|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
252-1163 |
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: 593.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 252 PSLIWSIYGVYGwPYFRLG-LLKVFNDCIGFAGPLLLNRLIKYLEKGSGSS-VGYTLAISLGFISIFKSFLDTQYTFRLS 329
Cdd:TIGR00957 305 PSLFKVLYKTFG-PYFLMSfCFKAIHDLMMFIGPQILSLLIRFVNDPMAPDwQGYFYTGLLFVCACLQTLILHQYFHICF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 330 KLKLKLRSSIMSVIYRKCLWVNTANRSGFSEGEIQTFMSVDADRIVNLCNSLHDLWSLPLQIGIALYLLYTQVKFAFLSG 409
Cdd:TIGR00957 384 VSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAG 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 410 LAITILLIPVNKWISVLIASATEKMMKLKDERIRKTGELLTNIRTLKMYGWDNWFADWLKETRATEVTHLATRKYLDAWC 489
Cdd:TIGR00957 464 VAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVG 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 490 VFFWATTPTLFSLCTFGLFALMGHQ--LDAATVFTCLALFNSLISPLNSFPWVINGLIDAFISTRRVSKFLCCLEHSRDF 567
Cdd:TIGR00957 544 TFTWVCTPFLVALITFAVYVTVDENniLDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDS 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 568 ----SIDSGftsEDLAVCVEDASCTWSsnveEDYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSIL 643
Cdd:TIGR00957 624 ierrTIKPG---EGNSITVHNATFTWA----RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVH 696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 644 LNGSVAYVPQVPWLLSGTVRENILFGKPFDSKRYFETLSACALDVDISLMVGGDMACIGDKGLNLSGGQRARFALARAVY 723
Cdd:TIGR00957 697 MKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVY 776
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 724 HGSDMYLLDDVLSAVDSQVGCWILQRaLLGP--LLNKKTRVMCTHNIQAISCADMIVVMDKGKV---------------- 785
Cdd:TIGR00957 777 SNADIYLFDDPLSAVDAHVGKHIFEH-VIGPegVLKNKTRILVTHGISYLPQVDVIIVMSGGKIsemgsyqellqrdgaf 855
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 786 ------------------NWSGSVTD-------MPKSISPTFSLTNEF-----DMSSPNHLTKRKETlSIKEDGVDEISE 835
Cdd:TIGR00957 856 aeflrtyapdeqqghledSWTALVSGegkeaklIENGMLVTDVVGKQLqrqlsASSSDSGDQSRHHG-SSAELQKAEAKE 934
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 836 AAADIVKLEERKEGRVEMMVYRNYAVFSGWFITIVILVSAVLMQGSRNGNDLWLSYWVDKTGKGVSHYSTSFYLMVLCIF 915
Cdd:TIGR00957 935 ETWKLMEADKAQTGQVELSVYWDYMKAIGLFITFLSIFLFVCNHVSALASNYWLSLWTDDPMVNGTQNNTSLRLSVYGAL 1014
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 916 CIINSILTLVRAFSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFILNILLANFVGLL 995
Cdd:TIGR00957 1015 GILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVI 1094
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 996 GIIVVLSYVQVLFLLLLLPFWYIYSKLQVFYRSTSRELRRLDSVSRSPIYASFTETLDGSSTIRAFKSEEHFVGRFIEHL 1075
Cdd:TIGR00957 1095 GALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKV 1174
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1076 TLYQRTSYSEIIASLWLSLRLQLLGSMIVLFVAVMAVLGSggnfpiSFGTPGLVGLALSYAAPLVSLLGSLLTSFTETEK 1155
Cdd:TIGR00957 1175 DENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISR------HSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMET 1248
|
....*...
