|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
27-1305 |
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: 1542.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 27 RRQEKSSQQNSGARLPGlNKNQSQSQDALVL---EDVEKKKKKSGTKKDVPKswLMKALFKTFYMVLLKSFLLKLVNDIF 103
Cdd:TIGR00957 256 KKECKKTRKQPVSAVYG-KKDPSKPKGSSQLdanEEVEALIVKSPHKPRKPS--LFKVLYKTFGPYFLMSFCFKAIHDLM 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 104 TFVSPQLLKLLISFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKKALTLSNLARKEY 183
Cdd:TIGR00957 333 MFIGPQILSLLIRFVNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSS 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 184 TVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTKSKTIQVKNMKNK 263
Cdd:TIGR00957 413 TVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSK 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 264 DKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFSVYVLVDSNNILD 343
Cdd:TIGR00957 493 DNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNILD 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 344 AQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERLEKYLGGDDLDTSAIRHDCNFD---KAMQFSEASFTWEHDSEA 420
Cdd:TIGR00957 573 AEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPgegNSITVHNATFTWARDLPP 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 421 TVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQNGTIKDNILFGTEFNEKRYQQ 500
Cdd:TIGR00957 653 TLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQ 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 501 VLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLGPNGLLKG 580
Cdd:TIGR00957 733 VLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLKN 812
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 581 KTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAKnlktFLRHTGPEEEatvhDGSEEEDDDYGLISSVE 660
Cdd:TIGR00957 813 KTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAE----FLRTYAPDEQ----QGHLEDSWTALVSGEGK 884
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 661 E--IPEDAASITMRRENSFRRTLSRSSRSNGRHLKSLRNSLKTRNVNSLKEDEELVKGQKlikkefIETGKVKFSIYLEY 738
Cdd:TIGR00957 885 EakLIENGMLVTDVVGKQLQRQLSASSSDSGDQSRHHGSSAELQKAEAKEETWKLMEADK------AQTGQVELSVYWDY 958
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 739 LQAIGLFSIFFIILAFVMNSVAFIGSNLWLSAWTSDSkIFNSTDypaSQRDMRVGVYGALGLAQGIFVFIAHFWSAFGFV 818
Cdd:TIGR00957 959 MKAIGLFITFLSIFLFVCNHVSALASNYWLSLWTDDP-MVNGTQ---NNTSLRLSVYGALGILQGFAVFGYSMAVSIGGI 1034
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 819 HASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPL 898
Cdd:TIGR00957 1035 QASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPL 1114
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 899 GIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNRWLAIR 978
Cdd:TIGR00957 1115 GLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVR 1194
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 979 LELVGNLTVFFSALMMVIYRDTLSGDTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYTKVENEAPW-VTDKR 1057
Cdd:TIGR00957 1195 LECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWqIQETA 1274
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1058 PPPDWPSKGKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIG 1137
Cdd:TIGR00957 1275 PPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG 1354
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1138 LHDLREKLTIIPQDPILFSGSLRMNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGR 1217
Cdd:TIGR00957 1355 LHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLAR 1434
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1218 ALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFY 1297
Cdd:TIGR00957 1435 ALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFY 1514
|
....*...
gi 578818931 1298 FMAKEAGI 1305
Cdd:TIGR00957 1515 SMAKDAGL 1522
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
74-1291 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 1045.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 74 PKSWLMKALFKTFYMVLLKSFLLKLVNDIFTFVSPQLLKLLISFASDRDTyLWIGYLCAILLFTAALIQSFCLQCYFQLC 153
Cdd:PLN03130 287 PKPWLLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQNGEP-AWIGYIYAFSIFVGVVLGVLCEAQYFQNV 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 154 FKLGVKVRTAIMASVYKKALTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLA 233
Cdd:PLN03130 366 MRVGFRLRSTLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLI 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 234 GVGVMVLVIPINAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCV 313
Cdd:PLN03130 446 GSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAF 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 314 VIFVFQLTPVLVSVVTFSVYVLVDSNniLDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERLEKYLGGDD---L 390
Cdd:PLN03130 526 NSFILNSIPVLVTVVSFGVFTLLGGD--LTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEErvlL 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 391 DTSAIRHDCnfdKAMQFSEASFTWEHDSE-ATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENV-HGHITIKGT 468
Cdd:PLN03130 604 PNPPLEPGL---PAISIKNGYFSWDSKAErPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRsDASVVIRGT 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 469 TAYVPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLD 548
Cdd:PLN03130 681 VAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 549 IYLLDDPLSAVDAHVGKHIFNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAKnlk 628
Cdd:PLN03130 761 VYIFDDPLSALDAHVGRQVFDKCI--KDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQK--- 835
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 629 tFLRHTGPEEEaTVHDGSEEEDDDyglissveeipedaasitmrrensfrrtlsrssrSNGRHLKSLRNSLKTRNVNSLK 708
Cdd:PLN03130 836 -LMENAGKMEE-YVEENGEEEDDQ----------------------------------TSSKPVANGNANNLKKDSSSKK 879
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 709 EDEElvKGQKLIKKEFIETGKVKFSIYLEYLQAI-GLFSIFFIILAFVMNSVAFIGSNLWLSAWT--SDSKIFNSTDYpa 785
Cdd:PLN03130 880 KSKE--GKSVLIKQEERETGVVSWKVLERYKNALgGAWVVMILFLCYVLTEVFRVSSSTWLSEWTdqGTPKTHGPLFY-- 955
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 786 sqrdmrVGVYGALGLAQGIFVFIAHFWSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQ 865
Cdd:PLN03130 956 ------NLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAV 1029
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 866 SLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFE 945
Cdd:PLN03130 1030 FVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYK 1109
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 946 HQQRFLKHNEVRIDTNQKCVFSWITSNRWLAIRLELVGNLTVFFSALMMVIYRDTLS-----GDTVGFVLSNALNITQTL 1020
Cdd:PLN03130 1110 AYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQNGRAEnqaafASTMGLLLSYALNITSLL 1189
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1021 NWLVRMTSEIETNIVAVERITEYTKVENEAPWVT-DKRPPPDWPSKGKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIG 1099
Cdd:PLN03130 1190 TAVLRLASLAENSLNAVERVGTYIDLPSEAPLVIeNNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVG 1269
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1100 VVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNLDPFNNYSDEEIWKALE 1179
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLE 1349
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1180 LAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITI 1259
Cdd:PLN03130 1350 RAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLII 1429
|
1210 1220 1230
....*....|....*....|....*....|..
gi 578818931 1260 AHRLHTIMDSDKVMVLDNGKIIECGSPEELLQ 1291
Cdd:PLN03130 1430 AHRLNTIIDCDRILVLDAGRVVEFDTPENLLS 1461
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
74-1307 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 963.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 74 PKSWLMKALFKTFYMVLLKSFLLKLVNDIFTFVSPQLLKLLISFASDRDTyLWIGYLCAILLFTAALIQSFCLQCYFQLC 153
Cdd:PLN03232 287 PKPWLLRALNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMQEGDP-AWVGYVYAFLIFFGVTFGVLCESQYFQNV 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 154 FKLGVKVRTAIMASVYKKALTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLA 233
Cdd:PLN03232 366 GRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLF 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 234 GVGVMVLVIPINAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCV 313
Cdd:PLN03232 446 GSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAF 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 314 VIFVFQLTPVLVSVVTFSVYVLVDSNniLDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERLEKYLGGDD---- 389
Cdd:PLN03232 526 NSFILNSIPVVVTLVSFGVFVLLGGD--LTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEErila 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 390 ----LDTSAirhdcnfdKAMQFSEASFTWEHDSE-ATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVH-GHI 463
Cdd:PLN03232 604 qnppLQPGA--------PAISIKNGYFSWDSKTSkPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtSSV 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 464 TIKGTTAYVPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARAT 543
Cdd:PLN03232 676 VIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAV 755
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 544 YQNLDIYLLDDPLSAVDAHVGKHIFNKVLGPNglLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYsALLAKKGEF 623
Cdd:PLN03232 756 YSNSDIYIFDDPLSALDAHVAHQVFDSCMKDE--LKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTF-AELSKSGSL 832
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 624 AKNLKtflrhtgpeEEATVHDGSEEEDddygliSSVEEIPEDAASITMRRENsfrrtlsrssrsngRHLKSLRNSLKTRN 703
Cdd:PLN03232 833 FKKLM---------ENAGKMDATQEVN------TNDENILKLGPTVTIDVSE--------------RNLGSTKQGKRGRS 883
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 704 VnslkedeelvkgqkLIKKEFIETGKVKFSIYLEYLQAIG-LFSIFFIILAFVMNSVAFIGSNLWLSAWTSDSKIFNSTd 782
Cdd:PLN03232 884 V--------------LVKQEERETGIISWNVLMRYNKAVGgLWVVMILLVCYLTTEVLRVSSSTWLSIWTDQSTPKSYS- 948
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 783 yPAsqrdMRVGVYGALGLAQGIFVFIAHFWSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDT 862
Cdd:PLN03232 949 -PG----FYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRN 1023
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 863 LPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIR 942
Cdd:PLN03232 1024 VANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIR 1103
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 943 AFEHQQRFLKHNEVRIDTNQKCVFSWITSNRWLAIRLELVGNLTVFFSALMMVI-YRDTLS----GDTVGFVLSNALNIT 1017
Cdd:PLN03232 1104 AYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLrNGNAENqagfASTMGLLLSYTLNIT 1183
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1018 QTLNWLVRMTSEIETNIVAVERITEYTKVENEAPWV-TDKRPPPDWPSKGKIQFNNYQVRYRPELDLVLRGITCDIGSME 1096
Cdd:PLN03232 1184 TLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIiENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSE 1263
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1097 KIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNLDPFNNYSDEEIWK 1176
Cdd:PLN03232 1264 KVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWE 1343
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1177 ALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTV 1256
Cdd:PLN03232 1344 ALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTM 1423
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|..
gi 578818931 1257 ITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFYF-MAKEAGIEN 1307
Cdd:PLN03232 1424 LVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFrMVHSTGPAN 1475
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
78-1289 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 827.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 78 LMKALFKTFYMVLLKSFLLKLVNDIFTFVSPQLLKLLISFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLG 157
Cdd:PTZ00243 234 LLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRFYYISIRCG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 158 VKVRTAIMASVYKKALTLSN--LARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGV 235
Cdd:PTZ00243 314 LQYRSALNALIFEKCFTISSksLAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALMAV 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 236 GVMVLVIPINAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVI 315
Cdd:PTZ00243 394 AVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVATS 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 316 FVFQLTPVLVSVVTFSVYVLvdSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERLEKYLGGDDLDTSAI 395
Cdd:PTZ00243 474 FVNNATPTLMIAVVFTVYYL--LGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLECDNATCSTV 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 396 R-----------HDCNFDKAMQFSEASFT--------------------------------------------------- 413
Cdd:PTZ00243 552 QdmeeywreqreHSTACQLAAVLENVDVTafvpvklprapkvktsllsralrmlcceqcrptkrhpspsvvvedtdygsp 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 414 ------------------------------------WEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEME 457
Cdd:PTZ00243 632 ssasrhiveggtgggheatptsersaktpkmktddfFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFE 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 458 NVHGHITIKGTTAYVPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRI 537
Cdd:PTZ00243 712 ISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARV 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 538 SLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALL 617
Cdd:PTZ00243 792 SLARAVYANRDVYLLDDPLSALDAHVGERVVEECF--LGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM 869
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 618 AKkgefakNLKTFLRHTGPEEEATVHDGSEEEDDDyglISSVEEIPEDAAsitmrrensfrrtlsrssrsngrhlkslRN 697
Cdd:PTZ00243 870 RT------SLYATLAAELKENKDSKEGDADAEVAE---VDAAPGGAVDHE----------------------------PP 912
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 698 SLKTRNVNslkEDEELVKGQ----KLIKKEFIETGKVKFSIYLEYLQAIG-LFSIFFIILAFVMNSVAFIGSNLWLSAWT 772
Cdd:PTZ00243 913 VAKQEGNA---EGGDGAALDaaagRLMTREEKASGSVPWSTYVAYLRFCGgLHAAGFVLATFAVTELVTVSSGVWLSMWS 989
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 773 SDSKIFNSTDYpasqrdmrVGVYGALGLAQGIFVFIAHFWSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRF 852
Cdd:PTZ00243 990 TRSFKLSAATY--------LYVYLGIVLLGTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRF 1061
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 853 AGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFS 932
Cdd:PTZ00243 1062 SRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLE 1141
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 933 ETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNRWLAIRLELVGNLTVFFSALMMVIYR-DTLSGDTVGFV-- 1009
Cdd:PTZ00243 1142 EALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGVIGTmLRATSQEIGLVsl 1221
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1010 -LSNALNITQTLNWLVRMTSEIETNIVAVERITEYT-KVENEA-PWVTD------KR-----------------PPPDWP 1063
Cdd:PTZ00243 1222 sLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTdEVPHEDmPELDEevdaleRRtgmaadvtgtvviepasPTSAAP 1301
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1064 ---SKGKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHD 1140
Cdd:PTZ00243 1302 hpvQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRE 1381
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1141 LREKLTIIPQDPILFSGSLRMNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALL 1220
Cdd:PTZ00243 1382 LRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALL 1461
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1221 RK-SKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEEL 1289
Cdd:PTZ00243 1462 KKgSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
78-1290 |
1.48e-164 |
|
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: 531.41 E-value: 1.48e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 78 LMKALFKTFYMVLLKSFLLKLVNDIFTFVSPQLLKLLI-SFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKL 156
Cdd:TIGR01271 70 LLNALRRCFFWRFVFYGILLYFGEATKAVQPLLLGRIIaSYDPFNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGLHHL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 157 GVKVRTAIMASVYKKALTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVG 236
Cdd:TIGR01271 150 GMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLG 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 237 VMVLVIPINAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIF 316
Cdd:TIGR01271 230 FLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSS 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 317 VFQLTPVLVSVVTFSVYVLVDSnniLDAQKAFTSITLFNILRFPLS-MLPMMISSMLQASVSTERLEKYLGGDD------ 389
Cdd:TIGR01271 310 AFFFSGFFVVFLSVVPYALIKG---IILRRIFTTISYCIVLRMTVTrQFPGAIQTWYDSLGAITKIQDFLCKEEyktley 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 390 -LDTSAI--------------------------RHDCNFDKAMQFSEASFTwehdSEATVRDVNLDIMAGQLVAVIGPVG 442
Cdd:TIGR01271 387 nLTTTEVemvnvtaswdegigelfekikqnnkaRKQPNGDDGLFFSNFSLY----VTPVLKNISFKLEKGQLLAVAGSTG 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 443 SGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEI 522
Cdd:TIGR01271 463 SGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVL 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 523 GEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLGPngLLKGKTRLLVTHSMHFLPQVDEIVVL 602
Cdd:TIGR01271 543 GEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCK--LMSNKTRILVTSKLEHLKKADKILLL 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 603 GNGTIVEKGSYSALLAKKGEFAKNL------------------KTFLRHTGPEEEATVHDGSEE-------------EDD 651
Cdd:TIGR01271 621 HEGVCYFYGTFSELQAKRPDFSSLLlgleafdnfsaerrnsilTETLRRVSIDGDSTVFSGPETikqsfkqpppefaEKR 700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 652 DYGLI----------SSVEEIPEDAASITM----------------------------------------RRENSFRRTL 681
Cdd:TIGR01271 701 KQSIIlnpiasarkfSFVQMGPQKAQATTIedavrepserkfslvpedeqgeeslprgnqyhhglqhqaqRRQSVLQLMT 780
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 682 SRSSRSNGRHLK--SLRNSLKTRNVNSLKE---------------------DEELVKgQKLIKKEFIETGKVKFSIYLEY 738
Cdd:TIGR01271 781 HSNRGENRREQLqtSFRKKSSITQQNELASeldiysrrlskdsvyeiseeiNEEDLK-ECFADERENVFETTTWNTYLRY 859
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 739 LqAIGLFSIFFIILAFVMNSVAFIGS--NLWLSAWTSDSKIFNSTDYP-ASQRDMRVGVYGALGLAQGIF---VFIAHFW 812
Cdd:TIGR01271 860 I-TTNRNLVFVLIFCLVIFLAEVAASllGLWLITDNPSAPNYVDQQHAnASSPDVQKPVIITPTSAYYIFyiyVGTADSV 938
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 813 SAFGF------VHA----SNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLV 882
Cdd:TIGR01271 939 LALGFfrglplVHTlltvSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIF 1018
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 883 MICMATPVFTIIVIPLGIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQ 962
Cdd:TIGR01271 1019 VVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHT 1098
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 963 KCVFSWITSNRWLAIRLELVgnLTVFFSALMMVIYRDTLSGD-TVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERIT 1041
Cdd:TIGR01271 1099 ANWFLYLSTLRWFQMRIDII--FVFFFIAVTFIAIGTNQDGEgEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVF 1176
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1042 EYTKVENEAPWVTDKRPPPD---------------WPSKGKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGA 1106
Cdd:TIGR01271 1177 KFIDLPQEEPRPSGGGGKYQlstvlvienphaqkcWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGS 1256
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1107 GKSSLTNCLFRILeAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNLDPFNNYSDEEIWKALELAHLKSF 1186
Cdd:TIGR01271 1257 GKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSV 1335
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1187 VASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTI 1266
Cdd:TIGR01271 1336 IEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEAL 1415
|
1370 1380
....*....|....*....|....
gi 578818931 1267 MDSDKVMVLDNGKIIECGSPEELL 1290
Cdd:TIGR01271 1416 LECQQFLVIEGSSVKQYDSIQKLL 1439
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
747-1044 |
3.60e-162 |
|
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: 486.22 E-value: 3.60e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 747 IFFIILAFVMNSVAFIGSNLWLSAWTSDSKIFNSTDYpaSQRDMRVGVYGALGLAQGIFVFIAHFWSAFGFVHASNILHK 826
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDT--EQRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 827 QLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIYVSVQ 906
Cdd:cd18603 79 KLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 907 MFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNRWLAIRLELVGNLT 986
Cdd:cd18603 159 RFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLI 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 578818931 987 VFFSALMMVIYRDTLSGDTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYT 1044
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, ... |
92-381 |
2.84e-152 |
|
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: 460.01 E-value: 2.84e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 92 KSFLLKLVNDIFTFVSPQLLKLLISFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKK 171
Cdd:cd18595 1 LAALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 172 ALTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTK 251
Cdd:cd18595 81 ALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 252 SKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFS 331
Cdd:cd18595 161 IKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 578818931 332 VYVLVDSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 381
Cdd:cd18595 241 TYVLSDPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1066-1286 |
2.88e-135 |
|
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: 412.27 E-value: 2.88e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1066 GKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKL 1145
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1146 TIIPQDPILFSGSLRMNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKI 1225
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578818931 1226 LVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSP 1286
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
792-1297 |
2.41e-120 |
|
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: 2.41e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 792 VGVYGALGLAQGIFVFIAHFWSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWI 871
Cdd:COG1132 64 LLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 872 TCFLGIISTLVMICMATPVFTIIVIPLGIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFL 951
Cdd:COG1132 144 RSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREEREL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 952 KHNEVRIDTNQKCVFSWITSNRWLAIRLELVGNLT---VFFSALMMVIyRDTLS-GDTVGFVLSnALNITQTLNWLVRMT 1027
Cdd:COG1132 224 ERFREANEELRRANLRAARLSALFFPLMELLGNLGlalVLLVGGLLVL-SGSLTvGDLVAFILY-LLRLFGPLRQLANVL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1028 SEIETNIVAVERITEYTKVENEAPWVTDKRPPPdwPSKGKIQFNNYQVRYRPElDLVLRGITCDIGSMEKIGVVGRTGAG 1107
Cdd:COG1132 302 NQLQRALASAERIFELLDEPPEIPDPPGAVPLP--PVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSG 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1108 KSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNL---DPfnNYSDEEIWKALELAHLK 1184
Cdd:COG1132 379 KSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAKAAQAH 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1185 SFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLH 1264
Cdd:COG1132 457 EFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLS 536
|
490 500 510
....*....|....*....|....*....|...
gi 578818931 1265 TIMDSDKVMVLDNGKIIECGSPEELLQIPGPFY 1297
Cdd:COG1132 537 TIRNADRILVLDDGRIVEQGTHEELLARGGLYA 569
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
93-381 |
5.23e-117 |
|
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: 366.43 E-value: 5.23e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 93 SFLLKLVNDIFTFVSPQLLKLLISFASDRDTY-LWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKK 171
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEpLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 172 ALTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTK 251
Cdd:cd18579 82 ALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 252 SKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFS 331
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 578818931 332 VYVLVDsnNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 381
Cdd:cd18579 242 TYVLLG--NPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
405-606 |
3.65e-115 |
|
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: 3.65e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 405 MQFSEASFTW---EHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQNG 481
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 482 TIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 561
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 578818931 562 HVGKHIFNKVLGPNgLLKGKTRLLVTHSMHFLPQVDEIVVLGNGT 606
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 ... |
747-1044 |
4.75e-114 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 358.74 E-value: 4.75e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 747 IFFIILAFVMNSVAFIGSNLWLSAWTSDSkifnsTDYPASQRDMRVGVYGALGL-AQGIFVFIAHFWSAFGFVHASNILH 825
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDW-----SSSPNSSSGYYLGVYAALLVlASVLLVLLRWLLFVLAGLRASRRLH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 826 KQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIYVSV 905
Cdd:cd18580 76 DKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 906 QMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNRWLAIRLELVGNL 985
Cdd:cd18580 156 QRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGAL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 986 TVFFSALMMVIYRDTLSGDTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYT 1044
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 ... |
747-1044 |
1.24e-105 |
|
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: 335.98 E-value: 1.24e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 747 IFFIILAFVMNSVAFIGSNLWLSAWTSDSKIFNSTDYpasqrdmrVGVYGALGLAQGIFVFIAHFWSAFGFVHASNILHK 826
Cdd:cd18606 1 LPLLLLLLILSQFAQVFTNLWLSFWTEDFFGLSQGFY--------IGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 827 QLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIYVSVQ 906
Cdd:cd18606 73 KALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 907 MFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNRWLAIRLELVGNLT 986
Cdd:cd18606 153 NYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 578818931 987 VFFSALMMVIYRDTLSGDTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYT 1044
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; ... |
747-1044 |
3.58e-99 |
|
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: 318.64 E-value: 3.58e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 747 IFFIILAFVMNSVAFIGSNLWLSAWTSDSKifNSTDYPASQRDMR--VGVYGALGLAQGIFVFIAHFWSAFGFVHASNIL 824
Cdd:cd18604 1 WALLLLLFVLSQLLSVGQSWWLGIWASAYE--TSSALPPSEVSVLyyLGIYALISLLSVLLGTLRYLLFFFGSLRASRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 825 HKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIYVS 904
Cdd:cd18604 79 HERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 905 VQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNRWLAIRLELVGN 984
Cdd:cd18604 159 IGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGA 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 985 LTVFFSALMMVIYRDTLSGdTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYT 1044
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 ... |
1062-1286 |
3.47e-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: 306.65 E-value: 3.47e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1062 WPSKGKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDL 1141
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1142 REKLTIIPQDPILFSGSLRMNLDPFNNYSDEEIWKALelahlksfvaslqlglshEVTEAGGNLSIGQRQLLCLGRALLR 1221
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 1222 KSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSP 1286
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
797-1302 |
2.18e-92 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 314.08 E-value: 2.18e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 797 ALGLAQGIFVFiahFWSAFGFV------HASN----ILHKQLLNNILRAPMRFFDTTPTGRIVNRFaGDISTVDDTLP-Q 865
Cdd:COG2274 197 VLAIGLLLALL---FEGLLRLLrsylllRLGQridlRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTgS 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 866 SLRSWITCFLGIISTLVMICMAtPVFTIIVIPLGIIYVSVQMFyvsTSRQLRRLD---SVTRSPIYSHFSETVSGLPVIR 942
Cdd:COG2274 273 LLTALLDLLFVLIFLIVLFFYS-PPLALVVLLLIPLYVLLGLL---FQPRLRRLSreeSEASAKRQSLLVETLRGIETIK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 943 AFEHQQRFLKHNEVR----IDTNQKcVFSWITSNRWLAIRLELVGNLTVFFSALMMVIyrdtlSGD-TVG-FVLSNALnI 1016
Cdd:COG2274 349 ALGAESRFRRRWENLlakyLNARFK-LRRLSNLLSTLSGLLQQLATVALLWLGAYLVI-----DGQlTLGqLIAFNIL-S 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1017 TQTLNWLVRMTS---EIETNIVAVERITEYTKVENEAPWVTDKRPPPdwPSKGKIQFNNYQVRYRPELDLVLRGITCDIG 1093
Cdd:COG2274 422 GRFLAPVAQLIGllqRFQDAKIALERLDDILDLPPEREEGRSKLSLP--RLKGDIELENVSFRYPGDSPPVLDNISLTIK 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1094 SMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNL---DPfnNYS 1170
Cdd:COG2274 500 PGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDP--DAT 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1171 DEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNE 1250
Cdd:COG2274 578 DEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL 657
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 578818931 1251 FAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFYFMAKE 1302
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 ... |
747-1044 |
1.45e-86 |
|
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: 284.11 E-value: 1.45e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 747 IFFIILAFVMNSVAFIGSNLWLSAWTS-----DSKIFNSTDYPASQRDMR--VGVYGALGLAQGIFVFIAHFWSAFGFVH 819
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWTEanhdvASVVFNITSSSLEDDEVSyyISVYAGLSLGAVILSLVTNLAGELAGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 820 ASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLG 899
Cdd:cd18602 81 AARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 900 IIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNRWLAIRL 979
Cdd:cd18602 161 IVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578818931 980 ELVGNLTVFFSAL--MMVIYRDTLSGDTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYT 1044
Cdd:cd18602 241 DYLGAVIVFLAALssLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
748-1044 |
7.28e-86 |
|
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: 281.73 E-value: 7.28e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 748 FFIILAFVMNSVAFIGSNLWLSAWTSDSKIFNSTDYPASQRDMRVgVYGALGLAQGIFVFIAHFWSAFGFVHASNILHKQ 827
Cdd:cd18605 2 ILILLSLILMQASRNLIDFWLSYWVSHSNNSFFNFINDSFNFFLT-VYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 828 LLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIYVSVQM 907
Cdd:cd18605 81 LLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 908 FYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNRWLAIRLELVGNLTV 987
Cdd:cd18605 161 YYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVLIV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 988 FF---SALMMVIYRDTLSGDTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYT 1044
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; ... |
94-381 |
3.55e-84 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350040 [Multi-domain] Cd Length: 309 Bit Score: 277.45 E-value: 3.55e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 94 FLLKLVNDIFTFVSPQLLK-LLISFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKKA 172
Cdd:cd18596 3 ALLAVLSSVLSFAPPFFLNrLLRYLEDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 173 LTLSNLA-------------------RKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLA 233
Cdd:cd18596 83 LRRRDKSgssksseskkkdkeededeKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 234 GVGVMVLVIPINAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCV 313
Cdd:cd18596 163 GLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578818931 314 VIFVFQLTPVLVSVVTFSVYVLVdSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 381
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 ... |
93-381 |
8.17e-84 |
|
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: 275.87 E-value: 8.17e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 93 SFLLKLVNDIFTFVSPQLLKLLISFASDR-----DTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMAS 167
Cdd:cd18597 2 AGLLKLLADVLQVLSPLLLKYLINFVEDAylggpPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 168 VYKKALTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAI 247
Cdd:cd18597 82 IYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 248 LSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSV 327
Cdd:cd18597 162 LMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASM 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 578818931 328 VTFSVYVLVdsNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 381
Cdd:cd18597 242 LSFITYYAT--GHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
93-381 |
1.18e-77 |
|
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: 258.30 E-value: 1.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 93 SFLLKLVNDIFTFVSPQLLKLLISFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKKA 172
Cdd:cd18559 2 FLLIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 173 LTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTKS 252
Cdd:cd18559 82 LRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 253 KTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFSV 332
Cdd:cd18559 162 RQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 578818931 333 YVLVDSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 381
Cdd:cd18559 242 YVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1066-1296 |
1.80e-77 |
|
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: 256.76 E-value: 1.80e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1066 GKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKL 1145
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1146 TIIPQDPILFSGSLRMNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKI 1225
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578818931 1226 LVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELL-QIPGPF 1296
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVF 249
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
95-381 |
2.39e-77 |
|
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: 257.48 E-value: 2.39e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 95 LLKLVNDIFTFVSPQLLKLLISFASDRDTYLWIGYLCAILLFTAALIQSFC-LQCYFQLCfKLGVKVRTAIMASVYKKAL 173
Cdd:cd18598 4 LLKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLsSHYNFQMN-KVSLKVRAALVTAVYRKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 174 TLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTKSK 253
Cdd:cd18598 83 RVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 254 TIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFSVY 333
Cdd:cd18598 163 ALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPVLISILTFATY 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 578818931 334 VLVdsNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 381
Cdd:cd18598 243 VLM--GNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
77-625 |
2.15e-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: 2.15e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 77 WLMKALFKTFYMVLLKSFLLKLVNDIFTFVSPQLLKLLISFASDRDTYLWIGYLCAILLFtAALIQSFCLQCYFQLCFKL 156
Cdd:COG1132 10 RRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLG-LALLRALLSYLQRYLLARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 157 GVKVRTAIMASVYKKALTLSNLARKEYTVGETVNLMSVDAQKLMD-VTNFMHMLWSSVLQIVLSI---FFLWRELGPSVL 232
Cdd:COG1132 89 AQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQfLAHGLPQLVRSVVTLIGALvvlFVIDWRLALIVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 233 AGVGVMVLVIpinAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPS----FRDQVQNLRKKELKNLLAFS 308
Cdd:COG1132 169 LVLPLLLLVL---RLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERelerFREANEELRRANLRAARLSA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 309 QLQCVVIFVFQLTPVLVsvVTFSVYvLVdSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERLEKYL--G 386
Cdd:COG1132 246 LFFPLMELLGNLGLALV--LLVGGL-LV-LSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLdeP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 387 GDDLDTSAIRHDCNFDKAMQFSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIK 466
Cdd:COG1132 322 PEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPV-LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 467 GT-------------TAYVPQQSWIQNGTIKDNILFG-TEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGG 532
Cdd:COG1132 401 GVdirdltleslrrqIGVVPQDTFLFSGTIRENIRYGrPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 533 QKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGS 612
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL---ERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
570
....*....|...
gi 578818931 613 YSALLAKKGEFAK 625
Cdd:COG1132 558 HEELLARGGLYAR 570
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
741-1294 |
3.65e-75 |
|
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: 260.85 E-value: 3.65e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 741 AIGLFSIFFIILAFVMnsVAFIGSNLWLSAWTSDSkifnstdypasqrdmrvgVYGALGLAQGIFVF---IAHFWSAFGF 817
Cdd:COG4988 24 LLGLLSGLLIIAQAWL--LASLLAGLIIGGAPLSA------------------LLPLLGLLLAVLLLralLAWLRERAAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 818 VHASNI---LHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDD----TLPQSLRSWITC--------FLGIISTLV 882
Cdd:COG4988 84 RAAARVkrrLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGyfarYLPQLFLAALVPllilvavfPLDWLSGLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 883 MICmatpvfTIIVIPLGIIyvsvqMFYVSTSRQLRR-LDSVTR-SpiySHFSETVSGLPVIRAF----EHQQRFLKHNE- 955
Cdd:COG4988 164 LLV------TAPLIPLFMI-----LVGKGAAKASRRqWRALARlS---GHFLDRLRGLTTLKLFgrakAEAERIAEASEd 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 956 VRIDT--------NQKCVFSWITSnrwLAI---------RLeLVGNLTvFFSALMMVI-----Y---RDtlsgdtvgfvL 1010
Cdd:COG4988 230 FRKRTmkvlrvafLSSAVLEFFAS---LSIalvavyigfRL-LGGSLT-LFAALFVLLlapefFlplRD----------L 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1011 SNAlnitqtlnWLVRMTseietNIVAVERITEYtkVENEAPWVTDKRPPPDWPSKGKIQFNNYQVRYrPELDLVLRGITC 1090
Cdd:COG4988 295 GSF--------YHARAN-----GIAAAEKIFAL--LDAPEPAAPAGTAPLPAAGPPSIELEDVSFSY-PGGRPALDGLSL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1091 DIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNLDPFN-NY 1169
Cdd:COG4988 359 TIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRpDA 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1170 SDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQN 1249
Cdd:COG4988 439 SDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR 518
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 578818931 1250 EFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPG 1294
Cdd:COG4988 519 LAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
743-1044 |
3.56e-74 |
|
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: 249.40 E-value: 3.56e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 743 GLFSIFFIILAFVMNSVAFIGSNLWLSAW------TSDSKIFNSTDYPASQRD-----MRVGVYGALGLAQGIFVFIAHF 811
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWlkqgsgNTTNNVDNSTVDSGNISDnpdlnFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 812 WSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVF 891
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 892 TIIVIPLGIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITS 971
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578818931 972 NRWLAIRLELVGNLTVFFSALMMVIYRDTLSGDTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYT 1044
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1066-1294 |
9.22e-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: 242.13 E-value: 9.22e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1066 GKIQFNNYQVRYRPElDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKL 1145
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1146 TIIPQDPILFSGSLRMNLDPFNNYS-DEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSK 1224
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNAtDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1225 ILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPG 1294
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
743-1044 |
4.50e-72 |
|
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: 243.38 E-value: 4.50e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 743 GLFSIFFIILAFVMNSVAFIGSNLWLSAW----------TSDSKIFNST--DYPASQRDMRVGVYGALGLAQGIFVFIAH 810
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWanleeklndtTDRVQGENSTnvDIEDLDRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 811 FWSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPV 890
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 891 FTIIVIPLGIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWIT 970
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578818931 971 SNRWLAIRLELVGNLTVFFSALMMVIYRDTLSGDTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYT 1044
Cdd:cd18601 241 TSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEYS 314
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
74-625 |
6.83e-71 |
|
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: 252.45 E-value: 6.83e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 74 PKSWLMKALF---KTFYMVLLKSFLLKLvndiFTFVSPQLLKLLISF---ASDRDTyLWIgylCAILLFTAALIQSF--C 145
Cdd:COG2274 143 GLRWFLRLLRryrRLLLQVLLASLLINL----LALATPLFTQVVIDRvlpNQDLST-LWV---LAIGLLLALLFEGLlrL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 146 LQCYFQLcfKLGVKVRTAIMASVYKKALTLSNLARKEYTVGETVNLMSvDAQKLMD-VTNFMHMLWSSVLQIVLSIFFLW 224
Cdd:COG2274 215 LRSYLLL--RLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREfLTGSLLTALLDLLFVLIFLIVLF 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 225 RELGPSVLAGVGVMVLVIPINAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKK----- 299
Cdd:COG2274 292 FYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKylnar 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 300 -ELKNLLAFSQLqcVVIFVFQLTPVLVsvVTFSVYvLVDSNNIldaqkaftsiTL-----FNIL--RF--PLSMLPMMIS 369
Cdd:COG2274 372 fKLRRLSNLLST--LSGLLQQLATVAL--LWLGAY-LVIDGQL----------TLgqliaFNILsgRFlaPVAQLIGLLQ 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 370 SMLQASVSTERLEKYLGGD---DLDTSAIRHDcNFDKAMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKS 446
Cdd:COG2274 437 RFQDAKIALERLDDILDLPperEEGRSKLSLP-RLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKS 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 447 SLISAMLGEMENVHGHITIKGT-------------TAYVPQQSWIQNGTIKDNILFG-TEFNEKRYQQVLEACALLPDLE 512
Cdd:COG2274 516 TLLKLLLGLYEPTSGRILIDGIdlrqidpaslrrqIGVVLQDVFLFSGTIRENITLGdPDATDEEIIEAARLAGLHDFIE 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 513 MLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHF 592
Cdd:COG2274 596 ALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENL---RRLLKGRTVIIIAHRLST 672
|
570 580 590
....*....|....*....|....*....|...
gi 578818931 593 LPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAK 625
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 ... |
95-381 |
3.70e-69 |
|
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: 234.82 E-value: 3.70e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 95 LLKLVNDIFTFVSPQLLKLLISFASDR------------------DTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKL 156
Cdd:cd18591 4 ILKLLGDLLGFVGPLCISGIVDYVEENtysssnstdklsvsyvtvEEFFSNGYVLAVILFLALLLQATFSQASYHIVIRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 157 GVKVRTAIMASVYKKALTLS--NLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAG 234
Cdd:cd18591 84 GIRLKTALQAMIYEKALRLSswNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 235 VGVMVLVIPINAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVV 314
Cdd:cd18591 164 AALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSLM 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578818931 315 IFVFQLTPVLVSVVTFSVYVLVDSNNiLDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 381
Cdd:cd18591 244 TFLTQASPILVTLVTFGLYPYLEGEP-LTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
845-1297 |
5.14e-68 |
|
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: 240.44 E-value: 5.14e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 845 TGRIVNRFAGDISTVDDTLpqsLRSW------------ITCFLGIIS-TLVMICMATPVFTIIVIPLgiiyvsvqMFYVS 911
Cdd:COG4987 111 SGDLLNRLVADVDALDNLY---LRVLlpllvallvilaAVAFLAFFSpALALVLALGLLLAGLLLPL--------LAARL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 912 TSRQLRRLdSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKH---NEVRIDTNQKcvfswiTSNRWLAIR---LELVGNL 985
Cdd:COG4987 180 GRRAGRRL-AAARAALRARLTDLLQGAAELAAYGALDRALARldaAEARLAAAQR------RLARLSALAqalLQLAAGL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 986 TVFFSALMMV--IYRDTLSG-DTVGFVLSnALNITQTLNWLVRMTSEIETNIVAVERITEytkVENEAPWVTDKRPPPDW 1062
Cdd:COG4987 253 AVVAVLWLAAplVAAGALSGpLLALLVLA-ALALFEALAPLPAAAQHLGRVRAAARRLNE---LLDAPPAVTEPAEPAPA 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1063 PSKGKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLR 1142
Cdd:COG4987 329 PGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLR 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1143 EKLTIIPQDPILFSGSLRMNL---DPfnNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRAL 1219
Cdd:COG4987 409 RRIAVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARAL 486
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578818931 1220 LRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFY 1297
Cdd:COG4987 487 LRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYR 564
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
798-1290 |
7.33e-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: 240.00 E-value: 7.33e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 798 LGLAQGIFVFIAHF---WSAFGFVHAsniLHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCF 874
Cdd:TIGR02203 63 LAVLRGICSFVSTYllsWVSNKVVRD---IRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRET 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 875 LGIIS-TLVMICMATPVFTIIVIPLGIIYVSVQMFyvstSRQLRRLDS---VTRSPIYSHFSETVSGLPVIRAFEHQ--- 947
Cdd:TIGR02203 140 LTVIGlFIVLLYYSWQLTLIVVVMLPVLSILMRRV----SKRLRRISKeiqNSMGQVTTVAEETLQGYRVVKLFGGQaye 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 948 -QRFLKHNEvridtnqkcvfswitSNRWLAIRLELVGNLT------VFFSALMMVIY-------RDTLS-GDTVGFVLSn 1012
Cdd:TIGR02203 216 tRRFDAVSN---------------RNRRLAMKMTSAGSISspitqlIASLALAVVLFialfqaqAGSLTaGDFTAFITA- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1013 ALNITQTLNWLVRMTSEIETNIVAVERITEYTKVENEAPwvTDKRPPPDwpSKGKIQFNNYQVRYRPELDLVLRGITCDI 1092
Cdd:TIGR02203 280 MIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKD--TGTRAIER--ARGDVEFRNVTFRYPGRDRPALDSISLVI 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1093 GSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNL---DPfNNY 1169
Cdd:TIGR02203 356 EPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT-EQA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1170 SDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQN 1249
Cdd:TIGR02203 435 DRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALER 514
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 578818931 1250 EFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELL 1290
Cdd:TIGR02203 515 LMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELL 555
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1068-1290 |
1.41e-63 |
|
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: 215.94 E-value: 1.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTI 1147
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1148 IPQDPILFSGSLRMNL---DPfnNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSK 1224
Cdd:cd03251 81 VSQDVFLFNDTVAENIaygRP--GATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 1225 ILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELL 1290
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELL 224
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
797-1299 |
5.18e-62 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 223.44 E-value: 5.18e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 797 ALGLAQGIFV--FIA---HFWSAFGFVHASNILHKQL----LNNILRAPMRFFDTTPTGRIVNRFAGDISTVDD----TL 863
Cdd:PRK10790 64 VAGLAAAYVGlqLLAaglHYAQSLLFNRAAVGVVQQLrtdvMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDlyvtVV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 864 PQSLRSwiTCFLGIIstLV--------MICMATPVFTIIVIPLgIIYvsvQMFYVSTSRQLRRLdsvtRSPIYSHFSETV 935
Cdd:PRK10790 144 ATVLRS--AALIGAM--LVamfsldwrMALVAIMIFPAVLVVM-VIY---QRYSTPIVRRVRAY----LADINDGFNEVI 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 936 SGLPVIRAFEHQQRFLK--------HNEVRIDTnqkcvfswitsnrwlaIRLE--LVGNLTVFFSAL----MMVIYRDTL 1001
Cdd:PRK10790 212 NGMSVIQQFRQQARFGErmgeasrsHYMARMQT----------------LRLDgfLLRPLLSLFSALilcgLLMLFGFSA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1002 SGdTVGF-VLSNALNITQTLNW-LVRMTSE---IETNIVAVERITEYTKVENEaPWVTDKRPPpdwpSKGKIQFNNYQVR 1076
Cdd:PRK10790 276 SG-TIEVgVLYAFISYLGRLNEpLIELTTQqsmLQQAVVAGERVFELMDGPRQ-QYGNDDRPL----QSGRIDIDNVSFA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1077 YRPElDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFS 1156
Cdd:PRK10790 350 YRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLA 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1157 GSLRMNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVD 1236
Cdd:PRK10790 429 DTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578818931 1237 LETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFYFM 1299
Cdd:PRK10790 509 SGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQM 571
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
95-382 |
6.23e-61 |
|
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: 210.57 E-value: 6.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 95 LLKLVNDIFTFVSPQLLKLLI-SFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKKAL 173
Cdd:cd18594 4 ILLFLEESLKIVQPLLLGRLVaYFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 174 TLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTKSK 253
Cdd:cd18594 84 KLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 254 TIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFSVY 333
Cdd:cd18594 164 KYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPY 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 578818931 334 VLvdSNNILDAQKAFTSITLFNILRFPLSM-LPMMISSMLQASVSTERLE 382
Cdd:cd18594 244 VL--TGNTLTARKVFTVISLLNALRMTITRfFPESIQTLSESRVSLKRIQ 291
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
405-606 |
1.86e-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: 1.86e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 405 MQFSEASFTWEHDSeATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHI-----------------TIKG 467
Cdd:cd03290 1 VQVTNGYFSWGSGL-ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 468 TTAYVPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNL 547
Cdd:cd03290 80 SVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578818931 548 DIYLLDDPLSAVDAHVGKHIFNKvlgpnGLLK-----GKTRLLVTHSMHFLPQVDEIVVLGNGT 606
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQE-----GILKflqddKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
799-1299 |
2.45e-59 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 218.44 E-value: 2.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 799 GLAQGIFVFiahfwsAFGFVHASniLHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGII 878
Cdd:TIGR00958 219 GLRGGSFNY------TMARINLR--IREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 879 STLVMICMATPVFTII-VIPLGIIYVSVQMF---YVSTSRQLRrlDSVTRSPIYSHfsETVSGLPVIRAF--EHQ--QRF 950
Cdd:TIGR00958 291 GLLGFMLWLSPRLTMVtLINLPLVFLAEKVFgkrYQLLSEELQ--EAVAKANQVAE--EALSGMRTVRSFaaEEGeaSRF 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 951 LKHNEVRIDTNQK-----CVFSWITSNRWLAIRLelvgnlTVFFSALMMVIYRDTLSGDTVGFVLSNaLNITQTLNWLVR 1025
Cdd:TIGR00958 367 KEALEETLQLNKRkalayAGYLWTTSVLGMLIQV------LVLYYGGQLVLTGKVSSGNLVSFLLYQ-EQLGEAVRVLSY 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1026 MTSEIETNIVAVERITEYTKVENEAPWVTDKRPPPDwpsKGKIQFNNYQVRY--RPELdLVLRGITCDIGSMEKIGVVGR 1103
Cdd:TIGR00958 440 VYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNL---EGLIEFQDVSFSYpnRPDV-PVLKGLTFTLHPGEVVALVGP 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1104 TGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNLD-PFNNYSDEEIWKALELAH 1182
Cdd:TIGR00958 516 SGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPDEEIMAAAKAAN 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1183 LKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTiqNEFAHCTVITIAHR 1262
Cdd:TIGR00958 596 AHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHR 673
|
490 500 510
....*....|....*....|....*....|....*..
gi 578818931 1263 LHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFYFM 1299
Cdd:TIGR00958 674 LSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1068-1299 |
3.81e-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: 203.23 E-value: 3.81e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELDlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTI 1147
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1148 IPQDPILFSGSLRMNL---DPfnNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSK 1224
Cdd:cd03253 80 VPQDTVLFNDTIGYNIrygRP--DATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 1225 ILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFYFM 1299
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
991-1291 |
8.48e-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: 211.22 E-value: 8.48e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 991 ALMMVIYRDTLSGD-TVG-FVLSNA--LNITQTLNWLVRMTSEIETNIVAVERITEYTKVENEapwVTDKRPPPDWPSK- 1065
Cdd:COG5265 279 AMMLMAAQGVVAGTmTVGdFVLVNAylIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPE---VADAPDAPPLVVGg 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1066 GKIQFNNYQVRYRPElDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKL 1145
Cdd:COG5265 356 GEVRFENVSFGYDPE-RPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAI 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1146 TIIPQDPILFSGSLRMNLdpfnNY-----SDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALL 1220
Cdd:COG5265 435 GIVPQDTVLFNDTIAYNI----AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLL 510
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578818931 1221 RKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQ 1291
Cdd:COG5265 511 KNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLA 581
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1068-1279 |
1.76e-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: 196.06 E-value: 1.76e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTI 1147
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1148 IPQDPILFSGSLRMNLdpfnnysdeeiwkalelahlksfvaslqlglshevteaggnLSIGQRQLLCLGRALLRKSKILV 1227
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578818931 1228 LDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGK 1279
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1068-1303 |
2.62e-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: 198.15 E-value: 2.62e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRY--RPELdLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKL 1145
Cdd:cd03249 1 IEFKNVSFRYpsRPDV-PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1146 TIIPQDPILFSGSLRMNL---DpfNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRK 1222
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIrygK--PDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1223 SKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFYFMAKE 1302
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
.
gi 578818931 1303 A 1303
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, ... |
93-381 |
1.01e-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: 198.55 E-value: 1.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 93 SFLLKLVNDIFTFVSPQ-LLKLLISFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKK 171
Cdd:cd18592 2 SILLLLISLIFGFIGPTiLIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 172 ALTLSNLarKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTK 251
Cdd:cd18592 82 ILRLRSL--GDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 252 SKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFS 331
Cdd:cd18592 160 TGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 578818931 332 VYVLvdSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 381
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 ... |
1068-1299 |
1.98e-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: 1.98e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTI 1147
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1148 IPQDPILFSGSLRMNL---DPfnNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSK 1224
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 1225 ILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFYFM 1299
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
102-381 |
7.26e-54 |
|
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: 190.12 E-value: 7.26e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 102 IFTF-------VSPQLLKLLIS-FASDRDTY-LWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKKA 172
Cdd:cd18593 4 IFLFleeairvVQPIFLGKLIRyFEGNGSSIsLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIYRKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 173 LTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTKS 252
Cdd:cd18593 84 LRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFGKLF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 253 KTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFSV 332
Cdd:cd18593 164 SKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTFLA 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 578818931 333 YVLVDsnNILDAQKAFTSITLFNILRFPLSM-LPMMISSMLQASVSTERL 381
Cdd:cd18593 244 YILLG--NILTAERVFVTMALYNAVRLTMTLfFPFAIQFGSELSVSIRRI 291
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
404-621 |
7.79e-54 |
|
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: 198.44 E-value: 7.79e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 404 AMQFSEASFTWEhDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-------------TA 470
Cdd:COG4988 336 SIELEDVSFSYP-GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpaswrrqIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 471 YVPQQSWIQNGTIKDNILFGT-EFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDI 549
Cdd:COG4988 415 WVPQNPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPL 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578818931 550 YLLDDPLSAVDAHVGKHIFNKVLgpnGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKG 621
Cdd:COG4988 495 LLLDEPTAHLDAETEAEILQALR---RLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
748-1043 |
9.61e-53 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 187.04 E-value: 9.61e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 748 FFIILAFVMNSVAFIGSNLWLSAWTSDSKifnstDYPASQRDMRVGVYGALGLAQGIFVFIAHFWSAFGFVHASNILHKQ 827
Cdd:cd18559 2 FLLIKLVLCNHVFSGPSNLWLLLWFDDPV-----NGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 828 LLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIvIPLGIIYVSVQM 907
Cdd:cd18559 77 LYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVG-IPLGLLYVPVNR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 908 FYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDtNQKCVFSWITSNRWLAIRLELVGNLTV 987
Cdd:cd18559 156 VYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIV 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 988 FFSALMMVIYRDTLSGdTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEY 1043
Cdd:cd18559 235 LFASFFAYVSRHSLAG-LVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLER 289
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
154-625 |
1.30e-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: 194.98 E-value: 1.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 154 FKLGVKVRTaimaSVYKKALTLSNLARKEYTVGETVNLMSVDAQKLMDVtnFMHML---WSSVLQIVLSIFFLWR---EL 227
Cdd:COG4987 84 LRLLADLRV----RLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNL--YLRVLlplLVALLVILAAVAFLAFfspAL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 228 GPSVLAGVGVMVLVIPINAILSTKSKTIQVKNMKNkDKRLKIMnEILSGIKILKYFAWEPSFRDQVQNL------RKKEL 301
Cdd:COG4987 158 ALVLALGLLLAGLLLPLLAARLGRRAGRRLAAARA-ALRARLT-DLLQGAAELAAYGALDRALARLDAAearlaaAQRRL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 302 KNLLAFSQLqcVVIFVFQLTpvLVSVVTFSVYvLVDSNNILDAQKA---FTSITLFNILrfplSMLPMMISSMLQASVST 378
Cdd:COG4987 236 ARLSALAQA--LLQLAAGLA--VVAVLWLAAP-LVAAGALSGPLLAllvLAALALFEAL----APLPAAAQHLGRVRAAA 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 379 ERLEKyLGGDDLDTSAIRHDCNFDK--AMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEM 456
Cdd:COG4987 307 RRLNE-LLDAPPAVTEPAEPAPAPGgpSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 457 ENVHGHITIKGT-------------TAYVPQQSWIQNGTIKDNILFGT-EFNEKRYQQVLEACALLPDLEMLPGGDLAEI 522
Cdd:COG4987 386 DPQSGSITLGGVdlrdldeddlrrrIAVVPQRPHLFDTTLRENLRLARpDATDEELWAALERVGLGDWLAALPDGLDTWL 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 523 GEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLgpnGLLKGKTRLLVTHSMHFLPQVDEIVVL 602
Cdd:COG4987 466 GEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLL---EALAGRTVLLITHRLAGLERMDRILVL 542
|
490 500
....*....|....*....|...
