAeigEKGIN-LSGGQKQRISLARATYQ-----NLD--IYLL 784
Cdd:PRK03695 81 PFAMPVFQyltlhqpdktRTEAVASALNEVaEALGLDDKL---GRSVNqLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLL 157
|
....*...
gi 1388169353 785 DDPLSAVD 792
Cdd:PRK03695 158 DEPMNSLD 165
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1328-1508 |
5.31e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 41.31 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1328 EKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDgVDIASiglhdlreKLTIIPQDpilFSGSLRMNL-----DPF-NNY 1401
Cdd:COG1245 367 EVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKISY--------KPQYISPD---YDGTVEEFLrsantDDFgSSY 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1402 SDEEIWKALELAHLksfvaslqlgLSHEVTEaggnLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQN 1481
Cdd:COG1245 435 YKTEIIKPLGLEKL----------LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRR 500
|
170 180 190
....*....|....*....|....*....|
gi 1388169353 1482 --EFAHCTVITIAHRLHTI-MDSDKVMVLD 1508
Cdd:COG1245 501 faENRGKTAMVVDHDIYLIdYISDRLMVFE 530
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
433-613 |
5.58e-03 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 40.59 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 433 DVTNFMHMLWSSVL----QIVLSIFFLWRELGPSVLAGV-GVMVLVIPINAILSTKSKTIQVKNMKNKDKRLKIMNEILS 507
Cdd:cd18583 105 SINDLLEQILFQIVpmiiDLVIAIVYLYYLFDPYMGLIVaVVMVLYVWSTIKLTSWRTKLRRDMIDADREERSILTESLL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 508 GIKILKYFAWEP----SFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTpvLVSVVTFSVYvlvdsnNILDAQKA---F 580
Cdd:cd18583 185 NWETVKYFNREPyekeRYREAVKNYQKAERKYLFSLNLLNAVQSLILTLG--LLAGCFLAAY------QVSQGQATvgdF 256
|
170 180 190
....*....|....*....|....*....|....
gi 1388169353 581 -TSITLFNILRFPLSMLPMMISSMLQASVSTERL 613
Cdd:cd18583 257 vTLLTYWAQLSGPLNFFATLYRSIQSDLIDAERL 290
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1316-1511 |
6.09e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 41.02 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAG--GQIIIDGVDIASiglhDLREKLTIIPQDPIL------- 1386
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK----QILKRTGFVTQDDILyphltvr 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1387 ----FSGSLRMnldPFNNYSDEEIWKAlelahlKSFVAslQLGLSHEVTEAGGN-----LSIGQRQLLCLGRALLRKSKI 1457
Cdd:PLN03211 159 etlvFCSLLRL---PKSLTKQEKILVA------ESVIS--ELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSL 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1388169353 1458 LVLDEATAAVDLETD-NLIQTTIQNEFAHCTVITIAH----RLHTIMDSdkVMVLDNGK 1511
Cdd:PLN03211 228 LILDEPTSGLDATAAyRLVLTLGSLAQKGKTIVTSMHqpssRVYQMFDS--VLVLSEGR 284
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1316-1522 |
6.11e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 40.45 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1316 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTI---------------- 1379
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEklviqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1380 ---------------------IPQDpILFsGSLRMNLDPfnnysdEEiwkALELAhlKSFVASLQLGLSHeVTEAGGNLS 1438
Cdd:PRK13651 102 eirrrvgvvfqfaeyqlfeqtIEKD-IIF-GPVSMGVSK------EE---AKKRA--AKYIELVGLDESY-LQRSPFELS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1439 IGQRQLLCLGRALLRKSKILVLDEATAAVD----LETDNLIQTTIQNefaHCTVITIAHRLHTIMD-SDKVMVLDNGKII 1513
Cdd:PRK13651 168 GGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEIFDNLNKQ---GKTIILVTHDLDNVLEwTKRTIFFKDGKII 244
|
....*....