gi 1063701384 1156 EMVSVERV 1163
Cdd:TIGR00957 1249 NIVAVERL 1256
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
101-1163 |
5.52e-157 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 510.05 E-value: 5.52e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 101 WIAVILSLkfaCCACHVFTSQilcFWWIFRF------LTDALHLNMIFTLQE----------ICLIMLDIAFGISINV-L 163
Cdd:PLN03130 122 WCSMLVMI---GVETKIYIRE---FRWYVRFaviyvlVGDAVMLNLVLSVKEyyssfvlylyISEVAAQVLFGILLLVyF 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 164 RIKQAHPKIIPLEDPLIED-------DDDQKRIEKNGSWWDLFTFGYIGSIMKHGSVKQLELENLLTLppemDPFTCCEN 236
Cdd:PLN03130 196 PNLDPYPGYTPIGSESVDDyeyeelpGGEQICPERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKL----DTWDQTET 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 237 LLR----CWQlQECNNySTPSLIWSIYGVYGWPYFRLGLLKVFNDCIGFAGPLLLNRLIKYLEKGSGSSVGYTLAISLgF 312
Cdd:PLN03130 272 LYRsfqkCWD-EELKK-PKPWLLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQNGEPAWIGYIYAFSI-F 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 313 ISIFKSFL-DTQYTFRLSKLKLKLRSSIMSVIYRKCLWVNTANRSGFSEGEIQTFMSVDADRIVNLCNSLHDLWSLPLQI 391
Cdd:PLN03130 349 VGVVLGVLcEAQYFQNVMRVGFRLRSTLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 392 GIALYLLYTQVKFAFLSGLAITILLIPVNKWISVLIASATEKMMKLKDERIRKTGELLTNIRTLKMYGWDNWFADWLKET 471
Cdd:PLN03130 429 IIAMVLLYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTV 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 472 RATEVTHLATRKYLDAWCVFFWATTPTLFSLCTFGLFALMGHQLDAATVFTCLALFNSLISPLNSFPWVINGLIDAFIST 551
Cdd:PLN03130 509 RDDELSWFRKAQLLSAFNSFILNSIPVLVTVVSFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSL 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 552 RRVSKFLccLEHSRDFSIDSGFTSEDLAVCVEDASCTWSSNVEEDynlTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSL 631
Cdd:PLN03130 589 KRLEELL--LAEERVLLPNPPLEPGLPAISIKNGYFSWDSKAERP---TLSNINLDVPVGSLVAIVGSTGEGKTSLISAM 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 632 LGEMRCV-HGSILLNGSVAYVPQVPWLLSGTVRENILFGKPFDSKRYFETLSACALDVDISLMVGGDMACIGDKGLNLSG 710
Cdd:PLN03130 664 LGELPPRsDASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISG 743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 711 GQRARFALARAVYHGSDMYLLDDVLSAVDSQVGCWILQRALLGPlLNKKTRVMCTHNIQAISCADMIVVMDKGKVNWSGS 790
Cdd:PLN03130 744 GQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDE-LRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGT 822
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 791 VTDMPKSiSPTF------------SLTNEFDMSSPNHLTKRKET-----LSIKEDGVDEISEAAADIVKLEERKEGRVEM 853
Cdd:PLN03130 823 YEELSNN-GPLFqklmenagkmeeYVEENGEEEDDQTSSKPVANgnannLKKDSSSKKKSKEGKSVLIKQEERETGVVSW 901
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 854 MVYRNY-AVFSGWFITIVILVSAVLMQGSRNGNDLWLSYWVDKTGKgvSHYSTSFYLMVLCIFCIINSILTLVRAFSFAF 932
Cdd:PLN03130 902 KVLERYkNALGGAWVVMILFLCYVLTEVFRVSSSTWLSEWTDQGTP--KTHGPLFYNLIYALLSFGQVLVTLLNSYWLIM 979
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 933 GGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFILNILLANFVGLLGIIVVLSYVQVLFLLLL 1012
Cdd:PLN03130 980 SSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAI 1059
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1013 LPFWYIYSKLQVFYRSTSRELRRLDSVSRSPIYASFTETLDGSSTIRAFKSEEHFVGRFIEHLTLYQRTSYSEIIASLWL 1092
Cdd:PLN03130 1060 MPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWL 1139
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063701384 1093 SLRLQLLGSMIVLFVAVMAVLGSG-GNFPISFGTpgLVGLALSYAAPLVSLLGSLLTSFTETEKEMVSVERV 1163
Cdd:PLN03130 1140 AIRLETLGGLMIWLTASFAVMQNGrAENQAAFAS--TMGLLLSYALNITSLLTAVLRLASLAENSLNAVERV 1209
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
190-1163 |
9.22e-154 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 498.73 E-value: 9.22e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 190 EKNGSWWDLFTFGYIGSIMKHGSVKQLELENLLTLPPEMDPFTCCENLLRCWQlqECNNYSTPSLIWSIYGVYGWPYFRL 269
Cdd:PLN03232 229 ERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWT--EESRRPKPWLLRALNNSLGGRFWLG 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 270 GLLKVFNDCIGFAGPLLLNRLIKYLEKGSGSSVGYTLAISLGFISIFKSFLDTQYTFRLSKLKLKLRSSIMSVIYRKCLW 349