gi 578818931 603 GNGTIVEKGSYSALLAKKGEFAK 625
Cdd:COG4987 543 EDGRIVEQGTHEELLAQNGRYRQ 565
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
422-630 |
3.60e-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: 185.06 E-value: 3.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQNGTIKDNILFGTEFNEKRYQQV 501
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 502 LEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLGPngLLKGK 581
Cdd:cd03291 133 VKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCK--LMANK 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 578818931 582 TRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAKNLKTF 630
Cdd:cd03291 211 TRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGY 259
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1066-1281 |
2.27e-51 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 180.48 E-value: 2.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1066 GKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKL 1145
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1146 TIIPQDPILFSGSLRMNLDPFNNY-SDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSK 1224
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 578818931 1225 ILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKII 1281
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
874-1305 |
1.32e-50 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 189.40 E-value: 1.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 874 FLGIISTLVMICMATPV---FTIIVIPLGIIYVSVQMFYVSTSRQLRRldSVTR--SPIYSHFSETVSGLPVIRAF---E 945
Cdd:PRK13657 138 LATLVALVVLLPLALFMnwrLSLVLVVLGIVYTLITTLVMRKTKDGQA--AVEEhyHDLFAHVSDAIGNVSVVQSYnriE 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 946 HQQRFLKHNEVRIDTNQKCVFSWitsnrWlairlELVGNLTVFFSAL-MMVIY--------RDTLS-GDTVGFVLSNALN 1015
Cdd:PRK13657 216 AETQALRDIADNLLAAQMPVLSW-----W-----ALASVLNRAASTItMLAILvlgaalvqKGQLRvGEVVAFVGFATLL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1016 ITQtlnwLVRMTSEIETNIVAVERITEYTKVENEAPWVTDkrpPPDWPS----KGKIQFNNYQVRY---RPELDlvlrGI 1088
Cdd:PRK13657 286 IGR----LDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRD---PPGAIDlgrvKGAVEFDDVSFSYdnsRQGVE----DV 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1089 TCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNL---DP 1165
Cdd:PRK13657 355 SFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIrvgRP 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1166 fnNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQT 1245
Cdd:PRK13657 435 --DATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKA 512
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1246 TIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFYFMAKEAGI 1305
Cdd:PRK13657 513 ALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQGM 572
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
833-1301 |
2.39e-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: 184.77 E-value: 2.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 833 LRAPMRFFDTTPTGRIVNRFAGdISTVDDTLPQS-LRSWITCFLGIISTLVMIC----MATPVFTIIVIPLGIIYVSvQM 907
Cdd:TIGR03797 220 LRLPVSFFRQYSTGDLASRAMG-ISQIRRILSGStLTTLLSGIFALLNLGLMFYyswkLALVAVALALVAIAVTLVL-GL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 908 FYVSTSRQLRRLDSvtrsPIYSHFSETVSGLPVIRAFEHQQRFLkhnevridtnqkcvFSW---ITSNRWLAIRLELVGN 984
Cdd:TIGR03797 298 LQVRKERRLLELSG----KISGLTVQLINGISKLRVAGAENRAF--------------ARWaklFSRQRKLELSAQRIEN 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 985 -LTVFFSAL----MMVIY--------RDTLS-GDTVGF------VLSNALNITQTLnwlvrmtseieTNIVAVERITEYT 1044
Cdd:TIGR03797 360 lLTVFNAVLpvltSAALFaaaisllgGAGLSlGSFLAFntafgsFSGAVTQLSNTL-----------ISILAVIPLWERA 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1045 K-VENEAPWVTDKRPPPDWPSkGKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLtnclFRIL---E 1120
Cdd:TIGR03797 429 KpILEALPEVDEAKTDPGKLS-GAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTL----LRLLlgfE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1121 AAG-GQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVT 1199
Cdd:TIGR03797 504 TPEsGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVIS 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1200 EAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETdnliQTTIQNEFA--HCTVITIAHRLHTIMDSDKVMVLDN 1277
Cdd:TIGR03797 584 EGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRT----QAIVSESLErlKVTRIVIAHRLSTIRNADRIYVLDA 659
|
490 500
....*....|....*....|....
gi 578818931 1278 GKIIECGSPEELLQIPGPFYFMAK 1301
Cdd:TIGR03797 660 GRVVQQGTYDELMAREGLFAQLAR 683
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
829-1297 |
1.18e-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: 1.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 829 LNNILRAPMRFFDTTPTGRIVNRFAgDISTVDDTLPQSLRS-----WITCFLGIIstLVMICMATPVFTIIVIPlgiIYV 903
Cdd:TIGR01193 236 IKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTILSlfldmWILVIVGLF--LVRQNMLLFLLSLLSIP---VYA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 904 SVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNR-WLAIR--LE 980
Cdd:TIGR01193 310 VIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQgQQAIKavTK 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 981 LVGNLTVFFSALMMVIYRDTLSGDTVGFvlsNAL--NITQTLNWLVRMTSEIETNIVAVERITEYTKVENEapWVTDKRP 1058
Cdd:TIGR01193 390 LILNVVILWTGAYLVMRGKLTLGQLITF---NALlsYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSE--FINKKKR 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1059 PPDWPSKGKIQFNNYQVRYRPElDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGL 1138
Cdd:TIGR01193 465 TELNNLNGDIVINDVSYSYGYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDR 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1139 HDLREKLTIIPQDPILFSGSLRMNLDPFN--NYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLG 1216
Cdd:TIGR01193 544 HTLRQFINYLPQEPYIFSGSILENLLLGAkeNVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALA 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1217 RALLRKSKILVLDEATAAVDLETDNLIQTTIQNeFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPF 1296
Cdd:TIGR01193 624 RALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFY 702
|
.
gi 578818931 1297 Y 1297
Cdd:TIGR01193 703 A 703
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
824-1290 |
2.44e-47 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 179.83 E-value: 2.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 824 LHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIyV 903
Cdd:PRK11176 100 MRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVIAPI-V 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 904 SVQMFYVSTS-RQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQ----RFlkhNEVRIDTNQ---KCVFSWITSNrwl 975
Cdd:PRK11176 179 SIAIRVVSKRfRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEvetkRF---DKVSNRMRQqgmKMVSASSISD--- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 976 aIRLELVGNLtvffsALMMVIY-------RDTLSGDTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYTKVEN 1048
Cdd:PRK11176 253 -PIIQLIASL-----ALAFVLYaasfpsvMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQ 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1049 EAPwvTDKRPPPdwPSKGKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIII 1128
Cdd:PRK11176 327 EKD--EGKRVIE--RAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILL 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1129 DGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNLD--PFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLS 1206
Cdd:PRK11176 403 DGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAyaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLS 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1207 IGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSP 1286
Cdd:PRK11176 483 GGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTH 562
|
....
gi 578818931 1287 EELL 1290
Cdd:PRK11176 563 AELL 566
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1066-1290 |
4.78e-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: 4.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1066 GKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGgQIIIDGVDIASIGLHDLREKL 1145
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEG-DIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1146 TIIPQDPILFSGSLRMNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKI 1225
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 1226 LVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELL 1290
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1096-1299 |
3.96e-45 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 173.11 E-value: 3.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1096 EKIGVVGRTGAGKSSLTNCLFRILeAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNL---DPfnNYSDE 1172
Cdd:PRK11174 377 QRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllgNP--DASDE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1173 EIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFA 1252
Cdd:PRK11174 454 QLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR 533
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 578818931 1253 HCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFYFM 1299
Cdd:PRK11174 534 RQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1065-1280 |
1.82e-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: 1.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1065 KGKIQFNNYQVRYRPELD-LVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLRE 1143
Cdd:cd03248 9 KGIVKFQNVTFAYPTRPDtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1144 KLTIIPQDPILFSGSLRMNLD-PFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRK 1222
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578818931 1223 SKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKI 1280
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
407-625 |
1.57e-41 |
|
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: 152.77 E-value: 1.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 407 FSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-------------TAYVP 473
Cdd:cd03251 3 FKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqIGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 474 QQSWIQNGTIKDNILFGTEfNEKRyQQVLEAC--ALLPDLEM-LPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIY 550
Cdd:cd03251 83 QDVFLFNDTVAENIAYGRP-GATR-EEVEEAAraANAHEFIMeLPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 551 LLDDPLSAVDAhVGKHIFNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAK 625
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 ... |
406-621 |
6.67e-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: 150.84 E-value: 6.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 406 QFSEASFTWEHDsEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYV 472
Cdd:cd03254 4 EFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDirdisrkslrsmiGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 473 PQQSWIQNGTIKDNILFGTEFN-EKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYL 551
Cdd:cd03254 83 LQDTFLFSGTIMENIRLGRPNAtDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 552 LDDPLSAVDAHVGKHIFNKVLgpnGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKG 621
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALE---KLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1053-1275 |
1.55e-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: 158.22 E-value: 1.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1053 VTDKRPPPDWPSKGK-------IQFNNYQVRYrPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQ 1125
Cdd:TIGR02857 300 VLDAAPRPLAGKAPVtaapassLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGS 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1126 IIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNLDPFNNY-SDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGN 1204
Cdd:TIGR02857 379 IAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAG 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578818931 1205 LSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVL 1275
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
405-605 |
2.32e-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: 147.14 E-value: 2.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 405 MQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-------------TAY 471
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdlrdldleslrknIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 472 VPQQSWIQNGTIKDNILfgtefnekryqqvleacallpdlemlpggdlaeigekginlSGGQKQRISLARATYQNLDIYL 551
Cdd:cd03228 81 VPQDPFLFSGTIRENIL-----------------------------------------SGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 578818931 552 LDDPLSAVDAHVGKHIFNKVLgpnGLLKGKTRLLVTHSMHFLPQVDEIVVLGNG 605
Cdd:cd03228 120 LDEATSALDPETEALILEALR---ALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
406-625 |
6.90e-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: 148.15 E-value: 6.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 406 QFSEASFTWeHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAYV 472
Cdd:cd03253 2 EFENVTFAY-DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 473 PQQSWIQNGTIKDNILFG----TEfnekryQQVLEAC--ALLPDLEM-LPGGDLAEIGEKGINLSGGQKQRISLARATYQ 545
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGrpdaTD------EEVIEAAkaAQIHDKIMrFPDGYDTIVGERGLKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 546 NLDIYLLDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAK 625
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAAL---RDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAE 231
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
406-611 |
1.02e-39 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 146.97 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 406 QFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTA-------------YV 472
Cdd:cd03245 4 EFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIrqldpadlrrnigYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 473 PQQSWIQNGTIKDNILFG-TEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYL 551
Cdd:cd03245 84 PQDVTLFYGTLRDNITLGaPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 552 LDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKG 611
Cdd:cd03245 164 LDEPTSAMDMNSEERLKERL---RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
845-1263 |
1.05e-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: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 845 TGRIVNRFAGDISTVDDTLPQSLRSWITCFL-GIISTLVMICMATPVFTIIVIPLGIIYVSVQMFYVSTSRQLRRLDSVT 923
Cdd:TIGR02868 109 RGDLLGRLGADVDALQDLYVRVIVPAGVALVvGAAAVAAIAVLSVPAALILAAGLLLAGFVAPLVSLRAARAAEQALARL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 924 RSPIYSHFSETVSGLPVIRAFEHQQRFLK------HNEVRIDTNQKCVFSWITSNRWLAIRLELVGNLTVFFSALMmviy 997
Cdd:TIGR02868 189 RGELAAQLTDALDGAAELVASGALPAALAqveeadRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVA---- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 998 RDTLSGDTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYTKVENEAPWVTDKRPPPDWPSKGKIQFNNYQVRY 1077
Cdd:TIGR02868 265 DGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGY 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1078 rPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSG 1157
Cdd:TIGR02868 345 -PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDT 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1158 SLRMNL---DPfnNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAA 1234
Cdd:TIGR02868 424 TVRENLrlaRP--DATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEH 501
|
410 420
....*....|....*....|....*....
gi 578818931 1235 VDLETDNLIQTTIQNEFAHCTVITIAHRL 1263
Cdd:TIGR02868 502 LDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
747-1017 |
3.65e-39 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 147.40 E-value: 3.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 747 IFFIILAFVMNSVAFIGSNLWLSAWTSDskIFNSTDYPASQRDMRVGVYGALGLAQGIFVFIAHFWSAFGFVHASNILHK 826
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDV--LLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 827 QLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIYVSVQ 906
Cdd:pfam00664 79 KLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 907 MFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNRWLAIRLELVGNLT 986
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLS 238
|
250 260 270
....*....|....*....|....*....|....
gi 578818931 987 VFFSALM---MVIYRDTLSGDTVGFVLSNALNIT 1017
Cdd:pfam00664 239 YALALWFgayLVISGELSVGDLVAFLSLFAQLFG 272
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
425-637 |
5.20e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 154.62 E-value: 5.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 425 VNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMeNVHGHITIKGT-------TAYVPQQSWI-QN-----GTIKDNILFG- 490
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIelreldpESWRKHLSWVgQNpqlphGTLRDNVLLGn 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 491 TEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNK 570
Cdd:PRK11174 448 PDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578818931 571 VlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAknlkTFLRHTGPE 637
Cdd:PRK11174 528 L---NAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFA----TLLAHRQEE 587
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1034-1297 |
6.87e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 154.21 E-value: 6.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1034 IVAVERITEYTKVENEAPWVTDKRPPPDwpsKGKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTN 1113
Cdd:PRK11160 308 IASARRINEITEQKPEVTFPTTSTAAAD---QVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1114 CLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNL---DPfnNYSDEEIWKALELAHLKSFVASL 1190
Cdd:PRK11160 385 LLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKLLEDD 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1191 QlGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSD 1270
Cdd:PRK11160 463 K-GLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFD 541
|
250 260
....*....|....*....|....*..
gi 578818931 1271 KVMVLDNGKIIECGSPEELLQIPGPFY 1297
Cdd:PRK11160 542 RICVMDNGQIIEQGTHQELLAQQGRYY 568
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
731-1040 |
1.70e-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: 144.17 E-value: 1.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 731 KFSIYLEYLQA-----IGLFSIFFIILAFVMNSVA---FIGSNLWLSAWTSDSKIFNSTDYPASQRDMRVGVYGALGLAQ 802
Cdd:cd18600 2 TWNTYLRYITShksliFVLILCLVIFAIEVAASLVglwLLRSQADRVNTTRPESSSNTYAVIVTFTSSYYVFYIYVGVAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 803 GIFVFiaHFWSAFGFVHA----SNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGII 878
Cdd:cd18600 82 SLLAM--GFFRGLPLVHTlitvSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 879 STLVMICMATPVFTIIVIPLGIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRI 958
Cdd:cd18600 160 GAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 959 DTNQKCVFSWITSNRWLAIRLELVgnLTVFFSALMMVIYRDTLSGD-TVGFVLSNALNITQTLNWLVRMTSEIETNIVAV 1037
Cdd:cd18600 240 NLHTANWFLYLSTLRWFQMRIEMI--FVIFFTAVTFISIGTTGDGEgRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSV 317
|
...
gi 578818931 1038 ERI 1040
Cdd:cd18600 318 SRI 320
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
404-602 |
2.16e-37 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 148.97 E-value: 2.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 404 AMQFSEASFTWEhDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------A 470
Cdd:TIGR02857 321 SLEFSGVSVAYP-GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPladadadswrdqiA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 471 YVPQQSWIQNGTIKDNILFGT-EFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDI 549
Cdd:TIGR02857 400 WVPQHPFLFAGTIAENIRLARpDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578818931 550 YLLDDPLSAVDAHVGKHIFNKVLgpnGLLKGKTRLLVTHSMHFLPQVDEIVVL 602
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALR---ALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
423-628 |
1.22e-36 |
|
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: 138.83 E-value: 1.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 423 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYVPQQSWIQNGTIKDNILF 489
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDirdlnlrwlrsqiGLVSQEPVLFDGTIAENIRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 490 GTefNEKRYQQVLEAC--ALLPD-LEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKH 566
Cdd:cd03249 100 GK--PDATDEEVEEAAkkANIHDfIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578818931 567 IFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAKNLK 628
Cdd:cd03249 178 VQEAL---DRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVK 236
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1068-1280 |
6.94e-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: 131.57 E-value: 6.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTI 1147
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1148 IPQDPILFSGSLRMNLdpfnnysdeeiwkalelahlksfvaslqlglshevteaggnLSIGQRQLLCLGRALLRKSKILV 1227
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 578818931 1228 LDEATAAVDLETDNLIQTTIQN-EFAHCTVITIAHRLHTIMDSDKVMVLDNGKI 1280
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
402-612 |
2.08e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 129.82 E-value: 2.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 402 DKAMQFSEASFTWehDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--------AYVP 473
Cdd:COG1121 4 MPAIELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPprrarrriGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 474 QQSWIQNG---TIKDNILFGT--------EFNEKRYQQVLEAcallpdLEMLPGGDLAE--IGEkginLSGGQKQRISLA 540
Cdd:COG1121 82 QRAEVDWDfpiTVRDVVLMGRygrrglfrRPSRADREAVDEA------LERVGLEDLADrpIGE----LSGGQQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578818931 541 RATYQNLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK-----GKTRLLVTHSMHFLPQ-VDEIVVLgNGTIVEKGS 612
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYE-------LLRelrreGKTILVVTHDLGAVREyFDRVLLL-NRGLVAHGP 221
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
404-625 |
4.70e-33 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 136.49 E-value: 4.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 404 AMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TAY---------- 471
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiADYseaalrqais 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 472 -VPQQSWIQNGTIKDNILFGT-EFNEKRYQQVLEACALLPDLEMLPGGDlAEIGEKGINLSGGQKQRISLARATYQNLDI 549
Cdd:PRK11160 418 vVSQRVHLFSATLRDNLLLAApNASDEALIEVLQQVGLEKLLEDDKGLN-AWLGEGGRQLSGGEQRRLGIARALLHDAPL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 550 YLLDDPLSAVDAHVGKHIFNkvlgpngLL----KGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAK 625
Cdd:PRK11160 497 LLLDEPTEGLDAETERQILE-------LLaehaQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQ 569
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
272-625 |
8.26e-33 |
|
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: 8.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 272 EILSGIKILKYFAWEPSFRDQVQ----NLRKKELKNLLAfSQLQCVVIFVFQLTpvLVSVVTFSVYVLVDSNNILDAQka 347
Cdd:TIGR01193 339 EDLNGIETIKSLTSEAERYSKIDsefgDYLNKSFKYQKA-DQGQQAIKAVTKLI--LNVVILWTGAYLVMRGKLTLGQ-- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 348 ftSITLFNILRFPLSMLPMMIS---SMLQASVSTERL-EKYL-GGDDLDTSAIRHDCNFDKAMQFSEASFTWEHDSEAtV 422
Cdd:TIGR01193 414 --LITFNALLSYFLTPLENIINlqpKLQAARVANNRLnEVYLvDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNI-L 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 423 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYVPQQSWIQNGTIKDNILF 489
Cdd:TIGR01193 491 SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlkdidrhtlrqfiNYLPQEPYIFSGSILENLLL 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 490 GTEFNEKRyQQVLEACALLP---DLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKH 566
Cdd:TIGR01193 571 GAKENVSQ-DEIWAACEIAEikdDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKK 649
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 567 IFNKVLGpnglLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAK 625
Cdd:TIGR01193 650 IVNNLLN----LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYAS 704
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
90-361 |
1.10e-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: 128.53 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 90 LLKSFLLKLVNDIFTFVSPQLLKLLI-SFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASV 168
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILdVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 169 YKKALTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSV-LAGVGVMVLVIPINAI 247
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLtLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 248 LSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSV 327
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 578818931 328 VTFSVYVLVDSNNILDAQKAFTSITLFNILRFPL 361
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1068-1290 |
1.32e-32 |
|
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: 126.68 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPElDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTI 1147
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1148 IPQDPI--LFSGSLR-------MNLdpfnNYSDEEIWK----ALELahlksfvaslqLGLSHEVTEAGGNLSIGQRQLLC 1214
Cdd:COG1122 80 VFQNPDdqLFAPTVEedvafgpENL----GLPREEIRErveeALEL-----------VGLEHLADRPPHELSGGQKQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1215 LGRALLRKSKILVLDEATAAVDLE-TDNLIQT--TIQNEfaHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELL 1290
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRgRRELLELlkRLNKE--GKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVF 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1068-1284 |
1.40e-31 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 122.04 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGlHDLREKLTI 1147
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1148 IPQDPILFSGSLRMNLdpfnnysdeeiwkalelahlksfvaslqlglshevteaGGNLSIGQRQLLCLGRALLRKSKILV 1227
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 578818931 1228 LDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECG 1284
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1073-1291 |
2.86e-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: 130.02 E-value: 2.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1073 YQVRYRPELDlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIG---LHDLREKLTIIP 1149
Cdd:COG1123 270 YPVRGKGGVR-AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQMVF 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1150 QDPilfSGSL--RMNLdpfnnysDEEIWKALELAHLKSF------VASL--QLGLSHEVTEA-GGNLSIGQRQLLCLGRA 1218
Cdd:COG1123 349 QDP---YSSLnpRMTV-------GDIIAEPLRLHGLLSRaerrerVAELleRVGLPPDLADRyPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1219 LLRKSKILVLDEATAAVDLetdnLIQTTI-------QNEFaHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELL 1290
Cdd:COG1123 419 LALEPKLLILDEPTSALDV----SVQAQIlnllrdlQREL-GLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVF 493
|
.
gi 578818931 1291 Q 1291
Cdd:COG1123 494 A 494
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
422-625 |
4.00e-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: 4.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYVPQQSWIQNGTIKDNIL 488
Cdd:TIGR02204 356 LDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDlrqldpaelrarmALVPQDPVLFAASVMENIR 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 489 FGTEfnEKRYQQVLEACALLPDLEM---LPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHvGK 565
Cdd:TIGR02204 436 YGRP--DATDEEVEAAARAAHAHEFisaLPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAE-SE 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 566 HIFNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAK 625
Cdd:TIGR02204 513 QLVQQAL--ETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYAR 570
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1058-1291 |
5.53e-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: 5.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1058 PPPdwpsKGKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIG 1137
Cdd:COG4618 325 PRP----KGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1138 LHDLREKLTIIPQDPILFSGSLRMNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGR 1217
Cdd:COG4618 401 REELGRHIGYLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLAR 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 1218 ALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAH-CTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQ 1291
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
185-625 |
1.37e-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: 129.86 E-value: 1.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 185 VGETVNLMsvdaQKLMDVTNFmhmLWSSVLQIVLSIFFLWRELG------PSVlagVGVMVLVIPINAILSTKSKTIQVK 258
Cdd:TIGR01846 235 VGDTVARV----RELEQIRNF---LTGSALTVVLDLLFVVVFLAvmffysPTL---TGVVIGSLVCYALLSVFVGPILRK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 259 NMKNKDKR----LKIMNEILSGIKILKYFAWEPsfrdQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFSVYV 334
Cdd:TIGR01846 305 RVEDKFERsaaaTSFLVESVTGIETIKATATEP----QFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILL 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 335 LVDSNNILDAQKAFTSITLFNIL----RFPLSMLPMMISSMLQASVSTERLekylgGDDLDT-SAIRHD-----CNFDKA 404
Cdd:TIGR01846 381 WFGAHLVIGGALSPGQLVAFNMLagrvTQPVLRLAQLWQDFQQTGIALERL-----GDILNSpTEPRSAglaalPELRGA 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 405 MQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAY 471
Cdd:TIGR01846 456 ITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGvdlaiadpawlrrQMGV 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 472 VPQQSWIQNGTIKDNILFGTEfnEKRYQQVLEACALLPDLEM---LPGGDLAEIGEKGINLSGGQKQRISLARATYQNLD 548
Cdd:TIGR01846 536 VLQENVLFSRSIRDNIALCNP--GAPFEHVIHAAKLAGAHDFiseLPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPR 613
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578818931 549 IYLLDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAK 625
Cdd:TIGR01846 614 ILIFDEATSALDYESEALIMRNM---REICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYAR 687
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
405-612 |
2.22e-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: 120.29 E-value: 2.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 405 MQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG---TT----------AY 471
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiSKiglhdlrsriSI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 472 VPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYL 551
Cdd:cd03244 83 IPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578818931 552 LDDPLSAVDAHVGKHIfNKVLGPNglLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGS 612
Cdd:cd03244 163 LDEATASVDPETDALI-QKTIREA--FKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
522-1297 |
3.90e-30 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 130.15 E-value: 3.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 522 IGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDaHVGKHIFNKVLgpNGLLKGKTRL--LVTHSMHFLPQVDEI 599
Cdd:PTZ00265 573 VGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTI--NNLKGNENRItiIIAHRLSTIRYANTI 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 600 VVLGN-----------------------------------------------GTIVEKGSYSALLAKKG----EFAKNLK 628
Cdd:PTZ00265 650 FVLSNrergstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnagSYIIEQGTHDALMKNKNgiyyTMINNQK 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 629 TFLRHT-------GPEEEATVHDGSE---EEDDDYGLISSVEEIPEDAASITMRRENSFRRTLsrssrsnGRHLKSLRNS 698
Cdd:PTZ00265 730 VSSKKSsnndndkDSDMKSSAYKDSErgyDPDEMNGNSKHENESASNKKSCKMSDENASENNA-------GGKLPFLRNL 802
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 699 LKTRNvnslKEDEELvkgqKLIKKEFIETGKVKFSIYLEYLQAIGLFSIFFIILAFVMNSVaFIGSNLWlsawtsdskiF 778
Cdd:PTZ00265 803 FKRKP----KAPNNL----RIVYREIFSYKKDVTIIALSILVAGGLYPVFALLYAKYVSTL-FDFANLE----------A 863
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 779 NSTDYpasqrdmrvGVYgALGLAQGIFV--FIAHFWSAFGFVHASNILHKQLLNNILRAPMRFFDT---TPtGRIVNRFA 853
Cdd:PTZ00265 864 NSNKY---------SLY-ILVIAIAMFIseTLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHIN 932
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 854 GDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIplGIIYVSVQMFYV----STSRQLRRL---------- 919
Cdd:PTZ00265 933 RDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVAAVLT--GTYFIFMRVFAIrarlTANKDVEKKeinqpgtvfa 1010
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 920 ----DSVTRSPIYShFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNRWL-----AIRLeLVGNLTVFFS 990
Cdd:PTZ00265 1011 ynsdDEIFKDPSFL-IQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLwgfsqSAQL-FINSFAYWFG 1088
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 991 ALMmvIYRDTLSGDTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVER----ITEYTKVEneapwVTDK---RPPPDWP 1063
Cdd:PTZ00265 1089 SFL--IRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKyyplIIRKSNID-----VRDNggiRIKNKND 1161
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1064 SKGKIQFNNYQVRY--RPELDlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAA------------------- 1122
Cdd:PTZ00265 1162 IKGKIEIMDVNFRYisRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtndmtneq 1240
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1123 -----------------------------------GGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNLDpF- 1166
Cdd:PTZ00265 1241 dyqgdeeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-Fg 1319
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1167 -NNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQT 1245
Cdd:PTZ00265 1320 kEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1399
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 1246 TIQN--EFAHCTVITIAHRLHTIMDSDKVMVLDN----GKIIEC-GSPEELLQIPGPFY 1297
Cdd:PTZ00265 1400 TIVDikDKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAhGTHEELLSVQDGVY 1458
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
422-608 |
5.53e-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: 118.79 E-value: 5.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--------AYVPQQS---WIQNGTIKDNIL-- 488
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPlekerkriGYVPQRRsidRDFPISVRDVVLmg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 489 ------FGTEFNEKRYQQVLEAcallpdLEMLPGGDLAE--IGEkginLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 560
Cdd:cd03235 95 lyghkgLFRRLSKADKAKVDEA------LERVGLSELADrqIGE----LSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 578818931 561 AHvGKHIFNKVLgpNGL-LKGKTRLLVTHSMH-FLPQVDEIVVLgNGTIV 608
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 ... |
407-624 |
1.33e-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: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 407 FSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAYVP 473
Cdd:cd03252 3 FEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 474 QQSWIQNGTIKDNILFGTEFNEKRyqQVLEACALLPDLEM---LPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIY 550
Cdd:cd03252 83 QENVLFNRSIRDNIALADPGMSME--RVIEAAKLAGAHDFiseLPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578818931 551 LLDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFA 624
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNM---HDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1033-1294 |
2.69e-29 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 124.82 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1033 NIVavERITE-YTKVE---NEAPWVTD-KRPPPDwpSKGKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAG 1107
Cdd:PRK10789 278 NIV--ERGSAaYSRIRamlAEAPVVKDgSEPVPE--GRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSG 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1108 KSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNL---DPfnNYSDEEIWKALELAHLK 1184
Cdd:PRK10789 354 KSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIalgRP--DATQQEIEHVARLASVH 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1185 SFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLH 1264
Cdd:PRK10789 432 DDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLS 511
|
250 260 270
....*....|....*....|....*....|
gi 578818931 1265 TIMDSDKVMVLDNGKIIECGSPEELLQIPG 1294
Cdd:PRK10789 512 ALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
411-607 |
2.79e-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: 115.39 E-value: 2.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 411 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYVPQQSW 477
Cdd:cd03246 7 SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADisqwdpnelgdhvGYLPQDDE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 478 IQNGTIKDNILfgtefnekryqqvleacallpdlemlpggdlaeigekginlSGGQKQRISLARATYQNLDIYLLDDPLS 557
Cdd:cd03246 87 LFSGSIAENIL-----------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNS 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 578818931 558 AVDaHVGKHIFNKVLGpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTI 607
Cdd:cd03246 126 HLD-VEGERALNQAIA-ALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
420-608 |
9.63e-29 |
|
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: 9.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 420 ATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTA-------------YVPQQSWIQNGTIKDN 486
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLsqwdreelgrhigYLPQDVELFDGTIAEN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 487 IlfgTEFNEKRYQQVLEAcALLPDL-EM---LPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAh 562
Cdd:COG4618 426 I---ARFGDADPEKVVAA-AKLAGVhEMilrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD- 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 578818931 563 VGKHIFNKVLgpnGLLK--GKTRLLVTHSMHFLPQVDEIVVLGNGTIV 608
Cdd:COG4618 501 EGEAALAAAI---RALKarGATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1068-1290 |
1.44e-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: 115.91 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELdlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTI 1147
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1148 IPQDPIL-FSGSLR----M----NLDPFNNYSDEE---IWKALElahlksfvaslQLGLSH----EVTEaggnLSIGQRQ 1211
Cdd:COG1120 80 VPQEPPApFGLTVRelvaLgrypHLGLFGRPSAEDreaVEEALE-----------RTGLEHladrPVDE----LSGGERQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1212 LLCLGRALLRKSKILVLDEATAAVDL----ETDNLIQTtiQNEFAHCTVITIAHRL-HTIMDSDKVMVLDNGKIIECGSP 1286
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRR--LARERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPP 222
|
....
gi 578818931 1287 EELL 1290
Cdd:COG1120 223 EEVL 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1085-1233 |
1.63e-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: 112.36 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1085 LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSG-SLRMNL 1163
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1164 -------DPFNNYSDEEIWKALElahlksfvaslQLGLSHE----VTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEAT 1232
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALE-----------KLGLGDLadrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 578818931 1233 A 1233
Cdd:pfam00005 150 A 150
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
421-619 |
2.39e-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: 2.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 421 TVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAYVPQQSWIQNGTIKDNI 487
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGadlkqwdretfgkHIGYLPQDVELFPGTVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 488 L-FGTEFNEkryQQVLEACALLPDLEM---LPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAhV 563
Cdd:TIGR01842 413 ArFGENADP---EKIIEAAKLAGVHELilrLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDE-E 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 564 GKHIFNKVLGpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAK 619
Cdd:TIGR01842 489 GEQALANAIK-ALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
390-646 |
2.68e-28 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 121.99 E-value: 2.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 390 LDTSAIRHD-------CNFDKAMQFSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGH 462
Cdd:PRK13657 313 EDAVPDVRDppgaidlGRVKGAVEFDDVSFSYDNSRQG-VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 463 ITIKGTT-------------AYVPQQSWIQNGTIKDNILFGTE-FNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGIN 528
Cdd:PRK13657 392 ILIDGTDirtvtraslrrniAVVFQDAGLFNRSIEDNIRVGRPdATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQ 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 529 LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIV 608
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAAL---DELMKGRTTFIIAHRLSTVRNADRILVFDNGRVV 548
|
250 260 270
....*....|....*....|....*....|....*....
gi 578818931 609 EKGSYSALLAKKGEFAKNLKT-FLRHTGPEEEATVHDGS 646
Cdd:PRK13657 549 ESGSFDELVARGGRFAALLRAqGMLQEDERRKQPAAEGA 587
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
405-625 |
3.45e-28 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 121.66 E-value: 3.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 405 MQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSlISAMLGEMENV-HGHITIKGTT-------------A 470
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKST-IANLLTRFYDIdEGEILLDGHDlrdytlaslrnqvA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 471 YVPQQSWIQNGTIKDNILFGTEFNEKRYQqvLEACALLPD----LEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQN 546
Cdd:PRK11176 421 LVSQNVHLFNDTIANNIAYARTEQYSREQ--IEEAARMAYamdfINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRD 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 547 LDIYLLDDPLSAVDAHvGKHIFNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAK 625
Cdd:PRK11176 499 SPILILDEATSALDTE-SERAIQAAL--DELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQ 574
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
101-624 |
3.55e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 122.52 E-value: 3.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 101 DIFTFVSPQLLKLLISFASdrdtYLWIGYLCAILLFTAALIQSfclqcyfqlcfklgvKVRTAIMASVYKKALTLSNlar 180
Cdd:TIGR00958 196 GPPALASAIFFMCLLSIAS----SVSAGLRGGSFNYTMARINL---------------RIREDLFRSLLRQDLGFFD--- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 181 kEYTVGETVNLMSVDAQKLMDV--TNFMHMLWSSVLQIVLSIFFLWreLGPSvLAGVGV--MVLVIPINAILSTKSKTIQ 256
Cdd:TIGR00958 254 -ENKTGELTSRLSSDTQTMSRSlsLNVNVLLRNLVMLLGLLGFMLW--LSPR-LTMVTLinLPLVFLAEKVFGKRYQLLS 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 257 VKNMKNKDKRLKIMNEILSGIKILKYFAWEPS----FRDQVQNLRKKELKNLLAFSqLQCVVIFVFQLTpVLVSVVTFSV 332
Cdd:TIGR00958 330 EELQEAVAKANQVAEEALSGMRTVRSFAAEEGeasrFKEALEETLQLNKRKALAYA-GYLWTTSVLGML-IQVLVLYYGG 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 333 YVLVDSnnildaqkAFTSITLFNILRFPLSM------LPMMISSMLQASVSTERLEKYLggD---DLDTSAIRHDCNFDK 403
Cdd:TIGR00958 408 QLVLTG--------KVSSGNLVSFLLYQEQLgeavrvLSYVYSGMMQAVGASEKVFEYL--DrkpNIPLTGTLAPLNLEG 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 404 AMQFSEASFTWEHDSEATV-RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-------------T 469
Cdd:TIGR00958 478 LIEFQDVSFSYPNRPDVPVlKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplvqydhhylhrqV 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 470 AYVPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEM-LPGGDLAEIGEKGINLSGGQKQRISLARATYQNLD 548
Cdd:TIGR00958 558 ALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMeFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPR 637
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 549 IYLLDDPLSAVDAHVgkhifNKVLGPNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFA 624
Cdd:TIGR00958 638 VLILDEATSALDAEC-----EQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYK 708
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
411-621 |
6.03e-28 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 120.59 E-value: 6.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 411 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITI-------------KGTTAYVPQQSW 477
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFhdipltklqldswRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 478 IQNGTIKDNILFGtefNEKRYQQVLEACALLP----DLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLD 553
Cdd:PRK10789 400 LFSDTVANNIALG---RPDATQQEIEHVARLAsvhdDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578818931 554 DPLSAVDAHVGKHIFNKvLGPNGllKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKG 621
Cdd:PRK10789 477 DALSAVDGRTEHQILHN-LRQWG--EGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
407-589 |
7.74e-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: 7.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 407 FSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAYVP 473
Cdd:TIGR02868 337 LRDLSAGYPGAPPV-LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssldqdevrrRVSVCA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 474 QQSWIQNGTIKDNILFGT-EFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLL 552
Cdd:TIGR02868 416 QDAHLFDTTVRENLRLARpDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....*..
gi 578818931 553 DDPLSAVDAHVGKHIFNKVLGPnglLKGKTRLLVTHS 589
Cdd:TIGR02868 496 DEPTEHLDAETADELLEDLLAA---LSGRTVVLITHH 529
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
405-609 |
9.82e-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: 112.57 E-value: 9.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 405 MQFSEASFTWEHDSEAT--VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--------TAYVPQ 474
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgpdRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 475 QS----WIqngTIKDNILFGTEFN----EKRYQQVLEAcallpdlemlpggdLAEIGEKGI------NLSGGQKQRISLA 540
Cdd:cd03293 81 QDallpWL---TVLDNVALGLELQgvpkAEARERAEEL--------------LELVGLSGFenayphQLSGGMRQRVALA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 541 RATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLgpnGLLK--GKTRLLVTHSMH---FLPqvDEIVVLGN--GTIVE 609
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELL---DIWRetGKTVLLVTHDIDeavFLA--DRVVVLSArpGRIVA 214
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1084-1291 |
1.26e-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: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNL 1163
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1164 DPF-NNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDN- 1241
Cdd:TIGR01842 413 ARFgENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQa 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 578818931 1242 LIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQ 1291
Cdd:TIGR01842 493 LANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1068-1293 |
1.57e-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: 112.59 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELDL--VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKL 1145
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1146 TIIPQDPIlfsGSL--RMNLD-----PFNNY----SDEEIWKALELAHLKSFVASLqlgLSHEvteaggnLSIGQRQLLC 1214
Cdd:COG1124 82 QMVFQDPY---ASLhpRHTVDrilaePLRIHglpdREERIAELLEQVGLPPSFLDR---YPHQ-------LSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1215 LGRALLRKSKILVLDEATAAVDL----ETDNLIQtTIQNEFaHCTVITIAHRLHTI--MdSDKVMVLDNGKIIECGSPEE 1288
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVsvqaEILNLLK-DLREER-GLTYLFVSHDLAVVahL-CDRVAVMQNGRIVEELTVAD 225
|
....*
gi 578818931 1289 LLQIP 1293
Cdd:COG1124 226 LLAGP 230
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1068-1284 |
1.70e-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: 112.21 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELDLV--LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLRE-- 1143
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1144 -KLTIIPQDPIlfsGSL--RMN-----LDPFNNYSDEEIWKALELAHLKSFVaslQLGLS--------HEvteaggnLSI 1207
Cdd:cd03257 82 kEIQMVFQDPM---SSLnpRMTigeqiAEPLRIHGKLSKKEARKEAVLLLLV---GVGLPeevlnrypHE-------LSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1208 GQRQLLCLGRALLRKSKILVLDEATAAVDLETD----NLIQtTIQNEFAhCTVITIAHRLHTI-MDSDKVMVLDNGKIIE 1282
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQaqilDLLK-KLQEELG-LTLLFITHDLGVVaKIADRVAVMYAGKIVE 226
|
..
gi 578818931 1283 CG 1284
Cdd:cd03257 227 EG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1068-1293 |
2.55e-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: 118.08 E-value: 2.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAG---GQIIIDGVDIASIGLHDLREK 1144
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1145 LTIIPQDPilfsgslRMNLDPFNnySDEEIWKALEL-----AHLKSFVASL--QLGLSHEVTEAGGNLSIGQRQLLCLGR 1217
Cdd:COG1123 85 IGMVFQDP-------MTQLNPVT--VGDQIAEALENlglsrAEARARVLELleAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 1218 ALLRKSKILVLDEATAAVDLETDNLIQTTIQ--NEFAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1293
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAAP 234
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1084-1296 |
2.69e-27 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 111.82 E-value: 2.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIAS---IGLHDLREKLTIIPQDPILFSG--- 1157
Cdd:cd03261 15 VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseAELYRLRRRMGMLFQSGALFDSltv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1158 ------SLRMNLdpfnNYSDEEIwkaLELAHLKsfvasLQL-GLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDE 1230
Cdd:cd03261 95 fenvafPLREHT----RLSEEEI---REIVLEK-----LEAvGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578818931 1231 ATAAVD----LETDNLIQTTiqNEFAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIPGPF 1296
Cdd:cd03261 163 PTAGLDpiasGVIDDLIRSL--KKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRASDDPL 231
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1084-1291 |
6.43e-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: 110.72 E-value: 6.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHdLREKLTIIPQDPILFSG-SLRMN 1162
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLPDERGLYDRlTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1163 LD---PFNNYSDEEIWKALE-LAHLksfvaslqLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLE 1238
Cdd:COG4555 95 IRyfaELYGLFDEELKKRIEeLIEL--------LGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 1239 TdnliQTTIQNEFAHC-----TVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQ 1291
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 ... |
1069-1279 |
1.57e-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: 108.71 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1069 QFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTII 1148
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1149 PQDP------------ILFsgSLRmNLdpfnNYSDEEIWKALELAhLKsfvaslQLGLSHEVTEAGGNLSIGQRQLLCLG 1216
Cdd:cd03225 81 FQNPddqffgptveeeVAF--GLE-NL----GLPEEEIEERVEEA-LE------LVGLEGLRDRSPFTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578818931 1217 RALLRKSKILVLDEATAAVDLE-TDNLIQT--TIQNEFAhcTVITIAHRLHTIMD-SDKVMVLDNGK 1279
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAgRRELLELlkKLKAEGK--TIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1074-1279 |
2.10e-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: 2.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1074 QVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQdpi 1153
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1154 lfsgslrmnldpfnnysdeeiwkalelahlksfvaslqlglshevteaggnLSIGQRQLLCLGRALLRKSKILVLDEATA 1233
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 578818931 1234 AVDLETDNLIQTTIQNEFAH-CTVITIAHRLHTIMD-SDKVMVLDNGK 1279
Cdd:cd00267 110 GLDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
423-607 |
2.49e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 107.98 E-value: 2.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 423 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-------------TAYVPQQSWIQNGTIKDNILF 489
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKplsampppewrrqVAYVPQEPALWGGTVRDNLPF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 490 GTEFNEKRYQQVlEACALLPDLEmLPGGDLaeigEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHvGKHIF 568
Cdd:COG4619 97 PFQLRERKFDRE-RALELLERLG-LPPDIL----DKPVeRLSGGERQRLALIRALLLQPDVLLLDEPTSALDPE-NTRRV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 578818931 569 NKVLGPNGLLKGKTRLLVTHSMHFLPQV-DEIVVLGNGTI 607
Cdd:COG4619 170 EELLREYLAEEGRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
271-623 |
3.70e-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: 3.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 271 NEILSGIKILKYFAWEPSF--------------RDQVQNLRKKELKNLLA-FSQL-QCVVIFVFQLTPVlvsvVTFSVYV 334
Cdd:PRK10790 208 NEVINGMSVIQQFRQQARFgermgeasrshymaRMQTLRLDGFLLRPLLSlFSALiLCGLLMLFGFSAS----GTIEVGV 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 335 LVdsnnildaqkAFtsITLFNILRFPLSMLPMMISSMLQASVSTERL--------EKYlGGDDLDTSAIRHDCNfdkamq 406
Cdd:PRK10790 284 LY----------AF--ISYLGRLNEPLIELTTQQSMLQQAVVAGERVfelmdgprQQY-GNDDRPLQSGRIDID------ 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 407 fsEASFTWEHDsEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAYVP 473
Cdd:PRK10790 345 --NVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsslshsvlrqGVAMVQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 474 QQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLD 553
Cdd:PRK10790 422 QDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILD 501
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578818931 554 DPLSAVDAHVGKHIfNKVLgpnGLLKGKTRLLV-THSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEF 623
Cdd:PRK10790 502 EATANIDSGTEQAI-QQAL---AAVREHTTLVViAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRY 568
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
422-609 |
4.13e-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: 4.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--------AYVPQQS----WIqngTIKDNILF 489
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPvtgpgpdrGVVFQEPallpWL---TVLDNVAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 490 GTEFN----EKRYQQVLEAcallpdlemlpggdLAEIGEKGI------NLSGGQKQRISLARATYQNLDIYLLDDPLSAV 559
Cdd:COG1116 104 GLELRgvpkAERRERAREL--------------LELVGLAGFedayphQLSGGMRQRVAIARALANDPEVLLMDEPFGAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 560 DAHVGKHIfnkvlgpNGLL------KGKTRLLVTHSmhflpqVDE-------IVVLGN--GTIVE 609
Cdd:COG1116 170 DALTRERL-------QDELlrlwqeTGKTVLFVTHD------VDEavfladrVVVLSArpGRIVE 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1084-1284 |
6.53e-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: 6.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQdpilfsgslrmnl 1163
Cdd:cd03214 14 VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1164 dpfnnysdeeiwkALELahlksfvaslqLGLSH----EVTEaggnLSIGQRQLLCLGRALLRKSKILVLDEATAAVDL-- 1237
Cdd:cd03214 81 -------------ALEL-----------LGLAHladrPFNE----LSGGERQRVLLARALAQEPPILLLDEPTSHLDIah 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 578818931 1238 --ETDNLIQTTIQNEfaHCTVITIAHRL-HTIMDSDKVMVLDNGKIIECG 1284
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 ... |
406-606 |
1.88e-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: 105.63 E-value: 1.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 406 QFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-------------TAYV 472
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKdltklslkelrrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 473 PQ--QSWIQNGTIKDNILFGTEF----NEKRYQQVLEACALLpdlemlpggDLAEIGEKGI-NLSGGQKQRISLARATYQ 545
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGLENlglpEEEIEERVEEALELV---------GLEGLRDRSPfTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578818931 546 NLDIYLLDDPLSAVDAHVGKHIFNKVLGPNGllKGKTRLLVTHSMHFLPQV-DEIVVLGNGT 606
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLKA--EGKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
422-557 |
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: 103.11 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYVPQQSWIQNG-TIKDNI 487
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltdderkslrkeiGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 488 LFGTEF----NEKRYQQVLEAcallpdLEMLPGGDLAE--IGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLS 557
Cdd:pfam00005 81 RLGLLLkglsKREKDARAEEA------LEKLGLGDLADrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
405-611 |
2.81e-25 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 103.93 E-value: 2.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 405 MQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT------------TAYV 472
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 473 PQQSWIQNGTIKDNIlfgtefnekryqqvleacallpdlemlpggdlaeigekGINLSGGQKQRISLARATYQNLDIYLL 552
Cdd:cd03247 81 NQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 553 DDPLSAVDAHVGKHIFNKVLgpnGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKG 611
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIF---EVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1082-1308 |
3.45e-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: 105.50 E-value: 3.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1082 DLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIAsiGLHDLREKLTIIPQDPILFSgslrm 1161
Cdd:cd03299 12 EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFP----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1162 NLDPFNN---------YSDEEI-WKALELAHLksfvaslqLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEA 1231
Cdd:cd03299 85 HMTVYKNiayglkkrkVDKKEIeRKVLEIAEM--------LGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1232 TAAVDLET-DNLIQ--TTIQNEFAhCTVITIAHRLHTI-MDSDKVMVLDNGKIIECGSPEELLQIPGPfYFMAKEAGIEN 1307
Cdd:cd03299 157 FSALDVRTkEKLREelKKIRKEFG-VTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKKPKN-EFVAEFLGFNN 234
|
.