gi 1388169353 1514 ECGSPEELL 1522
Cdd:PRK13651 245 KDGDTYDIL 253
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
1023-1181 |
6.63e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 40.19 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1023 RVGVYGALG----LAQGIFVFIAhFWSAFGFV------HASNI----LHKQLLNNILRAPMRFFDTTPTGRIVnRFAGDI 1088
Cdd:cd18783 31 KVLVHQSYStlyvLTIGVVIALL-FEGILGYLrrylllVATTRidarLALRTFDRLLSLPIDFFERTPAGVLT-KHMQQI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1089 STVDDTLPQSLrswITCFLGIISTLVMI---CMATPVFTIIVIPLGIIYVSVQMFYVSTSRqlRRLDSVTRSPI--YSHF 1163
Cdd:cd18783 109 ERIRQFLTGQL---FGTLLDATSLLVFLpvlFFYSPTLALVVLAFSALIALIILAFLPPFR--RRLQALYRAEGerQAFL 183
|
170 180
....*....|....*....|
gi 1388169353 1164 SETVSGLPVIRAF--EHQQR 1181
Cdd:cd18783 184 VETVHGIRTVKSLalEPRQR 203
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
1329-1387 |
6.67e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 37.98 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1329 KIGVVGRTGAGKSSLTNCL------------------FRILEAAGGQIIIdgVDI------ASIGLHDLREKLTIIPQDP 1384
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALtgakaivsdypgttrdpnEGRLELKGKQIIL--VDTpgliegASEGEGLGRAFLAIIEADL 78
|
...
gi 1388169353 1385 ILF 1387
Cdd:pfam01926 79 ILF 81
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
657-793 |
7.20e-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: 40.96 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 657 VNLDIMAGQLVAVIGPVGSGKSSLISAMLGemenVHGHITIKGTTAYVPQQ---------------------SWIQNGTI 715
Cdd:TIGR02633 20 IDLEVRPGECVGLCGENGAGKSTLMKILSG----VYPHGTWDGEIYWSGSPlkasnirdteragiviihqelTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 716 KDNILFGTEFNEKRY-----QQVLEACALLPDLEMLPGGDLAEIGEKGinlsGGQKQRISLARATYQNLDIYLLDDPLSA 790
Cdd:TIGR02633 96 AENIFLGNEITLPGGrmaynAMYLRAKNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSS 171
|
...
gi 1388169353 791 VDA 793
Cdd:TIGR02633 172 LTE 174
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1437-1521 |
7.63e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1437 LSIGQRQLLCLGRALLRKSK---ILVLDEATAAVDLETDNLIQTTIQ------NefahcTVITIAHRLHTIMDSDKVMVL 1507
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQrlvdkgN-----TVVVIEHNLDVIKTADYIIDL 904
|
90 100
....*....|....*....|
gi 1388169353 1508 ------DNGKIIECGSPEEL 1521
Cdd:TIGR00630 905 gpeggdGGGTVVASGTPEEV 924
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1024-1176 |
8.79e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 40.24 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1024 VGVYGALGLAQGIFvfiAHFWSAFgfvhASNILHK---QLLNNILRAPMRFFDTTPTGRIVNRFAGDIST----VDDTLP 1096
Cdd:cd18565 61 VAAFLLESLFQYLS---GVLWRRF----AQRVQHDlrtDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQlerfLDDGAN 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388169353 1097 QSLRSWITcFLGIISTLVMICMATPVFTIIVIPLgIIYVSVqmFYvstSRQLRRLDSVTRSP---IYSHFSETVSGLPVI 1173
Cdd:cd18565 134 SIIRVVVT-VLGIGAILFYLNWQLALVALLPVPL-IIAGTY--WF---QRRIEPRYRAVREAvgdLNARLENNLSGIAVI 206
|
...
gi 1388169353 1174 RAF 1176
Cdd:cd18565 207 KAF 209
|
|
| |