Cdd:PLN03232 307 GIFKIGHDLSQFVGPVILSHLLQSMQEGDPAWVGYVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHKSLR 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 350 VNTANRSGFSEGEIQTFMSVDADRIVNLCNSLHDLWSLPLQIGIALYLLYTQVKFAFLSGLAITILLIPVNKWISVLIAS 429
Cdd:PLN03232 387 LTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRK 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 430 ATEKMMKLKDERIRKTGELLTNIRTLKMYGWDNWFADWLKETRATEVTHLATRKYLDAWCVFFWATTPTLFSLCTFGLFA 509
Cdd:PLN03232 467 LTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFV 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 510 LMGHQLDAATVFTCLALFNSLISPLNSFPWVINGLIDAFISTRRVSKFLccLEHSRDFSIDSGFTSEDLAVCVEDASCTW 589
Cdd:PLN03232 547 LLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELL--LSEERILAQNPPLQPGAPAISIKNGYFSW 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 590 SSNVEedyNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVH-GSILLNGSVAYVPQVPWLLSGTVRENILF 668
Cdd:PLN03232 625 DSKTS---KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtSSVVIRGSVAYVPQVSWIFNATVRENILF 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 669 GKPFDSKRYFETLSACALDVDISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQVGCWILQ 748
Cdd:PLN03232 702 GSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFD 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 749 rALLGPLLNKKTRVMCTHNIQAISCADMIVVMDKGKVNWSGSVTDMPKSiSPTFS--LTNEFDMSSPNHLTKRKETLSIK 826
Cdd:PLN03232 782 -SCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKS-GSLFKklMENAGKMDATQEVNTNDENILKL 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 827 EDGVD-EISEAAAD-----------IVKLEERKEGRVEMMVYRNY-AVFSGWFITIVILVSAVLMQGSRNGNDLWLSYWV 893
Cdd:PLN03232 860 GPTVTiDVSERNLGstkqgkrgrsvLVKQEERETGIISWNVLMRYnKAVGGLWVVMILLVCYLTTEVLRVSSSTWLSIWT 939
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 894 DKTgkGVSHYSTSFYLMVLCIFCIINSILTLVRAFSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFSSDL 973
Cdd:PLN03232 940 DQS--TPKSYSPGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDI 1017
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 974 YTIDDSLPFILNILLANFVGLLGIIVVLSYVQVLFLLLLLPFWYIYSKLQVFYRSTSRELRRLDSVSRSPIYASFTETLD 1053
Cdd:PLN03232 1018 GDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALN 1097
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1054 GSSTIRAFKSEEHFV---GRFIEHLTlyqRTSYSEIIASLWLSLRLQLLGSMIVLFVAVMAVLGSgGNFPISFGTPGLVG 1130
Cdd:PLN03232 1098 GLSSIRAYKAYDRMAkinGKSMDNNI---RFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLRN-GNAENQAGFASTMG 1173
|
970 980 990
....*....|....*....|....*....|...
gi 1063701384 1131 LALSYAAPLVSLLGSLLTSFTETEKEMVSVERV 1163
Cdd:PLN03232 1174 LLLSYTLNITTLLSGVLRQASKAENSLNSVERV 1206
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
269-554 |
2.31e-130 |
|
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: 399.62 E-value: 2.31e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 269 LGLLKVFNDCIGFAGPLLLNRLIKYLEKGSGS-SVGYTLAISLGFISIFKSFLDTQYTFRLSKLKLKLRSSIMSVIYRKC 347
Cdd:cd18598 2 LGLLKLLADVLGFAGPLLLNKLVEFLEDSSEPlSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 348 LWVNTANRSGFSEGEIQTFMSVDADRIVNLCNSLHDLWSLPLQIGIALYLLYTQVKFAFLSGLAITILLIPVNKWISVLI 427
Cdd:cd18598 82 LRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 428 ASATEKMMKLKDERIRKTGELLTNIRTLKMYGWDNWFADWLKETRATEVTHLATRKYLDAWCVFFWATTPTLFSLCTFGL 507
Cdd:cd18598 162 GALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPVLISILTFAT 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1063701384 508 FALMGHQLDAATVFTCLALFNSLISPLNSFPWVINGLIDAFISTRRV 554
Cdd:cd18598 242 YVLMGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
271-1164 |
9.26e-128 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 428.43 E-value: 9.26e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 271 LLKVFNDCIGFAGPLLLNRLIKYLEKGSGS-SVGYTLAISLGFISIFKSFLDTQYTFRLSKLKLKLRSSIMSVIYRKCLW 349