gi 578818931 1308 V 1308
Cdd:cd03299 235 I 235
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
406-625 |
5.48e-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: 104.72 E-value: 5.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 406 QFSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYV 472
Cdd:COG1122 2 ELENLSFSYPGGTPA-LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDitkknlrelrrkvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 473 PQQSWIQ--NGTIKDNILFGTEfN-----EKRYQQVLEAcallpdLEMLpggDLAEIGEKGI-NLSGGQKQRISLARATY 544
Cdd:COG1122 81 FQNPDDQlfAPTVEEDVAFGPE-NlglprEEIRERVEEA------LELV---GLEHLADRPPhELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 545 QNLDIYLLDDPLSAVDAHvGKHIFNKVLgpNGLLK-GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLAKKGE 622
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPR-GRRELLELL--KRLNKeGKTVIIVTHDLDLVAELaDRVIVLDDGRIVADGTPREVFSDYEL 227
|
...
gi 578818931 623 FAK 625
Cdd:COG1122 228 LEE 230
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
422-611 |
6.48e-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: 102.90 E-value: 6.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYVPQqswiqngtikdnil 488
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDlaslspkelarkiAYVPQ-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 489 fgtefnekryqqVLEACallpdlemlpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHI 567
Cdd:cd03214 81 ------------ALELL------------GLAHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 578818931 568 FNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 611
Cdd:cd03214 137 LE-------LLRrlarerGKTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
417-631 |
9.01e-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: 104.55 E-value: 9.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 417 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTA------------YVPQQSWI-QNGTI 483
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVrkeprearrqigVLPDERGLyDRLTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 484 KDNILFGTEFNEKRYQQVLEACALLpdLEMLpggDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAh 562
Cdd:COG4555 92 RENIRYFAELYGLFDEELKKRIEEL--IELL---GLEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV- 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578818931 563 VGKHIFNKVLgpnGLLK--GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLAKKGEfaKNLKTFL 631
Cdd:COG4555 166 MARRLLREIL---RALKkeGKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIGE--ENLEDAF 232
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
404-624 |
1.19e-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: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 404 AMQFSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG------TTAY------ 471
Cdd:COG5265 357 EVRFENVSFGYDPERPI-LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdirdvTQASlraaig 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 472 -VPQQSWIQNGTIKDNILFG-TEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDI 549
Cdd:COG5265 436 iVPQDTVLFNDTIAYNIAYGrPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPI 515
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 550 YLLDDPLSAVDAHVGKHIfNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFA 624
Cdd:COG5265 516 LIFDEATSALDSRTERAI-QAAL--REVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYA 587
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1084-1288 |
2.01e-24 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 103.29 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDlREKLTIIP--QDPILFSG---- 1157
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE-IARLGIGRtfQIPRLFPEltvl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1158 -----------SLRMNLDPFNNYSDEEIWKALELAHlksfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKIL 1226
Cdd:cd03219 94 envmvaaqartGSGLLLARARREEREARERAEELLE--------RVGLADLADRPAGELSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578818931 1227 VLDEATAAVDL-ETDNLIQTTIQNEFAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEE 1288
Cdd:cd03219 166 LLDEPAAGLNPeETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDE 229
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
966-1262 |
2.97e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 109.13 E-value: 2.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 966 FSWITSNRWLAIRLELvgNLTVF---FSALMMVI--------YrdtLSGD-TVGFV--LSNALNITQT-LNWLVRMTSEI 1030
Cdd:COG4178 251 FDAVIANWRRLIRRQR--NLTFFttgYGQLAVIFpilvaaprY---FAGEiTLGGLmqAASAFGQVQGaLSWFVDNYQSL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1031 eTNIVA-VERITEYTKVENEAPWVTDKRPPPDWPSKGKIQFNNYQVRyRPELDLVLRGITCDIGSMEKIGVVGRTGAGKS 1109
Cdd:COG4178 326 -AEWRAtVDRLAGFEEALEAADALPEAASRIETSEDGALALEDLTLR-TPDGRPLLEDLSLSLKPGERLLITGPSGSGKS 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1110 SLtnclFRILeaAG------GQIII-DGVDIAsiglhdlrekltIIPQDPILFSGSLRMNL---DPFNNYSDEEIWKALE 1179
Cdd:COG4178 404 TL----LRAI--AGlwpygsGRIARpAGARVL------------FLPQRPYLPLGTLREALlypATAEAFSDAELREALE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1180 LAHLKSFVASLqlglsHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITI 1259
Cdd:COG4178 466 AVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISV 540
|
...
gi 578818931 1260 AHR 1262
Cdd:COG4178 541 GHR 543
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1084-1296 |
3.07e-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: 103.14 E-value: 3.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIG---LHDLREKLTIIPQDPILFSG--- 1157
Cdd:COG1127 20 VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRIGMLFQGGALFDSltv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1158 ------SLRMNLDpfnnYSDEEIwkaLELAHLKsfvasLQL-GLSHevteAG----GNLSIGQRQLLCLGRALLRKSKIL 1226
Cdd:COG1127 100 fenvafPLREHTD----LSEAEI---RELVLEK-----LELvGLPG----AAdkmpSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 1227 VLDEATAAVD----LETDNLIQtTIQNEFaHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIPGPF 1296
Cdd:COG1127 164 LYDEPTAGLDpitsAVIDELIR-ELRDEL-GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLASDDPW 236
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
413-612 |
3.24e-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: 103.20 E-value: 3.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 413 TWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYVPQQSWIQ 479
Cdd:COG1120 8 SVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlaslsrrelarriAYVPQEPPAP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 480 NG-TIKDNILFG--------TEFNEKRYQQVLEAcallpdLEMLpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDI 549
Cdd:COG1120 88 FGlTVRELVALGryphlglfGRPSAEDREAVEEA------LERT---GLEHLADRPVDeLSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578818931 550 YLLDDPLSAVDAHvgkHIFnKVLgpnGLLK------GKTRLLVThsmHFLPQV----DEIVVLGNGTIVEKGS 612
Cdd:COG1120 159 LLLDEPTSHLDLA---HQL-EVL---ELLRrlarerGRTVVMVL---HDLNLAaryaDRLVLLKDGRIVAQGP 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1084-1294 |
4.48e-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: 102.27 E-value: 4.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLfRILEA-AGGQIIIDGVDIASI---GLHDLREKLTIIPQDPILFSgsl 1159
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI-NGLERpTSGSVLVDGTDLTLLsgkELRKARRRIGMIFQHFNLLS--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1160 rmNLDPFNNysdeeIWKALELAHL-KSFVAS-----LQL-GLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEAT 1232
Cdd:cd03258 96 --SRTVFEN-----VALPLEIAGVpKAEIEErvlelLELvGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 1233 AAVDLE-TDNLIQ--TTIQNEFAhCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIPG 1294
Cdd:cd03258 169 SALDPEtTQSILAllRDINRELG-LTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1084-1288 |
6.11e-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: 102.42 E-value: 6.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDlREKLTI-----IPQdpiLFSG- 1157
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHR-IARLGIartfqNPR---LFPEl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1158 ----------------SLRMNLDPFNNYSDEEIW---KALELAHlksfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGRA 1218
Cdd:COG0411 95 tvlenvlvaaharlgrGLLAALLRLPRARREEREareRAEELLE--------RVGLADRADEPAGNLSYGQQRRLEIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578818931 1219 LLRKSKILVLDEATAAVDL-ETDNLIQTTIQ-NEFAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEE 1288
Cdd:COG0411 167 LATEPKLLLLDEPAAGLNPeETEELAELIRRlRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAE 239
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
422-639 |
6.19e-24 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 102.06 E-value: 6.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT------------TAYVPQQSWIQNG-TIKDNIL 488
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvardpaevrrrIGYVPQEPALYPDlTVRENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 489 F-------GTEFNEKRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 561
Cdd:COG1131 96 FfarlyglPRKEARERIDELLELFGLTDAADRKVG-----------TLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 562 hVGKHIFNKVLgpNGLLK-GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLAKKGEFAknlktFLRHTGPEEE 639
Cdd:COG1131 165 -EARRELWELL--RELAAeGKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKARLLEDV-----FLELTGEEAR 236
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1084-1289 |
1.90e-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: 100.33 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEA-----AGGQIIIDGVDIASIGLHD--LREKLTIIPQDPILFS 1156
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVleLRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1157 GSLRMNLD--------PFNNYSDEEIWKALELAHLKSFVASLQLGLShevteaggnLSIGQRQLLCLGRALLRKSKILVL 1228
Cdd:cd03260 95 GSIYDNVAyglrlhgiKLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQRLCLARALANEPEVLLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578818931 1229 DEATAAVDLETDNLIQTTIQnEFAH-CTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEEL 1289
Cdd:cd03260 166 DEPTSALDPISTAKIEELIA-ELKKeYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1068-1279 |
2.06e-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: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRP---ELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGvdiaSIGLhdlrek 1144
Cdd:cd03250 1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG----SIAY------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1145 ltiIPQDPILFSGSLRMNL---DPFNNysdEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLR 1221
Cdd:cd03250 71 ---VSQEPWIQNGTIRENIlfgKPFDE---ERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1222 KSKILVLDEATAAVDLET-DNLIQTTIQNEFAHC-TVITIAHRLHTIMDSDKVMVLDNGK 1279
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
417-611 |
2.27e-23 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 99.52 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 417 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-----------TAYVPQQ-SWIQNGTIK 484
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvpperrnIGMVFQDyALFPHLTVA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 485 DNILFGTEFNEKRYQQVLEACALLpdLEMLpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHV 563
Cdd:cd03259 91 ENIAFGLKLRGVPKAEIRARVREL--LELV---GLEGLLNRYPHeLSGGQQQRVALARALAREPSLLLLDEPLSALDAKL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 578818931 564 GKHIFNKVLgpnGLLK--GKTRLLVTHSM-HFLPQVDEIVVLGNGTIVEKG 611
Cdd:cd03259 166 REELREELK---ELQRelGITTIYVTHDQeEALALADRIAVMNEGRIVQVG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
411-618 |
2.83e-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: 105.37 E-value: 2.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 411 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMEN---VHGHITIKGTT-------------AYVPQ 474
Cdd:COG1123 11 SVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDllelsealrgrriGMVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 475 QSWIQ-NG-TIKDNILFGTEfNEKRYQQVLEACAllpdLEMLPGGDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYL 551
Cdd:COG1123 91 DPMTQlNPvTVGDQIAEALE-NLGLSRAEARARV----LELLEAVGLERRLDRYPHqLSGGQRQRVAIAMALALDPDLLI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578818931 552 LDDPLSAVDAHVGKHIFnkvlgpnGLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 618
Cdd:COG1123 166 ADEPTTALDVTTQAEIL-------DLLRelqrerGTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEILA 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
422-618 |
3.18e-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: 105.37 E-value: 3.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT----------------AYVPQ---QSWIQNGT 482
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltklsrrslrelrrrvQMVFQdpySSLNPRMT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 483 IKDNILFGTEFN--------EKRYQQVLEACALLPD-LEMLPGGdlaeigekginLSGGQKQRISLARATYQNLDIYLLD 553
Cdd:COG1123 361 VGDIIAEPLRLHgllsraerRERVAELLERVGLPPDlADRYPHE-----------LSGGQRQRVAIARALALEPKLLILD 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578818931 554 DPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 618
Cdd:COG1123 430 EPTSALDVSVQAQILN-------LLRdlqrelGLTYLFISHDLAVVRYIaDRVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1068-1289 |
4.47e-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: 99.56 E-value: 4.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYrPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIG---LHDLREK 1144
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1145 LTIIPQDPIL----------FSGSL-RMNLDP--FNNYSDEEIWKALELahLKsfvaslQLGLSHEVTEAGGNLSIGQRQ 1211
Cdd:cd03256 80 IGMIFQQFNLierlsvlenvLSGRLgRRSTWRslFGLFPKEEKQRALAA--LE------RVGLLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1212 LLCLGRALLRKSKILVLDEATAAVDLETDNLIQ---TTIQNEFAHCTVITIaHRLHTIMD-SDKVMVLDNGKIIECGSPE 1287
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMdllKRINREEGITVIVSL-HQVDLAREyADRIVGLKDGRIVFDGPPA 230
|
..
gi 578818931 1288 EL 1289
Cdd:cd03256 231 EL 232
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
410-618 |
6.06e-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: 99.49 E-value: 6.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 410 ASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSW----IQ------ 479
Cdd:COG1124 9 VSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrrrVQmvfqdp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 480 ------NGTIKDNI-----LFGTEFNEKRYQQVLEACALLPD-LEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNL 547
Cdd:COG1124 89 yaslhpRHTVDRILaeplrIHGLPDREERIAELLEQVGLPPSfLDRYPH-----------QLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 548 DIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSM----HFlpqVDEIVVLGNGTIVEKGSYSALL 617
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILN-------LLKdlreerGLTYLFVSHDLavvaHL---CDRVAVMQNGRIVEELTVADLL 227
|
.
gi 578818931 618 A 618
Cdd:COG1124 228 A 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1068-1291 |
6.06e-23 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 99.39 E-value: 6.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELdlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIAsiglhdlREKLTI 1147
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR-------RARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1148 --IPQD-------PILFSGSLRMNLDP----FNNYSDEE---IWKALELAHLKSFvASLQLGlshevteaggNLSIGQRQ 1211
Cdd:COG1121 78 gyVPQRaevdwdfPITVRDVVLMGRYGrrglFRRPSRADreaVDEALERVGLEDL-ADRPIG----------ELSGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1212 LLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQnEFAH--CTVITIAHRLHTIMD-SDKVMVLdNGKIIECGSPEE 1288
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLR-ELRRegKTILVVTHDLGAVREyFDRVLLL-NRGLVAHGPPEE 224
|
...
gi 578818931 1289 LLQ 1291
Cdd:COG1121 225 VLT 227
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
90-381 |
6.92e-23 |
|
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: 100.32 E-value: 6.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 90 LLKSFLLKLVNDIFTFVSPQLLKLLISFASDRDTYLWIGYLCAILLFtAALIQSFCLQCYFQLCFKLGVKVRTAIMASVY 169
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLL-LALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 170 KKALTLSNLARKEYTVGETVNLMSVDAQKLMD-VTNFMHMLWSSVLQIVLSIFFL----WRelgpSVLAGVGVMVLVIPI 244
Cdd:cd07346 80 RHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNlVSSGLLQLLSDVLTLIGALVILfylnWK----LTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 245 NAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPS----FRDQVQNLRKKELKNLLAFSQLQCVVIFVFQL 320
Cdd:cd07346 156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEReierFREANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578818931 321 TPVLVSVvtFSVYvLVdSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 381
Cdd:cd07346 236 GTALVLL--YGGY-LV-LQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1084-1279 |
7.28e-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: 96.87 E-value: 7.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLH--DLREKLTIIPQDPILFSgslrm 1161
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRIGMVFQDFALFP----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1162 NLDPFNNysdeeiwkalelahlksfvasLQLGLShevteaGgnlsiGQRQLLCLGRALLRKSKILVLDEATAAVDLETDN 1241
Cdd:cd03229 90 HLTVLEN---------------------IALGLS------G-----GQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 578818931 1242 LIQTTIQNEFAH--CTVITIAHRLHTIMD-SDKVMVLDNGK 1279
Cdd:cd03229 138 EVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
422-611 |
1.18e-22 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 97.96 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT----------------TAYVPQQSwiqNG---- 481
Cdd:cd03257 21 LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllklsrrlrkirrkeIQMVFQDP---MSslnp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 482 --TIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSA 558
Cdd:cd03257 98 rmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVG--LPEEVLNRYPHeLSGGQRQRVAIARALALNPKLLIADEPTSA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 559 VDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 611
Cdd:cd03257 176 LDVSVQAQILD-------LLKklqeelGLTLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1068-1311 |
1.74e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 98.91 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTI 1147
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1148 IPQDP------------ILFSGSLRMnLDPfnnysdEEIWKALELAHLKSFVASLqlgLSHEVTeaggNLSIGQRQLLCL 1215
Cdd:PRK13632 88 IFQNPdnqfigatveddIAFGLENKK-VPP------KKMKDIIDDLAKKVGMEDY---LDKEPQ----NLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1216 GRALLRKSKILVLDEATAAVDLETDNLIQTTIQN--EFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELL--- 1290
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILnnk 233
|
250 260
....*....|....*....|....*...
gi 578818931 1291 ------QIPGPF-YFMAKEagIENVNST 1311
Cdd:PRK13632 234 eilekaKIDSPFiYKLSKK--LKGIDPT 259
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1084-1284 |
3.30e-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: 96.43 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHdlREKLTIIPQDPILF-------- 1155
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFphltvaen 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1156 --SGsLRMNLDPfnnySDEEIWKALELAhlksfvasLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATA 1233
Cdd:cd03259 93 iaFG-LKLRGVP----KAEIRARVRELL--------ELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 578818931 1234 AVDLETDNLIQTTIQN--EFAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECG 1284
Cdd:cd03259 160 ALDAKLREELREELKElqRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
422-606 |
3.46e-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: 94.23 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIkgttayvpqqswiqngtikdnilFGTEFNEKRYQQV 501
Cdd:cd00267 15 LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI-----------------------DGKDIAKLPLEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 502 LEACALLPDLemlpggdlaeigekginlSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLGPNglLKGK 581
Cdd:cd00267 72 RRRIGYVPQL------------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELA--EEGR 131
|
170 180
....*....|....*....|....*.
gi 578818931 582 TRLLVTHSMHFLPQV-DEIVVLGNGT 606
Cdd:cd00267 132 TVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
411-607 |
3.62e-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: 96.40 E-value: 3.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 411 SFTWEHDSEAT--VRDVNLDIMAGQLVAVIGPVGSGKSSLISaMLGEMENV-HGHITIKGTTA----------------- 470
Cdd:cd03255 7 SKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVRVDGTDIsklsekelaafrrrhig 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 471 YVPQQ-SWIQNGTIKDNILFGTEFNEKRYQQVLEACALLpdLEMLpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLD 548
Cdd:cd03255 86 FVFQSfNLLPDLTALENVELPLLLAGVPKKERRERAEEL--LERV---GLGDRLNHYPSeLSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 549 IYLLDDPLSAVDAHVGKHIFNKVLGPNGlLKGKTRLLVTHSMHFLPQVDEIVVLGNGTI 607
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNK-EAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1007-1277 |
5.32e-22 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 103.57 E-value: 5.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1007 GFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYTKVENEAPWVTDKRPPPDWPSKGKIQFNNYQVRYRPELDL-VL 1085
Cdd:PTZ00265 322 GSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYDTRKDVeIY 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1086 RGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIII-DGVDIASIGLHDLREKLTIIPQDPILFSGSLRMN-- 1162
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNik 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1163 --------LDPFNNYSDEEIWKAL---------------------------ELAHLKS---------------------F 1186
Cdd:PTZ00265 482 yslyslkdLEALSNYYNEDGNDSQenknkrnscrakcagdlndmsnttdsnELIEMRKnyqtikdsevvdvskkvlihdF 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1187 VASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVIT--IAHRLH 1264
Cdd:PTZ00265 562 VSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITiiIAHRLS 641
|
330
....*....|...
gi 578818931 1265 TIMDSDKVMVLDN 1277
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 ... |
1084-1291 |
1.33e-21 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 94.81 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHD-LREKLTIIPQDPILFSG----- 1157
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPEltvee 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1158 SLRMNLDPFNNYSDEEIW-KALEL-AHLKSFVASLqlglshevteaGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAv 1235
Cdd:cd03224 95 NLLLGAYARRRAKRKARLeRVYELfPRLKERRKQL-----------AGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 1236 dletdnlIQTTIQNEFAHC---------TVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQ 1291
Cdd:cd03224 163 -------LAPKIVEEIFEAirelrdegvTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
423-618 |
4.62e-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: 93.72 E-value: 4.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 423 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT----------------TAYVPQQSWIQNG-TIKD 485
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrrMGMLFQSGALFDSlTVFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 486 NILFG----TEFNEKRYQQV----LEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLS 557
Cdd:cd03261 97 NVAFPlrehTRLSEEEIREIvlekLEAVGLRGAEDLYPA-----------ELSGGMKKRVALARALALDPELLLYDEPTA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578818931 558 AVDAhVGKHIFNK-VLGPNGLLkGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 618
Cdd:cd03261 166 GLDP-IASGVIDDlIRSLKKEL-GLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1069-1280 |
8.32e-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: 92.21 E-value: 8.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1069 QFNNYQVRYRPELdlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIAsiglhDLREKLTII 1148
Cdd:cd03235 1 EVEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-----KERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1149 PQD-------PILFSGSLRMNLDP----FNNYSDEEIWKALELahLKsfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGR 1217
Cdd:cd03235 74 PQRrsidrdfPISVRDVVLMGLYGhkglFRRLSKADKAKVDEA--LE------RVGLSELADRQIGELSGGQQQRVLLAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 1218 ALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAH-CTVITIAHRLHTIMDS-DKVMVLDNGKI 1280
Cdd:cd03235 146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYfDRVLLLNRTVV 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
422-607 |
1.00e-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: 90.53 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIkgttayvpqqswiqngtikdnilFGTEFNEKRyQQV 501
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV-----------------------LGKDIKKEP-EEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 502 LEACALLPDLEMLPGgDLaeIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAhVGKHIFNKVLgpNGLLK-G 580
Cdd:cd03230 72 KRRIGYLPEEPSLYE-NL--TVRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREFWELL--RELKKeG 145
|
170 180
....*....|....*....|....*...
gi 578818931 581 KTRLLVTHSMHFLPQV-DEIVVLGNGTI 607
Cdd:cd03230 146 KTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
422-612 |
1.11e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 95.21 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLG-EMENvHGHITIKGTTAYV---PQQSWI----QNG------TIKDNI 487
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGlETPD-SGRIVLNGRDLFTnlpPRERRVgfvfQHYalfphmTVAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 488 LFG----TEFNEKRYQQVLEacalLpdLEMLpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAH 562
Cdd:COG1118 97 AFGlrvrPPSKAEIRARVEE----L--LELV---QLEGLADRYPSqLSGGQRQRVALARALAVEPEVLLLDEPFGALDAK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578818931 563 VGKHIfNKVLGpnGLLK--GKTRLLVTHSmhflpQV------DEIVVLGNGTIVEKGS 612
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 ... |
411-612 |
1.23e-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: 92.24 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 411 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAM-----LGEMENVHGHITIKGTTAYVPQQSWIQ------ 479
Cdd:cd03260 5 DLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLDVDVLElrrrvg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 480 ---------NGTIKDNILFG--------TEFNEKRYQQVLEACALLPDLemlpgGDLAeigeKGINLSGGQKQRISLARA 542
Cdd:cd03260 85 mvfqkpnpfPGSIYDNVAYGlrlhgiklKEELDERVEEALRKAALWDEV-----KDRL----HALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578818931 543 TYQNLDIYLLDDPLSAVDAhVGKHIFNKVLGpnGLLKGKTRLLVTHSMHflpQV----DEIVVLGNGTIVEKGS 612
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 ... |
422-606 |
1.65e-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: 90.32 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT---------------AYVPQQ-SWIQNGTIKD 485
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDltdledelpplrrriGMVFQDfALFPHLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 486 NILFGtefnekryqqvleacallpdlemlpggdlaeigekginLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGK 565
Cdd:cd03229 96 NIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 578818931 566 HIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGT 606
Cdd:cd03229 138 EVRA-------LLKslqaqlGITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
406-607 |
1.90e-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: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 406 QFSEASFTWEHDSEATV-RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TAY----------- 471
Cdd:cd03248 13 KFQNVTFAYPTRPDTLVlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpiSQYehkylhskvsl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 472 VPQQSWIQNGTIKDNILFG---TEFNE-KRYQQVLEACALLPDLEMlpgGDLAEIGEKGINLSGGQKQRISLARATYQNL 547
Cdd:cd03248 93 VGQEPVLFARSLQDNIAYGlqsCSFECvKEAAQKAHAHSFISELAS---GYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 548 DIYLLDDPLSAVDAHVGKHIFNKVLGPNgllKGKTRLLVTHSMHFLPQVDEIVVLGNGTI 607
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWP---ERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
422-609 |
1.97e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 91.64 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISaMLGEMENV-HGHITIKGTTA-----------------YVPQQS-WIQNGT 482
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVLIDGQDIsslserelarlrrrhigFVFQFFnLLPELT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 483 IKDNILFGTEFN----EKRYQQVLEAcallpdLEMLpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLS 557
Cdd:COG1136 103 ALENVALPLLLAgvsrKERRERAREL------LERV---GLGDRLDHRPSqLSGGQQQRVAIARALVNRPKLILADEPTG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578818931 558 AVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQVDEIVVLGNGTIVE 609
Cdd:COG1136 174 NLDSKTGEEVLE-------LLRelnrelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1084-1280 |
3.22e-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: 89.38 E-value: 3.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGlHDLREKLTIIPQDPILFSG-SLRMN 1162
Cdd:cd03230 15 ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGYLPEEPSLYENlTVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1163 LDpfnnysdeeiwkalelahlksfvaslqlglshevteaggnLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNL 1242
Cdd:cd03230 94 LK----------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRRE 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 578818931 1243 IQTTIQNEFAH-CTVITIAHRLHTIMD-SDKVMVLDNGKI 1280
Cdd:cd03230 134 FWELLRELKKEgKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1084-1293 |
3.38e-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: 3.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEA---AGGQIIIDGVDIASIGLHDLRE----KLTIIPQDPilfs 1156
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDP---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1157 gslrMN-LDP--------------FNNYSDEEIW-KALEL----------AHLKSFvaslqlglSHEvteaggnLSIGQR 1210
Cdd:COG0444 96 ----MTsLNPvmtvgdqiaeplriHGGLSKAEAReRAIELlervglpdpeRRLDRY--------PHE-------LSGGMR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1211 QLLCLGRALLRKSKILVLDEATAAVD-------LetdNLIQtTIQNEFaHCTVITIAHRLHTI--MdSDKVMVLDNGKII 1281
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDvtiqaqiL---NLLK-DLQREL-GLAILFITHDLGVVaeI-ADRVAVMYAGRIV 230
|
250
....*....|..
gi 578818931 1282 ECGSPEELLQIP 1293
Cdd:COG0444 231 EEGPVEELFENP 242
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
407-618 |
3.44e-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: 91.21 E-value: 3.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 407 FSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISaMLGEM-ENVHGHITIKG-------------TTAYV 472
Cdd:cd03295 3 FENVTKRYGGGKKA-VNNLNLEIAKGEFLVLIGPSGSGKTTTMK-MINRLiEPTSGEIFIDGedireqdpvelrrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 473 PQQ-SWIQNGTIKDNI-----LFGTEfNEKRYQQVLEACALLPdlemLPGGDLAE--IGEkginLSGGQKQRISLARATY 544
Cdd:cd03295 81 IQQiGLFPHMTVEENIalvpkLLKWP-KEKIRERADELLALVG----LDPAEFADryPHE----LSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 545 QNLDIYLLDDPLSAVDAHVGKHIFNKVLGPNGLLkGKTRLLVTHSM-HFLPQVDEIVVLGNGTIVEKGSYSALLA 618
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQEL-GKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
422-612 |
5.83e-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: 93.24 E-value: 5.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGeMENV-HGHITIKGT-----------TAYVPQqswiqNG------TI 483
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAG-FETPdSGRILLDGRdvtglppekrnVGMVFQ-----DYalfphlTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 484 KDNILFGTEF----NEKRYQQVLEAcallpdLEMLpggDLAEIGEKGIN-LSGGQKQRISLARAtyqnL----DIYLLDD 554
Cdd:COG3842 95 AENVAFGLRMrgvpKAEIRARVAEL------LELV---GLEGLADRYPHqLSGGQQQRVALARA----LapepRVLLLDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 555 PLSAVDAHVGKH----IFNkvlgpngLLK--GKTRLLVTHSmhflpQV------DEIVVLGNGTIVEKGS 612
Cdd:COG3842 162 PLSALDAKLREEmreeLRR-------LQRelGITFIYVTHD-----QEealalaDRIAVMNDGRIEQVGT 219
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
423-608 |
7.88e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 90.69 E-value: 7.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 423 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--------AYVPQQS----WIqngTIKDNILFG 490
Cdd:COG4525 24 QDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVFQKDallpWL---NVLDNVAFG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 491 TEFN----EKRYQQVLEACALLpdlemlpggDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGK 565
Cdd:COG4525 101 LRLRgvpkAERRARAEELLALV---------GLADFARRRIwQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTRE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 578818931 566 HIfnKVLgpngLLK-----GKTRLLVTHSmhflpqVDEIVVLGNGTIV 608
Cdd:COG4525 172 QM--QEL----LLDvwqrtGKGVFLITHS------VEEALFLATRLVV 207
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1084-1281 |
8.15e-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: 87.87 E-value: 8.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHD-LREKLTIIPQdpilfsgslrmn 1162
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1163 ldpfnnysdeeiwkalelahlksfvaslqlglshevteaggnLSIGQRQLLCLGRALLRKSKILVLDEATAAVDL-ETDN 1241
Cdd:cd03216 83 ------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPaEVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 578818931 1242 LIQT--TIQNEfaHCTVITIAHRLHTIMD-SDKVMVLDNGKII 1281
Cdd:cd03216 121 LFKVirRLRAQ--GVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1068-1254 |
1.20e-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: 88.69 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELdlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGlHDLREKLTI 1147
Cdd:COG4133 3 LEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1148 IPQDPILFSG-SLRMNLDpF------NNYSDEEIWKALElahlksfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGRALL 1220
Cdd:COG4133 80 LGHADGLKPElTVRENLR-FwaalygLRADREAIDEALE-----------AVGLAGLADLPVRQLSAGQKRRVALARLLL 147
|
170 180 190
....*....|....*....|....*....|....
gi 578818931 1221 RKSKILVLDEATAAVDLETDNLIQTTIQnefAHC 1254
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIA---AHL 178
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
422-612 |
1.57e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 91.67 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGeMENV-HGHITIKGT-----------TAYVPQqSWI--QNGTIKDNI 487
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG-LEDPtSGEILIGGRdvtdlppkdrnIAMVFQ-SYAlyPHMTVYENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 488 LFGTEFN----EKRYQQVLEACALLpDLEML----PGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAV 559
Cdd:COG3839 97 AFPLKLRkvpkAEIDRRVREAAELL-GLEDLldrkPK-----------QLSGGQRQRVALGRALVREPKVFLLDEPLSNL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578818931 560 DAHvgkhifnkvlgpnglLKGKTR--------------LLVTHSmhflpQV------DEIVVLGNGTIVEKGS 612
Cdd:COG3839 165 DAK---------------LRVEMRaeikrlhrrlgtttIYVTHD-----QVeamtlaDRIAVMNDGRIQQVGT 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1096-1293 |
1.81e-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: 93.60 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1096 EKIGVVGRTGAGKSSLTNCLFRiLEAAGGQIIIDGVDIASIG---LHDLREKLTIIPQDPilFsGSL--RMN-------- 1162
Cdd:COG4172 313 ETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--F-GSLspRMTvgqiiaeg 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1163 ---LDPFNNYS--DEEIWKALElahlksfvaslQLGLS--------HEvteaggnLSIGQRQLLCLGRALLRKSKILVLD 1229
Cdd:COG4172 389 lrvHGPGLSAAerRARVAEALE-----------EVGLDpaarhrypHE-------FSGGQRQRIAIARALILEPKLLVLD 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578818931 1230 EATAAVDLetdnLIQTTI-------QNEFaHCTVITIAHRLHTI--MdSDKVMVLDNGKIIECGSPEELLQIP 1293
Cdd:COG4172 451 EPTSALDV----SVQAQIldllrdlQREH-GLAYLFISHDLAVVraL-AHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
416-602 |
2.13e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 87.67 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 416 HDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--AYVPQQSWIQNG---TIKDNILFG 490
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGArvAYVPQRSEVPDSlplTVRDLVAMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 491 TeFNE--------KRYQQVLEACallpdLEMLPGGDLAE--IGEkginLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 560
Cdd:NF040873 82 R-WARrglwrrltRDDRAAVDDA-----LERVGLADLAGrqLGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 578818931 561 AHVGKHIfnkvlgpNGLLK-----GKTRLLVTHSMHFLPQVDEIVVL 602
Cdd:NF040873 152 AESRERI-------IALLAeeharGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
744-1040 |
2.51e-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: 89.92 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 744 LFSIFFIILAFVMNSVAfigsnLWLSAWTsdskifnsTDYPASQRDMR-----VGVYGALGLAQGIFVFIAHFWSAFGFV 818
Cdd:cd07346 2 LLALLLLLLATALGLAL-----PLLTKLL--------IDDVIPAGDLSlllwiALLLLLLALLRALLSYLRRYLAARLGQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 819 HASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPL 898
Cdd:cd07346 69 RVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 899 GIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAF--EHQ--QRFLKHNEVRIDTNqkcvfswITSNRW 974
Cdd:cd07346 149 LPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFaaEEReiERFREANRDLRDAN-------LRAARL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578818931 975 LAIRLELVGNLTVFFSALMMV-----IYRDTLS-GDTVGFVLSNALnITQTLNWLVRMTSEIETNIVAVERI 1040
Cdd:cd07346 222 SALFSPLIGLLTALGTALVLLyggylVLQGSLTiGELVAFLAYLGM-LFGPIQRLANLYNQLQQALASLERI 292
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1068-1282 |
2.77e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 88.19 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELDlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASI---GLHDLREK 1144
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1145 LTIIPQDpilfsGSLRMNLDPFNN---------YSDEEIWKALELAhLKsfvaslQLGLSHEVTEAGGNLSIGQRQLLCL 1215
Cdd:COG2884 81 IGVVFQD-----FRLLPDRTVYENvalplrvtgKSRKEIRRRVREV-LD------LVGLSDKAKALPHELSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578818931 1216 GRALLRKSKILVLDEATAAVDLET-DNLIQttIQNEFAH--CTVItIA-HRLHtIMDS--DKVMVLDNGKIIE 1282
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 ... |
1068-1280 |
2.88e-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: 87.85 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYrPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIAsiGLHD-----LR 1142
Cdd:cd03292 1 IEFINVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS--DLRGraipyLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1143 EKLTIIPQDPILFSgslrmNLDPFNN--YSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALL 1220
Cdd:cd03292 78 RKIGVVFQDFRLLP-----DRNVYENvaFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578818931 1221 RKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMD--SDKVMVLDNGKI 1280
Cdd:cd03292 153 NSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDttRHRVIALERGKL 214
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1074-1297 |
4.28e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 91.25 E-value: 4.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1074 QVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLRE----KLTIIP 1149
Cdd:PRK10070 33 QILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1150 QDpilFSGSLRMNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLD 1229
Cdd:PRK10070 113 QS---FALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMD 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 1230 EATAAVdletDNLIQTTIQNEFAHC------TVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIPGPFY 1297
Cdd:PRK10070 190 EAFSAL----DPLIRTEMQDELVKLqakhqrTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
424-612 |
1.32e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 88.99 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 424 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-----------TAYVPQQ-SWIQNGTIKDNILFGT 491
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHyALFRHMTVFDNIAFGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 492 EFNEKRY--------QQVLEAcallpdLEMLPGGDLAEigEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHV 563
Cdd:PRK10851 100 TVLPRRErpnaaaikAKVTQL------LEMVQLAHLAD--RYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 578818931 564 GKHIFNKVLGPNGLLKgKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 612
Cdd:PRK10851 172 RKELRRWLRQLHEELK-FTSVFVTHDQEEAMEVaDRVVVMSQGNIEQAGT 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
415-610 |
1.37e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.06 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 415 EHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--------AYVPQQS----WiQNgt 482
Cdd:PRK11248 10 DYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPvegpgaerGVVFQNEgllpW-RN-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 483 IKDNILFGTEF-NEKRYQQVLEAcallpdLEMLPGGDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 560
Cdd:PRK11248 87 VQDNVAFGLQLaGVEKMQRLEIA------HQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 561 AhvgkhiFNKVLGPNGLLK-----GKTRLLVTHSMH---FLpqVDEIVVL--GNGTIVEK 610
Cdd:PRK11248 161 A------FTREQMQTLLLKlwqetGKQVLLITHDIEeavFM--ATELVLLspGPGRVVER 212
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1085-1288 |
1.50e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 87.41 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1085 LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIA--SIGLHDLREKLTIIPQDP--ILFSGSLR 1160
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1161 MNLD--PFN-NYSDEEI----WKALELahlksfvaslqLGLSHEV--TEAGGNLSIGQRQLLCLGRALLRKSKILVLDEA 1231
Cdd:PRK13637 103 KDIAfgPINlGLSEEEIenrvKRAMNI-----------VGLDYEDykDKSPFELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1232 TAAVDLETDNLIQTTIQN--EFAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEE 1288
Cdd:PRK13637 172 TAGLDPKGRDEILNKIKElhKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
411-608 |
2.61e-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: 84.62 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 411 SFTWEHDSEaTVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG----------TTAYVPQQSWIQN 480
Cdd:cd03226 6 SFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQDVDYQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 481 G--TIKDNILFGTEFNEKRYQQVLEacaLLPDLemlpggDLAEIGEKG-INLSGGQKQRISLARATYQNLDIYLLDDPLS 557
Cdd:cd03226 85 FtdSVREELLLGLKELDAGNEQAET---VLKDL------DLYALKERHpLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 558 AVDAH----VGKhIFNKVLGpngllKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIV 608
Cdd:cd03226 156 GLDYKnmerVGE-LIRELAA-----QGKAVIVITHDYEFLAKVcDRVLLLANGAIV 205
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
422-619 |
3.16e-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: 85.33 E-value: 3.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISaMLGEMEN-VHGHITIKGT----------------TAYVPQQ-SWIQNGTI 483
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIR-CINGLERpTSGSVLVDGTdltllsgkelrkarrrIGMIFQHfNLLSSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 484 KDNILFGTEF----NEKRYQQVLEACALLpDLEmlpggDLAEIGEKgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAV 559
Cdd:cd03258 100 FENVALPLEIagvpKAEIEERVLELLELV-GLE-----DKADAYPA--QLSGGQKQRVGIARALANNPKVLLCDEATSAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578818931 560 DAHVGKHIFNKVLGPNGLLkGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLAK 619
Cdd:cd03258 172 DPETTQSILALLRDINREL-GLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
423-607 |
3.22e-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: 84.89 E-value: 3.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 423 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQ----------------NGTIKDN 486
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElrqkvgmvfqqfnlfpHLTVLEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 487 ILFG--TEFNEKRYQQVLEACALLPDLemlpgGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVg 564
Cdd:cd03262 97 ITLApiKVKGMSKAEAEERALELLEKV-----GLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 578818931 565 khiFNKVLgpnGLLK-----GKTRLLVTHSMHFLPQV-DEIVVLGNGTI 607
Cdd:cd03262 171 ---VGEVL---DVMKdlaeeGMTMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1084-1289 |
3.41e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.31 E-value: 3.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDG--VDIASIglHDLREK-LTIIPQDPIL------ 1154
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSP--RDAQAAgIAIIHQELNLvpnlsv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1155 ----FSGSLRMNLDPFNnysdeeiWKALE---LAHLKsfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILV 1227
Cdd:COG1129 97 aeniFLGREPRRGGLID-------WRAMRrraRELLA------RLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578818931 1228 LDEATAAVDL-ETDNLiqttiqneFAH--------CTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEEL 1289
Cdd:COG1129 164 LDEPTASLTErEVERL--------FRIirrlkaqgVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1068-1285 |
3.90e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 87.55 E-value: 3.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNN----YQVRYRPELdlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASI---GLHD 1140
Cdd:PRK11153 2 IELKNiskvFPQGGRTIH--ALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1141 LREKLTIIPQDPILFSG-------SLRMNLDpfnNYSDEEIWK-ALELahlksfvasLQL-GLSHEVTEAGGNLSIGQRQ 1211
Cdd:PRK11153 80 ARRQIGMIFQHFNLLSSrtvfdnvALPLELA---GTPKAEIKArVTEL---------LELvGLSDKADRYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1212 LLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQ--NEFAHCTVITIAHRlhtiMD-----SDKVMVLDNGKIIECG 1284
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKdiNRELGLTIVLITHE----MDvvkriCDRVAVIDAGRLVEQG 223
|
.
gi 578818931 1285 S 1285
Cdd:PRK11153 224 T 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1068-1295 |
3.92e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 84.81 E-value: 3.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRpelDLVLRgITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDlReKLTI 1147
Cdd:COG3840 2 LRLDDLTYRYG---DFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-R-PVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1148 IPQDPILFSG-SLRMN----LDPFNNYSDEEIWKALELAHlksfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRK 1222
Cdd:COG3840 76 LFQENNLFPHlTVAQNiglgLRPGLKLTAEQRAQVEQALE--------RVGLAGLLDRLPGQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578818931 1223 SKILVLDEATAAVD----LETDNLIQTTIQNEFAhcTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIPGP 1295
Cdd:COG3840 148 RPILLLDEPFSALDpalrQEMLDLVDELCRERGL--TVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGEPP 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1068-1290 |
4.64e-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: 4.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRY--RPeldlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFR-ILEAAGGQIII-----DGVDI----AS 1135
Cdd:COG1119 4 LELRNVTVRRggKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLfgerrGGEDVwelrKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1136 IGL------HDLREKLTIIpqDPIL--FSGSLrmnlDPFNNYSDEEIWKALELAHLksfvaslqLGLSHEVTEAGGNLSI 1207
Cdd:COG1119 80 IGLvspalqLRFPRDETVL--DVVLsgFFDSI----GLYREPTDEQRERARELLEL--------LGLAHLADRPFGTLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1208 GQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIqNEFAH---CTVITIAHRLHTIMDS-DKVMVLDNGKIIEC 1283
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALL-DKLAAegaPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAA 224
|
....*..
gi 578818931 1284 GSPEELL 1290
Cdd:COG1119 225 GPKEEVL 231
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
418-611 |
7.24e-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: 84.31 E-value: 7.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 418 SEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-----------TAYVPQQ-SWIQNGTIKD 485
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 486 NILFG----TEFNEKRYQQVLEACALLPDLEMLpggdlaeiGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 561
Cdd:cd03299 91 NIAYGlkkrKVDKKEIERKVLEIAEMLGIDHLL--------NRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578818931 562 HVGKHIFN--KVLGPNgllKGKTRLLVTHSM-HFLPQVDEIVVLGNGTIVEKG 611
Cdd:cd03299 163 RTKEKLREelKKIRKE---FGVTVLHVTHDFeEAWALADKVAIMLNGKLIQVG 212
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
426-631 |
7.77e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 84.04 E-value: 7.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 426 NLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TAYVPQQ---SWI-QNG------TIKDNILFG--- 490
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdlTALPPAErpvSMLfQENnlfphlTVAQNIGLGlrp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 491 ----TEFNEKRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAvdahvgkh 566
Cdd:COG3840 99 glklTAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSA-------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 567 ifnkvLGPN------GLLK------GKTRLLVTHSmhflPQ-----VDEIVVLGNGTIVEKGSYSALLAkkGEFAKNLKT 629
Cdd:COG3840 160 -----LDPAlrqemlDLVDelcrerGLTVLMVTHD----PEdaariADRVLLVADGRIAADGPTAALLD--GEPPPALAA 228
|
..
gi 578818931 630 FL 631
Cdd:COG3840 229 YL 230
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1084-1280 |
8.82e-18 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 83.69 E-value: 8.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDL----REKLTIIPQDPILFSG-- 1157
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafrRRHIGFVFQSFNLLPDlt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1158 -----SLRMNLDPFNNYSDEEiwKALELAHlksfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEAT 1232
Cdd:cd03255 99 alenvELPLLLAGVPKKERRE--RAEELLE--------RVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 578818931 1233 AAVDLETDNLIQTTIQ--NEFAHCTVITIAHRLHTIMDSDKVMVLDNGKI 1280
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 ... |
422-618 |
9.54e-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: 83.64 E-value: 9.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--------------TAYVPQ-QSWIQNGTIKDN 486
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEgRRIFPELTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 487 ILFG--TEFNEKRYQQVLEACALLPDL-EMLpggdlaeiGEKGINLSGGQKQRISLARATYQNLDIYLLDDP---LSAVd 560
Cdd:cd03224 96 LLLGayARRRAKRKARLERVYELFPRLkERR--------KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPsegLAPK- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 561 ahVGKHIFNKVLGPNGllKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 618
Cdd:cd03224 167 --IVEEIFEAIRELRD--EGVTILLVEQNARFALEIaDRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1068-1280 |
1.19e-17 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 82.96 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELdlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDI--ASIGLHDLREKL 1145
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1146 TIIPQDPILFSgslrmNLDPFNNYSDEEIW-------KALELA--HLKsfvaslQLGLSHEVTEAGGNLSIGQRQLLCLG 1216
Cdd:cd03262 79 GMVFQQFNLFP-----HLTVLENITLAPIKvkgmskaEAEERAleLLE------KVGLADKADAYPAQLSGGQQQRVAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578818931 1217 RALLRKSKILVLDEATAAVDLETDNLIQTTIQNeFAH--CTVITIAHRlhtiMD-----SDKVMVLDNGKI 1280
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPELVGEVLDVMKD-LAEegMTMVVVTHE----MGfarevADRVIFMDDGRI 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
186-644 |
1.29e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 89.26 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 186 GETVNLMSVDAQKL-MDVTNFMHMLWSSVLQIvLSIFFLWRELgpSVLAGVGVMVLVIPI-NAILSTKSKTIQVKNMKN- 262
Cdd:PLN03232 1007 GRVINRFSKDIGDIdRNVANLMNMFMNQLWQL-LSTFALIGTV--STISLWAIMPLLILFyAAYLYYQSTSREVRRLDSv 1083
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 263 -KDKRLKIMNEILSGIK-ILKYFAWepsfrDQVQNLRKKELKNLLAFSQLQC-----VVIFVFQLTPVLVSVV-TFSVYV 334
Cdd:PLN03232 1084 tRSPIYAQFGEALNGLSsIRAYKAY-----DRMAKINGKSMDNNIRFTLANTssnrwLTIRLETLGGVMIWLTaTFAVLR 1158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 335 LVDSNNildaQKAFTSiTLFNILRFPLSMLPMMISSMLQASV------STERLEKYLggdDLDTSAIRHDCN-------- 400
Cdd:PLN03232 1159 NGNAEN----QAGFAS-TMGLLLSYTLNITTLLSGVLRQASKaenslnSVERVGNYI---DLPSEATAIIENnrpvsgwp 1230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 401 FDKAMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG------------- 467
Cdd:PLN03232 1231 SRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcdvakfgltdlrr 1310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 468 TTAYVPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNL 547
Cdd:PLN03232 1311 VLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRS 1390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 548 DIYLLDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGE-FAKn 626
Cdd:PLN03232 1391 KILVLDEATASVDVRTDSLIQRTI---REEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSaFFR- 1466
|
490
....*....|....*...
gi 578818931 627 lktFLRHTGPEEEATVHD 644
Cdd:PLN03232 1467 ---MVHSTGPANAQYLSN 1481
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
417-612 |
1.46e-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: 82.85 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 417 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAYVPQQSWIQNGTI 483
Cdd:cd03369 19 DLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 484 KDNIlfgTEFNEKRYQQVLEACallpdlemlpggdlaEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHV 563
Cdd:cd03369 99 RSNL---DPFDEYSDEEIYGAL---------------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 578818931 564 gKHIFNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGS 612
Cdd:cd03369 161 -DALIQKTI--REEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
423-618 |
1.57e-17 |
|
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: 83.49 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 423 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG---TTAYVPQQSWI--------QNG------TIKD 485
Cdd:COG1127 22 DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqdiTGLSEKELYELrrrigmlfQGGalfdslTVFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 486 NILFG----TEFNEK-RYQQVLEAcallpdLEM--LPG-GDL--AEigekginLSGGQKQRISLARATYQNLDIYLLDDP 555
Cdd:COG1127 102 NVAFPlrehTDLSEAeIRELVLEK------LELvgLPGaADKmpSE-------LSGGMRKRVALARALALDPEILLYDEP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 556 LSAVDAhVGKHIFNKvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 618
Cdd:COG1127 169 TAGLDP-ITSAVIDE------LIRelrdelGLTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1100-1293 |
1.95e-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: 83.85 E-value: 1.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1100 VVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLRE-----------KLTIIPQDPILfsgslrmnldpfnn 1168
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkkismvfqSFALLPHRTVL-------------- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1169 ysdEEIWKALELAHL-------KSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVdletDN 1241
Cdd:cd03294 121 ---ENVAFGLEVQGVpraereeRAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL----DP 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 1242 LIQTTIQNEF------AHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1293
Cdd:cd03294 194 LIRREMQDELlrlqaeLQKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1068-1289 |
2.24e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 84.01 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELD-LVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLT 1146
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1147 IIPQDPI-LFSGSLRMNLDPF--NNysdeeiwKALELAHLKSFV-ASLQL-GLSHEVTEAGGNLSIGQRQLLCLGRALLR 1221
Cdd:PRK13650 85 MVFQNPDnQFVGATVEDDVAFglEN-------KGIPHEEMKERVnEALELvGMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578818931 1222 KSKILVLDEATAAVDLETD-NLIQT--TIQNEFaHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEEL 1289
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRlELIKTikGIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
422-612 |
2.36e-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: 82.77 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG--TTAYVPQQSWI----------QNGTIKDNILF 489
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedATDVPVQERNVgfvfqhyalfRHMTVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 490 GTEFnEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIf 568
Cdd:cd03296 98 GLRV-KPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAqLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKEL- 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 578818931 569 nkvlgpNGLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 612
Cdd:cd03296 176 ------RRWLRrlhdelHVTTVFVTHDQEEALEVaDRVVVMNKGRIEQVGT 220
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
425-618 |
3.16e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 82.88 E-value: 3.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 425 VNLDIMAGQLVAVIGPVGSGKSSLISAM--LGEMENVH---GHITIKGTTAYVPQQSWI-----------QN------GT 482
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCInlLEQPEAGTirvGDITIDTARSLSQQKGLIrqlrqhvgfvfQNfnlfphRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 483 IKDNILFGTEFNEKRYQQvlEACALLPDLemlpggdLAEIGEKGIN------LSGGQKQRISLARATYQNLDIYLLDDPL 556
Cdd:PRK11264 102 VLENIIEGPVIVKGEPKE--EATARAREL-------LAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVILFDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578818931 557 SAVDAHVGKHIFNKVlgpNGLLKGK-TRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 618
Cdd:PRK11264 173 SALDPELVGEVLNTI---RQLAQEKrTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKALFA 233
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
411-612 |
3.40e-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: 83.25 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 411 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSW---------IQN- 480
Cdd:TIGR04520 7 SFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeirkkvgmvFQNp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 481 ------GTIKDNILFGTEfN--------EKRYQQVLEACALLPDLEMLPggdlaeigekgINLSGGQKQRISLARATYQN 546
Cdd:TIGR04520 87 dnqfvgATVEDDVAFGLE-NlgvpreemRKRVDEALKLVGMEDFRDREP-----------HLLSGGQKQRVAIAGVLAMR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578818931 547 LDIYLLDDPLSAVDAhVGK-------HIFNKVlgpngllKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGS 612
Cdd:TIGR04520 155 PDIIILDEATSMLDP-KGRkevletiRKLNKE-------EGITVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
421-611 |
3.41e-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: 81.92 E-value: 3.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 421 TVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-----------TTAYVPQQ-SWIQNGTIKDNIL 488
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkdrDIAMVFQNyALYPHMTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 489 FGTEFNEKRY----QQVLEACALLpDLEMLpggdlaeIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVG 564
Cdd:cd03301 95 FGLKLRKVPKdeidERVREVAELL-QIEHL-------LDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 565 KHIFNKVlgpNGLLK--GKTRLLVTHSmhflpQV------DEIVVLGNGTIVEKG 611
Cdd:cd03301 167 VQMRAEL---KRLQQrlGTTTIYVTHD-----QVeamtmaDRIAVMNDGQIQQIG 213
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1084-1281 |
4.26e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 82.83 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDlREKLtI--IPQDPIL-FSGSL- 1159
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK-RAKY-IgrVFQDPMMgTAPSMt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1160 -------------RMNLDPFNNYSDEEIWKALelahlksfVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKIL 1226
Cdd:COG1101 99 ieenlalayrrgkRRGLRRGLTKKRRELFREL--------LATLGLGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 1227 VLDEATAAVDLET-DNLIQTT--IQNEFaHCTVITIAHRLH--------TIMdsdkvmvLDNGKII 1281
Cdd:COG1101 171 LLDEHTAALDPKTaALVLELTekIVEEN-NLTTLMVTHNMEqaldygnrLIM-------MHEGRII 228
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1084-1290 |
4.51e-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: 81.95 E-value: 4.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDL-REKLTIIPQDPILFSG-SLRM 1161
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1162 NLD--PFNNYSDEEIWKALELAH-----LKSFVASLqlglshevteaGGNLSIGQRQLLCLGRALLRKSKILVLDEATAA 1234
Cdd:COG0410 98 NLLlgAYARRDRAEVRADLERVYelfprLKERRRQR-----------AGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578818931 1235 -----VDlETDNLIQ------TTI----QN-EFAhctvITIAHRlhtimdsdkVMVLDNGKIIECGSPEELL 1290
Cdd:COG0410 167 lapliVE-EIFEIIRrlnregVTIllveQNaRFA----LEIADR---------AYVLERGRIVLEGTAAELL 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1068-1284 |
5.28e-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: 81.09 E-value: 5.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELdlVLRGITCDIGS-MekIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIaSIGLHDLREKLT 1146
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPgM--YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1147 IIPQDpilFSGSLRMNLDPFNNY-----------SDEEIWKALELahlksfvaslqLGLSHEVTEAGGNLSIGQRQLLCL 1215
Cdd:cd03264 76 YLPQE---FGVYPNFTVREFLDYiawlkgipskeVKARVDEVLEL-----------VNLGDRAKKKIGSLSGGMRRRVGI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1216 GRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDS-DKVMVLDNGKIIECG 1284
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
794-1040 |
5.41e-17 |
|
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: 82.99 E-value: 5.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 794 VYGALGLAQGIFVFI-AHFWSAFGFvHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWIT 872
Cdd:cd18557 41 ILLAIYLLQSVFTFVrYYLFNIAGE-RIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 873 CFLGIISTLVMICMATPVFTIIVIPLGIIYVSVQMFYVSTSRQLRR--LDSVTRSPiySHFSETVSGLPVIRAF---EHQ 947
Cdd:cd18557 120 NILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKevQDALAKAG--QVAEESLSNIRTVRSFsaeEKE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 948 -QRFLKHNEVRIDTNQKCVFsWITSNRWLAIRLELVGNLTVFFSALMMVIYRDTLSGDTVGFVLSnALNITQTLNWLVRM 1026
Cdd:cd18557 198 iRRYSEALDRSYRLARKKAL-ANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILY-TIMVASSVGGLSSL 275
|
250
....*....|....
gi 578818931 1027 TSEIETNIVAVERI 1040
Cdd:cd18557 276 LADIMKALGASERV 289
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
424-611 |
5.88e-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: 5.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 424 DVNLDI---MAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-----------------AYVPQQ-SWIQNGT 482
Cdd:cd03297 12 DFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrkiGLVFQQyALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 483 IKDNILFGTEFNEKRYQQVLEAcallpdlEMLPGGDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 561
Cdd:cd03297 92 VRENLAFGLKRKRNREDRISVD-------ELLDLLGLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578818931 562 HVGKHIFNKVlgpNGLLK--GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 611
Cdd:cd03297 165 ALRLQLLPEL---KQIKKnlNIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
423-562 |
6.18e-17 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 80.99 E-value: 6.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 423 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT------------TAYVPQQS-WIQNGTIKDNILF 489
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpirdaredyrrrLAYLGHADgLKPELTVRENLRF 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578818931 490 -----GTEFNEKRYQQVLEACALlPDLEMLPGGdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAH 562
Cdd:COG4133 99 waalyGLRADREAIDEALEAVGL-AGLADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA 165
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1068-1290 |
1.06e-16 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 83.20 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELDLV--LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRiLEAA-GGQIIIDGVDIASI---GLHDL 1141
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL-LERPtSGSVLVDGVDLTALserELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1142 REKLTIIPQDPILFSG---------SLRMnldpfNNYSDEEIW-KALELahlksfvasLQL-GLSHEVTEAGGNLSIGQR 1210
Cdd:COG1135 81 RRKIGMIFQHFNLLSSrtvaenvalPLEI-----AGVPKAEIRkRVAEL---------LELvGLSDKADAYPSQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1211 QLLCLGRALLRKSKILVLDEATAAVDLETD----NLIQtTIQNEFaHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGS 1285
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALDPETTrsilDLLK-DINREL-GLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
....*
gi 578818931 1286 PEELL 1290
Cdd:COG1135 225 VLDVF 229
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
413-616 |
1.10e-16 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 81.08 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 413 TWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT----------------TAYVPQQ- 475
Cdd:cd03256 9 TYPNGKKA-LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrrqIGMIFQQf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 476 SWIQNGTIKDNILFG---------TEFNEKRYQQVLEACALLPDLEMLpggDLAEIgeKGINLSGGQKQRISLARATYQN 546
Cdd:cd03256 88 NLIERLSVLENVLSGrlgrrstwrSLFGLFPKEEKQRALAALERVGLL---DKAYQ--RADQLSGGQQQRVAIARALMQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 547 LDIYLLDDPLSAVD---AHvgkhifnKVLgpnGLLK------GKTRLLVTHSMHF-LPQVDEIVVLGNGTIVEKGSYSAL 616
Cdd:cd03256 163 PKLILADEPVASLDpasSR-------QVM---DLLKrinreeGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
403-604 |
1.50e-16 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 81.15 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 403 KAMQFSEASFTWEHDSEAT-----VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------- 469
Cdd:cd03294 16 KAFKLLAKGKSKEEILKKTgqtvgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDiaamsrke 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 470 ----------------AYVPQQswiqngTIKDNILFGTEFN-------EKRYQQVLEACALLPDLEMLPGgdlaeigekg 526
Cdd:cd03294 96 lrelrrkkismvfqsfALLPHR------TVLENVAFGLEVQgvpraerEERAAEALELVGLEGWEHKYPD---------- 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578818931 527 iNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLGPNGLLKgKTRLLVTHSMhflpqvDEIVVLGN 604
Cdd:cd03294 160 -ELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQ-KTIVFITHDL------DEALRLGD 229
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1068-1262 |
1.92e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 78.35 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVrYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLtnclFRIL----EAAGGQIIIDGvdiasiglhdlRE 1143
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSL----FRALaglwPWGSGRIGMPE-----------GE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1144 KLTIIPQDPILFSGSLRmnldpfnnysdEEI---WKAlelahlksfvaslqlglshevteaggNLSIGQRQLLCLGRALL 1220
Cdd:cd03223 65 DLLFLPQRPYLPLGTLR-----------EQLiypWDD--------------------------VLSGGEQQRLAFARLLL 107
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 578818931 1221 RKSKILVLDEATAAVDLETDNLIQTTIQNEFAhcTVITIAHR 1262
Cdd:cd03223 108 HKPKFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1084-1282 |
2.31e-16 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 79.70 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDL----REKLTIIPQD-------- 1151
Cdd:COG1136 23 ALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlrRRHIGFVFQFfnllpelt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1152 -------PILFSGSLRmnldpfnNYSDEEIWKALElahlksfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSK 1224
Cdd:COG1136 103 alenvalPLLLAGVSR-------KERRERARELLE-----------RVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1225 ILVLDEATAAVDLETDNLIQTTIQ--NEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIE 1282
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRelNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
404-644 |
4.17e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.93 E-value: 4.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 404 AMQFSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT----------TAYVP 473
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTA-LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 474 QQS---WIQNGTIKDNILFGT--------EFNEKRYQQVLEACALLPDLEMlpggDLAEIGEkginLSGGQKQRISLARA 542
Cdd:PRK15056 85 QSEevdWSFPVLVEDVVMMGRyghmgwlrRAKKRDRQIVTAALARVDMVEF----RHRQIGE----LSGGQKKRVFLARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 543 TYQNLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK-----GKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKG-SYSAL 616
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIIS-------LLRelrdeGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGpTETTF 229
|
250 260 270
....*....|....*....|....*....|.
gi 578818931 617 LAKKGEFAknLKTFLRH---TGPEEEATVHD 644
Cdd:PRK15056 230 TAENLELA--FSGVLRHvalNGSEESIITDD 258
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1084-1293 |
4.43e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 79.71 E-value: 4.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGV------DIASIGLHDLREKLTIIPQDPILFSG 1157
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1158 -SLRMNLD-PFNNY---SDEEIWKALELAHLKsfvaslqLGLSHEVTE----AGGNLSIGQRQLLCLGRALLRKSKILVL 1228
Cdd:PRK14246 105 lSIYDNIAyPLKSHgikEKREIKKIVEECLRK-------VGLWKEVYDrlnsPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 1229 DEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1293
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
406-609 |
5.96e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 78.56 E-value: 5.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 406 QFSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG------TTAYVPQ----- 474
Cdd:COG2884 3 RFENVSKRYPGGREA-LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlKRREIPYlrrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 475 ----QSW--IQNGTIKDNILFG---TEFNEKRYQQ-VLEAcallpdLEMLpggdlaEIGEKG----INLSGGQKQRISLA 540
Cdd:COG2884 82 gvvfQDFrlLPDRTVYENVALPlrvTGKSRKEIRRrVREV------LDLV------GLSDKAkalpHELSGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 541 RATYQNLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK-----GKTRLLVTHSMHFLPQVDE-IVVLGNGTIVE 609
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIME-------LLEeinrrGTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
423-612 |
9.91e-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: 78.11 E-value: 9.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 423 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGeMENV-HGHITIKGTTAYVPQQSWIQ----------------NGTIKD 485
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKSTLLRCINL-LEEPdSGTITVDGEDLTDSKKDINKlrrkvgmvfqqfnlfpHLTVLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 486 NILFGTEFNEKRYQQVLEACAllpdLEMLpggDLAEIGEKG----INLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 561
Cdd:COG1126 97 NVTLAPIKVKKMSKAEAEERA----MELL---ERVGLADKAdaypAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578818931 562 H-VGkhifnKVLgpnGLLK-----GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 612
Cdd:COG1126 170 ElVG-----EVL---DVMRdlakeGMTMVVVTHEMGFAREVaDRVVFMDGGRIVEEGP 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
424-655 |
1.18e-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: 80.14 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 424 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-----------------AYVPQQSwiq-ngTIKD 485
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargiflpphrrriGYVFQEArlfphlSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 486 NILFGTEFNEK--RYQQVLEACALL---PDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 560
Cdd:COG4148 97 NLLYGRKRAPRaeRRISFDEVVELLgigHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 561 AHVGKHIfnkvlgpngL-----LKGKTR---LLVTHSMhflpqvDEI-------VVLGNGTIVEKGSYSALLAKKGefak 625
Cdd:COG4148 166 LARKAEI---------LpylerLRDELDipiLYVSHSL------DEVarladhvVLLEQGRVVASGPLAEVLSRPD---- 226
|
250 260 270
....*....|....*....|....*....|..
gi 578818931 626 nlktfLRHTGPEEEA-TVHDGS-EEEDDDYGL 655
Cdd:COG4148 227 -----LLPLAGGEEAgSVLEATvAAHDPDYGL 253
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
421-590 |
1.44e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.89 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 421 TVRDVNLDIMAGQLVAVIGPVGSGKSSLISAmLGEMENVHGHITIKGTTAY---------------------VPQQSWIQ 479
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRS-INRMNDLNPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 480 NGTIKDNILFGTEFNEKRYQQVLEACALlpdlEMLPGGDLAE-----IGEKGINLSGGQKQRISLARATYQNLDIYLLDD 554
Cdd:PRK14239 99 PMSIYENVVYGLRLKGIKDKQVLDEAVE----KSLKGASIWDevkdrLHDSALGLSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 578818931 555 PLSAVDAHVGKHIFNKVLGpnglLKGK-TRLLVTHSM 590
Cdd:PRK14239 175 PTSALDPISAGKIEETLLG----LKDDyTMLLVTRSM 207
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
424-655 |
1.67e-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: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 424 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-----------------AYVPQQ-SWIQNGTIKD 485
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlfdsrkgiflppekrriGYVFQEaRLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 486 NILFGTEF-----NEKRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 560
Cdd:TIGR02142 95 NLRYGMKRarpseRRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 561 AHVGKHIFnkvlgPngLLKGKTR------LLVTHSM-HFLPQVDEIVVLGNGTIVEKGSYSALLAKkgefaKNLKTFLRh 633
Cdd:TIGR02142 164 DPRKYEIL-----P--YLERLHAefgipiLYVSHSLqEVLRLADRVVVLEDGRVAAAGPIAEVWAS-----PDLPWLAR- 230
|
250 260
....*....|....*....|...
gi 578818931 634 tgpEEEATVHDGS-EEEDDDYGL 655
Cdd:TIGR02142 231 ---EDQGSLIEGVvAEHDQHYGL 250
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1068-1289 |
2.22e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 77.87 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTI 1147
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1148 IPQDPI-LFSGS---------LRMNLDPFNNYSdEEIWKALElahlksfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGR 1217
Cdd:PRK13648 88 VFQNPDnQFVGSivkydvafgLENHAVPYDEMH-RRVSEALK-----------QVDMLERADYEPNALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578818931 1218 ALLRKSKILVLDEATAAVDLETDNLIQTTIQ--NEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEEL 1289
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1067-1289 |
3.23e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 77.00 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1067 KIQFNNYQVRYRPELdlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILE-----AAGGQIIIDGVDI--ASIGLH 1139
Cdd:COG1117 11 KIEVRNLNVYYGDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlipgaRVEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1140 DLREKLTIIPQDPILFSGS--------LRMNLDPFNNYSDEEIWKALELAhlksfvaslqlGLSHEV----TEAGGNLSI 1207
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSiydnvaygLRLHGIKSKSELDEIVEESLRKA-----------ALWDEVkdrlKKSALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1208 GQRQLLCLGRALLRKSKILVLDEATAAVD-LETDNlIQTTIQNEFAHCTVITIAHRlhtiMD-----SDKVMVLDNGKII 1281
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDpISTAK-IEELILELKKDYTIVIVTHN----MQqaarvSDYTAFFYLGELV 232
|
....*...
gi 578818931 1282 ECGSPEEL 1289
Cdd:COG1117 233 EFGPTEQI 240
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1085-1290 |
3.42e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 77.58 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1085 LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDG--VDIASIGLHDLREKLTIIPQDP--ILFSGSLR 1160
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGMVFQDPdnQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1161 MNLD--PFN-NYSDEEIWKALELAHLKSFVASLQlglsHEVTEAggnLSIGQRQLLCLGRALLRKSKILVLDEATAAVD- 1236
Cdd:PRK13636 102 QDVSfgAVNlKLPEDEVRKRVDNALKRTGIEHLK----DKPTHC---LSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDp 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578818931 1237 ---LETDNLIQTTiQNEFAhCTVITIAHRLHTI-MDSDKVMVLDNGKIIECGSPEELL 1290
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 ... |
422-608 |
3.53e-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: 74.39 E-value: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTayvpqqswIQNGTIKDNILFGTEFnekRYQqv 501
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE--------VSFASPRDARRAGIAM---VYQ-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 502 leacallpdlemlpggdlaeigekginLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVlgpnGLLK-- 579
Cdd:cd03216 83 ---------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVI----RRLRaq 131
|
170 180 190
....*....|....*....|....*....|
gi 578818931 580 GKTRLLVTHSMHFLPQV-DEIVVLGNGTIV 608
Cdd:cd03216 132 GVAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
424-616 |
3.55e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 78.61 E-value: 3.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 424 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTayVPQQSwIQNG---------------TIKDNIL 488
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED--VTHRS-IQQRdicmvfqsyalfphmSLGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 489 FGTEF----NEKRYQQVLEACALLpdlemlpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHV 563
Cdd:PRK11432 101 YGLKMlgvpKEERKQRVKEALELV---------DLAGFEDRYVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 578818931 564 GKHIFNKVLGPNGLLkGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSAL 616
Cdd:PRK11432 172 RRSMREKIRELQQQF-NITSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
422-616 |
3.87e-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: 76.00 E-value: 3.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT------------TAYVPQqswiqngtikDNILF 489
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsirtdrkaarqsLGYCPQ----------FDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 490 gTEFNekryqqVLEACALLPDLEMLPGGDLAEIGEKGI--------------NLSGGQKQRISLARATYQNLDIYLLDDP 555
Cdd:cd03263 88 -DELT------VREHLRFYARLKGLPKSEIKEEVELLLrvlgltdkankrarTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578818931 556 LSAVDAHVGKHIFNKVLgpnGLLKGKTRLLVTHSMH---FLpqVDEIVVLGNGTIVEKGSYSAL 616
Cdd:cd03263 161 TSGLDPASRRAIWDLIL---EVRKGRSIILTTHSMDeaeAL--CDRIAIMSDGKLRCIGSPQEL 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1068-1293 |
4.43e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.95 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYrPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIG-LHDLREKLT 1146
Cdd:PRK13644 2 IRLENVSYSY-PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1147 IIPQDP-----------ILFSGSLRMNLDPFnnysdeEIWKALELAhlksfvaSLQLGLSHEVTEAGGNLSIGQRQLLCL 1215
Cdd:PRK13644 81 IVFQNPetqfvgrtveeDLAFGPENLCLPPI------EIRKRVDRA-------LAEIGLEKYRHRSPKTLSGGQGQCVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 1216 GRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHC-TVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIP 1293
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
405-629 |
4.48e-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: 76.87 E-value: 4.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 405 MQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-TAYVPQQSWIQNGTI 483
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIdISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 484 --KDNILFG--TEFN--------EKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYL 551
Cdd:cd03288 100 ilQDPILFSgsIRFNldpeckctDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 552 LDDPLSAVDAHVgKHIFNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKK-GEFAKNLKT 629
Cdd:cd03288 180 MDEATASIDMAT-ENILQKVV--MTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLVRT 255
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
422-611 |
4.83e-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: 75.65 E-value: 4.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQ-QSWIQNG-TIKDNILF-GTEFN--EK 496
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGlGGGFNPElTGRENIYLnGRLLGlsRK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 497 RYQQVLEACAllpdlemlpggDLAEIGE------KgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAH----VGKH 566
Cdd:cd03220 118 EIDEKIDEII-----------EFSELGDfidlpvK--TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfqekCQRR 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 578818931 567 IFNKVlgpnglLKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 611
Cdd:cd03220 185 LRELL------KQGKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
417-561 |
4.92e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 79.85 E-value: 4.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 417 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITI--KGTTAYVPQQSWIQNGTIKDNILF---GT 491
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQRPYLPLGTLREALLYpatAE 453
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 492 EFNEKRYQQVLEACAlLPDLEmlpgGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 561
Cdd:COG4178 454 AFSDAELREALEAVG-LGHLA----ERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
423-562 |
5.79e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 75.30 E-value: 5.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 423 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG----TTAYVPQQSWI--QNG-----TIKDNILFGT 491
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdidDPDVAEACHYLghRNAmkpalTVAENLEFWA 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 492 EFNEKRYQQVLEA-CAL-LPDLEMLPGGdlaeigekgiNLSGGQKQRISLAR--ATYQNldIYLLDDPLSAVDAH 562
Cdd:PRK13539 99 AFLGGEELDIAAAlEAVgLAPLAHLPFG----------YLSAGQKRRVALARllVSNRP--IWILDEPTAALDAA 161
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1067-1293 |
6.21e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 76.10 E-value: 6.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1067 KIQFNNYQVryrpeldlvLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILE-----AAGGQIIIDGVDIASIGLHDL 1141
Cdd:PRK14247 10 KVSFGQVEV---------LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1142 REKLTIIPQDP-------ILFSGSLRMNLDPFNNYSDE---EIWKALELAHLKSFVaslqlglSHEVTEAGGNLSIGQRQ 1211
Cdd:PRK14247 81 RRRVQMVFQIPnpipnlsIFENVALGLKLNRLVKSKKElqeRVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1212 LLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAH------RLhtimdSDKVMVLDNGKIIECGS 1285
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVEWGP 228
|
....*...
gi 578818931 1286 PEELLQIP 1293
Cdd:PRK14247 229 TREVFTNP 236
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
400-620 |
6.64e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 76.57 E-value: 6.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 400 NFDKAMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQ 479
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 480 N---------------GTIKDNILFGTE---FNEKRYQQVLEACALLPDLEMLpggdlaeIGEKGINLSGGQKQRISLAR 541
Cdd:PRK13632 83 KkigiifqnpdnqfigATVEDDIAFGLEnkkVPPKKMKDIIDDLAKKVGMEDY-------LDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 542 ATYQNLDIYLLDDPLSAVDAHvGKHIFNKVLGPNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKK 620
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPK-GKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1090-1284 |
8.40e-15 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 74.84 E-value: 8.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1090 CDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDlrEKLTIIPQDPILFSgslrmNLDPFNNY 1169
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFA-----HLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1170 S---------DEEIWKALElahlksfVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETD 1240
Cdd:cd03298 92 GlglspglklTAEDRQAIE-------VALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 578818931 1241 NLIQTTIqNEFAHCTVITIAHRLHTIMDS----DKVMVLDNGKIIECG 1284
Cdd:cd03298 165 AEMLDLV-LDLHAETKMTVLMVTHQPEDAkrlaQRVVFLDNGRIAAQG 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
422-640 |
8.61e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 77.43 E-value: 8.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLI---------SAmlgemenvhGHITIKGT--TAY--------------VPQQ- 475
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIrcinllerpTS---------GSVLVDGVdlTALserelraarrkigmIFQHf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 476 SWIQNGTIKDNILFGTEFN----EKRYQQVLEacaLLpdlemlpggDLAEIGEKG----INLSGGQKQRISLARATYQNL 547
Cdd:COG1135 92 NLLSSRTVAENVALPLEIAgvpkAEIRKRVAE---LL---------ELVGLSDKAdaypSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 548 DIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS-YSALLAK 619
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILD-------LLKdinrelGLTIVLITHEMDVVRRIcDRVAVLENGRIVEQGPvLDVFANP 232
|
250 260
....*....|....*....|..
gi 578818931 620 KGEFAKNL-KTFLRHTGPEEEA 640
Cdd:COG1135 233 QSELTRRFlPTVLNDELPEELL 254
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
415-612 |
1.44e-14 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 74.58 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 415 EHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TAYVPQQSWI----QNG------T 482
Cdd:cd03300 9 FYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKdiTNLPPHKRPVntvfQNYalfphlT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 483 IKDNILFGTEFNEKRYQQVLEACAllpdlEMLPGGDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 561
Cdd:cd03300 89 VFENIAFGLRLKKLPKAEIKERVA-----EALDLVQLEGYANRKPSqLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578818931 562 HVGKHI------FNKVLgpngllkGKTRLLVTH------SMHflpqvDEIVVLGNGTIVEKGS 612
Cdd:cd03300 164 KLRKDMqlelkrLQKEL-------GITFVFVTHdqeealTMS-----DRIAVMNKGKIQQIGT 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
423-622 |
1.48e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.18 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 423 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITI-KGTT-AYVPQ-QSWIQNGTIKDNILFGtefNEKRYQ 499
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpKGLRiGYLPQePPLDDDLTVLDTVLDG---DAELRA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 500 QVLEACALLPDLEMlPGGDLAEIGEK-----------------------GI----------NLSGGQKQRISLARATYQN 546
Cdd:COG0488 92 LEAELEELEAKLAE-PDEDLERLAELqeefealggweaearaeeilsglGFpeedldrpvsELSGGWRRRVALARALLSE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 547 LDIYLLDDP-----LSAVD---AHVGKHifnkvlgPNGLlkgktrLLVTHSMHFLPQV-DEIVVLGNGTIVE-KGSYSAL 616
Cdd:COG0488 171 PDLLLLDEPtnhldLESIEwleEFLKNY-------PGTV------LVVSHDRYFLDRVaTRILELDRGKLTLyPGNYSAY 237
|
....*.
gi 578818931 617 LAKKGE 622
Cdd:COG0488 238 LEQRAE 243
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
411-611 |
1.77e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 75.44 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 411 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTaYVPQQSW---------IQN- 480
Cdd:PRK13635 12 SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV-LSEETVWdvrrqvgmvFQNp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 481 ------GTIKDNILFGTEFNE-------KRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNL 547
Cdd:PRK13635 91 dnqfvgATVQDDVAFGLENIGvpreemvERVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578818931 548 DIYLLDDPLSAVDAhVGKHifnKVLGPNGLLKGKTRLLV---THSMHFLPQVDEIVVLGNGTIVEKG 611
Cdd:PRK13635 160 DIIILDEATSMLDP-RGRR---EVLETVRQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEEG 222
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
424-562 |
1.80e-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: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 424 DVNLDIMAGQLVAVIGPVGSGKSSL---ISAMLGEMENVHGHITIKG----------TTAYVPQQS-WIQNGTIKDNILF 489
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLldaISGRVEGGGTTSGQILFNGqprkpdqfqkCVAYVRQDDiLLPGLTVRETLTY 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 490 -----GTEFNEKRYQQVLEACALLPDLEMLP-GGDLAEigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAH 562
Cdd:cd03234 105 tailrLPRKSSDAIRKKRVEDVLLRDLALTRiGGNLVK------GISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
424-611 |
1.83e-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: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 424 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG---TTAYV---PQQSWIQNG------TIKDNILFG- 490
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvTAAPPadrPVSMLFQENnlfahlTVEQNVGLGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 491 ------TEFNEKRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVG 564
Cdd:cd03298 96 spglklTAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 578818931 565 KHIFNKVLGPNGlLKGKTRLLVTHSMHFLPQVDE-IVVLGNGTIVEKG 611
Cdd:cd03298 165 AEMLDLVLDLHA-ETKMTVLMVTHQPEDAKRLAQrVVFLDNGRIAAQG 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
422-611 |
1.88e-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: 73.79 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQNGTI------------KDNILF 489
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALieapgfypnltaRENLRL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 490 ---GTEFNEKRYQQVLEAcallpdlemlpgGDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGK 565
Cdd:cd03268 96 larLLGIRKKRIDEVLDV------------VGLKDSAKKKVkGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 578818931 566 HIFNKVLGPNGllKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 611
Cdd:cd03268 164 ELRELILSLRD--QGITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1084-1291 |
2.17e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 74.67 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSG-SLR-- 1160
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRel 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1161 --MNLDPFNNY----SDEE---IWKALELAHLKSFVaslqlglSHEVTEaggnLSIGQRQLLCLGRALLRKSKILVLDEA 1231
Cdd:PRK11231 97 vaYGRSPWLSLwgrlSAEDnarVNQAMEQTRINHLA-------DRRLTD----LSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 1232 TAAVDL----ETDNLIQTTIQNefaHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQ 1291
Cdd:PRK11231 166 TTYLDInhqvELMRLMRELNTQ---GKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1068-1295 |
2.18e-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: 74.26 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYrPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTI 1147
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1148 IPQDPILFSG-SLRMN--LDP-FNNYSDEEIWK----ALELAHLKSfvASLQLGLSHEvteaggnLSIGQRQLLCLGRAL 1219
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPkLLKWPKEKIREradeLLALVGLDP--AEFADRYPHE-------LSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1220 LRKSKILVLDEATAAVDLETdnliQTTIQNEFA------HCTVITIAHRL-HTIMDSDKVMVLDNGKIIECGSPEELLQI 1292
Cdd:cd03295 151 AADPPLLLMDEPFGALDPIT----RDQLQEEFKrlqqelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
...
gi 578818931 1293 PGP 1295
Cdd:cd03295 227 PAN 229
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1067-1291 |
2.67e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 74.67 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1067 KIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLT 1146
Cdd:PRK13635 5 IIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1147 IIPQDPI-LFSGSLRMNLDPF----NNYSDEEIWK----ALELAHLKSFvaslqlgLSHEVTeaggNLSIGQRQLLCLGR 1217
Cdd:PRK13635 85 MVFQNPDnQFVGATVQDDVAFglenIGVPREEMVErvdqALRQVGMEDF-------LNREPH----RLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 1218 ALLRKSKILVLDEATAAVDLETDNLIQTTIQ--NEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQ 1291
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
426-618 |
2.89e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 73.85 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 426 NLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TAYVPQQSWI-----QNG-----TIKDNILFG--- 490
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhTTTPPSRRPVsmlfqENNlfshlTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 491 ----TEFNEKRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKH 566
Cdd:PRK10771 99 glklNAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578818931 567 IFNkvlgpngLL------KGKTRLLVTHS----MHFLPQVdeiVVLGNGTIVEKGSYSALLA 618
Cdd:PRK10771 168 MLT-------LVsqvcqeRQLTLLMVSHSledaARIAPRS---LVVADGRIAWDGPTDELLS 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
422-609 |
2.96e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 74.30 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISA---MLGEMENVH--GHITIKGTTAY---------------VPQQSwiqN- 480
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRClnrMNDLIPGARveGEILLDGEDIYdpdvdvvelrrrvgmVFQKP---Np 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 481 --GTIKDNILFGtefnekryqqvleacalLPDLEMLPGGDLAEIGEK------------------GINLSGGQKQRISLA 540
Cdd:COG1117 104 fpKSIYDNVAYG-----------------LRLHGIKSKSELDEIVEEslrkaalwdevkdrlkksALGLSGGQQQRLCIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578818931 541 RATYQNLDIYLLDDPLSAVD----AHVGKHIFNkvlgpnglLKGK-TRLLVTHSMHflpQV----DEIVVLGNGTIVE 609
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDpistAKIEELILE--------LKKDyTIVIVTHNMQ---QAarvsDYTAFFYLGELVE 233
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
402-612 |
3.13e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 74.84 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 402 DKAMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSS---LISAMLGEMENVHGHITIKGTTaYVPQQSW- 477
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGIT-LTAKTVWd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 478 --------IQN-------GTIKDNILFGTEFNEKRYQQVLEACA-LLPDLEMLPggdlaEIGEKGINLSGGQKQRISLAR 541
Cdd:PRK13640 82 irekvgivFQNpdnqfvgATVGDDVAFGLENRAVPRPEMIKIVRdVLADVGMLD-----YIDSEPANLSGGQKQRVAIAG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578818931 542 ATYQNLDIYLLDDPLSAVDAHVGKHIFN---KVLGPNGLlkgkTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGS 612
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKlirKLKKKNNL----TVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
411-618 |
4.82e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 73.72 E-value: 4.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 411 SFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT---------------------- 468
Cdd:COG4167 19 GLFRRQQFEA-VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleygdykyrckhirmifqdpn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 469 TAYVPQQswiQNGTIKDNIL-FGTEFNEK-RYQQV---LEACALLPD-----LEMLpggdlaeigekginlSGGQKQRIS 538
Cdd:COG4167 98 TSLNPRL---NIGQILEEPLrLNTDLTAEeREERIfatLRLVGLLPEhanfyPHML---------------SSGQKQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 539 LARATYQNLDIYLLDDPLSAVDAHVGKHIFNKvlgpngLLKGKTRL-----LVTHSM----HFlpqVDEIVVLGNGTIVE 609
Cdd:COG4167 160 LARALILQPKIIIADEALAALDMSVRSQIINL------MLELQEKLgisyiYVSQHLgivkHI---SDKVLVMHQGEVVE 230
|
....*....
gi 578818931 610 KGSYSALLA 618
Cdd:COG4167 231 YGKTAEVFA 239
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1084-1284 |
4.96e-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: 4.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCL--FRILEAAGGQIIIDGVdiaSIGLHDLREKLTIIPQDPILFsGSLrm 1161
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGR---PLDKRSFRKIIGYVPQDDILH-PTL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1162 nldpfnnysdeEIWKALEL-AHLKSfvaslqlglshevteaggnLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETD 1240
Cdd:cd03213 98 -----------TVRETLMFaAKLRG-------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 578818931 1241 NLIQTTIQNE-FAHCTVITIAHRLHTIMDS--DKVMVLDNGKIIECG 1284
Cdd:cd03213 148 LQVMSLLRRLaDTGRTIICSIHQPSSEIFElfDKLLLLSQGRVIYFG 194
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
422-641 |
5.00e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 73.66 E-value: 5.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAM-----LGEMENVHGHITIKGTTAYVPQQSWIQ---------------NG 481
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYAPDVDPVEvrrrigmvfqkpnpfPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 482 TIKDNILFGTEFN------EKRYQQVLEACALLPDLEmlpggdlAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDP 555
Cdd:PRK14243 106 SIYDNIAYGARINgykgdmDELVERSLRQAALWDEVK-------DKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 556 LSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLakkGEFAKNLKTFlrhTG 635
Cdd:PRK14243 179 CSALDPISTLRIEELM---HELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYL---VEFDRTEKIF---NS 249
|
....*.
gi 578818931 636 PEEEAT 641
Cdd:PRK14243 250 PQQQAT 255
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1083-1289 |
5.13e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.97 E-value: 5.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1083 LVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIG-LHDLREKLTIIPQDP--------- 1152
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQNPdnqivativ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1153 ---ILFsGSLRMNLDPfnnysdEEIWKALELAhLKSfvaslqLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLD 1229
Cdd:PRK13633 104 eedVAF-GPENLGIPP------EEIRERVDES-LKK------VGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578818931 1230 EATAAVDLETDNLIQTTIQ--NEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEEL 1289
Cdd:PRK13633 170 EPTAMLDPSGRREVVNTIKelNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1068-1282 |
5.33e-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: 72.50 E-value: 5.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELD--LVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHdlrekL 1145
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1146 TIIPQDPILF---------SGSLRMNLDPFNNySDEEIWKALELAHLKSFVASLqlglSHEvteaggnLSIGQRQLLCLG 1216
Cdd:cd03293 76 GYVFQQDALLpwltvldnvALGLELQGVPKAE-ARERAEELLELVGLSGFENAY----PHQ-------LSGGMRQRVALA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578818931 1217 RALLRKSKILVLDEATAAVDLETDNLIQTTIQN--EFAHCTVITIAHRLH-TIMDSDKVMVLDN--GKIIE 1282
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
792-955 |
5.90e-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: 5.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 792 VGVYGALGLAQGIFVFIAHFWSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWI 871
Cdd:cd18547 48 LLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 872 TCFLGIISTLVMICMATPVFTIIVIPLGIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQ---- 947
Cdd:cd18547 128 SSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREeeai 207
|
....*...
gi 578818931 948 QRFLKHNE 955
Cdd:cd18547 208 EEFDEINE 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1068-1293 |
6.08e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 72.82 E-value: 6.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELdlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDI--ASIGLHDLREKL 1145
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1146 TIIPQDPILFS----------GSLRMNldpfnNYSDEEiwkALELAhlKSFVAslQLGLSHEVTEAGGNLSIGQRQLLCL 1215
Cdd:PRK09493 80 GMVFQQFYLFPhltalenvmfGPLRVR-----GASKEE---AEKQA--RELLA--KVGLAERAHHYPSELSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1216 GRALLRKSKILVLDEATAAVDLETDNLIQTTIQ---NEFAHCTVITiahrlHTIMDSDKV----MVLDNGKIIECGSPEE 1288
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELRHEVLKVMQdlaEEGMTMVIVT-----HEIGFAEKVasrlIFIDKGRIAEDGDPQV 222
|
....*
gi 578818931 1289 LLQIP 1293
Cdd:PRK09493 223 LIKNP 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1084-1291 |
6.20e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 73.27 E-value: 6.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPIL-FSGS---- 1158
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTveev 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1159 LRMNLDPFNNYSDEE---IWKALELAHLKSFVASLQLGLShevteagGnlsiGQRQLLCLGRALLR------KSKILVLD 1229
Cdd:PRK13548 97 VAMGRAPHGLSRAEDdalVAAALAQVDLAHLAGRDYPQLS-------G----GEQQRVQLARVLAQlwepdgPPRWLLLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578818931 1230 EATAAVDLETDnliQTTIQ--NEFAH---CTVITIAHRLH-TIMDSDKVMVLDNGKIIECGSPEELLQ 1291
Cdd:PRK13548 166 EPTSALDLAHQ---HHVLRlaRQLAHergLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1100-1306 |
6.83e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 73.68 E-value: 6.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1100 VVGRTGAGKSS---LTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPI-LFSGSlrmnldpfnNYSDEEIW 1175
Cdd:PRK13640 38 LIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREKVGIVFQNPDnQFVGA---------TVGDDVAF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1176 ----KALELAHLKSFVASL--QLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQN 1249
Cdd:PRK13640 109 glenRAVPRPEMIKIVRDVlaDVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRK 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 1250 --EFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGpfyfMAKEAGIE 1306
Cdd:PRK13640 189 lkKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVE----MLKEIGLD 243
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
405-633 |
7.16e-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: 7.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 405 MQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLgEMENVHGHITIKGTT-------------AY 471
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGVSwnsvplqkwrkafGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 472 VPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYL 551
Cdd:cd03289 82 IPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 552 LDDPLSAVDAhVGKHIFNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEF------AK 625
Cdd:cd03289 162 LDEPSAHLDP-ITYQVIRKTL--KQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFkqaispSD 238
|
....*...
gi 578818931 626 NLKTFLRH 633
Cdd:cd03289 239 RLKLFPRR 246
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1099-1288 |
8.29e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.83 E-value: 8.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1099 GVVGRTGAGKSSLTNCLFRILEAAGGQIIIDG--VDIAS--------IGLhdlrekltiIPQDPILFsgslrmnlDPFN- 1167
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSprdaialgIGM---------VHQHFMLV--------PNLTv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1168 --NY--SDEEIWKA-LELAHLKSFVASL--QLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATaAV--DLE 1238
Cdd:COG3845 98 aeNIvlGLEPTKGGrLDRKAARARIRELseRYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPT-AVltPQE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578818931 1239 TDNLIQtTIQNeFAH--CTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEE 1288
Cdd:COG3845 177 ADELFE-ILRR-LAAegKSIIFITHKLREVMAiADRVTVLRRGKVVGTVDTAE 227
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
424-633 |
8.37e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 72.43 E-value: 8.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 424 DVNLDIMAGQLVAVIGPVGSGKSSLISAM--LGEMEN----VHGhITIKGTTA----------YVPQQSWI-QNGTIKDN 486
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITSgdliVDG-LKVNDPKVderlirqeagMVFQQFYLfPHLTALEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 487 ILFGTEFNEKRYQQVLEACALlpdlEMLPGGDLAE-IGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVgK 565
Cdd:PRK09493 98 VMFGPLRVRGASKEEAEKQAR----ELLAKVGLAErAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL-R 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578818931 566 HIFNKV---LGPNGLlkgkTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLAKKGefAKNLKTFLRH 633
Cdd:PRK09493 173 HEVLKVmqdLAEEGM----TMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIKNPP--SQRLQEFLQH 238
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
422-618 |
8.53e-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: 72.32 E-value: 8.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--------------AYVPQqswiqnG------ 481
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDitglpphriarlgiGYVPE------Grrifps 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 482 -TIKDNILFG--TEFNEKRYQQVLE-ACALLPDL-EML--PGGdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDD 554
Cdd:COG0410 93 lTVEENLLLGayARRDRAEVRADLErVYELFPRLkERRrqRAG----------TLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578818931 555 P---LSAVdahVGKHIFNKVLGPNGllKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 618
Cdd:COG0410 163 PslgLAPL---IVEEIFEIIRRLNR--EGVTILLVEQNARFALEIaDRAYVLERGRIVLEGTAAELLA 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
422-612 |
8.69e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 72.88 E-value: 8.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAYVPQQS-----WiqngTI 483
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHSslsfpF----TV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 484 KDNILFGTE---FNEKRYQQVLEACALLPDLEMLPGGDLAEigekginLSGGQKQRISLARA----TYQNLD--IYLLDD 554
Cdd:PRK13548 94 EEVVAMGRAphgLSRAEDDALVAAALAQVDLAHLAGRDYPQ-------LSGGEQQRVQLARVlaqlWEPDGPprWLLLDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 555 PLSAVD-AHvgKHIfnkVLgpnGLLKGKTR---LLVTHSMHFLPQV----DEIVVLGNGTIVEKGS 612
Cdd:PRK13548 167 PTSALDlAH--QHH---VL---RLARQLAHergLAVIVVLHDLNLAaryaDRIVLLHQGRLVADGT 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1068-1290 |
9.40e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 73.20 E-value: 9.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELDL-VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLT 1146
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1147 IIPQDPI-LFSGSLRMNLDPF----NNYSDEEIWKALELAHLKSFVASLQlglshevTEAGGNLSIGQRQLLCLGRALLR 1221
Cdd:PRK13642 85 MVFQNPDnQFVGATVEDDVAFgmenQGIPREEMIKRVDEALLAVNMLDFK-------TREPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578818931 1222 KSKILVLDEATAAVDLETDNLIQTTIQ--NEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELL 1290
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHeiKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1068-1284 |
1.16e-13 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 71.63 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELDLV--LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIAS--------IG 1137
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKepaearrrLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1138 LHD----LREKLTIIPQdpILFSGSLR-MNLDPFNNYSDEeiwkalelahlksfVASlQLGLSHEVTEAGGNLSIGQRQL 1212
Cdd:cd03266 82 FVSdstgLYDRLTAREN--LEYFAGLYgLKGDELTARLEE--------------LAD-RLGMEELLDRRVGGFSTGMRQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578818931 1213 LCLGRALLRKSKILVLDEATAAVD-LETDNLIQTTIQNEFAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECG 1284
Cdd:cd03266 145 VAIARALVHDPPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1084-1291 |
1.36e-13 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 71.81 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDlREKLTII--PQDPILFSG-SLR 1160
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIGylPQEASIFRKlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1161 MNLD---PFNNYSDEEIWKALElAHLKSFvaslqlGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDL 1237
Cdd:cd03218 94 ENILavlEIRGLSKKEREEKLE-ELLEEF------HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 1238 ETDNLIQTTIQN--EFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQ 1291
Cdd:cd03218 167 IAVQDIQKIIKIlkDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1082-1254 |
1.73e-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: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1082 DLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIAsiglhdlreKLTIIPQDPILFSG---- 1157
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA---------EQRDEPHENILYLGhlpg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1158 -----SLRMNLD---PFNNYSDEEIWKALElahlksfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLD 1229
Cdd:TIGR01189 84 lkpelSALENLHfwaAIHGGAQRTIEDALA-----------AVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILD 152
|
170 180
....*....|....*....|....*
gi 578818931 1230 EATAAVDLETDNLIQTTIQnefAHC 1254
Cdd:TIGR01189 153 EPTTALDKAGVALLAGLLR---AHL 174
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1087-1293 |
1.77e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.20 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1087 GITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREK---LTIIPQDPiLFSGSLRMNL 1163
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDP-LASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1164 -----DPFNNYSDEeiwkaLELAHLKSFVAS--LQLGL--------SHEvteaggnLSIGQRQLLCLGRALLRKSKILVL 1228
Cdd:PRK15079 118 geiiaEPLRTYHPK-----LSRQEVKDRVKAmmLKVGLlpnlinryPHE-------FSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1229 DEATAAVDLETD----NLIQtTIQNEFAhCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1293
Cdd:PRK15079 186 DEPVSALDVSIQaqvvNLLQ-QLQREMG-LSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
417-612 |
1.92e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.44 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 417 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-TTAYVPQ---------QSW--IQNGTIK 484
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqDITHVPAenrhvntvfQSYalFPHMTVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 485 DNILFGTEF----NEKRYQQVLEAcallpdLEMLPGGDLAEigEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 560
Cdd:PRK09452 105 ENVAFGLRMqktpAAEITPRVMEA------LRMVQLEEFAQ--RKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578818931 561 AHVGKHIFNKvlgpnglLK------GKTRLLVTH------SMHflpqvDEIVVLGNGTIVEKGS 612
Cdd:PRK09452 177 YKLRKQMQNE-------LKalqrklGITFVFVTHdqeealTMS-----DRIVVMRDGRIEQDGT 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1068-1266 |
1.94e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 71.99 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYrpELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAG-----GQIIIDGVDIAS--IGLHD 1140
Cdd:PRK14258 8 IKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYErrVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1141 LREKLTIIPQDPILFSGSLRMNLdpfnNYSDEEI-WK-ALEL-----AHLKSfvASLQLGLSHEVTEAGGNLSIGQRQLL 1213
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNV----AYGVKIVgWRpKLEIddiveSALKD--ADLWDEIKHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 1214 CLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEF--AHCTVITIAHRLHTI 1266
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQV 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1085-1289 |
2.19e-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: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1085 LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASiGLHDLREKLTIIPQDPILFSG-SLRMNL 1163
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDElTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1164 DPF-------NNYSDEEIWKALELahlksfvaslqLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVD 1236
Cdd:cd03265 95 YIHarlygvpGAERRERIDELLDF-----------VGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1237 LETDNLIQTTIQ--NEFAHCTVITIAHrlhtIMD-----SDKVMVLDNGKIIECGSPEEL 1289
Cdd:cd03265 164 PQTRAHVWEYIEklKEEFGMTILLTTH----YMEeaeqlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
422-618 |
2.23e-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: 71.31 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TAYVPQQSW-------------IQNGTIKDN 486
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEdiTGLPPHEIArlgigrtfqiprlFPELTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 487 ILFGTEFNEKRYQ-----------------QVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDI 549
Cdd:cd03219 96 VMVAAQARTGSGLllararreereareraeELLERVGLADLADRPAG-----------ELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578818931 550 YLLDDP---LSAVDAHVGKHIFNKVLGpngllKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 618
Cdd:cd03219 165 LLLDEPaagLNPEETEELAELIRELRE-----RGITVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1085-1278 |
2.31e-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: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1085 LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREK----LTIIPQDPILFSGSLR 1160
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1161 MNL---DPFNnysdEEIWKAL-ELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVD 1236
Cdd:cd03290 97 ENItfgSPFN----KQRYKAVtDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 578818931 1237 LE-TDNLIQTTIQnEFAH---CTVITIAHRLHTIMDSDKVMVLDNG 1278
Cdd:cd03290 173 IHlSDHLMQEGIL-KFLQddkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
400-611 |
2.54e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 71.71 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 400 NFDKAMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHI-------------TIK 466
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfeKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 467 GTTAYVPQQSWIQ--NGTIKDNILFGTEFNEKRYQQVLEACA-LLPDLEMLPGGDlaeigEKGINLSGGQKQRISLARAT 543
Cdd:PRK13648 83 KHIGIVFQNPDNQfvGSIVKYDVAFGLENHAVPYDEMHRRVSeALKQVDMLERAD-----YEPNALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578818931 544 YQNLDIYLLDDPLSAVDAHVGKHIFNKVLGPNGlLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKG 611
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKS-EHNITIISITHDLSEAMEADHVIVMNKGTVYKEG 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
422-619 |
2.84e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.95 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIkGTT---AYVPQQswiQ-----NGTIKDNIlfgTEF 493
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETvkiGYFDQH---QeeldpDKTVLDEL---RDG 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 494 NEKRYQQvlEACALLPDLeMLPGGD-LAEIGekgiNLSGGQKQRISLARATYQNLDIYLLDDP-----LSAVDAhvgkhi 567
Cdd:COG0488 404 APGGTEQ--EVRGYLGRF-LFSGDDaFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPtnhldIETLEA------ 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 578818931 568 fnkvLgpNGLL---KGkTRLLVTHSMHFLPQV-DEIVVLGNGTIVEK-GSYSALLAK 619
Cdd:COG0488 471 ----L--EEALddfPG-TVLLVSHDRYFLDRVaTRILEFEDGGVREYpGGYDDYLEK 520
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1084-1293 |
2.88e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 71.76 E-value: 2.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDP--ILFSGSLRM 1161
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1162 NL--DPFNNYSDEEiwkalELAHLKSFVASLqLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLE- 1238
Cdd:PRK13652 99 DIafGPINLGLDEE-----TVAHRVSSALHM-LGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQg 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 1239 TDNLIQttIQNEFAH---CTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1293
Cdd:PRK13652 173 VKELID--FLNDLPEtygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
422-620 |
3.02e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 70.88 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTA--------YVPQQSwiqnGtiKDNILF---- 489
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSallelgagFHPELT----G--RENIYLngrl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 490 -GteFNEKRYQQVLEACAllpdlemlpggDLAEIGEKgINL-----SGGQKQRISLARATYQNLDIYLLDDPLSAVDAHV 563
Cdd:COG1134 116 lG--LSRKEIDEKFDEIV-----------EFAELGDF-IDQpvktySSGMRARLAFAVATAVDPDILLVDEVLAVGDAAF 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 564 GKHIFNKVlgpNGLLK-GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS-------YSALLAKK 620
Cdd:COG1134 182 QKKCLARI---RELREsGRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDpeeviaaYEALLAGR 244
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
405-620 |
3.02e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 71.73 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 405 MQFSEASFTWE----HDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT----------- 469
Cdd:PRK13646 3 IRFDNVSYTYQkgtpYEHQA-IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithktkdkyir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 470 ------AYVPQ--QSWIQNGTIKDNILFGTE-FNEKRYQQVLEACALLPDLemlpgGDLAEIGEKG-INLSGGQKQRISL 539
Cdd:PRK13646 82 pvrkriGMVFQfpESQLFEDTVEREIIFGPKnFKMNLDEVKNYAHRLLMDL-----GFSRDVMSQSpFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 540 ARATYQNLDIYLLDDPLSAVDAHvGKHIFNKVLGPNGLLKGKTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGSYSALLA 618
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQ-SKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFK 235
|
..
gi 578818931 619 KK 620
Cdd:PRK13646 236 DK 237
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
417-560 |
3.62e-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: 68.72 E-value: 3.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 417 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITI--KGTTAYVPQQSWIQNGTIKDNILFgtefn 494
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpeGEDLLFLPQRPYLPLGTLREQLIY----- 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 495 ekryqqvleacallpdlemlPGGDlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 560
Cdd:cd03223 87 --------------------PWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1068-1289 |
3.66e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 71.40 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELDLVLRG---ITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDI----ASIGLHD 1140
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGldnISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1141 LREKLTIIPQDP--ILFSGSLRMNLD--PFN-NYSDEEIwKALELAHLKsfvaslQLGLSHEVTEAGG-NLSIGQRQLLC 1214
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTVLKDVEfgPKNfGFSEDEA-KEKALKWLK------KVGLSEDLISKSPfELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578818931 1215 LGRALLRKSKILVLDEATAAVDLET-DNLIQTTIQNEFAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEEL 1289
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEI 232
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1084-1290 |
3.78e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.95 E-value: 3.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPIL---FSGS-- 1158
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfeFDVRqv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1159 LRMN-------LDPFNNYSDEEIWKALELAHLKSFVAslqlglsHEVTEaggnLSIGQRQLLCLGRALLRKSKILVLDEA 1231
Cdd:PRK09536 98 VEMGrtphrsrFDTWTETDRAAVERAMERTGVAQFAD-------RPVTS----LSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578818931 1232 TAAVDL----ETDNLIQTTIQNEFahcTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELL 1290
Cdd:PRK09536 167 TASLDInhqvRTLELVRRLVDDGK---TAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1081-1290 |
5.10e-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: 72.06 E-value: 5.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1081 LDLVLRGITcdigsmekiGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDG---VDIAS----------IGLhdlreklti 1147
Cdd:COG4148 20 FTLPGRGVT---------ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARgiflpphrrrIGY--------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1148 IPQDPILFSG-SLRMNLDpfnnYSDEEIWKALELAHLKSFVAslQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKIL 1226
Cdd:COG4148 82 VFQEARLFPHlSVRGNLL----YGRKRAPRAERRISFDEVVE--LLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578818931 1227 VLDEATAAVDLETDNLIQ---TTIQNEFAhCTVITIAH------RLhtimdSDKVMVLDNGKIIECGSPEELL 1290
Cdd:COG4148 156 LMDEPLAALDLARKAEILpylERLRDELD-IPILYVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVL 222
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
744-1040 |
1.05e-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: 70.14 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 744 LFSIFFIILAfvmnsVAFIGSNLWLSAWTSDsKIFNstdypasQRDMRVGVYGALGLAqGIFVF--IAHFWSAFGFVHAS 821
Cdd:cd18552 2 ALAILGMILV-----AATTAALAWLLKPLLD-DIFV-------EKDLEALLLVPLAII-GLFLLrgLASYLQTYLMAYVG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 822 N-ILH---KQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTL-VMICMATP--VFTII 894
Cdd:cd18552 68 QrVVRdlrNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLgVLFYLDWKltLIALV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 895 VIPLGIIYVSVqmfyvsTSRQLRRL-----DSVTRspIYSHFSETVSGLPVIRAF---EHQ-QRFLKHNEvridtnqkcv 965
Cdd:cd18552 148 VLPLAALPIRR------IGKRLRKIsrrsqESMGD--LTSVLQETLSGIRVVKAFgaeDYEiKRFRKANE---------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 966 fswitSNRWLAIRLELVGNLTV----FFSALMM--VIY---RDTLSGD-TVG-FV--LSNALNITQTLNWLVRMTSEIET 1032
Cdd:cd18552 210 -----RLRRLSMKIARARALSSplmeLLGAIAIalVLWyggYQVISGElTPGeFIsfITALLLLYQPIKRLSNVNANLQR 284
|
....*...
gi 578818931 1033 NIVAVERI 1040
Cdd:cd18552 285 GLAAAERI 292
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
422-612 |
1.41e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 69.27 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYVPQQSWIQNG-TIKDNI 487
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPismlssrqlarrlALLPQHHLTPEGiTVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 488 LFG-----------TEFNEKRYQQVLEACallpdlemlpggDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDP 555
Cdd:PRK11231 98 AYGrspwlslwgrlSAEDNARVNQAMEQT------------RINHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 556 LSAVDahvgkhiFNKVLGPNGLL-----KGKTRLLVTHSmhfLPQV----DEIVVLGNGTIVEKGS 612
Cdd:PRK11231 166 TTYLD-------INHQVELMRLMrelntQGKTVVTVLHD---LNQAsrycDHLVVLANGHVMAQGT 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
422-560 |
1.64e-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: 68.72 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--------------TAYVPQQSWI-QNGTIKDN 486
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarlgIGYLPQEASIfRKLTVEEN 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 487 ILFGTEFNEKRYQQVLE-ACALLPDLemlpggDLAEI-GEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 560
Cdd:cd03218 96 ILAVLEIRGLSKKEREEkLEELLEEF------HITHLrKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
413-613 |
1.90e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 70.63 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 413 TWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-AYVPQ---------QSW--IQN 480
Cdd:PRK11607 26 TKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDlSHVPPyqrpinmmfQSYalFPH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 481 GTIKDNILFGTEFNEKRYQQVLEACAllpdlEMLPGGDLAEI-GEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAV 559
Cdd:PRK11607 106 MTVEQNIAFGLKQDKLPKAEIASRVN-----EMLGLVHMQEFaKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 560 DAHVGKHIFNKVLgpnGLLK--GKTRLLVTHSmhflpQVDEIVVLGNGTIVEKGSY 613
Cdd:PRK11607 181 DKKLRDRMQLEVV---DILErvGVTCVMVTHD-----QEEAMTMAGRIAIMNRGKF 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
405-588 |
2.13e-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: 67.82 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 405 MQFSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT---------TAYVPQQ 475
Cdd:cd03292 1 IEFINVTKTYPNGTAA-LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdlrgraIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 476 --------SWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGG--DLAEigekgiNLSGGQKQRISLARATYQ 545
Cdd:cd03292 80 igvvfqdfRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKhrALPA------ELSGGEQQRVAIARAIVN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 578818931 546 NLDIYLLDDPLSAVDAHVGKHIFNKVLGPNglLKGKTRLLVTH 588
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKIN--KAGTTVVVATH 194
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
406-606 |
2.56e-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: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 406 QFSEASFTWEhdSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--AYVPQqswiqngti 483
Cdd:cd03221 2 ELENLSKTYG--GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVkiGYFEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 484 kdnilfgtefnekryqqvleacallpdlemlpggdlaeigekginLSGGQKQRISLARATYQNLDIYLLDDPLSAVDahv 563
Cdd:cd03221 71 ---------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD--- 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 578818931 564 gkhIFNKVLGPNGLLK-GKTRLLVTHSMHFLPQV-DEIVVLGNGT 606
Cdd:cd03221 103 ---LESIEALEEALKEyPGTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
422-612 |
2.64e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 69.83 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TAYVPQQ---------------SWIQNGTIK 484
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdlTALSEKElrkarrqigmifqhfNLLSSRTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 485 DNILFGTEFN----EKRYQQVLEacaLLpdlemlpggDLAEIGEKG----INLSGGQKQRISLARATYQNLDIYLLDDPL 556
Cdd:PRK11153 101 DNVALPLELAgtpkAEIKARVTE---LL---------ELVGLSDKAdrypAQLSGGQKQRVAIARALASNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578818931 557 SAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 612
Cdd:PRK11153 169 SALDPATTRSILE-------LLKdinrelGLTIVLITHEMDVVKRIcDRVAVIDAGRLVEQGT 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
424-626 |
2.68e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 68.89 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 424 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTayvpqqswIQNG---------------------- 481
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERV--------ITAGkknkklkplrkkvgivfqfpeh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 482 -----TIKDNILFG-------TEFNEKRYQQVLEACALLPD-LEMLPggdlaeigekgINLSGGQKQRISLARATYQNLD 548
Cdd:PRK13634 97 qlfeeTVEKDICFGpmnfgvsEEDAKQKAREMIELVGLPEElLARSP-----------FELSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 549 IYLLDDPLSAVDAHVGKHI---FNKVLGPNGLlkgkTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGSYSALLAKKGEFA 624
Cdd:PRK13634 166 VLVLDEPTAGLDPKGRKEMmemFYKLHKEKGL----TTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADPDELE 241
|
..
gi 578818931 625 KN 626
Cdd:PRK13634 242 AI 243
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
423-609 |
2.93e-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: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 423 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKgttayVPQQSWIQNGTIKDNILFGTEFNEKRYqqVL 502
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----VPDNQFGREASLIDAIGRKGDFKDAVE--LL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 503 EACALlpdlemlpgGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVD---AHVGKHIFNKVLGPngllK 579
Cdd:COG2401 120 NAVGL---------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQKLARR----A 186
|
170 180 190
....*....|....*....|....*....|..
gi 578818931 580 GKTRLLVTHSMHFLP--QVDEIVVLGNGTIVE 609
Cdd:COG2401 187 GITLVVATHHYDVIDdlQPDLLIFVGYGGVPE 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
423-561 |
3.49e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.17 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 423 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHI--------TIKGTTAYVPQQS----WiqnGTIKDNILFG 490
Cdd:PRK11247 29 NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELlagtaplaEAREDTRLMFQDArllpW---KKVIDNVGLG 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578818931 491 TEFN-EKRYQQVLEACALlpdlemlpgGDLAeiGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 561
Cdd:PRK11247 106 LKGQwRDAALQALAAVGL---------ADRA--NEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
411-611 |
3.64e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 68.14 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 411 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAmLGEMENVHGHITIKGTTAYVPQQSWIQNGTI------- 483
Cdd:PRK14258 12 NLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNIYERRVNLnrlrrqv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 484 -----KDNIlfgteFNEKRYQQVLEACALL---PDLEM-------LPGGDL-----AEIGEKGINLSGGQKQRISLARAT 543
Cdd:PRK14258 91 smvhpKPNL-----FPMSVYDNVAYGVKIVgwrPKLEIddivesaLKDADLwdeikHKIHKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 544 YQNLDIYLLDDPLSAVDAHVGKHIfnKVLGPNGLLKGK-TRLLVTHSMHFLPQVDEIVVL--GN----GTIVEKG 611
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKV--ESLIQSLRLRSElTMVIVSHNLHQVSRLSDFTAFfkGNenriGQLVEFG 238
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
423-609 |
3.71e-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: 3.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 423 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-----------------AYVpQQSW--IQNGTI 483
Cdd:COG4181 29 KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDlfaldedararlrarhvGFV-FQSFqlLPTLTA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 484 KDNI-----LFGTEFNEKRYQQVLEACALLPDLEMLPGGdlaeigekginLSGGQKQRISLARATYQNLDIYLLDDPLSA 558
Cdd:COG4181 108 LENVmlpleLAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 578818931 559 VDAHVGKHIFnkvlgpnGLL------KGKTRLLVTHSMHFLPQVDEIVVLGNGTIVE 609
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 ... |
1084-1289 |
3.88e-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: 3.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCL--FRILEAAGGQII---------------------------------I 1128
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtlepeeV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1129 DGVDIASIGLHDLREKLTIIPQDPILFSGSLR-----MNLDPFNNYS-DEEIWKALELAHlksfvaslQLGLSHEVTEAG 1202
Cdd:TIGR03269 95 DFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTvldnvLEALEEIGYEgKEAVGRAVDLIE--------MVQLSHRITHIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1203 GNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQN--EFAHCTVITIAHRLHTIMD-SDKVMVLDNGK 1279
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIEDlSDKAIWLENGE 246
|
250
....*....|
gi 578818931 1280 IIECGSPEEL 1289
Cdd:TIGR03269 247 IKEEGTPDEV 256
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
792-952 |
4.72e-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: 68.18 E-value: 4.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 792 VGVYGALGLAQGIFVFIAHFWSAFGfvhASNILH---KQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLR 868
Cdd:cd18544 44 ALLYLGLLLLSFLLQYLQTYLLQKL---GQRIIYdlrRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 869 SWITCFLGIISTLVMICMATP---VFTIIVIPLgIIYVSVqmFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFE 945
Cdd:cd18544 121 TLIGDLLLLIGILIAMFLLNWrlaLISLLVLPL-LLLATY--LFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFN 197
|
....*..
gi 578818931 946 HQQRFLK 952
Cdd:cd18544 198 REKREFE 204
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
422-611 |
5.10e-12 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 66.04 E-value: 5.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVH--GHITIKGT----------TAYVPQqswiqngtikDNILF 489
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRpldkrsfrkiIGYVPQ----------DDILH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 490 GTefnekryQQVLEAcallpdLEMlpggdLAEIgeKGInlSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFn 569
Cdd:cd03213 95 PT-------LTVRET------LMF-----AAKL--RGL--SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM- 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 578818931 570 kvlgpnGLLK-----GKTRLLVTH----SMHFLpqVDEIVVLGNGTIVEKG 611
Cdd:cd03213 152 ------SLLRrladtGRTIICSIHqpssEIFEL--FDKLLLLSQGRVIYFG 194
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1063-1282 |
5.28e-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: 67.42 E-value: 5.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1063 PSKGKIQFNNYQVRYRPELD--LVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGlhd 1140
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1141 lrEKLTIIPQDP-----------ILFSgsLRMNLDPfNNYSDEEIWKALELAHLKSFVASLqlglSHEvteaggnLSIGQ 1209
Cdd:COG1116 80 --PDRGVVFQEPallpwltvldnVALG--LELRGVP-KAERRERARELLELVGLAGFEDAY----PHQ-------LSGGM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1210 RQLLCLGRALLRKSKILVLDEATAAVDletdnlIQT--TIQNEFA------HCTVITIAH------RLhtimdSDKVMVL 1275
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDEPFGALD------ALTreRLQDELLrlwqetGKTVLFVTHdvdeavFL-----ADRVVVL 212
|
....*....
gi 578818931 1276 DN--GKIIE 1282
Cdd:COG1116 213 SArpGRIVE 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1084-1282 |
5.72e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 67.79 E-value: 5.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASI---GLHDLREKLTIIPQDPIlfsgslr 1160
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSI------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1161 mnlDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGG-----------NLSIGQRQLLCLGRALLRKSKILVLD 1229
Cdd:PRK10419 100 ---SAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDlddsvldkrppQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578818931 1230 EATAAVDLetdnLIQTTI-------QNEFA-HCTVITiaHRLHTIMD-SDKVMVLDNGKIIE 1282
Cdd:PRK10419 177 EAVSNLDL----VLQAGVirllkklQQQFGtACLFIT--HDLRLVERfCQRVMVMDNGQIVE 232
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
423-611 |
6.04e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.90 E-value: 6.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 423 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTA-YVPQ---------QSWI--QNGTIKDNILFG 490
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMnDVPPaergvgmvfQSYAlyPHLSVAENMSFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 491 TEFN-------EKRYQQVLEACALLPDLEMLPGGdlaeigekginLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA-- 561
Cdd:PRK11000 100 LKLAgakkeeiNQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAal 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 562 HVGKHI----FNKVLgpngllkGKTRLLVTHSmhflpQV------DEIVVLGNGTIVEKG 611
Cdd:PRK11000 169 RVQMRIeisrLHKRL-------GRTMIYVTHD-----QVeamtlaDKIVVLDAGRVAQVG 216
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
744-1040 |
6.34e-12 |
|
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: 67.84 E-value: 6.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 744 LFSIFFIILAFVMNSVafigsNLWLSAWTSDSKIfnstdypaSQRDMR-----VGVYGALGLAQGIFVFIAHFWSAFGFV 818
Cdd:cd18542 2 LLAILALLLATALNLL-----IPLLIRRIIDSVI--------GGGLREllwllALLILGVALLRGVFRYLQGYLAEKASQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 819 HASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLpqslrSWItcFLGIISTLVMICMATPV-------- 890
Cdd:cd18542 69 KVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFL-----AFG--LVELVRAVLLFIGALIImfsinwkl 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 891 --FTIIVIPLgIIYVSVQMF------YVSTSRQLRRLDSVTRspiyshfsETVSGLPVIRAF---EHQ-QRFLKHNEVRI 958
Cdd:cd18542 142 tlISLAIIPF-IALFSYVFFkkvrpaFEEIREQEGELNTVLQ--------ENLTGVRVVKAFareDYEiEKFDKENEEYR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 959 DTNqkcvfswITSNRWLAIR---LELVGNLTVFFSALM---MVIyRDTLS-GDTVGFVLsnalnITQTLNWLVRM----T 1027
Cdd:cd18542 213 DLN-------IKLAKLLAKYwplMDFLSGLQIVLVLWVggyLVI-NGEITlGELVAFIS-----YLWMLIWPVRQlgrlI 279
|
330
....*....|...
gi 578818931 1028 SEIETNIVAVERI 1040
Cdd:cd18542 280 NDMSRASASAERI 292
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1084-1289 |
6.46e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.69 E-value: 6.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIG---LHDLreKLTIIPQDPILFSgslr 1160
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakAHQL--GIYLVPQEPLLFP---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1161 mNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVteAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVD-LET 1239
Cdd:PRK15439 100 -NLSVKENILFGLPKRQASMQKMKQLLAALGCQLDLDS--SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpAET 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 578818931 1240 DNL---IQTTIQNEFAhctVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEEL 1289
Cdd:PRK15439 177 ERLfsrIRELLAQGVG---IVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1096-1281 |
7.73e-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: 7.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1096 EKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVdiasiglhdlrekltiipqdpILFSGSLRMNLDP--------FN 1167
Cdd:cd03297 24 EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT---------------------VLFDSRKKINLPPqqrkiglvFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1168 NYS-------DEEI---WKALELAHLKSFVASL--QLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAV 1235
Cdd:cd03297 83 QYAlfphlnvRENLafgLKRKRNREDRISVDELldLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 578818931 1236 DLETDNLIQ---TTIQNEFaHCTVITIAHRLHTI-MDSDKVMVLDNGKII 1281
Cdd:cd03297 163 DRALRLQLLpelKQIKKNL-NIPVIFVTHDLSEAeYLADRIVVMEDGRLQ 211
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1076-1290 |
8.09e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 67.34 E-value: 8.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1076 RYRPELdlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDG--VDIASIGLHDLREKLTIIPQDP- 1152
Cdd:PRK13638 10 RYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDPe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1153 --ILFSG-------SLRmNLdpfnNYSDEEIWK----ALELAHLKSFVASLQLGLSHevteaggnlsiGQRQLLCLGRAL 1219
Cdd:PRK13638 88 qqIFYTDidsdiafSLR-NL----GVPEAEITRrvdeALTLVDAQHFRHQPIQCLSH-----------GQKKRVAIAGAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578818931 1220 LRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCT-VITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELL 1290
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNhVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVF 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
422-617 |
9.54e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 68.71 E-value: 9.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-------------TAYVPQQSWIQ-NGTIKDNI 487
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsaraasrrVASVPQDTSLSfEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 488 LFGTEFNEKRYQQVLEACALLPDlEMLPGGDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHvgkH 566
Cdd:PRK09536 99 EMGRTPHRSRFDTWTETDRAAVE-RAMERTGVAQFADRPVtSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN---H 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578818931 567 IFNKVLGPNGLLK-GKTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGSYSALL 617
Cdd:PRK09536 175 QVRTLELVRRLVDdGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1084-1293 |
9.72e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 68.25 E-value: 9.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDiASIGLHDLREKLTIIPQDPILFsgslRmNL 1163
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD-LFTNLPPRERRVGFVFQHYALF----P-HM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1164 DPFNN---------YSDEEIwKA-----LELAHLKSFvaslqlglshevteAG---GNLSIGQRQLLCLGRALLRKSKIL 1226
Cdd:COG1118 91 TVAENiafglrvrpPSKAEI-RArveelLELVQLEGL--------------ADrypSQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578818931 1227 VLDEATAAVD------LEtDNLIQttIQNEFaHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1293
Cdd:COG1118 156 LLDEPFGALDakvrkeLR-RWLRR--LHDEL-GGTTVFVTHDQEEALElADRVVVMNQGRIEQVGTPDEVYDRP 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1087-1290 |
1.00e-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: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1087 GITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIII----DGVDIASIGLhDLREKLT----IIPQDPILFSGs 1158
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGP-DGRGRAKryigILHQEYDLYPH- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1159 lRMNLDPFNNYSDEEIWKalELAHLKSFVASLQLGLSHEVTEA-----GGNLSIGQRQLLCLGRALLRKSKILVLDEATA 1233
Cdd:TIGR03269 380 -RTVLDNLTEAIGLELPD--ELARMKAVITLKMVGFDEEKAEEildkyPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1234 AVDLETDNLIQTTIQN--EFAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELL 1290
Cdd:TIGR03269 457 TMDPITKVDVTHSILKarEEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
424-602 |
1.01e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.28 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 424 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TAYVPQQSWIQ-----------NGTIKDNILFG 490
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdiSTLKPEIYRQQvsycaqtptlfGDTVYDNLIFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 491 TEFnekRYQQVLEAcALLPDLEM--LPggdlAEIGEKGIN-LSGGQKQRISLARatyqNLD----IYLLDDPLSAVDAHv 563
Cdd:PRK10247 105 WQI---RNQQPDPA-IFLDDLERfaLP----DTILTKNIAeLSGGEKQRISLIR----NLQfmpkVLLLDEITSALDES- 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 578818931 564 GKHIFNKVLGPNGLLKGKTRLLVTHSMHFLPQVDEIVVL 602
Cdd:PRK10247 172 NKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
422-611 |
1.21e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 66.40 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAM-----LGEMENVHGHITIKGTTAYVPQQSWIQ----------------N 480
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIEvrrevgmvfqypnpfpH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 481 GTIKDNILFGTEFN---------EKRYQQVLEACALLPDLEmlpggdlAEIGEKGINLSGGQKQRISLARATYQNLDIYL 551
Cdd:PRK14267 100 LTIYDNVAIGVKLNglvkskkelDERVEWALKKAALWDEVK-------DRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578818931 552 LDDPLSAVDAhVGKHIFNKVLGPngLLKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 611
Cdd:PRK14267 173 MDEPTANIDP-VGTAKIEELLFE--LKKEYTIVLVTHSPAQAARVsDYVAFLYLGKLIEVG 230
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1084-1284 |
1.28e-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: 65.63 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGL-HDLREKLTIIpqDPILFSGSLrMN 1162
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLgGGFNPELTGR--ENIYLNGRL-LG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1163 LDPfnNYSDEEIWKALELAHLKSFvaslqlglsheVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNL 1242
Cdd:cd03220 114 LSR--KEIDEKIDEIIEFSELGDF-----------IDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 578818931 1243 IQTTIQNEFAHC-TVITIAHRLHTIMD-SDKVMVLDNGKIIECG 1284
Cdd:cd03220 181 CQRRLRELLKQGkTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
416-612 |
1.30e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 66.26 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 416 HDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG----TTAY--------VPQQSwiqNG-- 481
Cdd:COG4604 11 YGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvaTTPSrelakrlaILRQE---NHin 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 482 ---TIKDNILFGtefnekRY------------QQVLEACALLpdlemlpggDLAEIGEKGIN-LSGGQKQRISLARATYQ 545
Cdd:COG4604 88 srlTVRELVAFG------RFpyskgrltaedrEIIDEAIAYL---------DLEDLADRYLDeLSGGQRQRAFIAMVLAQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578818931 546 NLDIYLLDDPLSAVDAHVGKHIFnkvlgpnGLLK------GKTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGS 612
Cdd:COG4604 153 DTDYVLLDEPLNNLDMKHSVQMM-------KLLRrladelGKTVVIVLHDINFASCyADHIVAMKDGRVVAQGT 219
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
410-617 |
1.32e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.55 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 410 ASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGttAYVPQQSWI----------- 478
Cdd:PRK13536 45 AGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG--VPVPARARLararigvvpqf 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 479 ----QNGTIKDNIL-FGTEFNEKRYQqvLEAcaLLPDLEmlpggDLAEIGEKG----INLSGGQKQRISLARATYQNLDI 549
Cdd:PRK13536 123 dnldLEFTVRENLLvFGRYFGMSTRE--IEA--VIPSLL-----EFARLESKAdarvSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 550 YLLDDPLSAVDAHVGKHIFNKVLGPngLLKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALL 617
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSL--LARGKTILLTTHFMEEAERLcDRLCVLEAGRKIAEGRPHALI 260
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
417-612 |
1.55e-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: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 417 DSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISaMLGEM-------ENVHGH------ITIKGTTAYVPQQSWIQNG-T 482
Cdd:cd03265 12 DFEA-VRGVSFRVRRGEIFGLLGPNGAGKTTTIK-MLTTLlkptsgrATVAGHdvvrepREVRRRIGIVFQDLSVDDElT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 483 IKDNI-----LFGTEfNEKRYQQVLEACALLpdlemlpggDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPL 556
Cdd:cd03265 90 GWENLyiharLYGVP-GAERRERIDELLDFV---------GLLEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 557 SAVDAHVGKHIFNKVlgpNGLLK--GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 612
Cdd:cd03265 160 IGLDPQTRAHVWEYI---EKLKEefGMTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGT 215
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
417-618 |
1.69e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 66.55 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 417 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTA-----------------YVPQQSWIQ 479
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfsklqgirklvgivfQNPETQFVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 480 NgTIKDNILFGTEfnekryqqvlEACalLPDLEMLPGGD--LAEIG-EK-----GINLSGGQKQRISLARATYQNLDIYL 551
Cdd:PRK13644 93 R-TVEEDLAFGPE----------NLC--LPPIEIRKRVDraLAEIGlEKyrhrsPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578818931 552 LDDPLSAVDAHVGKHIFNKVLGPNGllKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLA 618
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHE--KGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1084-1291 |
1.73e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 65.69 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHD-LREKLTIIPQDPILFSgslrmN 1162
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFR-----R 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1163 LDPFNN-YSDEEIWKALELAHLKSFVASL--QLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLET 1239
Cdd:PRK10895 93 LSVYDNlMAVLQIRDDLSAEQREDRANELmeEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 578818931 1240 DNLIQTTIQN--EFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQ 1291
Cdd:PRK10895 173 VIDIKRIIEHlrDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
422-621 |
2.14e-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: 64.47 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEM--ENVHGHITIKGttayvpqqswiqngtikDNILFgTEFNEKryq 499
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKG-----------------EDITD-LPPEER--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 500 qvleacALL---------PDLEMLPGGD-LAEIGEkgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFN 569
Cdd:cd03217 75 ------ARLgiflafqypPEIPGVKNADfLRYVNE---GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 578818931 570 KVlgpNGLL-KGKTRLLVTHSMHFLPQV--DEIVVLGNGTIVEKGSYSAL--LAKKG 621
Cdd:cd03217 146 VI---NKLReEGKSVLIITHYQRLLDYIkpDRVHVLYDGRIVKSGDKELAleIEKKG 199
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
400-618 |
2.21e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 65.97 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 400 NFDKAMQFSEASFTWEHdSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG------------ 467
Cdd:PRK15112 9 NLSKTFRYRTGWFRRQT-VEA-VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysyrs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 468 ----------TTAYVPQQ--SWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDlemlpggdlaEIGEKGINLSGGQKQ 535
Cdd:PRK15112 87 qrirmifqdpSTSLNPRQriSQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPD----------HASYYPHMLAPGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 536 RISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLGPNGlLKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYS 614
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQE-KQGISYIYVTQHLGMMKHIsDQVLVMHQGEVVERGSTA 235
|
....
gi 578818931 615 ALLA 618
Cdd:PRK15112 236 DVLA 239
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
424-612 |
2.24e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 66.22 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 424 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT---------------TAYVPQQSWIQ--NGTIKDN 486
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVditdkkvklsdirkkVGLVFQYPEYQlfEETIEKD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 487 ILFGT----EFNEKRYQQVLEACALLpdlemlpGGDLAEIGEKG-INLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 561
Cdd:PRK13637 105 IAFGPinlgLSEEEIENRVKRAMNIV-------GLDYEDYKDKSpFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 562 HVGKHIFNKVlgpnGLLKGK---TRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGS 612
Cdd:PRK13637 178 KGRDEILNKI----KELHKEynmTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1084-1275 |
2.33e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 64.18 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVdiASIGLhdLREKLTIIPQDPILFSGSLRMNL 1163
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG--ARVAY--VPQRSEVPDSLPLTVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1164 dpfnnYSDEEIWKALELAHLKSFVASLQ-LGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNL 1242
Cdd:NF040873 83 -----WARRGLWRRLTRDDRAAVDDALErVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
|
170 180 190
....*....|....*....|....*....|....
gi 578818931 1243 IQTTIQNEFAH-CTVITIAHRLHTIMDSDKVMVL 1275
Cdd:NF040873 158 IIALLAEEHARgATVVVVTHDLELVRRADPCVLL 191
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
422-569 |
2.75e-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: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISaMLGEMENVHG---HITIKGTTAYVPQQSWIQNGTIKDNILF---GTEFNE 495
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIYpdsSEDMKR 546
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578818931 496 KRY-QQVLEACALLPDLEML--PGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFN 569
Cdd:TIGR00954 547 RGLsDKDLEQILDNVQLTHIleREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYR 623
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1085-1298 |
2.89e-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: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1085 LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHD-----------LREKLTIIpqDPI 1153
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQErnvgfvfqhyaLFRHMTVF--DNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1154 LFSgsLRM---NLDPFNNYSDEEIWKALELAHLKSFVASLQlglshevteagGNLSIGQRQLLCLGRALLRKSKILVLDE 1230
Cdd:cd03296 96 AFG--LRVkprSERPPEAEIRAKVHELLKLVQLDWLADRYP-----------AQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578818931 1231 ATAAVDLETDNLIQT---TIQNEFAHCTVItIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIPG-PFYF 1298
Cdd:cd03296 163 PFGALDAKVRKELRRwlrRLHDELHVTTVF-VTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYDHPAsPFVY 234
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1084-1289 |
3.10e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 66.64 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIAsiglhDLREK---LTIIPQDPILF----- 1155
Cdd:COG3839 18 ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT-----DLPPKdrnIAMVFQSYALYphmtv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1156 -----SGsLRMNldpfnNYSDEEIWKAL-ELAHLksfvaslqLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLD 1229
Cdd:COG3839 93 yeniaFP-LKLR-----KVPKAEIDRRVrEAAEL--------LGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 1230 E------ATAAVDLETDnLIQttIQNEFAHCTVI---------TIAhrlhtimdsDKVMVLDNGKIIECGSPEEL 1289
Cdd:COG3839 159 EplsnldAKLRVEMRAE-IKR--LHRRLGTTTIYvthdqveamTLA---------DRIAVMNDGRIQQVGTPEEL 221
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
472-628 |
3.12e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.52 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 472 VPQQSWIQNGTIKDNILFGTEfnEKRYQQVLEAC---ALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLD 548
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGKE--DATREDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPK 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 549 IYLLDDPLSAVDAHVGKHIFNKVLGpnglLKGK---TRLLVTHSMHFLPQVDEIVVLGN----GTIVE-KGSYSALL-AK 619
Cdd:PTZ00265 1379 ILLLDEATSSLDSNSEKLIEKTIVD----IKDKadkTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLsVQ 1454
|
....*....
gi 578818931 620 KGEFAKNLK 628
Cdd:PTZ00265 1455 DGVYKKYVK 1463
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
402-628 |
3.22e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.53 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 402 DKAMQFSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQN- 480
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKA-LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 481 --------------GTIKDNILFGTEFNEKRYQQVLEACAllpdlEMLPGGDLAEIGEKG-INLSGGQKQRISLARATYQ 545
Cdd:PRK13647 81 vglvfqdpddqvfsSTVWDDVAFGPVNMGLDKDEVERRVE-----EALKAVRMWDFRDKPpYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 546 NLDIYLLDDPLSAVDAHvGKHIFNKVLgpNGLLK-GKTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGSYSALLAKKGEF 623
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPR-GQETLMEIL--DRLHNqGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDEDIVE 232
|
....*
gi 578818931 624 AKNLK 628
Cdd:PRK13647 233 QAGLR 237
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1096-1291 |
3.69e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 64.60 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1096 EKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDiasiglHDL----REKLTIIPQDPILFSG-SLRMN----LDPF 1166
Cdd:PRK10771 26 ERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD------HTTtppsRRPVSMLFQENNLFSHlTVAQNiglgLNPG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1167 NNYSDEEIWKALELAHlksfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVD----LETDNL 1242
Cdd:PRK10771 100 LKLNAAQREKLHAIAR--------QMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalrQEMLTL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 578818931 1243 IQTTIQNEfaHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQ 1291
Cdd:PRK10771 172 VSQVCQER--QLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELLS 219
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
798-1230 |
4.03e-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: 67.13 E-value: 4.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 798 LGLAqgIFVFIAHFWSAFGFVHAS-NILHK---QLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDT---LPQSLRSW 870
Cdd:COG4615 55 AGLL--VLLLLSRLASQLLLTRLGqHAVARlrlRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAfvrLPELLQSV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 871 IT---CF--LGIISTLVMicmatpVFTIIVIPLGIIyvsvqMFYVSTSRQLRRLDSV--TRSPIYSHFSETVSG------ 937
Cdd:COG4615 133 ALvlgCLayLAWLSPPLF------LLTLVLLGLGVA-----GYRLLVRRARRHLRRAreAEDRLFKHFRALLEGfkelkl 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 938 -------------LPVIRAFEHQQrflkhneVRIDTNQKCVFSWITSNrWLAirleLVGnLTVFFSALMMVIYRDTLSGd 1004
Cdd:COG4615 202 nrrrrraffdedlQPTAERYRDLR-------IRADTIFALANNWGNLL-FFA----LIG-LILFLLPALGWADPAVLSG- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1005 tvgFVLSnALNITQTLNWLVRMTSEIETNIVAVERITEYT-KVENEAPWVTDKRPPPDWPSKGKIQFNNYQVRYRPE--- 1080
Cdd:COG4615 268 ---FVLV-LLFLRGPLSQLVGALPTLSRANVALRKIEELElALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEdgd 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1081 -------LDLVL-RGitcdigsmEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDP 1152
Cdd:COG4615 344 egftlgpIDLTIrRG--------ELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDF 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1153 ILFSGslrmNLDPFNNYSDEEIWKALElahlksfvaslQLGLSHEVTEAGG-----NLSIGQRQLLCLGRALLRKSKILV 1227
Cdd:COG4615 416 HLFDR----LLGLDGEADPARARELLE-----------RLELDHKVSVEDGrfsttDLSQGQRKRLALLVALLEDRPILV 480
|
...
gi 578818931 1228 LDE 1230
Cdd:COG4615 481 FDE 483
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
425-612 |
4.43e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.03 E-value: 4.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 425 VNLDIMAGQLVAVIGPVGSGKSSLI---SAMLGEMENVHGHITIKGTT------------------AYVPQQ-SWIQNGT 482
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLrhlSGLITGDKSAGSHIELLGRTvqregrlardirksrantGYIFQQfNLVNRLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 483 IKDNILFG------------TEFNEKRYQQVLEAcallpdlemLPGGDLAEIGEKGIN-LSGGQKQRISLARATYQNLDI 549
Cdd:PRK09984 103 VLENVLIGalgstpfwrtcfSWFTREQKQRALQA---------LTRVGMVHFAHQRVStLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578818931 550 YLLDDPLSAVDAHVGKHIFNKVLGPNGlLKGKTRLLVTHSMHF-LPQVDEIVVLGNGTIVEKGS 612
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQ-NDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGS 236
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
422-618 |
4.45e-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: 4.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLG---EMENVHGHITIKGT-----------------TAYVPQQS----- 476
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEdllklsekelrkirgreIQMIFQDPmtsln 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 477 --WiqngTIKDNI-----LFGTEFNEKRYQQVLEAcallpdLEMLpggdlaeigekGIN------------LSGGQKQRI 537
Cdd:COG0444 101 pvM----TVGDQIaeplrIHGGLSKAEARERAIEL------LERV-----------GLPdperrldrypheLSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 538 SLARATYQNLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEK 610
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILN-------LLKdlqrelGLAILFITHDLGVVAEIaDRVAVMYAGRIVEE 232
|
....*...
gi 578818931 611 GSYSALLA 618
Cdd:COG0444 233 GPVEELFE 240
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1082-1293 |
5.82e-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: 63.80 E-value: 5.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1082 DLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHdlREKLTIIPQDPILFSgslrm 1161
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALFP----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1162 NLDPFNNYS-------------DEEIWKALELAHLKsfvaslqlGLSHEVTEAggnLSIGQRQLLCLGRALLRKSKILVL 1228
Cdd:cd03300 86 HLTVFENIAfglrlkklpkaeiKERVAEALDLVQLE--------GYANRKPSQ---LSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 1229 DEATAAVDLETDNLIQ---TTIQNEFAhCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1293
Cdd:cd03300 155 DEPLGALDLKLRKDMQlelKRLQKELG-ITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1083-1293 |
6.44e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 64.24 E-value: 6.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1083 LVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREK--------------LTII 1148
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMgvvrtfqhvrlfreMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1149 PQDPI---------LFSGSLRMnldPFNNYSDEEiwkALELAH--LKsfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGR 1217
Cdd:PRK11300 99 ENLLVaqhqqlktgLFSGLLKT---PAFRRAESE---ALDRAAtwLE------RVGLLEHANRQAGNLAYGQQRRLEIAR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1218 ALLRKSKILVLDEATAAVD-LETDNLIQTTIQ--NEFAhCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1293
Cdd:PRK11300 167 CMVTQPEILMLDEPAAGLNpKETKELDELIAElrNEHN-VTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1096-1293 |
6.80e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 65.63 E-value: 6.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1096 EKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHdlREKLTIIPQDPILFSG-SLRMNLdPFNNYSDEei 1174
Cdd:PRK11607 46 EIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPINMMFQSYALFPHmTVEQNI-AFGLKQDK-- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1175 wkaLELAHLKSFVASLqLGLSHEVTEAG---GNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQN-- 1249
Cdd:PRK11607 121 ---LPKAEIASRVNEM-LGLVHMQEFAKrkpHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDil 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 578818931 1250 EFAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1293
Cdd:PRK11607 197 ERVGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIYEHP 241
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1076-1293 |
8.13e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.11 E-value: 8.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1076 RYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIiidgvdiasiglhdLREK-LTIIPQDPIL 1154
Cdd:PTZ00243 667 FFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------------WAERsIAYVPQQAWI 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1155 FSGSLRMNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAA 1234
Cdd:PTZ00243 733 MNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1235 VDLETDNLI-QTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIP 1293
Cdd:PTZ00243 813 LDAHVGERVvEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
804-1040 |
8.28e-11 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 64.39 E-value: 8.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 804 IFVFIAHFWSAFGFV------HASNILHKQLL----NNILRAPMRFFDTTPTGRIVNRFaGDISTVDDTLPQ-SLRSWIT 872
Cdd:cd18570 47 GLILLYLFQSLLSYIrsylllKLSQKLDIRLIlgyfKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISStTISLFLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 873 CFLGIISTLVMICMATPVFTIIVIPLgIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLK 952
Cdd:cd18570 126 LLMVIISGIILFFYNWKLFLITLLII-PLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 953 HNEVRIDTNQKCVFS---WITSNRWLAIRLELVGNLTVFFSALMMVIyRDTLS-GDTVGFvlsNAL--NITQTLNWLVRM 1026
Cdd:cd18570 205 KIEKKFSKLLKKSFKlgkLSNLQSSIKGLISLIGSLLILWIGSYLVI-KGQLSlGQLIAF---NALlgYFLGPIENLINL 280
|
250
....*....|....
gi 578818931 1027 TSEIETNIVAVERI 1040
Cdd:cd18570 281 QPKIQEAKVAADRL 294
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
411-628 |
8.61e-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: 64.06 E-value: 8.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 411 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT---------------------- 468
Cdd:TIGR02769 16 GLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQdlyqldrkqrrafrrdvqlvfq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 469 ---TAYVPQQS--WIQNGTIKDNILFGTEFNEKRYQQVLEACALLPD-LEMLPGgdlaeigekgiNLSGGQKQRISLARA 542
Cdd:TIGR02769 96 dspSAVNPRMTvrQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEdADKLPR-----------QLSGGQLQRINIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 543 TYQNLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSA 615
Cdd:TIGR02769 165 LAVKPKLIVLDEAVSNLDMVLQAVILE-------LLRklqqafGTAYLFITHDLRLVQSFcQRVAVMDKGQIVEECDVAQ 237
|
250
....*....|...
gi 578818931 616 LLAKKGEFAKNLK 628
Cdd:TIGR02769 238 LLSFKHPAGRNLQ 250
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
411-612 |
1.01e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 63.94 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 411 SFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWI----------QN 480
Cdd:PRK13639 8 KYSYPDGTEA-LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevrktvgivfQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 481 G-------TIKDNILFG-------TEFNEKRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQN 546
Cdd:PRK13639 87 PddqlfapTVEEDVAFGplnlglsKEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578818931 547 LDIYLLDDPLSAVDAHVGKHIFNKVLGPNGllKGKTRLLVTHSMHFLP-QVDEIVVLGNGTIVEKGS 612
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNK--EGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGT 220
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1084-1280 |
1.14e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 63.54 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIdgvdiASIGLHDLREKLTIIPQDPILFsgslrmnl 1163
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA-----GTAPLAEAREDTRLMFQDARLL-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1164 dPFNNYSD------EEIWKALELAHLKSfvaslqLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVD- 1236
Cdd:PRK11247 94 -PWKKVIDnvglglKGQWRDAALQALAA------VGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDa 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 578818931 1237 ---LETDNLIQTTIQNEfaHCTVITIAHRL-HTIMDSDKVMVLDNGKI 1280
Cdd:PRK11247 167 ltrIEMQDLIESLWQQH--GFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1098-1293 |
1.22e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 63.66 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1098 IGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPI-----------LFSGSLRMNLDPF 1166
Cdd:PRK15112 42 LAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPStslnprqrisqILDFPLRLNTDLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1167 NNYSDEEIWKALElahlksfvaslQLGLSHE-VTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLET-DNLIQ 1244
Cdd:PRK15112 122 PEQREKQIIETLR-----------QVGLLPDhASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMrSQLIN 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 578818931 1245 TTIQNEFAH-CTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1293
Cdd:PRK15112 191 LMLELQEKQgISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLASP 241
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
400-632 |
1.28e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 65.05 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 400 NFDKAMQFSEASFTWEHDSEAT-----VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGttayvpq 474
Cdd:PRK10070 17 HPQRAFKYIEQGLSKEQILEKTglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 475 qswIQNGTIKDNILfgTEFNEKRYQQVLEACALLPDLEMLP----GGDLAEIG-----EKGIN----------------- 528
Cdd:PRK10070 90 ---VDIAKISDAEL--REVRRKKIAMVFQSFALMPHMTVLDntafGMELAGINaeerrEKALDalrqvglenyahsypde 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 529 LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLGpnglLKGKTRLLVTHSMHFLPQV----DEIVVLGN 604
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVK----LQAKHQRTIVFISHDLDEAmrigDRIAIMQN 240
|
250 260
....*....|....*....|....*...
gi 578818931 605 GTIVEKGSYSALLAKKGEfaKNLKTFLR 632
Cdd:PRK10070 241 GEVVQVGTPDEILNNPAN--DYVRTFFR 266
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
424-633 |
1.39e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 63.11 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 424 DVNLDIMAGQLVAVIGPVGSGKSSLISAM-LGEMENvHGHITIKGT-------------------TAYVPQQS--WiQNG 481
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPR-SGTLNIAGNhfdfsktpsdkairelrrnVGMVFQQYnlW-PHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 482 TIKDNIL------FGTEFNE--KRYQQVLEACALLPDLEMLPggdlaeigekgINLSGGQKQRISLARATYQNLDIYLLD 553
Cdd:PRK11124 98 TVQQNLIeapcrvLGLSKDQalARAEKLLERLRLKPYADRFP-----------LHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 554 DPLSAVDAHVGKHIFN--KVLGPNGLlkgkTRLLVTHSMHFLPQVDEIVV-LGNGTIVEKGSYSALLAKKGEfakNLKTF 630
Cdd:PRK11124 167 EPTAALDPEITAQIVSiiRELAETGI----TQVIVTHEVEVARKTASRVVyMENGHIVEQGDASCFTQPQTE---AFKNY 239
|
...
gi 578818931 631 LRH 633
Cdd:PRK11124 240 LSH 242
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1082-1248 |
1.41e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.20 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1082 DLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDiasIGLHDLREKLTII-PQDPILFSGSLR 1160
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD---IDDPDVAEACHYLgHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1161 MNLdpfnnysdeEIWKALELAHLKSFVASLQ-LGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLET 1239
Cdd:PRK13539 92 ENL---------EFWAAFLGGEELDIAAALEaVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
....*....
gi 578818931 1240 DNLIQTTIQ 1248
Cdd:PRK13539 163 VALFAELIR 171
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
400-612 |
1.43e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 63.87 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 400 NFDKAMQFSEASFTWEHDSEATVRDVN---LDIMAGQLVAVIGPVGSGKSSLIS------------AMLGEMENVHGHIT 464
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTPFEFKALNntsLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqTIVGDYAIPANLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 465 IK---------GTTAYVPQQSWIQNgTIKDNILFGT----EFNEKRYQQVLEacalLPDLEMLPGgDLAEigEKGINLSG 531
Cdd:PRK13645 82 IKevkrlrkeiGLVFQFPEYQLFQE-TIEKDIAFGPvnlgENKQEAYKKVPE----LLKLVQLPE-DYVK--RSPFELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 532 GQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLGPNGlLKGKTRLLVTHSM-HFLPQVDEIVVLGNGTIVEK 610
Cdd:PRK13645 154 GQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNK-EYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISI 232
|
..
gi 578818931 611 GS 612
Cdd:PRK13645 233 GS 234
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1068-1291 |
1.46e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.60 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELDLVLRG---ITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIG----LHD 1140
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRAlfdIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1141 LREKLTIIPQDP--ILFSGSLRMNL--DPFN-NYSDEEIWKalelahlksfVASLQL---GLSHEVTEAGG-NLSIGQRQ 1211
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVafGPQNfGIPKEKAEK----------IAAEKLemvGLADEFWEKSPfELSGGQMR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1212 LLCLGRALLRKSKILVLDEATAAVD----LETDNLIQTTIQNefaHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSP 1286
Cdd:PRK13643 152 RVAIAGILAMEPEVLVLDEPTAGLDpkarIEMMQLFESIHQS---GQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTP 228
|
....*
gi 578818931 1287 EELLQ 1291
Cdd:PRK13643 229 SDVFQ 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
415-618 |
1.55e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.06 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 415 EHDseaTVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAY----------VPQQSWIQNGTIK 484
Cdd:PRK10619 17 EHE---VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkVADKNQLRLLRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 485 DNILFgTEFNEKRYQQVLEACALLPdLEMLP-----------------GGDLAEIGEKGINLSGGQKQRISLARATYQNL 547
Cdd:PRK10619 94 LTMVF-QHFNLWSHMTVLENVMEAP-IQVLGlskqeareravkylakvGIDERAQGKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 548 DIYLLDDPLSAVDAH-VGK--HIFNKVLGpngllKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 618
Cdd:PRK10619 172 EVLLFDEPTSALDPElVGEvlRIMQQLAE-----EGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1084-1293 |
1.70e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.94 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILE-----AAGGQIIIDGVDIASIGLH--DLREKLTIIPQDPILFS 1156
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDpiEVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1157 gslrmNLDPFNNY-----------SDEEIWKALELAHLKsfvASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKI 1225
Cdd:PRK14267 99 -----HLTIYDNVaigvklnglvkSKKELDERVEWALKK---AALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 1226 LVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHR-LHTIMDSDKVMVLDNGKIIECGSPEELLQIP 1293
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFENP 239
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
422-560 |
1.71e-10 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 62.74 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TA------------YVPQQSWI-QNGTIKDN 486
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdiTHlpmhkrarlgigYLPQEASIfRKLTVEDN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578818931 487 I---LFGTEFNEKRYQQVLEAcaLLPDLemlpggDLAEIGE-KGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 560
Cdd:COG1137 99 IlavLELRKLSKKEREERLEE--LLEEF------GITHLRKsKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
423-591 |
2.45e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 62.80 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 423 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-TAYVPQQ---SWI----QN---GT-----IKDN 486
Cdd:COG1101 23 DGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdVTKLPEYkraKYIgrvfQDpmmGTapsmtIEEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 487 IL----------FGTEFNEKRYQQVLEACALLpdlemlpggDL-------AEIGekgiNLSGGQKQRISLARATYQNLDI 549
Cdd:COG1101 103 LAlayrrgkrrgLRRGLTKKRRELFRELLATL---------GLglenrldTKVG----LLSGGQRQALSLLMATLTKPKL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 578818931 550 YLLDDPLSAVDAHVGKHIF---NKVLGPNGLlkgkTRLLVTHSMH 591
Cdd:COG1101 170 LLLDEHTAALDPKTAALVLeltEKIVEENNL----TTLMVTHNME 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
422-605 |
2.53e-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: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVP---QQSWIQN------GTIKDNILFGT- 491
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpdRMVVFQNysllpwLTVRENIALAVd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 492 ----EFNEKRYQQVLEAcallpDLEMLpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKH 566
Cdd:TIGR01184 81 rvlpDLSKSERRAIVEE-----HIALV---GLTEAADKRPGqLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 578818931 567 IFNKvlgpngLLK-----GKTRLLVTHSM-HFLPQVDEIVVLGNG 605
Cdd:TIGR01184 153 LQEE------LMQiweehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
413-596 |
2.53e-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: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 413 TWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT----TAYVPQQS--WI--QNG--- 481
Cdd:TIGR01189 7 ACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeQRDEPHENilYLghLPGlkp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 482 --TIKDNILFGTEFNEKRYQQVLEACAL--LPDLEMLPGGdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLS 557
Cdd:TIGR01189 87 elSALENLHFWAAIHGGAQRTIEDALAAvgLTGFEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 578818931 558 AVDAHvGKHIFNKVLGPNgLLKGKTRLLVTHsmHFLPQV 596
Cdd:TIGR01189 157 ALDKA-GVALLAGLLRAH-LARGGIVLLTTH--QDLGLV 191
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
422-618 |
3.30e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 62.90 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT------------AYVPQ-QSWIQNGTIKDNIL 488
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPvpsrarharqrvGVVPQfDNLDPDFTVRENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 489 -FGTEFNEKRyQQVLEACALLPDLEMLPGGDLAEIGEkginLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHI 567
Cdd:PRK13537 103 vFGRYFGLSA-AAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578818931 568 FNKVlgPNGLLKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 618
Cdd:PRK13537 178 WERL--RSLLARGKTILLTTHFMEEAERLcDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
411-608 |
3.63e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 64.36 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 411 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISaMLGEMEN-VHGHITIKGTTA------------------- 470
Cdd:PRK10535 13 SYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKpTSGTYRVAGQDVatldadalaqlrrehfgfi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 471 -----YVPQQSWIQNGTIKdNILFGTEFNEKRyqqvLEACALLPDLemlpggDLAE-IGEKGINLSGGQKQRISLARATY 544
Cdd:PRK10535 92 fqryhLLSHLTAAQNVEVP-AVYAGLERKQRL----LRAQELLQRL------GLEDrVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 545 QNLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK-----GKTRLLVTHSMHFLPQVDEIVVLGNGTIV 608
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMA-------ILHqlrdrGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1088-1293 |
3.63e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.49 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1088 ITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIG---LHDLREKLTIIPQDPIlfsgslrMNLD 1164
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY-------ASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1165 PFNN--YSDEEIWKALELAHLKSF---VASL--QLGLSHE-VTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVD 1236
Cdd:PRK10261 416 PRQTvgDSIMEPLRVHGLLPGKAAaarVAWLleRVGLLPEhAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578818931 1237 L----ETDNLIqTTIQNEFAhCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1293
Cdd:PRK10261 496 VsirgQIINLL-LDLQRDFG-IAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
422-611 |
3.63e-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: 61.05 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGqLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG------------TTAYVPQQ-SWIQNGTIKD--- 485
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQEfGVYPNFTVREfld 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 486 --NILFGTEFNE--KRYQQVLEACallpdlemlpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVD 560
Cdd:cd03264 95 yiAWLKGIPSKEvkARVDEVLELV------------NLGDRAKKKIGsLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 561 AhVGKHIFNKVLGpnGLLKGKTRLLVTH-----SMHflpqVDEIVVLGNGTIVEKG 611
Cdd:cd03264 163 P-EERIRFRNLLS--ELGEDRIVILSTHivedvESL----CNQVAVLNKGKLVFEG 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
422-611 |
3.76e-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: 61.14 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG---------TTAYVPQQSWI-QNGTIKDNILFgt 491
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaarnRIGYLPEERGLyPKMKVIDQLVY-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 492 eFNEKRYQQVLEACALLPD-LEMLpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVD---AHVGKH 566
Cdd:cd03269 94 -LAQLKGLKKEEARRRIDEwLERL---ELSEYANKRVEeLSKGNQQKVQFIAAVIHDPELLILDEPFSGLDpvnVELLKD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 578818931 567 IFNKVLGpngllKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 611
Cdd:cd03269 170 VIRELAR-----AGKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1084-1281 |
4.02e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 64.36 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDL----REKLTIIPQDPILFSgsl 1159
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLS--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1160 rmNLDPFNNYSDEEIWKALEL-AHLKSFVASLQ-LGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDL 1237
Cdd:PRK10535 100 --HLTAAQNVEVPAVYAGLERkQRLLRAQELLQrLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 578818931 1238 ETDNLIQTTIQ--NEFAHcTVITIAHRLHTIMDSDKVMVLDNGKII 1281
Cdd:PRK10535 178 HSGEEVMAILHqlRDRGH-TVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
390-609 |
4.12e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.01 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 390 LDTSAIRHdcnfdkamQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT- 468
Cdd:PRK10419 4 LNVSGLSH--------HYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 469 ------------------------TAYVPQQS--WIqngtIKDNILFGTEFNEK----RYQQVLEACALLP-DLEMLPGg 517
Cdd:PRK10419 76 laklnraqrkafrrdiqmvfqdsiSAVNPRKTvrEI----IREPLRHLLSLDKAerlaRASEMLRAVDLDDsVLDKRPP- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 518 dlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSM- 590
Cdd:PRK10419 151 ----------QLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIR-------LLKklqqqfGTACLFITHDLr 213
|
250 260
....*....|....*....|..
gi 578818931 591 ---HFLPQVdeiVVLGNGTIVE 609
Cdd:PRK10419 214 lveRFCQRV---MVMDNGQIVE 232
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1042-1262 |
4.20e-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: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1042 EYTKVENEAPWVTDKRPPPDWPSKGKIQFNNYQVRYR------PELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLtncl 1115
Cdd:TIGR00954 419 KRPRVEEIESGREGGRNSNLVPGRGIVEYQDNGIKFEniplvtPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSL---- 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1116 FRIL----EAAGGQIIIDGvdiasiglhdlREKLTIIPQDPILFSGSLR------MNLDPF--NNYSDEEIWKALELAHL 1183
Cdd:TIGR00954 495 FRILgelwPVYGGRLTKPA-----------KGKLFYVPQRPYMTLGTLRdqiiypDSSEDMkrRGLSDKDLEQILDNVQL 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1184 ksfvaslqlglSHEVTEAGG---------NLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNefAHC 1254
Cdd:TIGR00954 564 -----------THILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGI 630
|
....*...
gi 578818931 1255 TVITIAHR 1262
Cdd:TIGR00954 631 TLFSVSHR 638
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1075-1289 |
4.54e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 62.02 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1075 VRYR-PELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIA--SIGLHDLREKLTIIPQD 1151
Cdd:PRK13639 7 LKYSyPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKTVGIVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1152 P--ILFSGSLRMNL--DPFN-NYSDEEIWKALELAhLKsfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKIL 1226
Cdd:PRK13639 87 PddQLFAPTVEEDVafGPLNlGLSKEEVEKRVKEA-LK------AVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 1227 VLDEATAAVDLETDNLIQTTIQ--NEfAHCTVITIAHRLHTI-MDSDKVMVLDNGKIIECGSPEEL 1289
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYdlNK-EGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1084-1281 |
4.72e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.55 E-value: 4.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGvdiasiglhdlREKLTIIPQDPILFSG------ 1157
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLPQEPPLDDDltvldt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1158 ---------SLRMNLDPFNNYSDEEIWKALELAHLKSFVASL--------------QLGLSHEVTEAG-GNLSIGQRQLL 1213
Cdd:COG0488 82 vldgdaelrALEAELEELEAKLAEPDEDLERLAELQEEFEALggweaearaeeilsGLGFPEEDLDRPvSELSGGWRRRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578818931 1214 CLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEfaHCTVITIAH-R--LHTImdSDKVMVLDNGKII 1281
Cdd:COG0488 162 ALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNY--PGTVLVVSHdRyfLDRV--ATRILELDRGKLT 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
422-617 |
5.57e-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: 5.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHG-HITIKGTT-------------AYV-P--QQSWIQNGTIK 484
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERrggedvwelrkriGLVsPalQLRFPRDETVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 485 DNIL---FGT-----EFNEkryQQVLEACALLPDLEMlpgGDLAE--IGEkginLSGGQKQRISLARATYQNLDIYLLDD 554
Cdd:COG1119 99 DVVLsgfFDSiglyrEPTD---EQRERARELLELLGL---AHLADrpFGT----LSQGEQRRVLIARALVKDPELLILDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 555 PLSAVDAHvGKHIFNKVLgpNGLLK--GKTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGSYSALL 617
Cdd:COG1119 169 PTAGLDLG-ARELLLALL--DKLAAegAPTLVLVTHHVEEIPPgITHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
792-1040 |
6.47e-10 |
|
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: 61.71 E-value: 6.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 792 VGVYGALGLAQGIFVFIAHFWSAfgfVHASNILH---KQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLR 868
Cdd:cd18545 43 ALLFLALNLVNWVASRLRIYLMA---KVGQRILYdlrQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 869 SWITCFLGIISTLVM----------ICMAT-PVFTIIVIPLGIIyvsvqmfyvstSRQLRRLDSVTRSPIYSHFSETVSG 937
Cdd:cd18545 120 NLIPDLLTLVGIVIImfslnvrlalVTLAVlPLLVLVVFLLRRR-----------ARKAWQRVRKKISNLNAYLHESISG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 938 LPVIRAFEHQQRFLKHNEvriDTNQKCVFSWITSNRWLAIRLELVGNLTVFFSALMMVI-YRDTLSGD-TVGFVLSNALN 1015
Cdd:cd18545 189 IRVIQSFAREDENEEIFD---ELNRENRKANMRAVRLNALFWPLVELISALGTALVYWYgGKLVLGGAiTVGVLVAFIGY 265
|
250 260
....*....|....*....|....*...
gi 578818931 1016 IT---QTLNWLVRMTSEIETNIVAVERI 1040
Cdd:cd18545 266 VGrfwQPIRNLSNFYNQLQSAMASAERI 293
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1100-1293 |
7.99e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 61.27 E-value: 7.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1100 VVGRTGAGKSSLTNCLFRILEAAGG-----QIIIDGVDIASI-GLHDLREKLTIIPQDPILFSGSLRMNLdpfnnysdEE 1173
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPMSIMDNV--------LA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1174 IWKALELAHLKSFVASLQLGLSH---------EVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQ 1244
Cdd:PRK14271 124 GVRAHKLVPRKEFRGVAQARLTEvglwdavkdRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 578818931 1245 TTIQNEFAHCTVITIAHRL-HTIMDSDKVMVLDNGKIIECGSPEELLQIP 1293
Cdd:PRK14271 204 EFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSSP 253
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1068-1291 |
8.09e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 61.74 E-value: 8.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELdlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHdLREKLTI 1147
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1148 IPQ----DPILfsgSLRMNLDPFNNY-------SDEEIWKALELAHLKSfVASLQLGlshevteaggNLSIGQRQLLCLG 1216
Cdd:PRK13537 85 VPQfdnlDPDF---TVRENLLVFGRYfglsaaaARALVPPLLEFAKLEN-KADAKVG----------ELSGGMKRRLTLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1217 RALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITI-------AHRLhtimdSDKVMVLDNGKIIECGSPEEL 1289
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVIEEGRKIAEGAPHAL 225
|
..
gi 578818931 1290 LQ 1291
Cdd:PRK13537 226 IE 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
424-616 |
8.94e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 61.64 E-value: 8.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 424 DVNLDIMAGQLVAVIGPVGSGKSSLISAM-----------------------LGEMENVHGHITIKGTT----------- 469
Cdd:PRK13651 25 NVSVEINQGEFIAIIGQTGSGKTTFIEHLnalllpdtgtiewifkdeknkkkTKEKEKVLEKLVIQKTRfkkikkikeir 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 470 ---AYVPQQSWIQ--NGTIKDNILFG-------TEFNEKRYQQVLEACALlpDLEMLPggdlaeigEKGINLSGGQKQRI 537
Cdd:PRK13651 105 rrvGVVFQFAEYQlfEQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGL--DESYLQ--------RSPFELSGGQKRRV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 538 SLARATYQNLDIYLLDDPLSAVDAHVGKHIFNkvLGPNGLLKGKTRLLVTHSM-HFLPQVDEIVVLGNGTIVEKG-SYSA 615
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLdNVLEWTKRTIFFKDGKIIKDGdTYDI 252
|
.
gi 578818931 616 L 616
Cdd:PRK13651 253 L 253
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1085-1293 |
9.91e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.56 E-value: 9.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1085 LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILE-----AAGGQIIIDGVDIAS--IGLHDLREKLTIIPQDPILFSG 1157
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSprTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1158 SLRMNLD---PFNNYSDEEIwkaLELAHLKSFV-ASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATA 1233
Cdd:PRK14239 101 SIYENVVyglRLKGIKDKQV---LDEAVEKSLKgASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578818931 1234 AVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1293
Cdd:PRK14239 178 ALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQMFMNP 238
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1101-1281 |
1.05e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.71 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1101 VGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDI----------ASIGLhdLREKLTIIPQDPI---LFSGslRMNLDPFN 1167
Cdd:PRK10762 36 VGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpkssqeAGIGI--IHQELNLIPQLTIaenIFLG--REFVNRFG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1168 NYSdeeiWKAL--ELAHLKSfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAV-DLETDNLIQ 1244
Cdd:PRK10762 112 RID----WKKMyaEADKLLA-----RLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFR 182
|
170 180 190
....*....|....*....|....*....|....*...
gi 578818931 1245 TTIQNEFAHCTVITIAHRLHTIMD-SDKVMVLDNGKII 1281
Cdd:PRK10762 183 VIRELKSQGRGIVYISHRLKEIFEiCDDVTVFRDGQFI 220
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1073-1293 |
1.06e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 61.52 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1073 YQVR---YRPElDLV--LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIAS---IGLHDLREK 1144
Cdd:PRK11308 15 YPVKrglFKPE-RLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1145 LTIIPQDPIlfsGSLrmnlDPFNNYSD--EE---IWKALELAHLKSFVASL--QLGLSHEVTEAGGNL-SIGQRQLLCLG 1216
Cdd:PRK11308 94 IQIVFQNPY---GSL----NPRKKVGQilEEpllINTSLSAAERREKALAMmaKVGLRPEHYDRYPHMfSGGQRQRIAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1217 RALLRKSKILVLDEATAAVDLEtdnlIQTTIQNEFA------HCTVITIAHRL----HTimdSDKVMVLDNGKIIECGSP 1286
Cdd:PRK11308 167 RALMLDPDVVVADEPVSALDVS----VQAQVLNLMMdlqqelGLSYVFISHDLsvveHI---ADEVMVMYLGRCVEKGTK 239
|
....*..
gi 578818931 1287 EELLQIP 1293
Cdd:PRK11308 240 EQIFNNP 246
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1084-1290 |
1.08e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 61.77 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGlHDLREKLTIIPQ-DPILFSGSLRMN 1162
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA-RLARARIGVVPQfDNLDLEFTVREN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1163 LDPFNNY-------SDEEIWKALELAHLKSFVASlqlglshEVTEaggnLSIGQRQLLCLGRALLRKSKILVLDEATAAV 1235
Cdd:PRK13536 135 LLVFGRYfgmstreIEAVIPSLLEFARLESKADA-------RVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578818931 1236 DLETDNLIQTTIQNEFAHC-TVITIAHrlhtIMDS-----DKVMVLDNGKIIECGSPEELL 1290
Cdd:PRK13536 204 DPHARHLIWERLRSLLARGkTILLTTH----FMEEaerlcDRLCVLEAGRKIAEGRPHALI 260
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1096-1280 |
1.15e-09 |
|
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: 62.53 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1096 EKIGVVGRTGAGKSSLTNCLFRILEAA-GGQIIIDG--VDIASIgLHDLREKLTIIPQD-------PILFSGSlRMNLDP 1165
Cdd:TIGR02633 287 EILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNP-AQAIRAGIAMVPEDrkrhgivPILGVGK-NITLSV 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1166 FNNYSDE-EIWKALELAHLKSFVASLQLGLSHEVTEAGGnLSIGQRQLLCLGRALLRKSKILVLDEATAAVDL----ETD 1240
Cdd:TIGR02633 365 LKSFCFKmRIDAAAELQIIGSAIQRLKVKTASPFLPIGR-LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVgakyEIY 443
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 578818931 1241 NLIQTTIQNEFAhctVITIAHRLHTIMD-SDKVMVLDNGKI 1280
Cdd:TIGR02633 444 KLINQLAQEGVA---IIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
422-611 |
1.19e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 60.31 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAM-----LGEMENVHGHITIKGTTAY----------------VPQQswIQN 480
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQDIFkmdvielrrrvqmvfqIPNP--IPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 481 GTIKDNILFGTEFN---------EKRYQQVLEACALLPDLEmlpggdlAEIGEKGINLSGGQKQRISLARATYQNLDIYL 551
Cdd:PRK14247 97 LSIFENVALGLKLNrlvkskkelQERVRWALEKAQLWDEVK-------DRLDAPAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578818931 552 LDDPLSAVDAHVGKHIFNKVLgpnGLLKGKTRLLVThsmHFLPQV----DEIVVLGNGTIVEKG 611
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFL---ELKKDMTIVLVT---HFPQQAarisDYVAFLYKGQIVEWG 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
420-607 |
1.25e-09 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 58.98 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 420 ATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--------------AYVP----QQSWIQNG 481
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPvtrrsprdairagiAYVPedrkREGLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 482 TIKDNILfgtefnekryqqvleacalLPDLemlpggdlaeigekginLSGGQKQRISLARATYQNLDIYLLDDPLSAVDa 561
Cdd:cd03215 94 SVAENIA-------------------LSSL-----------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVD- 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 578818931 562 hVG--KHIFNKVLgpngLL--KGKTRLLVTHSMHFLPQV-DEIVVLGNGTI 607
Cdd:cd03215 137 -VGakAEIYRLIR----ELadAGKAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1084-1281 |
1.35e-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: 60.04 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVD--------IASIGLHdLREKLTIIPQDPILf 1155
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrrkkfLRRIGVV-FGQKTQLWWDLPVI- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1156 sGSLRMNLDPFNnysdeeiwkaLELAHLKSFVASLQ--LGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATA 1233
Cdd:cd03267 114 -DSFYLLAAIYD----------LPPARFKKRLDELSelLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 578818931 1234 AVDLETDNLIQTTIQ--NEFAHCTVITIAHRLHTIMD-SDKVMVLDNGKII 1281
Cdd:cd03267 183 GLDVVAQENIRNFLKeyNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
402-638 |
1.36e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 60.88 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 402 DKAMQFSEASFTWEHDSEAT-VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTaYVPQQSW--- 477
Cdd:PRK13642 2 NKILEVENLVFKYEKESDVNqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEL-LTAENVWnlr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 478 ------IQN-------GTIKDNILFGTEfNE--------KRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQR 536
Cdd:PRK13642 81 rkigmvFQNpdnqfvgATVEDDVAFGME-NQgipreemiKRVDEALLAVNMLDFKTREPA-----------RLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 537 ISLARATYQNLDIYLLDDPLSAVDAhVGKHIFNKVLGPnglLKGK---TRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSY 613
Cdd:PRK13642 149 VAVAGIIALRPEIIILDESTSMLDP-TGRQEIMRVIHE---IKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAP 224
|
250 260 270
....*....|....*....|....*....|....*..
gi 578818931 614 SALLAKKGE---------FAKNLKTFLRHTG---PEE 638
Cdd:PRK13642 225 SELFATSEDmveigldvpFSSNLMKDLRKNGfdlPEK 261
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1084-1291 |
1.63e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 59.71 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGvDIASI-----GLH-DL--REKltiipqdpILF 1155
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-RVSALlelgaGFHpELtgREN--------IYL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1156 SGSLrmnldpfNNYSDEEIwKAL-----ELAHLKSFvaslqlgLSHEVteagGNLSIGQRQLLCLGRALLRKSKILVLDE 1230
Cdd:COG1134 112 NGRL-------LGLSRKEI-DEKfdeivEFAELGDF-------IDQPV----KTYSSGMRARLAFAVATAVDPDILLVDE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 1231 ATAAVDLE----TDNLIQTTIQNefaHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQ 1291
Cdd:COG1134 173 VLAVGDAAfqkkCLARIRELRES---GRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
425-618 |
1.83e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 59.51 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 425 VNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG--------------TTAYVPQQSWI-QNGTIKDNILF 489
Cdd:PRK11614 24 VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditdwqtakimreAVAIVPEGRRVfSRMTVEENLAM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 490 GTEFNEK-RYQQVLEAC-ALLPDLemlpggdLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHI 567
Cdd:PRK11614 104 GGFFAERdQFQERIKWVyELFPRL-------HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578818931 568 FNKVLGPNGllKGKTRLLVTHSMH-FLPQVDEIVVLGNGTIVEKGSYSALLA 618
Cdd:PRK11614 177 FDTIEQLRE--QGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
422-591 |
1.89e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 59.44 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTayVPQQSWIQNGTIKDNIL-FGTEFNEkryqq 500
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQP--MSKLSSAAKAELRNQKLgFIYQFHH----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 501 vleacaLLPD---LE-----MLPGGD------------LAEIG-EKGIN-----LSGGQKQRISLARATYQNLDIYLLDD 554
Cdd:PRK11629 98 ------LLPDftaLEnvampLLIGKKkpaeinsralemLAAVGlEHRANhrpseLSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 578818931 555 PLSAVDAHVGKHIFNkVLGPNGLLKGKTRLLVTHSMH 591
Cdd:PRK11629 172 PTGNLDARNADSIFQ-LLGELNRLQGTAFLVVTHDLQ 207
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
423-620 |
1.92e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.87 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 423 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITI-KGTTA-YVPQQSWI-QNGTIKDNILFG--------T 491
Cdd:TIGR03719 22 KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIKVgYLPQEPQLdPTKTVRENVEEGvaeikdalD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 492 EFNE-------------------KRYQQVLEACA---LLPDLEM------LPGGDlAEIGekgiNLSGGQKQRISLARAT 543
Cdd:TIGR03719 102 RFNEisakyaepdadfdklaaeqAELQEIIDAADawdLDSQLEIamdalrCPPWD-ADVT----KLSGGERRRVALCRLL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 544 YQNLDIYLLDDPLSAVDAH----VGKHIFNkvlgpnglLKGkTRLLVTHSMHFLPQVDE-IVVLGNGT-IVEKGSYSALL 617
Cdd:TIGR03719 177 LSKPDMLLLDEPTNHLDAEsvawLERHLQE--------YPG-TVVAVTHDRYFLDNVAGwILELDRGRgIPWEGNYSSWL 247
|
...
gi 578818931 618 AKK 620
Cdd:TIGR03719 248 EQK 250
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
413-561 |
2.30e-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: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 413 TWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWI--------QNG--- 481
Cdd:cd03231 7 TCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIArgllylghAPGikt 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 482 --TIKDNILFGTEFNEKryQQVLEAcallpdlemlpggdLAEIGEKGI------NLSGGQKQRISLARATYQNLDIYLLD 553
Cdd:cd03231 87 tlSVLENLRFWHADHSD--EQVEEA--------------LARVGLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWILD 150
|
....*...
gi 578818931 554 DPLSAVDA 561
Cdd:cd03231 151 EPTTALDK 158
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
411-612 |
3.28e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 59.72 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 411 SFTWEHDSEAT----VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSW-IQNgtiKD 485
Cdd:PRK13633 11 SYKYESNEESTeklaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIRN---KA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 486 NILFGTEFNEKRYQQVLEACALLPdlEMLpGGDLAEIGE------KGIN-----------LSGGQKQRISLARATYQNLD 548
Cdd:PRK13633 88 GMVFQNPDNQIVATIVEEDVAFGP--ENL-GIPPEEIRErvdeslKKVGmyeyrrhaphlLSGGQKQRVAIAGILAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578818931 549 IYLLDDPLSAVDAHVGKHIFNKVLGPNGLlKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGS 612
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNTIKELNKK-YGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1096-1280 |
3.37e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1096 EKIGVVGRTGAGKSSLTNCLFRILEAA-GGQIIIDG--VDIASIgLHDLREKLTIIPQD-------PILFSG--SLRMNL 1163
Cdd:PRK13549 289 EILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGkpVKIRNP-QQAIAQGIAMVPEDrkrdgivPVMGVGknITLAAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1164 DPFNNYSdeEIWKALELAHLKSFVASLQLGLSHeVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDL----ET 1239
Cdd:PRK13549 368 DRFTGGS--RIDDAAELKTILESIQRLKVKTAS-PELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVgakyEI 444
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 578818931 1240 DNLIQTTIQNEFAhctVITIAHRLHTIMD-SDKVMVLDNGKI 1280
Cdd:PRK13549 445 YKLINQLVQQGVA---IIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
422-618 |
4.01e-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: 60.85 E-value: 4.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGeMENVHGHITIKGT-------TAYVPQQSWIQ------NG------T 482
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQdldglsrRALRPLRRRMQvvfqdpFGslsprmT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 483 IKDNI-----LFGTEFNEK-RYQQVLEAcallpdlemlpggdLAEIG-----------EkginLSGGQKQRISLARATYQ 545
Cdd:COG4172 381 VGQIIaeglrVHGPGLSAAeRRARVAEA--------------LEEVGldpaarhryphE----FSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 546 NLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 618
Cdd:COG4172 443 EPKLLVLDEPTSALDVSVQAQILD-------LLRdlqrehGLAYLFISHDLAVVRALaHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1086-1280 |
4.68e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.45 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1086 RGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHD-LREKLTIIPQDP----ILFSGSLR 1160
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDRqssgLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1161 MNLDPFnNYSDEEIW--KALELAHLKSFVASLQLGLSHEVTEAGGnLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLE 1238
Cdd:PRK15439 360 WNVCAL-THNRRGFWikPARENAVLERYRRALNIKFNHAEQAART-LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 578818931 1239 TDNLIQTTIQNEFA-HCTVITIAHRLHTIMD-SDKVMVLDNGKI 1280
Cdd:PRK15439 438 ARNDIYQLIRSIAAqNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
422-618 |
4.79e-09 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 58.51 E-value: 4.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TAYVPQQswI---------QNG------TIK 484
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRdiTGLPPHR--IarlgiartfQNPrlfpelTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 485 DNIL-----------FGTEFNEKRYQ-----------QVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARA 542
Cdd:COG0411 98 ENVLvaaharlgrglLAALLRLPRARreereareraeELLERVGLADRADEPAG-----------NLSYGQQRRLEIARA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 543 tyqnL----DIYLLDDP---LSAVDAHVGKHIFNKVLGPNGLlkgkTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYS 614
Cdd:COG0411 167 ----LatepKLLLLDEPaagLNPEETEELAELIRRLRDERGI----TILLIEHDMDLVMGLaDRIVVLDFGRVIAEGTPA 238
|
....
gi 578818931 615 ALLA 618
Cdd:COG0411 239 EVRA 242
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
423-609 |
5.09e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.42 E-value: 5.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 423 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGemenVH----GHITIKGTT--------------AYVPQQ-SWIQNGTI 483
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSG----VYqpdsGEILLDGEPvrfrsprdaqaagiAIIHQElNLVPNLSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 484 KDNILFGTE------FNEKR-YQQVLEACALLpDLEMLPGgdlAEIGEkginLSGGQKQRISLARATYQNLDIYLLDDPL 556
Cdd:COG1129 97 AENIFLGREprrgglIDWRAmRRRARELLARL-GLDIDPD---TPVGD----LSVAQQQLVEIARALSRDARVLILDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 557 SAVDAHVGKHIFNKVLGpnglLK--GKTRLLVThsmHFLPQV----DEIVVLGNGTIVE 609
Cdd:COG1129 169 ASLTEREVERLFRIIRR----LKaqGVAIIYIS---HRLDEVfeiaDRVTVLRDGRLVG 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1085-1278 |
5.17e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.57 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1085 LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDI--------ASIGLHDLREKLTIIPQDPI--- 1153
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnkldhklaAQLGIGIIYQELSVIDELTVlen 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1154 LFSGSLRMNLDPFNNYSDeeiWKALELahlKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATA 1233
Cdd:PRK09700 101 LYIGRHLTKKVCGVNIID---WREMRV---RAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 578818931 1234 AV-DLETDNL--IQTTIQNEFAhcTVITIAHRLHTIMD-SDKVMVLDNG 1278
Cdd:PRK09700 175 SLtNKEVDYLflIMNQLRKEGT--AIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
412-611 |
5.38e-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: 58.11 E-value: 5.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 412 FTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGttaYVPqqsWIQNGTIKDNI--LF 489
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG---LVP---WKRRKKFLRRIgvVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 490 GT---------------------EFNEKRYQQVLEACAllpdlEMLpggDLAEIGEKGI-NLSGGQKQRISLARATYQNL 547
Cdd:cd03267 101 GQktqlwwdlpvidsfyllaaiyDLPPARFKKRLDELS-----ELL---DLEELLDTPVrQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 548 DIYLLDDPLSAVDAHVGKHIFNKVLGPNGlLKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 611
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYNR-ERGTTVLLTSHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1084-1289 |
5.47e-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: 59.73 E-value: 5.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCL--FriLEAAGGQIIIDGVDIASIGLHdlREKLTIIPQDPILFS----- 1156
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIagF--ETPDSGRILLDGRDVTGLPPE--KRNVGMVFQDYALFPhltva 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1157 -----GsLRMNldpfnNYSDEEIWK----ALELAHLKSFvaslqlgLSHEVTEaggnLSIGQRQLLCLGRALLRKSKILV 1227
Cdd:COG3842 96 envafG-LRMR-----GVPKAEIRArvaeLLELVGLEGL-------ADRYPHQ----LSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578818931 1228 LDEATAAVDLET-----DNLIQttIQNEFaHCTVITIAHrlhtimD-------SDKVMVLDNGKIIECGSPEEL 1289
Cdd:COG3842 159 LDEPLSALDAKLreemrEELRR--LQREL-GITFIYVTH------DqeealalADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1084-1292 |
5.54e-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: 57.54 E-value: 5.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCL--FRILEAAGGQIIIDGVDIASIGLHD-LREKLTIIPQDPILFSGslr 1160
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEErARLGIFLAFQYPPEIPG--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1161 mnldpfnnysdeeiwkalelAHLKSFVASLQLGLShevteagGnlsiGQRQLLCLGRALLRKSKILVLDEATAAVDLETD 1240
Cdd:cd03217 92 --------------------VKNADFLRYVNEGFS-------G----GEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 1241 NLIQTTIqNEFA--HCTVITIAH--RLHTIMDSDKVMVLDNGKIIECGSPEELLQI 1292
Cdd:cd03217 141 RLVAEVI-NKLReeGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKELALEI 195
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
343-609 |
6.14e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 60.37 E-value: 6.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 343 DAQKAFT-SITLFnILRFPL-SM---LPMMISsmlqASVSTERLEKY-LGGD--DLDTSAIRHDCnfdKAMQFSEASFTW 414
Cdd:PRK10522 261 DTNVAATySLTLL-FLRTPLlSAvgaLPTLLS----AQVAFNKLNKLaLAPYkaEFPRPQAFPDW---QTLELRNVTFAY 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 415 eHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLisAML--GEMENVHGHITIKGTT-------AYVPQQSWIqngtIKD 485
Cdd:PRK10522 333 -QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTL--AMLltGLYQPQSGEILLDGKPvtaeqpeDYRKLFSAV----FTD 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 486 NILF-------GTEFNEKRYQQVLEACALLPDLEmLPGGDLAEIgekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSA 558
Cdd:PRK10522 406 FHLFdqllgpeGKPANPALVEKWLERLKMAHKLE-LEDGRISNL-----KLSKGQKKRLALLLALAEERDILLLDEWAAD 479
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 578818931 559 VDAHVgKHIFNKVLGPNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVE 609
Cdd:PRK10522 480 QDPHF-RREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1084-1293 |
6.54e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 58.22 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDI-ASIGL-------HDLREKLTIIPQDPILF 1155
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLsqqkgliRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1156 ----------SGSLRMNLDPfnnySDEEIWKALELAhlksfvasLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKI 1225
Cdd:PRK11264 98 phrtvleniiEGPVIVKGEP----KEEATARARELL--------AKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578818931 1226 LVLDEATAAVDLETDNLIQTTIQnEFAH--CTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1293
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNTIR-QLAQekRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1096-1293 |
6.80e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 58.97 E-value: 6.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1096 EKIGVVGRTGAGKSSLTNCLFRILEAAG---GQIIIDGVDIASIGLHDLR----EKLTIIPQDPIlfsgslrMNLDPFNN 1168
Cdd:PRK09473 43 ETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPEKELNklraEQISMIFQDPM-------TSLNPYMR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1169 YSdEEIWKALEL----AHLKSFVASLQLGLSHEVTEAGGNL-------SIGQRQLLCLGRALLRKSKILVLDEATAAVDL 1237
Cdd:PRK09473 116 VG-EQLMEVLMLhkgmSKAEAFEESVRMLDAVKMPEARKRMkmyphefSGGMRQRVMIAMALLCRPKLLIADEPTTALDV 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1238 ETDNLIQT---TIQNEFaHCTVITIAHRLHTIMDS-DKVMVLDNGKIIECGSPEELLQIP 1293
Cdd:PRK09473 195 TVQAQIMTllnELKREF-NTAIIMITHDLGVVAGIcDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1085-1281 |
7.14e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.94 E-value: 7.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1085 LRGITCDIGSMEKIGVVGRTGAGKSSLtnclFRILEAA------GGQIIIDGVDIASIGLHDLREK--------LTIIPQ 1150
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTL----MKVLSGVyphgtyEGEIIFEGEELQASNIRDTERAgiaiihqeLALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1151 DPIL---FSGSL-----RMNLDPFnnYSDEEIWKAlelahlksfvaslQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRK 1222
Cdd:PRK13549 97 LSVLeniFLGNEitpggIMDYDAM--YLRAQKLLA-------------QLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578818931 1223 SKILVLDEATAAV-DLETDNLIqTTIQNEFAH-CTVITIAHRLHTIMD-SDKVMVLDNGKII 1281
Cdd:PRK13549 162 ARLLILDEPTASLtESETAVLL-DIIRDLKAHgIACIYISHKLNEVKAiSDTICVIRDGRHI 222
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
405-614 |
9.56e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.21 E-value: 9.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 405 MQFSEASFTWEHDSEATVR---DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-TTAYVPQQSWIQN 480
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRalfDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDiVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 481 GTIKDNILFgtEFNEKRY--QQVLEACALLPD----------------LEMLpgGDLAEIGEKG-INLSGGQKQRISLAR 541
Cdd:PRK13643 82 VRKKVGVVF--QFPESQLfeETVLKDVAFGPQnfgipkekaekiaaekLEMV--GLADEFWEKSpFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578818931 542 ATYQNLDIYLLDDPLSAVDAHVGKHIFNkvLGPNGLLKGKTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGSYS 614
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQ--LFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPS 229
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
797-1040 |
9.65e-09 |
|
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: 58.29 E-value: 9.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 797 ALGLAQGIFVFIAHFWSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLG 876
Cdd:cd18564 62 GIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 877 IISTLVMICMATPVFTII---VIPLgiiyvsvqmFYVSTSRQLRRLDSVTR------SPIYSHFSETVSGLPVIRAF--- 944
Cdd:cd18564 142 LVGMLGVMFWLDWQLALIalaVAPL---------LLLAARRFSRRIKEASReqrrreGALASVAQESLSAIRVVQAFgre 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 945 -EHQQRFLKHNEVRIDTNQKcvfswitSNRwLAIRLELVGNLTVFFSALMMVIY------RDTLS-GDTVGFV--LSNAL 1014
Cdd:cd18564 213 eHEERRFARENRKSLRAGLR-------AAR-LQALLSPVVDVLVAVGTALVLWFgawlvlAGRLTpGDLLVFLayLKNLY 284
|
250 260
....*....|....*....|....*.
gi 578818931 1015 NITQTlnwLVRMTSEIETNIVAVERI 1040
Cdd:cd18564 285 KPVRD---LAKLTGRIAKASASAERV 307
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
422-560 |
1.00e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 57.60 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITI--------------KGTTAYVPQQSWI-QNGTIKDN 486
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllplharaRRGIGYLPQEASIfRRLSVYDN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 487 ILFGTEFNE--KRYQQVLEACALLPDLEMLPGGDlaeigEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 560
Cdd:PRK10895 99 LMAVLQIRDdlSAEQREDRANELMEEFHIEHLRD-----SMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1101-1312 |
1.04e-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: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1101 VGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASiGLHDLREKLTIIPQDPILFSgslRMNLDPFNNYSDEEIWKALEL 1180
Cdd:TIGR01257 962 LGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFH---HLTVAEHILFYAQLKGRSWEE 1037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1181 AHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIA 1260
Cdd:TIGR01257 1038 AQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMST 1117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578818931 1261 HRL-HTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFYFMAKEAGIENVNSTK 1312
Cdd:TIGR01257 1118 HHMdEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIQSQR 1170
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
422-611 |
1.14e-08 |
|
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: 56.99 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-TTAYVPQQSWIQNG------------TIKDNIL 488
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARRRLGfvsdstglydrlTARENLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 489 -FGTEFNEKRYQQVLEACALLPDLEMlpgGDLAEIGEKGinLSGGQKQRISLARATYQNLDIYLLDDPLSAVDahvgkhi 567
Cdd:cd03266 101 yFAGLYGLKGDELTARLEELADRLGM---EELLDRRVGG--FSTGMRQKVAIARALVHDPPVLLLDEPTTGLD------- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578818931 568 fnkVLGPNGLLK--------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 611
Cdd:cd03266 169 ---VMATRALREfirqlralGKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1084-1297 |
1.17e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.33 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILeAAGGQIIIDGVDIASIG---LHDLREKLTIIPQDPilfSGSL- 1159
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP---NSSLn 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1160 -RMNLDpfnnysdEEIWKALELAHLKSFVASLQLGLSHEVTEAG----------GNLSIGQRQLLCLGRALLRKSKILVL 1228
Cdd:PRK15134 377 pRLNVL-------QIIEEGLRVHQPTLSAAQREQQVIAVMEEVGldpetrhrypAEFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578818931 1229 DEATAAVDLETDNLIQT---TIQNEFaHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIPGPFY 1297
Cdd:PRK15134 450 DEPTSSLDKTVQAQILAllkSLQQKH-QLAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1100-1275 |
1.22e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.03 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1100 VVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNLD-PF---NNYSDEeiw 1175
Cdd:PRK10247 38 ITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNLIfPWqirNQQPDP--- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1176 kalelahlKSFVASL-QLGLSHEVTEAGGN-LSIGQRQLLCLGRALLRKSKILVLDEATAAVDleTDNliqTTIQNEFAH 1253
Cdd:PRK10247 115 --------AIFLDDLeRFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALD--ESN---KHNVNEIIH 181
|
170 180
....*....|....*....|....*....
gi 578818931 1254 -------CTVITIAHRLHTIMDSDKVMVL 1275
Cdd:PRK10247 182 ryvreqnIAVLWVTHDKDEINHADKVITL 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1068-1281 |
1.33e-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: 56.52 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELdlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHD------- 1140
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRigylpee 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1141 --LREKLTIIPQdpILFSGSLRmnldpfnNYSDEEIWKALElAHLKSFvaslqlGLSHEVTEAGGNLSIGQRQLLCLGRA 1218
Cdd:cd03269 79 rgLYPKMKVIDQ--LVYLAQLK-------GLKKEEARRRID-EWLERL------ELSEYANKRVEELSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 1219 LLRKSKILVLDEATAAVDLETDNLIQTTIqNEFAH--CTVITIAHRLHTIMD-SDKVMVLDNGKII 1281
Cdd:cd03269 143 VIHDPELLILDEPFSGLDPVNVELLKDVI-RELARagKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1084-1287 |
1.38e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.43 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIidgvdiasiglHDLREKLTIIPQ----DPIL-FSGS 1158
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLRIGYVPQklylDTTLpLTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1159 LRMNLDPfnNYSDEEIWKALE---LAHLKSfvASLQlglshevteaggNLSIGQRQLLCLGRALLRKSKILVLDEATAAV 1235
Cdd:PRK09544 88 RFLRLRP--GTKKEDILPALKrvqAGHLID--APMQ------------KLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 578818931 1236 D----LETDNLIQtTIQNEFaHCTVITIAHRLHTIM-DSDKVMVLdNGKIIECGSPE 1287
Cdd:PRK09544 152 DvngqVALYDLID-QLRREL-DCAVLMVSHDLHLVMaKTDEVLCL-NHHICCSGTPE 205
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
824-1040 |
1.45e-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: 57.90 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 824 LHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIV-IPLGIIY 902
Cdd:cd18563 78 LRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVlIPVPLVV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 903 VSVQMFYVSTSRQLRRLDSVtRSPIYSHFSETVSGLPVIRAF--EH--QQRFLKHNevridtnqkcvfswitsNRWLAIR 978
Cdd:cd18563 158 WGSYFFWKKIRRLFHRQWRR-WSRLNSVLNDTLPGIRVVKAFgqEKreIKRFDEAN-----------------QELLDAN 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578818931 979 LELVGNLTVFFSALMMVIY-----------RDTLSGD-TVGFVLSNALNITQ---TLNWLVRMTSEIETNIVAVERI 1040
Cdd:cd18563 220 IRAEKLWATFFPLLTFLTSlgtlivwyfggRQVLSGTmTLGTLVAFLSYLGMfygPLQWLSRLNNWITRALTSAERI 296
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1084-1284 |
1.96e-08 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 56.11 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIAsiglhDLREK---LTIIPQDPILFSgslR 1160
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT-----DLPPKdrdIAMVFQNYALYP---H 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1161 MNLdpFNNysdeeIWKALELAHLK--------SFVASLqLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEAT 1232
Cdd:cd03301 87 MTV--YDN-----IAFGLKLRKVPkdeidervREVAEL-LQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 1233 AAVD--------LETDNLIQ----TTI-----QNEfahctVITIAhrlhtimdsDKVMVLDNGKIIECG 1284
Cdd:cd03301 159 SNLDaklrvqmrAELKRLQQrlgtTTIyvthdQVE-----AMTMA---------DRIAVMNDGQIQQIG 213
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1099-1291 |
2.25e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 56.72 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1099 GVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQD-PILFSGSLRM-----------NLDPF 1166
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlPAAEGMTVRElvaigrypwhgALGRF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1167 NNYSDEEIWKALELAHLKSFvaslqlglSHEVTEAggnLSIGQRQLLCLGRALLRKSKILVLDEATAAVDL----ETDNL 1242
Cdd:PRK10575 121 GAADREKVEEAISLVGLKPL--------AHRLVDS---LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIahqvDVLAL 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578818931 1243 IQTTIQNEfaHCTVITIahrLHTI-MDS---DKVMVLDNGKIIECGSPEELLQ 1291
Cdd:PRK10575 190 VHRLSQER--GLTVIAV---LHDInMAArycDYLVALRGGEMIAQGTPAELMR 237
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
422-555 |
2.28e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.11 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--------------AYVP----QQSWIQNGTI 483
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPvrirsprdairagiAYVPedrkGEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 484 KDNIL---------FGTEFNEKRYQQVLEACALL----PDLEmlpggdlAEIGekgiNLSGGQKQRISLARATYQNLDIY 550
Cdd:COG1129 348 RENITlasldrlsrGGLLDRRRERALAEEYIKRLriktPSPE-------QPVG----NLSGGNQQKVVLAKWLATDPKVL 416
|
....*
gi 578818931 551 LLDDP 555
Cdd:COG1129 417 ILDEP 421
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
824-896 |
2.38e-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: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 824 LHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQS----LRSWITCFLGI-----IS---TLVMICMATPVF 891
Cdd:cd18573 76 LRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNlsdgLRSLVSGVGGIgmmlyISpklTLVMLLVVPPIA 155
|
....*
gi 578818931 892 TIIVI 896
Cdd:cd18573 156 VGAVF 160
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1084-1293 |
2.70e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 56.52 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSgSLRMNL 1163
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKNQLRLLRT-RLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1164 DPFNNYSDEEIWKALELAHLKSfvaslqLGLS-HEVTEAG------------------GNLSIGQRQLLCLGRALLRKSK 1224
Cdd:PRK10619 99 QHFNLWSHMTVLENVMEAPIQV------LGLSkQEARERAvkylakvgideraqgkypVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578818931 1225 ILVLDEATAAVDLETDNLIQTTIQnEFAH--CTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1293
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQ-QLAEegKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
432-612 |
2.70e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 58.13 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 432 GQLVAVIGPVGSGKSSLISAMLGEMEN---VHGHITIKGT----------TAYVPQQS-WIQNGTIKDNILFGTEFNEKR 497
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMpidakemraiSAYVQQDDlFIPTLTVREHLMFQAHLRMPR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 498 Y----QQVLEACALLPDLEMLPGGDLAeIGEKGI--NLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFnKV 571
Cdd:TIGR00955 131 RvtkkEKRERVDEVLQALGLRKCANTR-IGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVV-QV 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 578818931 572 LgpNGL-LKGKTRLLVTH--SMHFLPQVDEIVVLGNGTIVEKGS 612
Cdd:TIGR00955 209 L--KGLaQKGKTIICTIHqpSSELFELFDKIILMAEGRVAYLGS 250
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
417-612 |
2.71e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.59 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 417 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYV--------------------PQQS 476
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFgkdifqidaiklrkevgmvfQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 477 WIQNGTIKDNILFGTE---FNEKR-YQQVLEACallpdleMLPGGDLAEIGEK----GINLSGGQKQRISLARATYQNLD 548
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKshgIKEKReIKKIVEEC-------LRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 549 IYLLDDPLSAVDAhVGKHIFNKVLgpNGLLKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 612
Cdd:PRK14246 174 VLLMDEPTSMIDI-VNSQAIEKLI--TELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGS 235
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1084-1281 |
2.79e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.04 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDI-----ASIglhdLREKLTIIPQDPILFSgs 1158
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdwqtAKI----MREAVAIVPEGRRVFS-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1159 lRM----NLDPFNNYSDEEIWKalelaHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAA 1234
Cdd:PRK11614 94 -RMtveeNLAMGGFFAERDQFQ-----ERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 578818931 1235 VDLETDNLIQTTIQNEFAHCTVITIAHR--LHTIMDSDKVMVLDNGKII 1281
Cdd:PRK11614 168 LAPIIIQQIFDTIEQLREQGMTIFLVEQnaNQALKLADRGYVLENGHVV 216
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
800-1040 |
3.01e-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: 56.72 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 800 LAQGIFVFIAHFWsaFGFV--HASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDD----TLPQSLRSWITC 873
Cdd:cd18576 47 LLQAVFSFFRIYL--FARVgeRVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDtlttTLAEFLRQILTL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 874 FLGIIS--------TLVMICMAtPVFTIIVIPLGiiyvsvqmfyvstsRQLRRL-----DSVTRSpiYSHFSETVSGLPV 940
Cdd:cd18576 125 IGGVVLlffiswklTLLMLATV-PVVVLVAVLFG--------------RRIRKLskkvqDELAEA--NTIVEETLQGIRV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 941 IRAF---EHQ-QRFLKHNEVRIDTnqkcvfsWITSNRWLAIRLELVGnlTVFFSALMMVIY-------RDTLS-GDTVGF 1008
Cdd:cd18576 188 VKAFtreDYEiERYRKALERVVKL-------ALKRARIRALFSSFII--FLLFGAIVAVLWyggrlvlAGELTaGDLVAF 258
|
250 260 270
....*....|....*....|....*....|..
gi 578818931 1009 VLSnALNITQTLNWLVRMTSEIETNIVAVERI 1040
Cdd:cd18576 259 LLY-TLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1039-1282 |
3.16e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 57.77 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1039 RITEYTKVENEAPWVTDKRP----PPDWPSkGK--IQFNNYQVRY--RPeldlVLRGITCDIGSMEKIGVVGRTGAGKSS 1110
Cdd:COG0488 282 RIKALEKLEREEPPRRDKTVeirfPPPERL-GKkvLELEGLSKSYgdKT----LLDDLSLRIDRGDRIGLIGPNGAGKST 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1111 LTNCLFRILEAAGGQIII-DGVDIA--SIGLHDLREKLTIIpqdpilfsgslrmnldpfnnysdEEIWKALELA---HLK 1184
Cdd:COG0488 357 LLKLLAGELEPDSGTVKLgETVKIGyfDQHQEELDPDKTVL-----------------------DELRDGAPGGteqEVR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1185 SFVASlqLGLS-HEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNeFAHcTVITIAH-R 1262
Cdd:COG0488 414 GYLGR--FLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD-FPG-TVLLVSHdR 489
|
250 260
....*....|....*....|..
gi 578818931 1263 --LHTImdSDKVMVLDNGKIIE 1282
Cdd:COG0488 490 yfLDRV--ATRILEFEDGGVRE 509
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
422-604 |
3.24e-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: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG------------TTAYVPQQSWI-QNGTIKDNIL 488
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldavrqSLGMCPQHNILfHHLTVAEHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 489 FGTEFNEKRYQQV-LEACALLPDLemlpgGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHI 567
Cdd:TIGR01257 1026 FYAQLKGRSWEEAqLEMEAMLEDT-----GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190
....*....|....*....|....*....|....*..
gi 578818931 568 FNKVLgpnGLLKGKTRLLVTHSMhflpqvDEIVVLGN 604
Cdd:TIGR01257 1101 WDLLL---KYRSGRTIIMSTHHM------DEADLLGD 1128
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1057-1282 |
4.06e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 57.67 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1057 RPPPDWPskgKIQFNNYQVRYRPE------LDLVL-RGitcdigsmEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIID 1129
Cdd:PRK10522 315 QAFPDWQ---TLELRNVTFAYQDNgfsvgpINLTIkRG--------ELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLD 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1130 GVDIASIGLHDLREKLTIIPQDPILFSgslRMnLDPFNNYSDEEI---WkaleLAHLKsfvaslqlgLSHEVTEAGG--- 1203
Cdd:PRK10522 384 GKPVTAEQPEDYRKLFSAVFTDFHLFD---QL-LGPEGKPANPALvekW----LERLK---------MAHKLELEDGris 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1204 --NLSIGQRQLLCLGRALLRKSKILVLDEATAAVD--------LETDNLIQTTIQnefahcTVITIAHRLHTIMDSDKVM 1273
Cdd:PRK10522 447 nlKLSKGQKKRLALLLALAEERDILLLDEWAADQDphfrrefyQVLLPLLQEMGK------TIFAISHDDHYFIHADRLL 520
|
....*....
gi 578818931 1274 VLDNGKIIE 1282
Cdd:PRK10522 521 EMRNGQLSE 529
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1096-1293 |
4.11e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.56 E-value: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1096 EKIGVVGRTGAGKSSLTNCLFRILEAAGGQI-------------IID-------------GVDIASIglhdLREKLTIIp 1149
Cdd:PRK10261 43 ETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIElseqsaaqmrhvrGADMAMI----FQEPMTSL- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1150 qDPILFSG-----SLRMNldpfNNYSDEEiwkalELAHLKSFVASLQLGLSHEV-TEAGGNLSIGQRQLLCLGRALLRKS 1223
Cdd:PRK10261 118 -NPVFTVGeqiaeSIRLH----QGASREE-----AMVEAKRMLDQVRIPEAQTIlSRYPHQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578818931 1224 KILVLDEATAAVDLETDNLIQTTI---QNEFAhCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1293
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIkvlQKEMS-MGVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQIFHAP 260
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1084-1293 |
4.50e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 56.63 E-value: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLtnclFRI---LEA-AGGQIIIDGVDIAsiGLHDLREKLTIIPQDPILFSgsl 1159
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTL----LRIiagLEHqTSGHIRFHGTDVS--RLHARDRKVGFVFQHYALFR--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1160 RMNLdpFNNysdeeIWKALEL---------AHLKSFVASL--QLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVL 1228
Cdd:PRK10851 88 HMTV--FDN-----IAFGLTVlprrerpnaAAIKAKVTQLleMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 1229 DEATAAVDLETDNLIQTTIQN---EFAHCTVItIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1293
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQlheELKFTSVF-VTHDQEEAMEvADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1068-1293 |
4.74e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 56.18 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELDLVLRGITcDIGSMEKIG----VVGRTGAGKSSLTNCLFRILEAAGGQIIIdGVDIASIG-----L 1138
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFERRALY-DVNVSIPSGsyvaIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGkknkkL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1139 HDLREKLTIIPQDP--ILFSGSLRMNL--DPFN-NYSDEEiwkALELAHlksfvASLQL-GLSHEV-TEAGGNLSIGQRQ 1211
Cdd:PRK13634 81 KPLRKKVGIVFQFPehQLFEETVEKDIcfGPMNfGVSEED---AKQKAR-----EMIELvGLPEELlARSPFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1212 LLCLGRALLRKSKILVLDEATAAVDLETdnliQTTIQNEFA--H----CTVITIAHRlhtiMD-----SDKVMVLDNGKI 1280
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKG----RKEMMEMFYklHkekgLTTVLVTHS----MEdaaryADQIVVMHKGTV 224
|
250
....*....|...
gi 578818931 1281 IECGSPEELLQIP 1293
Cdd:PRK13634 225 FLQGTPREIFADP 237
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
824-1040 |
5.30e-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: 55.95 E-value: 5.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 824 LHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDI----STVDDTLPQSLRSWITcflgIISTLV-MICMATP--VFTIIVI 896
Cdd:cd18550 74 LRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVggaqSVVTGTLTSVVSNVVT----LVATLVaMLALDWRlaLLSLVLL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 897 PLGII---YVSvQMFYVSTSRQLRRLDSVTrspiySHFSET--VSGLPVIRAF----EHQQRFLKHNEVRIDtnqkcvfs 967
Cdd:cd18550 150 PLFVLptrRVG-RRRRKLTREQQEKLAELN-----SIMQETlsVSGALLVKLFgredDEAARFARRSRELRD-------- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 968 witsnrwLAIRLELVG-----NLTVFFSALMMVIY--------RDTLS-GDTVGFVlsnAL--NITQTLNWLVRMTSEIE 1031
Cdd:cd18550 216 -------LGVRQALAGrwffaALGLFTAIGPALVYwvggllviGGGLTiGTLVAFT---ALlgRLYGPLTQLLNIQVDLM 285
|
....*....
gi 578818931 1032 TNIVAVERI 1040
Cdd:cd18550 286 TSLALFERI 294
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1084-1236 |
5.70e-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: 55.13 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIID----GVDIASIG---LHDLREK--------LTII 1148
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASpreILALRRRtigyvsqfLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1149 PQDPilfsgslrmnldpfnnysdeeiwkALELahlksfVAS--LQLGLSHEVTEAGG-------NL------------SI 1207
Cdd:COG4778 106 PRVS------------------------ALDV------VAEplLERGVDREEARARArellarlNLperlwdlppatfSG 155
|
170 180
....*....|....*....|....*....
gi 578818931 1208 GQRQLLCLGRALLRKSKILVLDEATAAVD 1236
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLD 184
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1100-1309 |
6.30e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 55.78 E-value: 6.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1100 VVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDI-ASIG----LHDLREKLTIIPQDP--ILFSGSLRMNL--DPFNNYS 1170
Cdd:PRK13645 42 VIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKkikeVKRLRKEIGLVFQFPeyQLFQETIEKDIafGPVNLGE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1171 D-EEIWKAL-ELAHLKSfvaslqlgLSHE-VTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDL--ETD--NLI 1243
Cdd:PRK13645 122 NkQEAYKKVpELLKLVQ--------LPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPkgEEDfiNLF 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1244 QTTIQNEFAHctVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEEL---------LQIPGP----FYFMAKEAGIENVN 1309
Cdd:PRK13645 194 ERLNKEYKKR--IIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEIfsnqelltkIEIDPPklyqLMYKLKNKGIDLLN 271
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1099-1289 |
6.48e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.95 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1099 GVVGRTGAGKSSLTNCLFRILEAAGGQIIIDG--VDIAS--------IGL-------------HDLREKLTIipqdPILF 1155
Cdd:COG1129 282 GIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSprdairagIAYvpedrkgeglvldLSIRENITL----ASLD 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1156 SGSLRMNLDPfnnysdeeiwkALELAHLKSFVASLQL---GLSHEVteagGNLSIGQRQLLCLGRALLRKSKILVLDEAT 1232
Cdd:COG1129 358 RLSRGGLLDR-----------RRERALAEEYIKRLRIktpSPEQPV----GNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1233 AAVDLETDNLIQTTIqNEFAH--CTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEEL 1289
Cdd:COG1129 423 RGIDVGAKAEIYRLI-RELAAegKAVIVISSELPELLGlSDRILVMREGRIVGELDREEA 481
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
411-657 |
7.21e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.51 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 411 SFTWEHDSEA-TVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTtAYVPQQSW---------IQN 480
Cdd:PRK13650 11 TFKYKEDQEKyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-LLTEENVWdirhkigmvFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 481 -------GTIKDNILFGTEFNEKRYQQ----VLEAcallpdLEMLPGGDLAEigEKGINLSGGQKQRISLARATYQNLDI 549
Cdd:PRK13650 90 pdnqfvgATVEDDVAFGLENKGIPHEEmkerVNEA------LELVGMQDFKE--REPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 550 YLLDDPLSAVDahvgkhifnkvlgPNGLLK------------GKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALL 617
Cdd:PRK13650 162 IILDEATSMLD-------------PEGRLEliktikgirddyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELF 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 578818931 618 AKKGE---------FAKNLKTFLRHTGPEEEATVHDGSEEEDDDYGLIS 657
Cdd:PRK13650 229 SRGNDllqlgldipFTTSLVQSLRQNGYDLPEGYLTEKELEEQLWELIS 277
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1093-1313 |
7.88e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.88 E-value: 7.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1093 GSMekIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIA--SIGLHDLreklTIIPQDPILFSG---------SLRM 1161
Cdd:PRK11432 32 GTM--VTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVThrSIQQRDI----CMVFQSYALFPHmslgenvgyGLKM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1162 NldpfnNYSDEEIWK----ALELAHLKSFVASLqlglsheVTEAGGnlsiGQRQLLCLGRALLRKSKILVLDEATAAVDL 1237
Cdd:PRK11432 106 L-----GVPKEERKQrvkeALELVDLAGFEDRY-------VDQISG----GQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1238 ETDNLIQTTI---QNEFAhctvITIAHRLHTIMD----SDKVMVLDNGKIIECGSPEELLQIPGPFyFMAKEAGIENVNS 1310
Cdd:PRK11432 170 NLRRSMREKIrelQQQFN----ITSLYVTHDQSEafavSDTVIVMNKGKIMQIGSPQELYRQPASR-FMASFMGDANIFP 244
|
...
gi 578818931 1311 TKF 1313
Cdd:PRK11432 245 ATL 247
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1070-1289 |
8.99e-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: 8.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1070 FNNYQVRYRPeldlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGvdiasiglhdlreKLTIIP 1149
Cdd:cd03291 42 FSNLCLVGAP----VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1150 QDPILFSGSLRMNLdPFNNYSDEEIWKALELA-HLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVL 1228
Cdd:cd03291 105 QFSWIMPGTIKENI-IFGVSYDEYRYKSVVKAcQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578818931 1229 DEATAAVDLETDNLI-QTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEEL 1289
Cdd:cd03291 184 DSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
424-560 |
1.03e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 55.65 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 424 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-----------------AYVPQQSWI-QNGTIKD 485
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgiclppekrriGYVFQDARLfPHYKVRG 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 486 NILFG-TEFNEKRYQQVLEACALLPDLEMLPggdlaeigekgINLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 560
Cdd:PRK11144 96 NLRYGmAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1081-1288 |
1.22e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 55.27 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1081 LDLVLRGITcdigsmekiGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDG---VDIAS-IGLHDLREKLTIIPQDPILF- 1155
Cdd:PRK11144 19 LTLPAQGIT---------AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgICLPPEKRRIGYVFQDARLFp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1156 ----SGSLRMNLDPFNNysdeeiwkalelAHLKSFVAslQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEA 1231
Cdd:PRK11144 90 hykvRGNLRYGMAKSMV------------AQFDKIVA--LLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578818931 1232 TAAVDL----ETDNLIQTTIQNefAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEE 1288
Cdd:PRK11144 156 LASLDLprkrELLPYLERLARE--INIPILYVSHSLDEILRlADRVVVLEQGKVKAFGPLEE 215
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
429-558 |
1.59e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 429 IMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQqsWI---QNGTIKDNILF-GTEFNEKRYQQvlea 504
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQ--YIkpdYDGTVEDLLRSiTDDLGSSYYKS---- 435
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 505 callpdlEMLPGGDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPlSA 558
Cdd:PRK13409 436 -------EIIKPLQLERLLDKNVKdLSGGELQRVAIAACLSRDADLYLLDEP-SA 482
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1067-1289 |
1.67e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 54.40 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1067 KIQFNNYQVRYR---PELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIG----LH 1139
Cdd:PRK13646 2 TIRFDNVSYTYQkgtPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1140 DLREKLTIIPQDP------------ILFS-GSLRMNLDPFNNYsdeeiwkalelahlkSFVASLQLGLSHEVTEAGG-NL 1205
Cdd:PRK13646 82 PVRKRIGMVFQFPesqlfedtvereIIFGpKNFKMNLDEVKNY---------------AHRLLMDLGFSRDVMSQSPfQM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1206 SIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTI------QNEfahcTVITIAHRLHTIMD-SDKVMVLDNG 1278
Cdd:PRK13646 147 SGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLkslqtdENK----TIILVSHDMNEVARyADEVIVMKEG 222
|
250
....*....|.
gi 578818931 1279 KIIECGSPEEL 1289
Cdd:PRK13646 223 SIVSQTSPKEL 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
413-630 |
1.74e-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: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 413 TWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLG--EMENVHG----HITIKGTTAYVPQQS---------- 476
Cdd:TIGR03269 7 TKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGriiyHVALCEKCGYVERPSkvgepcpvcg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 477 ----------WIQNGTIKDN------ILFGTEF----NEKRYQQVLEAcalLPDLE------MLPGGDLAE-------IG 523
Cdd:TIGR03269 87 gtlepeevdfWNLSDKLRRRirkriaIMLQRTFalygDDTVLDNVLEA---LEEIGyegkeaVGRAVDLIEmvqlshrIT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 524 EKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLgpNGLLKGKTRLLVTHsmHFlPQV-----DE 598
Cdd:TIGR03269 164 HIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALE--EAVKASGISMVLTS--HW-PEViedlsDK 238
|
250 260 270
....*....|....*....|....*....|..
gi 578818931 599 IVVLGNGTIVEKGSYSALLAKKGEFAKNLKTF 630
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEVVAVFMEGVSEVEKE 270
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
423-562 |
1.88e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.88 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 423 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT------AYVPQQSWI--QNGtIKD------NIL 488
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPirrqrdEYHQDLLYLghQPG-IKTeltaleNLR 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578818931 489 F----GTEFNEKRYQQVLEACALLpDLEMLPGGdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAH 562
Cdd:PRK13538 97 FyqrlHGPGDDEALWEALAQVGLA-GFEDVPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1084-1291 |
1.90e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 53.49 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHdLREKLTI--IPQDPILFSG-SLR 1160
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMH-KRARLGIgyLPQEASIFRKlTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1161 MNldpfnnysdeeIWKALELAHL-----KSFVASL--QLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATA 1233
Cdd:COG1137 97 DN-----------ILAVLELRKLskkerEERLEELleEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 1234 AVD----LEtdnliqttIQNEFAHCT------VITiAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQ 1291
Cdd:COG1137 166 GVDpiavAD--------IQKIIRHLKergigvLIT-DHNVRETLGiCDRAYIISEGKVLAEGTPEEILN 225
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
411-612 |
2.20e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.84 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 411 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG--TTAYVPQQS------WIQNGT 482
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehIQHYASKEVarriglLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 483 IKDNILFGTEFNEKRY-QQVLEACALLPDLEMLPGG----DLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPL 556
Cdd:PRK10253 92 TPGDITVQELVARGRYpHQPLFTRWRKEDEEAVTKAmqatGITHLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578818931 557 SAVDahVGKHI-FNKVLGPNGLLKGKTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGS 612
Cdd:PRK10253 172 TWLD--ISHQIdLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGA 227
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
792-1010 |
2.20e-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: 54.08 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 792 VGVYGALGLAQGIFVFIAHFwSAFGFVHAsniLHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWI 871
Cdd:cd18778 47 LGAYLLRALLNFLRIYLNHV-AEQKVVAD---LRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 872 TCFLGIISTLVMICMATPVFTIIV-IPLGIIYVSVqMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQ-- 948
Cdd:cd18778 123 TNVLTLVGVAIILFSINPKLALLTlIPIPFLALGA-WLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEee 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578818931 949 --RFLKHNEVRIDTNQKCVFSWitsnrwlairlELVGNLTVFFSALMMVI---------YRDTLS-GDTVGFVL 1010
Cdd:cd18778 202 akRFEALSRRYRKAQLRAMKLW-----------AIFHPLMEFLTSLGTVLvlgfggrlvLAGELTiGDLVAFLL 264
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
775-997 |
2.39e-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: 54.02 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 775 SKIFNS-TDYPASQRD---------MRVGVYGALGLAQGIFVFIAHF-WSAFGFVHASNIlHKQLLNNILRAPMRFFDTT 843
Cdd:cd18577 23 GDLFDAfTDFGSGESSpdeflddvnKYALYFVYLGIGSFVLSYIQTAcWTITGERQARRI-RKRYLKALLRQDIAWFDKN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 844 PTGRIVNRFAGDISTVDD-------TLPQSLRSWITCFlgIIS-------TLVMICMaTPVftiIVIPLGIiyvsvqMFY 909
Cdd:cd18577 102 GAGELTSRLTSDTNLIQDgigeklgLLIQSLSTFIAGF--IIAfiyswklTLVLLAT-LPL---IAIVGGI------MGK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 910 VSTSRQLRRLDSVTRSpiYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKcvfswitsnrwLAIRLELVgnLTVFF 989
Cdd:cd18577 170 LLSKYTKKEQEAYAKA--GSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARK-----------AGIKKGLV--SGLGL 234
|
....*...
gi 578818931 990 SALMMVIY 997
Cdd:cd18577 235 GLLFFIIF 242
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
425-612 |
2.54e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.06 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 425 VNLDIMAGQLVAVIGPVGSGKSSLISAML-------GEMEnVHGHITIKGTTA-------Y-VPQQSWI-QNGTIKDNIL 488
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAgivppdsGTLE-IGGNPCARLTPAkahqlgiYlVPQEPLLfPNLSVKENIL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 489 FG---TEFNEKRYQQVLEA--CALlpDLEMLPGgdLAEIGEkginlsggqKQRISLARATYQNLDIYLLDDPLSAVDAHV 563
Cdd:PRK15439 109 FGlpkRQASMQKMKQLLAAlgCQL--DLDSSAG--SLEVAD---------RQIVEILRGLMRDSRILILDEPTASLTPAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 578818931 564 GKHIFNKVlgpNGLL-KGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 612
Cdd:PRK15439 176 TERLFSRI---RELLaQGVGIVFISHKLPEIRQLaDRISVMRDGTIALSGK 223
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1083-1293 |
2.88e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 53.25 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1083 LVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILE-----AAGGQIIIDGVDI--ASIGLHDLREKLTIIPQDPILF 1155
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1156 SGSLRMNLD---PFNNYS---DEEIWKALELAHLKSFVASlqlglshEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLD 1229
Cdd:PRK14243 104 PKSIYDNIAygaRINGYKgdmDELVERSLRQAALWDEVKD-------KLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578818931 1230 EATAAVD----LETDNLIQTTIQNEfahcTVITIAHRLHTIMD-SDKVMVLD---------NGKIIECGSPEELLQIP 1293
Cdd:PRK14243 177 EPCSALDpistLRIEELMHELKEQY----TIIIVTHNMQQAARvSDMTAFFNveltegggrYGYLVEFDRTEKIFNSP 250
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
792-963 |
3.06e-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: 53.57 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 792 VGVYGALGLAQGIFVFiahFWSAFGFVHASNI---LHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLR 868
Cdd:cd18541 43 ALLILLLALLIGIFRF---LWRYLIFGASRRIeydLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGIL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 869 SWI-TCFLGIISTLVMICMaTPVFTII------VIPLGIIYVSVQMFYVSTSRQ--LRRLDSVTRspiyshfsETVSGLP 939
Cdd:cd18541 120 YLVdALFLGVLVLVMMFTI-SPKLTLIallplpLLALLVYRLGKKIHKRFRKVQeaFSDLSDRVQ--------ESFSGIR 190
|
170 180
....*....|....*....|....*...
gi 578818931 940 VIRAF----EHQQRFLKHNEVRIDTNQK 963
Cdd:cd18541 191 VIKAFvqeeAEIERFDKLNEEYVEKNLR 218
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
423-560 |
3.58e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.75 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 423 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--------------TAYVPQqswiqnG------- 481
Cdd:NF033858 18 DDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGdmadarhrravcprIAYMPQ------Glgknlyp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 482 --TIKDNI-----LFG---TEfNEKRYQQVLEACALLPDLEMlPGGdlaeigekgiNLSGGQKQRISLARATYQNLDIYL 551
Cdd:NF033858 92 tlSVFENLdffgrLFGqdaAE-RRRRIDELLRATGLAPFADR-PAG----------KLSGGMKQKLGLCCALIHDPDLLI 159
|
....*....
gi 578818931 552 LDDPLSAVD 560
Cdd:NF033858 160 LDEPTTGVD 168
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1089-1290 |
3.88e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 52.63 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1089 TCDIGsmEKIGVVGRTGAGKSSLTNCLFRILEAAGgQIIIDGVDIASIGLHDL-REKLTIIPQDPILFSgslrMnldpfn 1167
Cdd:PRK03695 18 EVRAG--EILHLVGPNGAGKSTLLARMAGLLPGSG-SIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFA----M------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1168 nysdeEIWKALEL-----------AHLKSFVASLqLGLSHEVTEAGGNLSIGQRQLLCLGRALLR-------KSKILVLD 1229
Cdd:PRK03695 85 -----PVFQYLTLhqpdktrteavASALNEVAEA-LGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578818931 1230 EATAAVDLETDNLIQTTIqNEFAHC--TVITIAHRL-HTIMDSDKVMVLDNGKIIECGSPEELL 1290
Cdd:PRK03695 159 EPMNSLDVAQQAALDRLL-SELCQQgiAVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
777-944 |
3.91e-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: 53.58 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 777 IFNSTDYPASQRDMRVGVygALGLAQGIFVFI---AHFWSAFgFVH--ASNILH---KQLLNNILRAPMRFFDTTPTGRI 848
Cdd:cd18554 29 VIQGSSLTLDEKVYKLFT--IIGIMFFIFLILrppVEYYRQY-FAQwiANKILYdirKDLFDHLQKLSLRYYANNRSGEI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 849 VNRFAGDISTVDDTLPQSL-RSWITCFLGIISTLVMiCMATPVFTIIVIPLGIIYVSVQMFYVSTSRQLRRLDSVTRSPI 927
Cdd:cd18554 106 ISRVINDVEQTKDFITTGLmNIWLDMITIIIAICIM-LVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEV 184
|
170
....*....|....*..
gi 578818931 928 YSHFSETVSGLPVIRAF 944
Cdd:cd18554 185 QGFLHERIQGMSVIKSF 201
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1100-1290 |
4.51e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.68 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1100 VVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNLDPFNNYSDEEI---W- 1175
Cdd:PRK10253 38 IIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQELVARGRYPHQPLftrWr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1176 KALELAHLKSFVASlqlGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDL--ETDNLIQTTIQNEFAH 1253
Cdd:PRK10253 118 KEDEEAVTKAMQAT---GITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIshQIDLLELLSELNREKG 194
|
170 180 190
....*....|....*....|....*....|....*...
gi 578818931 1254 CTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELL 1290
Cdd:PRK10253 195 YTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIV 232
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
413-561 |
5.29e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 53.31 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 413 TWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISaMLGEMENV-HGHITIKGTT-----------AYV-------P 473
Cdd:PRK11650 12 SYDGKTQV-IKGIDLDVADGEFIVLVGPSGCGKSTLLR-MVAGLERItSGEIWIGGRVvnelepadrdiAMVfqnyalyP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 474 QQSWIQN--------GTIKDNIlfgtefnEKRyqqVLEACALLpdlemlpggdlaEIGE----KGINLSGGQKQRISLAR 541
Cdd:PRK11650 90 HMSVRENmayglkirGMPKAEI-------EER---VAEAARIL------------ELEPlldrKPRELSGGQRQRVAMGR 147
|
170 180
....*....|....*....|
gi 578818931 542 ATYQNLDIYLLDDPLSAVDA 561
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDA 167
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
419-619 |
5.49e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 53.04 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 419 EATVR---DVNLDIMAGQLVAVIGPVGSGKSSLiSAMLGEMEN-VHGHITIKGTTAYVPQQSWIQNGTIKDNILFGTEFN 494
Cdd:PRK11308 25 ERLVKaldGVSFTLERGKTLAVVGESGCGKSTL-ARLLTMIETpTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNPYG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 495 ----EKRYQQVLEAcALLPD------------LEMLpggdlAEIGEKGIN-------LSGGQKQRISLARATYQNLDIYL 551
Cdd:PRK11308 104 slnpRKKVGQILEE-PLLINtslsaaerrekaLAMM-----AKVGLRPEHydryphmFSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 552 LDDPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLAK 619
Cdd:PRK11308 178 ADEPVSALDVSVQAQVLN-------LMMdlqqelGLSYVFISHDLSVVEHIaDEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1085-1281 |
5.58e-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: 53.68 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1085 LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAG--GQIIIDGVDIASIGLHDLREK-LTIIPQDPILFSgslrm 1161
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVP----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1162 NLDPFNNysdeeIWKALELAH-------------LKSFVASLQLGLSHeVTEAGGNLSIGQRQLLCLGRALLRKSKILVL 1228
Cdd:TIGR02633 92 ELSVAEN-----IFLGNEITLpggrmaynamylrAKNLLRELQLDADN-VTRPVGDYGGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 1229 DEATAAVDLETDNLIQTTIQNEFAH-CTVITIAHRLHTIMD-SDKVMVLDNGKII 1281
Cdd:TIGR02633 166 DEPSSSLTEKETEILLDIIRDLKAHgVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
425-560 |
5.80e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 52.15 E-value: 5.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 425 VNLDIMAGQLVAVIGPVGSGKSSLISAMLGeMENVHGHITIKGTT-------------AYVPQQS----------WIQng 481
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPlsdwsaaelarhrAYLSQQQsppfampvfqYLA-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 482 tikdniLFG-----TEFNEKRYQQVLEACALLPDLemlpggdlaeigEKGIN-LSGGQKQRISLARATYQ-----NLD-- 548
Cdd:COG4138 92 ------LHQpagasSEAVEQLLAQLAEALGLEDKL------------SRPLTqLSGGEWQRVRLAAVLLQvwptiNPEgq 153
|
170
....*....|..
gi 578818931 549 IYLLDDPLSAVD 560
Cdd:COG4138 154 LLLLDEPMNSLD 165
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
792-957 |
5.82e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 52.93 E-value: 5.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 792 VGVYGALGLAQGIFVFIAHFWSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWI 871
Cdd:cd18572 39 VLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 872 TCFLGIISTLVMICMATPVFT----IIVIPLGIIYVSVQMFYVSTSRQLRrlDSVTRSpiYSHFSETVSGLPVIRAF--- 944
Cdd:cd18572 119 RNLVQLVGGLAFMFSLSWRLTllafITVPVIALITKVYGRYYRKLSKEIQ--DALAEA--NQVAEEALSNIRTVRSFate 194
|
170 180
....*....|....*....|.
gi 578818931 945 --------EHQQRFLKHNEVR 957
Cdd:cd18572 195 erearryeRALDKALKLSVRQ 215
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1084-1254 |
6.36e-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: 6.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNL 1163
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1164 D---PFNnySDEEIWKALELAHLKsfvaslqlGLSHEvteAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETD 1240
Cdd:cd03231 95 RfwhADH--SDEQVEEALARVGLN--------GFEDR---PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170
....*....|....
gi 578818931 1241 NLIQTTIQnefAHC 1254
Cdd:cd03231 162 ARFAEAMA---GHC 172
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1086-1293 |
6.42e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 53.11 E-value: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1086 RGITCDIGSMEKIGVVGRTGAGKSSLTNClfrileaaggqiiidgvdIAsiGLHDlrekltIIPQDpiLFSGSLRMNLDP 1165
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRM------------------IA--GLED------ITSGD--LFIGEKRMNDVP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1166 ---------FNNYSdeeIWKALELAHLKSF------------------VAS-LQLGlsHEVTEAGGNLSIGQRQLLCLGR 1217
Cdd:PRK11000 72 paergvgmvFQSYA---LYPHLSVAENMSFglklagakkeeinqrvnqVAEvLQLA--HLLDRKPKALSGGQRQRVAIGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 1218 ALLRKSKILVLDEATAAVD--LETDNLIQTTIQNEFAHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELLQIP 1293
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLDaaLRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTlADKIVVLDAGRVAQVGKPLELYHYP 225
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
413-596 |
6.70e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.77 E-value: 6.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 413 TWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWI-----------QNG 481
Cdd:PRK13543 18 AFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFmaylghlpglkADL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 482 TIKDNILFGTEFNEKRYQQvleacallpdlemLPGGDLAEIGEKGI------NLSGGQKQRISLARATYQNLDIYLLDDP 555
Cdd:PRK13543 98 STLENLHFLCGLHGRRAKQ-------------MPGSALAIVGLAGYedtlvrQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 578818931 556 LSAVDAHvGKHIFNKVLGPNgLLKGKTRLLVTHSMHFLPQV 596
Cdd:PRK13543 165 YANLDLE-GITLVNRMISAH-LRGGGAALVTTHGAYAAPPV 203
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
422-612 |
7.06e-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: 52.23 E-value: 7.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAML---------GEMENVHGHITIKGTTAY----VPQQSWIQNGT------ 482
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLypalarrlhLKKEQPGNHDRIEGLEHIdkviVIDQSPIGRTPrsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 483 ---IKDNI--LF-----GTEFN----EKRYQ-----QVL-----EACALLPD-------LEMLP--GGDLAEIGEKGINL 529
Cdd:cd03271 91 ytgVFDEIreLFcevckGKRYNretlEVRYKgksiaDVLdmtveEALEFFENipkiarkLQTLCdvGLGYIKLGQPATTL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 530 SGGQKQRISLA-----RATYQNLdiYLLDDPLSAVDAHVGKHIFNkVLgpNGLL-KGKTRLLVTHSMHFLPQVDEIVVLG 603
Cdd:cd03271 171 SGGEAQRIKLAkelskRSTGKTL--YILDEPTTGLHFHDVKKLLE-VL--QRLVdKGNTVVVIEHNLDVIKCADWIIDLG 245
|
250
....*....|....*
gi 578818931 604 ------NGTIVEKGS 612
Cdd:cd03271 246 peggdgGGQVVASGT 260
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
747-953 |
8.15e-07 |
|
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: 52.51 E-value: 8.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 747 IFFIILAFVMNSVAFIGSnlWLSAWTSDSKIFnstdyPASQRDMRVGVYGALG--LAQGIFVFIAHFWSAfgfvHASNIL 824
Cdd:cd18555 5 ISILLLSLLLQLLTLLIP--ILTQYVIDNVIV-----PGNLNLLNVLGIGILIlfLLYGLFSFLRGYIII----KLQTKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 825 HKQLLNN----ILRAPMRFFDTTPTGRIVNRfAGDISTVDDTLP-QSLRSWITCFLGIISTLVMICMaTPVFTIIVIPLG 899
Cdd:cd18555 74 DKSLMSDffehLLKLPYSFFENRSSGDLLFR-ANSNVYIRQILSnQVISLIIDLLLLVIYLIYMLYY-SPLLTLIVLLLG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 578818931 900 IIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKH 953
Cdd:cd18555 152 LLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKK 205
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
790-1010 |
9.94e-07 |
|
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: 52.11 E-value: 9.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 790 MRVGVYGALGLAQGIFVF--IAHFWSAFGFVHASNILHKQLLNNI--------LRAPMRFFDTTPTGRIVNRFAGDISTV 859
Cdd:cd18546 30 VRAGDLGVLLLAAAAYLAvvLAGWVAQRAQTRLTGRTGERLLYDLrlrvfahlQRLSLDFHERETSGRIMTRMTSDIDAL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 860 DDTLPQSLRSWITCFLGIISTLVMIC-----MATPVFTIIVIplgIIYVSVQmFYVSTSRQLRRldsvTR---SPIYSHF 931
Cdd:cd18546 110 SELLQTGLVQLVVSLLTLVGIAVVLLvldprLALVALAALPP---LALATRW-FRRRSSRAYRR----AReriAAVNADL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 932 SETVSGLPVIRAF----EHQQRFLKHNEVRIDTNqkcvfswITSNRWLAIR---LELVGNLT----VFFSALMMViyRDT 1000
Cdd:cd18546 182 QETLAGIRVVQAFrrerRNAERFAELSDDYRDAR-------LRAQRLVAIYfpgVELLGNLAtaavLLVGAWRVA--AGT 252
|
250
....*....|.
gi 578818931 1001 LS-GDTVGFVL 1010
Cdd:cd18546 253 LTvGVLVAFLL 263
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
431-617 |
1.04e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 51.71 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 431 AGQLVAVIGPVGSGKSSLISaMLGEMEN-VHGHITIKGTT-------------AYVPQQSWIQNG-TIKDNILFGT---- 491
Cdd:PRK10575 36 AGKVTGLIGHNGSGKSTLLK-MLGRHQPpSEGEILLDAQPleswsskafarkvAYLPQQLPAAEGmTVRELVAIGRypwh 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 492 ----EFNEKRYQQVLEACALLpdlemlpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVD-AHVgk 565
Cdd:PRK10575 115 galgRFGAADREKVEEAISLV---------GLKPLAHRLVDsLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiAHQ-- 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 566 hifNKVLGPNGLL---KGKTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGSYSALL 617
Cdd:PRK10575 184 ---VDVLALVHRLsqeRGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELM 236
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1205-1289 |
1.06e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 52.16 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1205 LSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHC-TVITIAHRLHTIMD-SDKVMVLDNGKIIE 1282
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNkTVFVITHTMEHVLEvADEVIVMDKGKILK 256
|
....*..
gi 578818931 1283 CGSPEEL 1289
Cdd:PRK13631 257 TGTPYEI 263
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
422-616 |
1.20e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.94 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------TTAYVPQQSWIQ------------NGT 482
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqridtlsPGKLQALRRDIQfifqdpyasldpRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 483 IKDNI--------LFGTEFNEKRYQQVLEACALLPDLEM-LPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLD 553
Cdd:PRK10261 420 VGDSImeplrvhgLLPGKAAAARVAWLLERVGLLPEHAWrYPH-----------EFSGGQRQRICIARALALNPKVIIAD 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578818931 554 DPLSAVDAHVGKHIFNKVLGPNGLLkGKTRLLVTHSMHFLPQVD-EIVVLGNGTIVEKGSYSAL 616
Cdd:PRK10261 489 EAVSALDVSIRGQIINLLLDLQRDF-GIAYLFISHDMAVVERIShRVAVMYLGQIVEIGPRRAV 551
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
424-612 |
1.38e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 51.77 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 424 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIK----------GTTAYVPQQSWIQN------------- 480
Cdd:PRK13631 44 NISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkknnHELITNPYSKKIKNfkelrrrvsmvfq 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 481 --------GTIKDNILFG-------TEFNEKRYQQVLEACALLPD-LEMLPGGdlaeigekginLSGGQKQRISLARATY 544
Cdd:PRK13631 124 fpeyqlfkDTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSyLERSPFG-----------LSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 545 QNLDIYLLDDPLSAVDAHVGKHIFNKVLGPNGllKGKTRLLVTHSM-HFLPQVDEIVVLGNGTIVEKGS 612
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKA--NNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGT 259
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1068-1290 |
1.40e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 51.27 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYRPELDlVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTI 1147
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1148 IPQDP--ILFS---------GSLRMNLDPfnNYSDEEIWKALELAHLKSFvaslqlglsheVTEAGGNLSIGQRQLLCLG 1216
Cdd:PRK13647 84 VFQDPddQVFSstvwddvafGPVNMGLDK--DEVERRVEEALKAVRMWDF-----------RDKPPYHLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578818931 1217 RALLRKSKILVLDEATAAVDLETDNLIqTTIQNEF--AHCTVITIAHRLHTIMD-SDKVMVLDNGKIIECGSPEELL 1290
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETL-MEILDRLhnQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLT 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1085-1291 |
1.72e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 51.28 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1085 LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIG----LHDLREKLTIIPQDP--ILFSGS 1158
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQIRKKVGLVFQFPesQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1159 LRMNL--DPFN-NYSDEEiwkALELAHLKsfvasLQL-GLSHEVTEAGG-NLSIGQRQLLCLGRALLRKSKILVLDEATA 1233
Cdd:PRK13649 103 VLKDVafGPQNfGVSQEE---AEALAREK-----LALvGISESLFEKNPfELSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578818931 1234 AVDLETDNLIQTTIQNefAHCTVITIAHRLHtIMD-----SDKVMVLDNGKIIECGSPEELLQ 1291
Cdd:PRK13649 175 GLDPKGRKELMTLFKK--LHQSGMTIVLVTH-LMDdvanyADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
822-948 |
2.01e-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: 51.16 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 822 NI-LHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQS----LRSWITCFlGIISTLVMICMATPVFTIIVI 896
Cdd:cd18784 68 NIrIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNlnifLRSLVKAI-GVIVFMFKLSWQLSLVTLIGL 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 578818931 897 PLGIIYVSVQ-MFYVSTSRQLRrlDSVTRSPiySHFSETVSGLPVIRAFEHQQ 948
Cdd:cd18784 147 PLIAIVSKVYgDYYKKLSKAVQ--DSLAKAN--EVAEETISSIRTVRSFANED 195
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1084-1308 |
2.24e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 51.49 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDlREKLTIIpQDPILF-------- 1155
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN-RHVNTVF-QSYALFphmtvfen 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1156 -SGSLRMNLDPFnnysdEEIWK----ALELAHLKSFVaslqlglSHEVTeaggNLSIGQRQLLCLGRALLRKSKILVLDE 1230
Cdd:PRK09452 107 vAFGLRMQKTPA-----AEITPrvmeALRMVQLEEFA-------QRKPH----QLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1231 ATAAVDLEtdnlIQTTIQNEFAH------CTVITIAH-RLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFyFMAKEA 1303
Cdd:PRK09452 171 SLSALDYK----LRKQMQNELKAlqrklgITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNL-FVARFI 245
|
....*
gi 578818931 1304 GIENV 1308
Cdd:PRK09452 246 GEINI 250
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
93-380 |
2.37e-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: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 93 SFLLKLVNDIFTFVSPQLLKLLISF---ASDRDTYLWIGYL---CAILLFTAALIQSFClqcyfqlCFKLGVKVRTAIMA 166
Cdd:cd18548 4 APLFKLLEVLLELLLPTLMADIIDEgiaNGDLSYILRTGLLmllLALLGLIAGILAGYF-------AAKASQGFGRDLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 167 SVYKKALTLSNLARKEYTVGETVNLMSVDAQKLMDVTN-FMHMLWSSVLQIVLSIFFLWR---ELGPSVLAGVGVMVLVI 242
Cdd:cd18548 77 DLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMmLLRMLVRAPIMLIGAIIMAFRinpKLALILLVAIPILALVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 243 pinAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEP----SFRDQVQNLRKKELKNLLAFSQLQCVVIFVF 318
Cdd:cd18548 157 ---FLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDyeeeRFDKANDDLTDTSLKAGRLMALLNPLMMLIM 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578818931 319 QLTpvLVSVVTFSVYvLVDSNNILDAQ-KAFTSItLFNILrFPLSMLPMMISSMLQASVSTER 380
Cdd:cd18548 234 NLA--IVAILWFGGH-LINAGSLQVGDlVAFINY-LMQIL-MSLMMLSMVFVMLPRASASAKR 291
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
417-622 |
2.91e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.17 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 417 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLG--EMENVHGHITIKGT--TAYVPQQSwiqngtIKDNILFGTE 492
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKdlLELSPEDR------AGEGIFMAFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 493 F--------NEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINL----------------SGGQKQRISLARATYQNLD 548
Cdd:PRK09580 86 YpveipgvsNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALlkmpedlltrsvnvgfSGGEKKRNDILQMAVLEPE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578818931 549 IYLLDDPLSAVDAHVGKHIFNkvlGPNGLLKGK-TRLLVTHSMHFLPQV--DEIVVLGNGTIVEKGSYSalLAKKGE 622
Cdd:PRK09580 166 LCILDESDSGLDIDALKIVAD---GVNSLRDGKrSFIIVTHYQRILDYIkpDYVHVLYQGRIVKSGDFT--LVKQLE 237
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
428-621 |
3.10e-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: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 428 DIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-AYVPQQswiqngtikdnilfgtefnekryqqvleaca 506
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITpVYKPQY------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 507 llpdlemlpggdlaeigekgINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA----HVGKHIfnKVLGPNGllkGKT 582
Cdd:cd03222 70 --------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAARAI--RRLSEEG---KKT 124
|
170 180 190
....*....|....*....|....*....|....*....
gi 578818931 583 RLLVTHSMHFLPQVDEIVVLGNGtivEKGSYSALLAKKG 621
Cdd:cd03222 125 ALVVEHDLAVLDYLSDRIHVFEG---EPGVYGIASQPKG 160
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1100-1281 |
3.55e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1100 VVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIA-SIGLHDLREKLTIIPQDpilfsgslrMNLDPFNNYSDEeIW--- 1175
Cdd:PRK10982 29 LMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQE---------LNLVLQRSVMDN-MWlgr 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1176 ---KALELAHLKSFVASL----QLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAV-DLETDNLIQTTI 1247
Cdd:PRK10982 99 yptKGMFVDQDKMYRDTKaifdELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtEKEVNHLFTIIR 178
|
170 180 190
....*....|....*....|....*....|....*
gi 578818931 1248 QNEFAHCTVITIAHRLHTIMD-SDKVMVLDNGKII 1281
Cdd:PRK10982 179 KLKERGCGIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
93-381 |
3.63e-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: 50.12 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 93 SFLLKLVNDIFTFVSPQLLKLLI-SFASDRDT-YLWIgylCAILLFTAALIQSFC--LQCYF--QLCFKLGVKVRTAIma 166
Cdd:cd18542 4 AILALLLATALNLLIPLLIRRIIdSVIGGGLReLLWL---LALLILGVALLRGVFryLQGYLaeKASQKVAYDLRNDL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 167 svYKKaltLSNLARKEYTVGETVNLMS-----VDAqklmdVTNFMHM----LWSSVLQIVLSIFFL----WRelgpsvLA 233
Cdd:cd18542 79 --YDH---LQRLSFSFHDKARTGDLMSrctsdVDT-----IRRFLAFglveLVRAVLLFIGALIIMfsinWK------LT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 234 GVgvMVLVIPINAILSTK-SKTIQvKNMKNKDKRLKIMN----EILSGIKILKYFAWEPS----FRDQVQNLRKKELKNL 304
Cdd:cd18542 143 LI--SLAIIPFIALFSYVfFKKVR-PAFEEIREQEGELNtvlqENLTGVRVVKAFAREDYeiekFDKENEEYRDLNIKLA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 305 LAFSQLQCVVIFVFQLTPVLVSVV--------TFSVYVLVdsnnildaqkAFTSitLFNILRFPLSMLPMMISSMLQASV 376
Cdd:cd18542 220 KLLAKYWPLMDFLSGLQIVLVLWVggylvingEITLGELV----------AFIS--YLWMLIWPVRQLGRLINDMSRASA 287
|
....*
gi 578818931 377 STERL 381
Cdd:cd18542 288 SAERI 292
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
800-918 |
3.74e-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: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 800 LAQGIFVF--IAhFWSAFGFVHASNiLHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDI----STVDDTLPQSLRSwITC 873
Cdd:cd18574 53 LLQSLLTFayIS-LLSVVGERVAAR-LRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVqefkSSFKQCVSQGLRS-VTQ 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 578818931 874 FLGIISTLVMICMATPVFTIIVIPLGIIyvsVQMFYVSTSRQLRR 918
Cdd:cd18574 130 TVGCVVSLYLISPKLTLLLLVIVPVVVL---VGTLYGSFLRKLSR 171
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1091-1276 |
4.22e-06 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 49.71 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1091 DIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASiglhdlrEKLTIIPQDPILFSGSLRMNLDPF--NN 1168
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY-------KPQYIKADYEGTVRDLLSSITKDFytHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1169 YSDEEIWKALELAHLksfvaslqlgLSHEVTEaggnLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLEtDNLIQTTIQ 1248
Cdd:cd03237 94 YFKTEIAKPLQIEQI----------LDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE-QRLMASKVI 158
|
170 180 190
....*....|....*....|....*....|..
gi 578818931 1249 NEFA---HCTVITIAHRLHTI-MDSDKVMVLD 1276
Cdd:cd03237 159 RRFAennEKTAFVVEHDIIMIdYLADRLIVFE 190
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1084-1284 |
4.39e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 49.63 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLfRILE-AAGGQIIIDG--------VDIASIGLhdLREKLTIIPQD--- 1151
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVL-NLLEmPRSGTLNIAGnhfdfsktPSDKAIRE--LRRNVGMVFQQynl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1152 -PILfsgSLRMNL--DPFN--NYSDEE-IWKALELA---HLKSFVASLQLglshevteaggNLSIGQRQLLCLGRALLRK 1222
Cdd:PRK11124 94 wPHL---TVQQNLieAPCRvlGLSKDQaLARAEKLLerlRLKPYADRFPL-----------HLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578818931 1223 SKILVLDEATAAVDLETDNLIQTTIQnEFAHcTVIT---------IAHRLHTimdsdKVMVLDNGKIIECG 1284
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIR-ELAE-TGITqvivtheveVARKTAS-----RVVYMENGHIVEQG 223
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1083-1276 |
5.29e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 48.65 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1083 LVLRGITCDIGSMEKIGVVGRTGAGKSSLtnclFRIL----EAAGGQIIIDGVDIASIGlHDLREKLtiipqdpiLFSG- 1157
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSL----LRILaglaRPDAGEVLWQGEPIRRQR-DEYHQDL--------LYLGh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1158 ------------SLRMNLDPFNNYSDEEIWKALElahlksfvaslQLGLshevteAG------GNLSIGQRQLLCLGRAL 1219
Cdd:PRK13538 82 qpgikteltaleNLRFYQRLHGPGDDEALWEALA-----------QVGL------AGfedvpvRQLSAGQQRRVALARLW 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578818931 1220 LRKSKILVLDEATAAVDLETDNLIQTTIQnefAHC-----TVITIAHRLHtiMDSDKVMVLD 1276
Cdd:PRK13538 145 LTRAPLWILDEPFTAIDKQGVARLEALLA---QHAeqggmVILTTHQDLP--VASDKVRKLR 201
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
425-609 |
5.53e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 49.01 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 425 VNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAY------------------------VPQQSWIQN 480
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmdeearaklrakhvgfvfqsfmlIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 481 GTIKdNILFGTEFNEKRYQ--QVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSA 558
Cdd:PRK10584 109 VELP-ALLRGESSRQSRNGakALLEQLGLGKRLDHLPA-----------QLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 578818931 559 VDAHVGKHIFNKVLGPNGLLkGKTRLLVTHSMHFLPQVDEIVVLGNGTIVE 609
Cdd:PRK10584 177 LDRQTGDKIADLLFSLNREH-GTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
818-951 |
5.88e-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: 49.77 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 818 VHASNILHKQLLNNI----LRAPMRFFDTTPTGRIVNRFaGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTI 893
Cdd:cd18567 67 LYLSTSLNLQWTSNLfrhlLRLPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLAL 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 578818931 894 IVIPLGIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFL 951
Cdd:cd18567 146 IVLAAVALYALLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAERE 203
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1085-1289 |
5.98e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 49.24 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1085 LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRIL---EAAGGQIIIDGVDIASIG--LHDLRE---------------- 1143
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGrlARDIRKsrantgyifqqfnlvn 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1144 KLTIIPQDPILFSGSLRMNLDPFNNYSDEEIWKALElahlksfvASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKS 1223
Cdd:PRK09984 100 RLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQ--------ALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 1224 KILVLDEATAAVDLETDNLIQTTIQ--NEFAHCTVITIAHRL-HTIMDSDKVMVLDNGKIIECGSPEEL 1289
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVdYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
428-601 |
7.34e-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: 50.17 E-value: 7.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 428 DIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQ-SWIQNGTIKDNI--LFGTEFNEKRYQQvlea 504
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQYiSPDYDGTVEEFLrsANTDDFGSSYYKT---- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 505 callpdlEMLPGGDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA----HVGKHIFNKVLGpngllK 579
Cdd:COG1245 438 -------EIIKPLGLEKLLDKNVkDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAIRRFAEN-----R 505
|
170 180
....*....|....*....|...
gi 578818931 580 GKTRLLVTHSMHFLPQV-DEIVV 601
Cdd:COG1245 506 GKTAMVVDHDIYLIDYIsDRLMV 528
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
405-607 |
9.68e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 9.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 405 MQFSEASFTWEhDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHI--TIKGTTAyVPQQSWIQNGT 482
Cdd:PLN03073 509 ISFSDASFGYP-GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrSAKVRMA-VFSQHHVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 483 IKDNILFgteFNEKRYQQVLEAC--ALLPDLEMlpGGDLAEigEKGINLSGGQKQRISLARATYQNLDIYLLDDP----- 555
Cdd:PLN03073 587 LSSNPLL---YMMRCFPGVPEQKlrAHLGSFGV--TGNLAL--QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPsnhld 659
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578818931 556 LSAVDAhvgkHIFNKVLGPNGLlkgktrLLVTHSMHFLP-QVDEIVVLGNGTI 607
Cdd:PLN03073 660 LDAVEA----LIQGLVLFQGGV------LMVSHDEHLISgSVDELWVVSEGKV 702
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
411-612 |
1.11e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 48.65 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 411 SFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAYVPQQS- 476
Cdd:PRK13652 10 CYSYSGSKEA-LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkenirevrkFVGLVFQNPd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 477 -WIQNGTIKDNILFG-------TEFNEKRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLD 548
Cdd:PRK13652 89 dQIFSPTVEQDIAFGpinlgldEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578818931 549 IYLLDDPLSAVDAHVGKHIFNKVlgpNGLLK--GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 612
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFL---NDLPEtyGMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGT 221
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1084-1291 |
1.48e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 48.28 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAG--------GQIIIDGVDIASIGLHDLREKLTIIPQ--DPI 1153
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaaQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1154 L-FSGSLRMNLDPF--------NNYSDEEI-WKALELAHLKSFVAslqlglsHEVTE-AGGNLSIGQ--RQLLCL--GRA 1218
Cdd:PRK13547 96 FaFSAREIVLLGRYpharragaLTHRDGEIaWQALALAGATALVG-------RDVTTlSGGELARVQfaRVLAQLwpPHD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578818931 1219 LLRKSKILVLDEATAAVDLETDN-LIQT--TIQNEFaHCTVITIAHRLH-TIMDSDKVMVLDNGKIIECGSPEELLQ 1291
Cdd:PRK13547 169 AAQPPRYLLLDEPTAALDLAHQHrLLDTvrRLARDW-NLGVLAIVHDPNlAARHADRIAMLADGAIVAHGAPADVLT 244
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1099-1282 |
1.77e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.14 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1099 GVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDI------ASI--GLHDLREKLTIIPQDPI---LFSGSLrmnldP-- 1165
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasttAALaaGVAIIYQELHLVPEMTVaenLYLGQL-----Phk 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1166 --FNNYSDEEIWKALELAHLksfvaslqlGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDL-ETDNL 1242
Cdd:PRK11288 109 ggIVNRRLLNYEAREQLEHL---------GVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSArEIEQL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 578818931 1243 IQtTIQNEFAHCTVIT-IAHRLHTIMD-SDKVMVLDNGKIIE 1282
Cdd:PRK11288 180 FR-VIRELRAEGRVILyVSHRMEEIFAlCDAITVFKDGRYVA 220
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
376-625 |
1.77e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.17 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 376 VSTERLEKYLGGDDLDTSAirhdcnfdKAMqfSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGE 455
Cdd:PRK14271 1 MACERLGGQSGAADVDAAA--------PAM--AAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRM 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 456 MENVHGH-----ITIKGTTAY--------------VPQQSWIQNGTIKDNILFGtefnekryqqvLEACALLPDLEM--L 514
Cdd:PRK14271 71 NDKVSGYrysgdVLLGGRSIFnyrdvlefrrrvgmLFQRPNPFPMSIMDNVLAG-----------VRAHKLVPRKEFrgV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 515 PGGDLAEIG----------EKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRL 584
Cdd:PRK14271 140 AQARLTEVGlwdavkdrlsDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFI---RSLADRLTVI 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 578818931 585 LVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA--KKGEFAK 625
Cdd:PRK14271 217 IVTHNLAQAARIsDRAALFFDGRLVEEGPTEQLFSspKHAETAR 260
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
417-555 |
1.81e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.12 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 417 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHI--TIKGTTAYVPQQS------------WI-QNG 481
Cdd:PRK15064 330 DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwSENANIGYYAQDHaydfendltlfdWMsQWR 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 482 TIKDNilfgtefnekryQQVLEACallpdL-EMLPGGDlaEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDP 555
Cdd:PRK15064 410 QEGDD------------EQAVRGT-----LgRLLFSQD--DIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
824-1040 |
1.95e-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: 48.24 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 824 LHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQ--SLRSW-ITCFLGIISTLVMICMATPVFTIIVIPlgI 900
Cdd:cd18589 71 LQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSEnlSLLMWyLARGLFLFIFMLWLSPKLALLTALGLP--L 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 901 IYV---SVQMFYVSTSRQLRrlDSVTRSPIYShfSETVSGLPVIRAFEHQQRFLKHNEVRIDT----NQK-----CVFSW 968
Cdd:cd18589 149 LLLvpkFVGKFQQSLAVQVQ--KSLARANQVA--VETFSAMKTVRSFANEEGEAQRYRQRLQKtyrlNKKeaaayAVSMW 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578818931 969 ITSNRWLAIRlelVGnltVFFSALMMVIYRDTLSGDTVGFVLSNaLNITQTLNWLVRMTSEIETNIVAVERI 1040
Cdd:cd18589 225 TSSFSGLALK---VG---ILYYGGQLVTAGTVSSGDLVTFVLYE-LQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
530-618 |
2.11e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.93 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 530 SGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLKG---KTRL---LVTHSMHFLPQV-DEIVVL 602
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILA-------LLKSlqqKHQLaylFISHDLHVVRALcHQVIVL 499
|
90
....*....|....*.
gi 578818931 603 GNGTIVEKGSYSALLA 618
Cdd:PRK15134 500 RQGEVVEQGDCERVFA 515
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1068-1279 |
2.14e-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: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1068 IQFNNYQVRYrpELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDgvdiasiglhdlreklti 1147
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG------------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1148 ipqdpilfsgslrmnldpfnnysdeeiwKALELAHLKsfvaslqlglshevteaggNLSIGQRQLLCLGRALLRKSKILV 1227
Cdd:cd03221 61 ----------------------------STVKIGYFE-------------------QLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 578818931 1228 LDEATAAVDLETDNLIQTTIQNEfaHCTVITIAHRlHTIMDS--DKVMVLDNGK 1279
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEY--PGTVILVSHD-RYFLDQvaTKIIELEDGK 144
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
792-950 |
2.23e-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: 47.86 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 792 VGVYGALGLAQGIFVFIAHFWSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVddtlpqslRSWI 871
Cdd:cd18543 42 VLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLV--------QRFL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 872 TCFLGIISTLVMICMATPVFTIIVIPLGIIY-VSVQMFYVSTSRQLRRLDSVTRSP------IYSHFSETVSGLPVIRAF 944
Cdd:cd18543 114 AFGPFLLGNLLTLVVGLVVMLVLSPPLALVAlASLPPLVLVARRFRRRYFPASRRAqdqagdLATVVEESVTGIRVVKAF 193
|
170
....*....|
gi 578818931 945 ---EHQ-QRF 950
Cdd:cd18543 194 greRRElDRF 203
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
824-992 |
2.28e-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: 47.86 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 824 LHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDI----STVDDTLPQSLRSWITcFLGiisTLVMICMATPVFTIIV---I 896
Cdd:cd18575 71 LRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTtliqTVVGSSLSIALRNLLL-LIG---GLVMLFITSPKLTLLVllvI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 897 PLGIIYVsvqmfyVSTSRQLRRLDSVTRSPI---YSHFSETVSGLPVIRAFEHQ----QRFLKHNEVRIDTNQK------ 963
Cdd:cd18575 147 PLVVLPI------ILFGRRVRRLSRASQDRLadlSAFAEETLSAIKTVQAFTREdaerQRFATAVEAAFAAALRrirara 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 578818931 964 --------CVFSWITSNRWLAIRLELVGNLT-------VFFSAL 992
Cdd:cd18575 221 lltalvifLVFGAIVFVLWLGAHDVLAGRMSagelsqfVFYAVL 264
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1076-1291 |
3.30e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 48.12 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1076 RYRPELDLvLRGITCDIGSMEKIGVVGRTGAGKSSLTNCL-FRILEAA--GGQIIIDGVdiaSIGLHDLREKLTIIPQDP 1152
Cdd:TIGR00955 33 RERPRKHL-LKNVSGVAKPGELLAVMGSSGAGKTTLMNALaFRSPKGVkgSGSVLLNGM---PIDAKEMRAISAYVQQDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1153 IL-----------FSGSLRMnldPFNNYSDEEIWKALELAhlksfvasLQLGLS---HEVTEAGGN---LSIGQRQLLCL 1215
Cdd:TIGR00955 109 LFiptltvrehlmFQAHLRM---PRRVTKKEKRERVDEVL--------QALGLRkcaNTRIGVPGRvkgLSGGERKRLAF 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 1216 GRALLRKSKILVLDEATAAVD-LETDNLIQTTIQNEFAHCTVITIAHR-LHTIMDS-DKVMVLDNGKIIECGSPEELLQ 1291
Cdd:TIGR00955 178 ASELLTDPPLLFCDEPTSGLDsFMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELfDKIILMAEGRVAYLGSPDQAVP 256
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
422-606 |
3.42e-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: 45.78 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLgemENVHGHITIKGTTAYVPQ--------QSWIQNGtikdnilfgtef 493
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL---YASGKARLISFLPKFSRNklifidqlQFLIDVG------------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 494 nekryqqvleacallpdLEMLPggdlaeIGEKGINLSGGQKQRISLARATYQNLD--IYLLDDPLSAVDAHVGKHIFNKV 571
Cdd:cd03238 76 -----------------LGYLT------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVI 132
|
170 180 190
....*....|....*....|....*....|....*.
gi 578818931 572 lgpNGLL-KGKTRLLVTHSMHFLPQVDEIVVLGNGT 606
Cdd:cd03238 133 ---KGLIdLGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
826-944 |
4.65e-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: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 826 KQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPV---FTIIVIPLG--- 899
Cdd:cd18551 73 RRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVltlVTLAVVPLAfli 152
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 578818931 900 IIYVSVQMFYVSTSRQlRRLDSVTrspiySHFSETVSGLPVIRAF 944
Cdd:cd18551 153 ILPLGRRIRKASKRAQ-DALGELS-----AALERALSAIRTVKAS 191
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
424-625 |
4.93e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.58 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 424 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQNG-TIKDNI-LFGTEFNEKRyQQV 501
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQlTGIENIeLKGLMMGLTK-EKI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 502 LEacaLLPDLEmlpggDLAEIGeKGIN-----LSGGQKQRISLARATYQNLDIYLLDDPLSavdahVGKHIF-NKVLGPN 575
Cdd:PRK13545 121 KE---IIPEII-----EFADIG-KFIYqpvktYSSGMKSRLGFAISVHINPDILVIDEALS-----VGDQTFtKKCLDKM 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 576 GLLK--GKTRLLVTHSmhfLPQVDEIVV----LGNGTIVEKGSYSALLAKKGEFAK 625
Cdd:PRK13545 187 NEFKeqGKTIFFISHS---LSQVKSFCTkalwLHYGQVKEYGDIKEVVDHYDEFLK 239
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
422-652 |
6.39e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 46.64 E-value: 6.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT---------AYVPqqswiqngtikdnilfgte 492
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPldpedrrriGYLP------------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 493 fnEKR--YQQ--VLEACALLPDLEMLPGGD-------------LAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDD 554
Cdd:COG4152 78 --EERglYPKmkVGEQLVYLARLKGLSKAEakrradewlerlgLGDRANKKVeELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 555 PLSAVDAhVGKHIFNKVlgpngLL----KGKTRLLVTHSMHflpQV----DEIVVLGNGTIVEKGSYSALlakKGEFAKN 626
Cdd:COG4152 156 PFSGLDP-VNVELLKDV-----IRelaaKGTTVIFSSHQME---LVeelcDRIVIINKGRKVLSGSVDEI---RRQFGRN 223
|
250 260
....*....|....*....|....*.
gi 578818931 627 lKTFLRHTGPEEEATVHDGSEEEDDD 652
Cdd:COG4152 224 -TLRLEADGDAGWLRALPGVTVVEED 248
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
830-1040 |
1.02e-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: 46.01 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 830 NNILRAPMRFFDTTPTGRIVNRFaGDISTVDDTL-PQSLRSWITCFLGIISTLVMICMaTPVFTIIVIPLGIIYVsvqMF 908
Cdd:cd18568 83 KHLLSLPLSFFASRKVGDIITRF-QENQKIRRFLtRSALTTILDLLMVFIYLGLMFYY-NLQLTLIVLAFIPLYV---LL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 909 YVSTSRQLRRLDS---VTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFS-WITSNRWLAIR--LELV 982
Cdd:cd18568 158 TLLSSPKLKRNSReifQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRgQKLSIVLQLISslINHL 237
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 983 GNLTVFFSALMMVIYRDTLSGDTVGFvlsNAL--NITQTLNWLVRMTSEIETNIVAVERI 1040
Cdd:cd18568 238 GTIAVLWYGAYLVISGQLTIGQLVAF---NMLfgSVINPLLALVGLWDELQETRISVERL 294
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
422-612 |
1.04e-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: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-TAYVPQQSW------IQ----------NG--T 482
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQdITGLSGRELrplrrrMQmvfqdpyaslNPrmT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 483 IKDNILFGTEFN--------EKRYQQVLEACALLPD-LEMLPGgdlaeigEkginLSGGQKQRISLARATYQNLDIYLLD 553
Cdd:COG4608 114 VGDIIAEPLRIHglaskaerRERVAELLELVGLRPEhADRYPH-------E----FSGGQRQRIGIARALALNPKLIVCD 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 554 DPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 612
Cdd:COG4608 183 EPVSALDVSIQAQVLN-------LLEdlqdelGLTYLFISHDLSVVRHIsDRVAVMYLGKIVEIAP 241
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1204-1295 |
1.05e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 45.85 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1204 NLSIGQR---QLLClgrALLRKSKILVLDEATAAVDLETDNLIQTTIQ--NEFAHCTVITIAHRLHTIMD-SDKVMVLDN 1277
Cdd:COG4586 154 QLSLGQRmrcELAA---ALLHRPKILFLDEPTIGLDVVSKEAIREFLKeyNRERGTTILLTSHDMDDIEAlCDRVIVIDH 230
|
90
....*....|....*...
gi 578818931 1278 GKIIECGSPEELLQIPGP 1295
Cdd:COG4586 231 GRIIYDGSLEELKERFGP 248
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
797-996 |
1.05e-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: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 797 ALGLAQGIFVFIAHFWSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLR----SWIT 872
Cdd:cd18548 47 LLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRmlvrAPIM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 873 CFLGIISTLVM-------ICMATPVFTIIVIplGIIYVSVQMFyvstSRQLRRLDSVTRSpiyshFSETVSGLPVIRAF- 944
Cdd:cd18548 127 LIGAIIMAFRInpklaliLLVAIPILALVVF--LIMKKAIPLF----KKVQKKLDRLNRV-----VRENLTGIRVIRAFn 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 945 --EHQ-QRFLKHNEVRIDTNQKcvfswitsnrwlairlelVGNLTVFFSALMMVI 996
Cdd:cd18548 196 reDYEeERFDKANDDLTDTSLK------------------AGRLMALLNPLMMLI 232
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
414-590 |
1.41e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 44.87 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 414 WEHDSEA------TVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG------TTAYVP-------- 473
Cdd:PRK10908 4 FEHVSKAylggrqALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlKNREVPflrrqigm 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 474 ---QQSWIQNGTIKDNILF-------GTEFNEKRYQQVLEACALLPDLEMLPggdlaeigekgINLSGGQKQRISLARAT 543
Cdd:PRK10908 84 ifqDHHLLMDRTVYDNVAIpliiagaSGDDIRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578818931 544 YQNLDIYLLDDPLSAVDAHVGKHI------FNKVlgpngllkGKTRLLVTHSM 590
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGIlrlfeeFNRV--------GVTVLMATHDI 197
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1096-1282 |
1.96e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.55 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1096 EKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASiglhdlREKLTIIPQDPILFSGSLRMNlDPFNNYSDEE-- 1173
Cdd:PRK09700 290 EILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP------RSPLDAVKKGMAYITESRRDN-GFFPNFSIAQnm 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1174 -IWKALELAHLKSfvaslQLGLSHEVTEAG--------------------GNLSIGQRQLLCLGRALLRKSKILVLDEAT 1232
Cdd:PRK09700 363 aISRSLKDGGYKG-----AMGLFHEVDEQRtaenqrellalkchsvnqniTELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578818931 1233 AAVDLETDNLIQtTIQNEFAH--CTVITIAHRLHTIMD-SDKVMVLDNGKIIE 1282
Cdd:PRK09700 438 RGIDVGAKAEIY-KVMRQLADdgKVILMVSSELPEIITvCDRIAVFCEGRLTQ 489
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1096-1298 |
2.08e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.87 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1096 EKIGVVGRTGAGKSSL----TNCLFRILEAAGGQIIIDGvdiasIGLHDLREK-----------------LTIipQDPIL 1154
Cdd:TIGR00956 88 ELTVVLGRPGSGCSTLlktiASNTDGFHIGVEGVITYDG-----ITPEEIKKHyrgdvvynaetdvhfphLTV--GETLD 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1155 FSGSLRMNLDPFNNYSDEEIWKalelaHLKSFVASLqLGLSHEVTEAGGN-----LSIGQRQLLCLGRALLRKSKILVLD 1229
Cdd:TIGR00956 161 FAARCKTPQNRPDGVSREEYAK-----HIADVYMAT-YGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWD 234
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578818931 1230 EATAAVD----LETDNLIQTtiQNEFAHCTV-ITIAHRLHTIMDS-DKVMVLDNGKIIECGSPEELLQipgpfYF 1298
Cdd:TIGR00956 235 NATRGLDsataLEFIRALKT--SANILDTTPlVAIYQCSQDAYELfDKVIVLYEGYQIYFGPADKAKQ-----YF 302
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
777-953 |
2.23e-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: 44.75 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 777 IFNSTDYPASQRDMRV--GVYGALGLAQGIFVFIAHFwsAFGFV--HASNILHKQLLNNILRAPMRFFDTTP--TGRIVN 850
Cdd:cd18578 38 VFSLPDDDELRSEANFwaLMFLVLAIVAGIAYFLQGY--LFGIAgeRLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 851 RFAGDISTV----DDTLPQSLRSWITCFLG-IIS-------TLVMICMAtPVFtiivipLGIIYVSVQMFYVSTSRQLRR 918
Cdd:cd18578 116 RLSTDASDVrglvGDRLGLILQAIVTLVAGlIIAfvygwklALVGLATV-PLL------LLAGYLRMRLLSGFEEKNKKA 188
|
170 180 190
....*....|....*....|....*....|....*
gi 578818931 919 LDSVTRspiysHFSETVSGLPVIRAFEHQQRFLKH 953
Cdd:cd18578 189 YEESSK-----IASEAVSNIRTVASLTLEDYFLEK 218
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
522-612 |
2.36e-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: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 522 IGEKGINLSGGQKQRISLA-----RATYQNLdiYLLDDPLSAVDAHVGKHIFNkVLGpnGLL-KGKTRLLVTHSMHFLPQ 595
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAkelskRSTGRTL--YILDEPTTGLHFDDIKKLLE-VLQ--RLVdKGNTVVVIEHNLDVIKT 897
|
90 100
....*....|....*....|...
gi 578818931 596 VDEIVVLG------NGTIVEKGS 612
Cdd:TIGR00630 898 ADYIIDLGpeggdgGGTVVASGT 920
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
422-562 |
2.36e-04 |
|
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: 43.96 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISamlgemenvhghiTIKGTtaYVPQQSWI----QNGTIkdNILFGTEfnekr 497
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLK-------------CIYGN--YLPDSGSIlvrhDGGWV--DLAQASP----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 498 yQQVLE------------------ACALlpDLEMLP----GGDLAEIGEKGINL------------------SGGQKQRI 537
Cdd:COG4778 85 -REILAlrrrtigyvsqflrviprVSAL--DVVAEPllerGVDREEARARARELlarlnlperlwdlppatfSGGEQQRV 161
|
170 180
....*....|....*....|....*
gi 578818931 538 SLARATYQNLDIYLLDDPLSAVDAH 562
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAA 186
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
90-380 |
2.54e-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: 44.42 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 90 LLKSFLLKLVNDIFTFVSPQLLKLLI---SFASDRDTYLWIGYLCAILLFTAALIQSFC--LQCYfqLCFKLGVKVRTAI 164
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIddvLIQLGPGGNTSLLLLLVLGLAGAYVLSALLgiLRGR--LLARLGERITADL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 165 MASVYKKA--LTLSNLARKEytVGETVNLMSVDAQKLMD-VTNFMHMLWSSVLQIVLSIFFL----WRelgpsvLAgvgV 237
Cdd:cd18563 79 RRDLYEHLqrLSLSFFDKRQ--TGSLMSRVTSDTDRLQDfLSDGLPDFLTNILMIIGIGVVLfslnWK------LA---L 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 238 MVLV-IPINAILSTK-SKTIQVKNMKNKDKRLK---IMNEILSGIKILKYFAWEPS----FRDQVQNLRKKELKNLLAFS 308
Cdd:cd18563 148 LVLIpVPLVVWGSYFfWKKIRRLFHRQWRRWSRlnsVLNDTLPGIRVVKAFGQEKReikrFDEANQELLDANIRAEKLWA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 309 QLQCVVIFVFQLTPVLVSVV--------TFSVYVLVdsnnildaqkAFTS-ITLFNilrFPLSMLPMMISSMLQASVSTE 379
Cdd:cd18563 228 TFFPLLTFLTSLGTLIVWYFggrqvlsgTMTLGTLV----------AFLSyLGMFY---GPLQWLSRLNNWITRALTSAE 294
|
.
gi 578818931 380 R 380
Cdd:cd18563 295 R 295
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
416-602 |
3.44e-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: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 416 HDSEATVRDVNLDimAGQLVAVIGPVGSGKSSLISAM----LGEMENVHGHITIKgTTAYVPQQSwiqngtikdnilfgt 491
Cdd:cd03227 7 FPSYFVPNDVTFG--EGSLTIITGPNGSGKSTILDAIglalGGAQSATRRRSGVK-AGCIVAAVS--------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 492 efnekryqqvLEACALLPdlemlpggdlaeigekgiNLSGGQKQRISLA----RATYQNLDIYLLDDPLSAVDAHVGKHI 567
Cdd:cd03227 69 ----------AELIFTRL------------------QLSGGEKELSALAlilaLASLKPRPLYILDEIDRGLDPRDGQAL 120
|
170 180 190
....*....|....*....|....*....|....*
gi 578818931 568 FNKVLgpnGLLKGKTRLLVThsMHFLPQVDEIVVL 602
Cdd:cd03227 121 AEAIL---EHLVKGAQVIVI--THLPELAELADKL 150
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
530-626 |
3.66e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 530 SGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVgkhifnkVLG-PNGLLK-GKTRLLVTHSMHFLPQ-VDEIVVLGNGT 606
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA-------VLWlETYLLKwPKTFIVVSHAREFLNTvVTDILHLHGQK 418
|
90 100
....*....|....*....|.
gi 578818931 607 IVE-KGSYSALLAKKGEFAKN 626
Cdd:PLN03073 419 LVTyKGDYDTFERTREEQLKN 439
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1096-1276 |
4.24e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.80 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1096 EKIGVVGRTGAGKSSLTNCLFRILEAAGGQIiidgvdiasiglhDLREKLTIIPQ----DpilFSGS----LRMNLDPFN 1167
Cdd:PRK13409 366 EVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-------------DPELKISYKPQyikpD---YDGTvedlLRSITDDLG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1168 -NYSDEEIWKALELAHLksfvaslqlgLSHEVTEaggnLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLE----TDNL 1242
Cdd:PRK13409 430 sSYYKSEIIKPLQLERL----------LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlaVAKA 495
|
170 180 190
....*....|....*....|....*....|....*
gi 578818931 1243 IQTTIQNEFAhcTVITIAHRLHTI-MDSDKVMVLD 1276
Cdd:PRK13409 496 IRRIAEEREA--TALVVDHDIYMIdYISDRLMVFE 528
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
89-381 |
4.47e-04 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 43.97 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 89 VLLKSFLLKLVNDIFTFVSPQLLKLLIsfasdrDTYLWIG-----YLCAILLFTAALIQSFcLQcYFQ--LCFKLGVKVR 161
Cdd:cd18570 3 LLILILLLSLLITLLGIAGSFFFQILI------DDIIPSGdinllNIISIGLILLYLFQSL-LS-YIRsyLLLKLSQKLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 162 TAIMASVYKKALTL-----SNlaRKeytVGETVNLMSvDAQKLMD-VTNFMHMLWSSVLQIVLSIFFLWR---ELGPSVL 232
Cdd:cd18570 75 IRLILGYFKHLLKLplsffET--RK---TGEIISRFN-DANKIREaISSTTISLFLDLLMVIISGIILFFynwKLFLITL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 233 AGVGVMVLVIpinAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQC 312
Cdd:cd18570 149 LIIPLYILII---LLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSN 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578818931 313 VVIFVFQLTPVLVSVVTF---SVYVLvdsNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 381
Cdd:cd18570 226 LQSSIKGLISLIGSLLILwigSYLVI---KGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1085-1280 |
5.08e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 42.94 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1085 LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHD---LREKLTIIPQDPILFsgslrM 1161
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLL-----M 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1162 NLDPFNNYSDEEIWKALELAHLKSFVASL--QLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLET 1239
Cdd:PRK10908 93 DRTVYDNVAIPLIIAGASGDDIRRRVSAAldKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 578818931 1240 DNLIQTTIQnEFAH--CTVITIAHRLHTIMDSD-KVMVLDNGKI 1280
Cdd:PRK10908 173 SEGILRLFE-EFNRvgVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1085-1292 |
5.12e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.34 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1085 LRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDL-----------REKLTIIPQDPI 1153
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAinhgfalvteeRRSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1154 LFSgSLRMNLDPFNNYsdeeiWKALELAHLKS----FVASLQLGL-SHEVTEagGNLSIGQRQLLCLGRALLRKSKILVL 1228
Cdd:PRK10982 344 GFN-SLISNIRNYKNK-----VGLLDNSRMKSdtqwVIDSMRVKTpGHRTQI--GSLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578818931 1229 DEATAAVDL----ETDNLIQTTIQNEFAhctVITIAHRLHTIMD-SDKVMVLDNGK---IIECG--SPEELLQI 1292
Cdd:PRK10982 416 DEPTRGIDVgakfEIYQLIAELAKKDKG---IIIISSEMPELLGiTDRILVMSNGLvagIVDTKttTQNEILRL 486
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
743-994 |
5.32e-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: 43.80 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 743 GLFSIFFIILAFVMNSVAFIGSnlwLSAWTSDSKIFNSTDYPASQRDmRVGVYGALGLAQGIFVFIAHFWSAFGFVHASN 822
Cdd:cd18558 13 GLLPAFMVIFGDMTDSFTNGGM---TNITGNSSGLNSSAGPFEKLEE-EMTLYAYYYLIIGAIVLITAYIQGSFWGLAAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 823 ILHKQLLNNILRAPMR----FFDTTPTGRIVNRFAGDISTVD----DTLPQSLRSWITCFLGIISTLVMICMATPVFTII 894
Cdd:cd18558 89 RQTKKIRYKFFHAIMRqeigWFDVNDTGELNTRLADDVSKINegigDKIGVIFQNIATFGTGFIIGFIRGWKLTLVILAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 895 VIPLGII-YVSVQMFYVSTSRQLRRLDSVTRSPiyshfSETVSGLPVIRAFEHQQRFLK--HNEVRIDTNqkcvfswits 971
Cdd:cd18558 169 SPVLGLSaVVWAKILSGFTDKEKKAYAKAGAVA-----EEVLEAFRTVIAFGGQQKEETryAQNLEIAKR---------- 233
|
250 260
....*....|....*....|...
gi 578818931 972 nrwLAIRLELVGNLTVFFSALMM 994
Cdd:cd18558 234 ---NGIKKAITFNISMGAAFLLI 253
|
|
| PilT |
COG2805 |
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ... |
434-465 |
5.33e-04 |
|
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures];
Pssm-ID: 442056 Cd Length: 342 Bit Score: 43.93 E-value: 5.33e-04
10 20 30
....*....|....*....|....*....|....
gi 578818931 434 LVAVIGPVGSGKSSLISAMLGEM-ENVHGHI-TI 465
Cdd:COG2805 127 LVLVTGPTGSGKSTTLAAMIDYInETRAKHIiTI 160
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
414-588 |
5.94e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 42.63 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 414 WEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT------------AYVPQQSWIQ-N 480
Cdd:PRK13540 9 FDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSikkdlctyqkqlCFVGHRSGINpY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 481 GTIKDNILFGTEFNEKRYQqVLEACAL--LPDLEMLPGGdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSA 558
Cdd:PRK13540 89 LTLRENCLYDIHFSPGAVG-ITELCRLfsLEHLIDYPCG----------LLSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157
|
170 180 190
....*....|....*....|....*....|
gi 578818931 559 VDAHVGKHIFNKVLGPNGllKGKTRLLVTH 588
Cdd:PRK13540 158 LDELSLLTIITKIQEHRA--KGGAVLLTSH 185
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
1098-1117 |
6.37e-04 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 43.60 E-value: 6.37e-04
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
422-555 |
7.20e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 43.86 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--------------AYVPQ----QSWIQNGTI 483
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDitglsprerrrlgvAYIPEdrlgRGLVPDMSV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 484 KDNILFGTEFNEK-------RYQQVLEACA-LLPDLEMLPGGDLAEIGekgiNLSGGQKQRISLARATYQNLDIYLLDDP 555
Cdd:COG3845 354 AENLILGRYRRPPfsrggflDRKAIRAFAEeLIEEFDVRTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQP 429
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
792-1040 |
8.66e-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: 349984 [Multi-domain] Cd Length: 295 Bit Score: 42.85 E-value: 8.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 792 VGVYGALGLAQGIFVFIahfwsafgFVH-ASNI-------LHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTL 863
Cdd:cd18540 45 ILLYLGLILIQALSVFL--------FIRlAGKIemgvsydLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEII 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 864 PQSLRSWITCFLGIISTLVMICMATP---VFTIIVIPLgIIYVSV--QMFYVSTSRQLRRLDSVtrspIYSHFSETVSGL 938
Cdd:cd18540 117 SWGLVDLVWGITYMIGILIVMLILNWklaLIVLAVVPV-LAVVSIyfQKKILKAYRKVRKINSR----ITGAFNEGITGA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 939 PVIRAFehqqrflkhneVRIDTNQKcVFSWITSN---------RWLAIRLELVGNLTVFFSALMMV-----IYRDTLSGD 1004
Cdd:cd18540 192 KTTKTL-----------VREEKNLR-EFKELTEEmrrasvraaRLSALFLPIVLFLGSIATALVLWyggilVLAGAITIG 259
|
250 260 270
....*....|....*....|....*....|....*.
gi 578818931 1005 TVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERI 1040
Cdd:cd18540 260 TLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
422-619 |
1.05e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 42.77 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGttaYVPQQSWIQNgtiKDNI--LFGT-------- 491
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG---YVPFKRRKEF---ARRIgvVFGQrsqlwwdl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 492 -------------EFNEKRYQQVLEACAllpdlEMLpggDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLS 557
Cdd:COG4586 112 paidsfrllkaiyRIPDAEYKKRLDELV-----ELL---DLGELLDTPVrQLSLGQRMRCELAAALLHRPKILFLDEPTI 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 558 AVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLAK 619
Cdd:COG4586 184 GLDVVSKEAIRE-------FLKeynrerGTTILLTSHDMDDIEALcDRVIVIDHGRIIYDGSLEELKER 245
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1096-1278 |
1.35e-03 |
|
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: 40.82 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1096 EKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIdgvdiasiglhdlrekltiipqdpilfsgslrMNLDPFNNYSDEEIW 1175
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------IDGEDILEEVLDQLL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1176 KALelahlksfvaslqlglsheVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQ-------TTIQ 1248
Cdd:smart00382 51 LII-------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrlLLLL 111
|
170 180 190
....*....|....*....|....*....|....*.
gi 578818931 1249 NEFAHCTVITIAHRLHTIMD------SDKVMVLDNG 1278
Cdd:smart00382 112 KSEKNLTVILTTNDEKDLGPallrrrFDRRIVLLLI 147
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1203-1282 |
1.41e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1203 GNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDlETD-----NLIQttiqnEFAH--CTVITIAHRLHTIMD-SDKVMV 1274
Cdd:NF040905 138 TDIGVGKQQLVEIAKALSKDVKLLILDEPTAALN-EEDsaallDLLL-----ELKAqgITSIIISHKLNEIRRvADSITV 211
|
....*...
gi 578818931 1275 LDNGKIIE 1282
Cdd:NF040905 212 LRDGRTIE 219
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
422-474 |
1.57e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 42.63 E-value: 1.57e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIkGT---TAYVPQ 474
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTkleVAYFDQ 389
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
529-618 |
2.04e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.38 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 529 LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFnkvlgpnGLLK------GKTRLLVTHSMHFLPQV-DEIVV 601
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQIL-------QLLRelqqelNMGLLFITHNLSIVRKLaDRVAV 229
|
90
....*....|....*..
gi 578818931 602 LGNGTIVEKGSYSALLA 618
Cdd:PRK15134 230 MQNGRCVEQNRAATLFS 246
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1072-1278 |
2.36e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.40 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1072 NYQVRYRPELDLVLRGIT--CDIGSMekIGVVGRTGAGKSSLTNCLfriLEAAGGQIIIDGVDIA-----------SIGL 1138
Cdd:TIGR00956 766 TYEVKIKKEKRVILNNVDgwVKPGTL--TALMGASGAGKTTLLNVL---AERVTTGVITGGDRLVngrpldssfqrSIGY 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1139 ---HDLR-EKLTIipQDPILFSGSLR----MNLDPFNNYSDEEIwKALELAHLKSFVaslqlglsheVTEAGGNLSIGQR 1210
Cdd:TIGR00956 841 vqqQDLHlPTSTV--RESLRFSAYLRqpksVSKSEKMEYVEEVI-KLLEMESYADAV----------VGVPGEGLNVEQR 907
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578818931 1211 QLLCLGRALLRKSKILV-LDEATAAVDLETDNLIQTTIQNEFAHCTVI--TIAHRLHTIMDS-DKVMVLDNG 1278
Cdd:TIGR00956 908 KRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAIlcTIHQPSAILFEEfDRLLLLQKG 979
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1076-1293 |
2.39e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.00 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1076 RYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAA-----GGQIIIDGVDIASIGLHDLR----EKLT 1146
Cdd:PRK15134 16 RQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRgvrgNKIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1147 IIPQDPILfsgslrmNLDPFNNysdeeIWKALelahlkSFVASLQLGLSHE--------------VTEAGG-------NL 1205
Cdd:PRK15134 96 MIFQEPMV-------SLNPLHT-----LEKQL------YEVLSLHRGMRREaargeilncldrvgIRQAAKrltdyphQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1206 SIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQT---TIQNEFaHCTVITIAHRLHTIMD-SDKVMVLDNGKII 1281
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQllrELQQEL-NMGLLFITHNLSIVRKlADRVAVMQNGRCV 236
|
250
....*....|..
gi 578818931 1282 ECGSPEELLQIP 1293
Cdd:PRK15134 237 EQNRAATLFSAP 248
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
201-381 |
2.54e-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: 41.36 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 201 DVTNFMHMLWSSVL----QIVLSIFFLWRELGPSVLAGV-GVMVLVIPINAILSTKSKTIQVKNMKNKDKRLKIMNEILS 275
Cdd:cd18583 105 SINDLLEQILFQIVpmiiDLVIAIVYLYYLFDPYMGLIVaVVMVLYVWSTIKLTSWRTKLRRDMIDADREERSILTESLL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 276 GIKILKYFAWEP----SFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTpvLVSVVTFSVYvlvdsnNILDAQKA---F 348
Cdd:cd18583 185 NWETVKYFNREPyekeRYREAVKNYQKAERKYLFSLNLLNAVQSLILTLG--LLAGCFLAAY------QVSQGQATvgdF 256
|
170 180 190
....*....|....*....|....*....|....
gi 578818931 349 -TSITLFNILRFPLSMLPMMISSMLQASVSTERL 381
Cdd:cd18583 257 vTLLTYWAQLSGPLNFFATLYRSIQSDLIDAERL 290
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
422-618 |
2.73e-03 |
|
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: 41.98 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 422 VRDVNLDIMAGQLVAVIGPVGSGKSslISAM-----LGE-MENVHGHITIKGTtayvpqqswiqngtikdNILfgtEFNE 495
Cdd:COG4172 26 VKGVSFDIAAGETLALVGESGSGKS--VTALsilrlLPDpAAHPSGSILFDGQ-----------------DLL---GLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 496 KR------------YQ--------------QVLEACAL---LPD-------LEMlpggdLAEIG----EKGIN-----LS 530
Cdd:COG4172 84 RElrrirgnriamiFQepmtslnplhtigkQIAEVLRLhrgLSGaaararaLEL-----LERVGipdpERRLDayphqLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 531 GGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLKGKTR------LLVTHSMHFLPQV-DEIVVLG 603
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILD-------LLKDLQRelgmalLLITHDLGVVRRFaDRVAVMR 231
|
250
....*....|....*
gi 578818931 604 NGTIVEKGSYSALLA 618
Cdd:COG4172 232 QGEIVEQGPTAELFA 246
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
827-949 |
2.97e-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: 41.42 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 827 QLLNNILRAPMRFFDTTPTGRIVNRFaGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIYVsVQ 906
Cdd:cd18782 80 TIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQL-LL 157
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 578818931 907 MFYVS--TSRQLRRLdSVTRSPIYSHFSETVSGLPVIRA--FEHQQR 949
Cdd:cd18782 158 TFLFGpiLRRQIRRR-AEASAKTQSYLVESLTGIQTVKAqnAELKAR 203
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
93-381 |
3.17e-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: 41.25 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 93 SFLLKLVNDIFTFVSPQLLKLLI--SFASDRDTYLWigYLCAILLFTAAL------IQSFCLQcyfqlcfKLGVKVRTAI 164
Cdd:cd18552 4 AILGMILVAATTAALAWLLKPLLddIFVEKDLEALL--LVPLAIIGLFLLrglasyLQTYLMA-------YVGQRVVRDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 165 MASVYKKALTLSnLAR-KEYTVGETVNLMSVDAQKLMD-VTNFMHMLWSSVLQIVLSIFFL----WReLgpSVLAGVGVM 238
Cdd:cd18552 75 RNDLFDKLLRLP-LSFfDRNSSGDLISRITNDVNQVQNaLTSALTVLVRDPLTVIGLLGVLfyldWK-L--TLIALVVLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 239 VLVIPINAI---LSTKSKTIQVK--NMknkdkrLKIMNEILSGIKILKYFAWEPS----FRDQVQNLRKKELKnLLAFSQ 309
Cdd:cd18552 151 LAALPIRRIgkrLRKISRRSQESmgDL------TSVLQETLSGIRVVKAFGAEDYeikrFRKANERLRRLSMK-IARARA 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578818931 310 LqcvvifvfqLTPV--LVSVVTFSVYVLVDSNNILDAQK---AFTS-ITLFNILRFPLSMLPMMISSMLQASVSTERL 381
Cdd:cd18552 224 L---------SSPLmeLLGAIAIALVLWYGGYQVISGELtpgEFISfITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
425-560 |
3.39e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 40.69 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 425 VNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENvHGHITIKGTT-------------AYVPQQSwiqngtikdnilfGT 491
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPleawsaaelarhrAYLSQQQ-------------TP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 492 EFNEKRYQ----------QVLEACALLPDL-EMLPGGDLAeigEKGIN-LSGGQKQRISLARATYQ-----NLD--IYLL 552
Cdd:PRK03695 81 PFAMPVFQyltlhqpdktRTEAVASALNEVaEALGLDDKL---GRSVNqLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLL 157
|
....*...
gi 578818931 553 DDPLSAVD 560
Cdd:PRK03695 158 DEPMNSLD 165
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
423-464 |
4.26e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 40.68 E-value: 4.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 578818931 423 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHIT 464
Cdd:PRK11701 23 RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH 64
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1084-1279 |
4.32e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 41.40 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1084 VLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAG--GQIIIDGVDIASiglhDLREKLTIIPQDPIL------- 1154
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK----QILKRTGFVTQDDILyphltvr 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1155 ----FSGSLRMnldPFNNYSDEEIWKAlelahlKSFVAslQLGLSHEVTEAGGN-----LSIGQRQLLCLGRALLRKSKI 1225
Cdd:PLN03211 159 etlvFCSLLRL---PKSLTKQEKILVA------ESVIS--ELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSL 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578818931 1226 LVLDEATAAVDLETD-NLIQTTIQNEFAHCTVITIAH----RLHTIMDSdkVMVLDNGK 1279
Cdd:PLN03211 228 LILDEPTSGLDATAAyRLVLTLGSLAQKGKTIVTSMHqpssRVYQMFDS--VLVLSEGR 284
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
792-944 |
4.62e-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: 40.63 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 792 VGVYGALGLAQGIFvfiAHFWSAFgfvhASNILHK---QLLNNILRAPMRFFDTTPTGRIVNRFAGDIST----VDDTLP 864
Cdd:cd18565 61 VAAFLLESLFQYLS---GVLWRRF----AQRVQHDlrtDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQlerfLDDGAN 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 865 QSLRSWITcFLGIISTLVMICMATPVFTIIVIPLgIIYVSVqmFYvstSRQLRRLDSVTRSP---IYSHFSETVSGLPVI 941
Cdd:cd18565 134 SIIRVVVT-VLGIGAILFYLNWQLALVALLPVPL-IIAGTY--WF---QRRIEPRYRAVREAvgdLNARLENNLSGIAVI 206
|
...
gi 578818931 942 RAF 944
Cdd:cd18565 207 KAF 209
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
791-949 |
4.73e-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: 40.58 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 791 RVGVYGALG----LAQGIFVFIAhFWSAFGFV------HASNI----LHKQLLNNILRAPMRFFDTTPTGRIVnRFAGDI 856
Cdd:cd18783 31 KVLVHQSYStlyvLTIGVVIALL-FEGILGYLrrylllVATTRidarLALRTFDRLLSLPIDFFERTPAGVLT-KHMQQI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 857 STVDDTLPQSLrswITCFLGIISTLVMI---CMATPVFTIIVIPLGIIYVSVQMFYVSTSRqlRRLDSVTRSPI--YSHF 931
Cdd:cd18783 109 ERIRQFLTGQL---FGTLLDATSLLVFLpvlFFYSPTLALVVLAFSALIALIILAFLPPFR--RRLQALYRAEGerQAFL 183
|
170 180
....*....|....*....|
gi 578818931 932 SETVSGLPVIRAF--EHQQR 949
Cdd:cd18783 184 VETVHGIRTVKSLalEPRQR 203
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1096-1276 |
5.92e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 40.92 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1096 EKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDgVDIASiglhdlreKLTIIPQDpilFSGSLRMNL-----DPF-NNY 1169
Cdd:COG1245 367 EVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKISY--------KPQYISPD---YDGTVEEFLrsantDDFgSSY 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1170 SDEEIWKALELAHLksfvaslqlgLSHEVTEaggnLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQN 1249
Cdd:COG1245 435 YKTEIIKPLGLEKL----------LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRR 500
|
170 180 190
....*....|....*....|....*....|
gi 578818931 1250 --EFAHCTVITIAHRLHTI-MDSDKVMVLD 1276
Cdd:COG1245 501 faENRGKTAMVVDHDIYLIdYISDRLMVFE 530
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1205-1289 |
6.36e-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: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1205 LSIGQRQLLCLGRALLRKSK---ILVLDEATAAVDLETDNLIQTTIQ------NefahcTVITIAHRLHTIMDSDKVMVL 1275
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQrlvdkgN-----TVVVIEHNLDVIKTADYIIDL 904
|
90 100
....*....|....*....|
gi 578818931 1276 ------DNGKIIECGSPEEL 1289
Cdd:TIGR00630 905 gpeggdGGGTVVASGTPEEV 924
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
1097-1155 |
7.10e-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: 37.60 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1097 KIGVVGRTGAGKSSLTNCL------------------FRILEAAGGQIIIdgVDI------ASIGLHDLREKLTIIPQDP 1152
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALtgakaivsdypgttrdpnEGRLELKGKQIIL--VDTpgliegASEGEGLGRAFLAIIEADL 78
|
...
gi 578818931 1153 ILF 1155
Cdd:pfam01926 79 ILF 81
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1204-1290 |
7.98e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 40.07 E-value: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 1204 NLSIGQRQLLCLGRALLRKSKILVLDEATAAVD----LETDNLIQTTIQNefaHCTVITIAHRLHTIMD-SDKVMVLDNG 1278
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEIFDNLNKQ---GKTIILVTHDLDNVLEwTKRTIFFKDG 241
|
90
....*....|..
gi 578818931 1279 KIIECGSPEELL 1290
Cdd:PRK13651 242 KIIKDGDTYDIL 253
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
425-561 |
9.13e-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: 40.19 E-value: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 425 VNLDIMAGQLVAVIGPVGSGKSSLISAMLGemenVHGHITIKGTTAYVPQQ---------------------SWIQNGTI 483
Cdd:TIGR02633 20 IDLEVRPGECVGLCGENGAGKSTLMKILSG----VYPHGTWDGEIYWSGSPlkasnirdteragiviihqelTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578818931 484 KDNILFGTEFNEKRY-----QQVLEACALLPDLEMLPGGDLAEIGEKGinlsGGQKQRISLARATYQNLDIYLLDDPLSA 558
Cdd:TIGR02633 96 AENIFLGNEITLPGGrmaynAMYLRAKNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSS 171
|
...
gi 578818931 559 VDA 561
Cdd:TIGR02633 172 LTE 174
|
|
| |