Cdd:PTZ00243 251 PFKLLSDVCTLTLPVLLKYFVKFLDADNATwGRGLGLVLTLFLTQLIQSVCLHRFYYISIRCGLQYRSALNALIFEKCFT 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 350 VNTAN--RSGFSEGEIQTFMSVDADRIVNLCNSLHDLWSLPLQIGIALYLLYTQVKFAFLSGLAITILLIPVNKWISVLI 427
Cdd:PTZ00243 331 ISSKSlaQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 428 ASATEKMMKLKDERIRKTGELLTNIRTLKMYGWDNWFADWLKETRATEVTHLATRKYLDAWCVFFWATTPTLFSLCTFGL 507
Cdd:PTZ00243 411 MAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVATSFVNNATPTLMIAVVFTV 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 508 FALMGHQLDAATVFTCLALFNSLISPLNSFPWVINGLIDAFISTRRVSKFLCCLEHSRDFSID---------SGFTSEDL 578
Cdd:PTZ00243 491 YYLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLECDNATCSTVQDmeeywreqrEHSTACQL 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 579 AVCVEDASCT-----------------------W------------------------------SSNVEED--------- 596
Cdd:PTZ00243 571 AAVLENVDVTafvpvklprapkvktsllsralrMlcceqcrptkrhpspsvvvedtdygspssaSRHIVEGgtgggheat 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 597 -----------------YNLTIKQ----VSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGSVAYVPQVP 655
Cdd:PTZ00243 651 ptsersaktpkmktddfFELEPKVllrdVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQA 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 656 WLLSGTVRENILFGKPFDSKRYFETLSACALDVDISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVL 735
Cdd:PTZ00243 731 WIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 736 SAVDSQVGCWILQRALLGPLLNkKTRVMCTHNIQAISCADMIVVMDKGKVNWSGSVTD-MPKSISPTF------------ 802
Cdd:PTZ00243 811 SALDAHVGERVVEECFLGALAG-KTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADfMRTSLYATLaaelkenkdske 889
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 803 --SLTNEFDMSSPNHLTKRKETLSIKEDGVDEISE------AAADIVKLEERKEGRVEMMVYRNYAVFSG----WFITIV 870
Cdd:PTZ00243 890 gdADAEVAEVDAAPGGAVDHEPPVAKQEGNAEGGDgaaldaAAGRLMTREEKASGSVPWSTYVAYLRFCGglhaAGFVLA 969
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 871 ILVSAVLMQGSrngNDLWLSYWVDKTGKgvshYSTSFYLMVLcIFCIINSILTLVRAFSFAFGGLK-AAVHVHNALISKL 949
Cdd:PTZ00243 970 TFAVTELVTVS---SGVWLSMWSTRSFK----LSAATYLYVY-LGIVLLGTFSVPLRFFLSYEAMRrGSRNMHRDLLRSV 1041
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 950 INAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFILNILLANFVGLLGIIVVLSYVQVLFLLLLLPFWYIYSKLQVFYRST 1029
Cdd:PTZ00243 1042 SRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSA 1121
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1030 SRELRRLDSVSRSPIYASFTETLDGSSTIRAFKSEEHFVGRFIEHLTLYQRTSYSEIIASLWLSLRLQLLGSMIVLFVAV 1109
Cdd:PTZ00243 1122 NREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIAL 1201
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*
gi 1063701384 1110 MAVLGSggNFPISFGTPGLVGLALSYAAPLVSLLGSLLTSFTETEKEMVSVERVL 1164
Cdd:PTZ00243 1202 IGVIGT--MLRATSQEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLL 1254
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
868-1165 |
3.40e-120 |
|
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: 373.40 E-value: 3.40e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 868 TIVILVSAVLMQGSRNGNDLWLSYWVDKTGKGVS---HYSTSFYLMVLCIFCIINSILTLVRAFSFAFGGLKAAVHVHNA 944
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWVSHSNNSFFnfiNDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 945 LISKLINAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFILNILLANFVGLLGIIVVLSYVQVLFLLLLLPFWYIYSKLQV 1024
Cdd:cd18605 81 LLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1025 FYRSTSRELRRLDSVSRSPIYASFTETLDGSSTIRAFKSEEHFVGRFIEHLTLYQRTSYSEIIASLWLSLRLQLLGSMIV 1104
Cdd:cd18605 161 YYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVLIV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063701384 1105 LFVAVMAVLGSGGNFPISfgtPGLVGLALSYAAPLVSLLGSLLTSFTETEKEMVSVERVLQ 1165
Cdd:cd18605 241 TFVALTAVVQHFFGLSID---AGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQ 298
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
580-784 |
5.97e-109 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 339.45 E-value: 5.97e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 580 VCVEDASCTWSSNvEEDYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGSVAYVPQVPWLLS 659
Cdd:cd03250 1 ISVEDASFTWDSG-EQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 660 GTVRENILFGKPFDSKRYFETLSACALDVDISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVD 739
Cdd:cd03250 80 GTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063701384 740 SQVGCWILQRALLGPLLNKKTRVMCTHNIQAISCADMIVVMDKGK 784
Cdd:cd03250 160 AHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
269-554 |
5.51e-92 |
|
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: 297.09 E-value: 5.51e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 269 LGLLKVFNDCIGFAGPLLLNRLIKYLEKGSGSSV--GYTLAISLGFISIFKSFLDTQYTFRLSKLKLKLRSSIMSVIYRK 346
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPLseGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 347 CLWVNTANRSGFSEGEIQTFMSVDADRIVNLCNSLHDLWSLPLQIGIALYLLYTQVKFAFLSGLAITILLIPVNKWISVL 426
Cdd:cd18579 82 ALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 427 IASATEKMMKLKDERIRKTGELLTNIRTLKMYGWDNWFADWLKETRATEVTHLATRKYLDAWCVFFWATTPTLFSLCTFG 506
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1063701384 507 LFALMGHQLDAATVFTCLALFNSLISPLNSFPWVINGLIDAFISTRRV 554
Cdd:cd18579 242 TYVLLGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
270-553 |
6.36e-84 |
|
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: 275.12 E-value: 6.36e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 270 GLLKVFNDCIGFAGPLLLNRLIKYLEKGSGSS-VGYTLAISLGFISIFKSFLDTQYTFRLSKLKLKLRSSIMSVIYRKCL 348
Cdd:cd18595 3 ALLKLLSDILLFASPQLLKLLINFVEDPDEPLwKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 349 WVNTANRSGFSEGEIQTFMSVDADRIVNLCNSLHDLWSLPLQIGIALYLLYTQVKFAFLSGLAITILLIPVNKWISVLIA 428
Cdd:cd18595 83 RLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 429 SATEKMMKLKDERIRKTGELLTNIRTLKMYGWDNWFADWLKETRATEVTHLATRKYLDAWCVFFWATTPTLFSLCTFGLF 508
Cdd:cd18595 163 KLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFATY 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1063701384 509 ALMG--HQLDAATVFTCLALFNSLISPLNSFPWVINGLIDAFISTRR 553
Cdd:cd18595 243 VLSDpdNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKR 289
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
189-1165 |
1.93e-78 |
|
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: 284.11 E-value: 1.93e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 189 IEKNGSWWDLFtFGYIGSIMKHGSVKQLELENLLTLPPEMDPFTCCENLLRCWQLQECNNYSTPSLIWSIYGVYGWPYFR 268
Cdd:TIGR01271 6 VEKANFLSKLF-FWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAKKNPKLLNALRRCFFWRFVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 269 LGLLKVFNDCIGFAGPLLLNRLIKYLEKGSG--SSVGYTLAISLGFISIFKSFLDTQYTFRLSKLKLKLRSSIMSVIYRK 346
Cdd:TIGR01271 85 YGILLYFGEATKAVQPLLLGRIIASYDPFNApeREIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSLIYKK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 347 CLWVNTANRSGFSEGEIQTFMSVDADRIVNLCNSLHDLWSLPLQIGIALYLLYTQVKFAFLSGLAITILLIPVNKWISvl 426
Cdd:TIGR01271 165 TLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQACLG-- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 427 iasatEKMMKLKDERIRK-------TGELLTNIRTLKMYGWDNWFADWLKETRATEVT---HLATRKYLDAWCVFFWATT 496
Cdd:TIGR01271 243 -----QKMMPYRDKRAGKiserlaiTSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKltrKIAYLRYFYSSAFFFSGFF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 497 PTLFSLCTFGLFalmgHQLDAATVFT----CLALFNSLIsplNSFPWVINGLIDAFISTRRVSKFLCCLEHSrdfSIDSG 572
Cdd:TIGR01271 318 VVFLSVVPYALI----KGIILRRIFTtisyCIVLRMTVT---RQFPGAIQTWYDSLGAITKIQDFLCKEEYK---TLEYN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 573 FTSEDlaVCVEDASCTWSSNVEEDY----------------------NLT------IKQVSLRVPKGSFVAVIGEVGSGK 624
Cdd:TIGR01271 388 LTTTE--VEMVNVTASWDEGIGELFekikqnnkarkqpngddglffsNFSlyvtpvLKNISFKLEKGQLLAVAGSTGSGK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 625 TSLLNSLLGEMRCVHGSILLNGSVAYVPQVPWLLSGTVRENILFGKPFDSKRYFETLSACALDVDISLMVGGDMACIGDK 704
Cdd:TIGR01271 466 SSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEG 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 705 GLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQVGCWILQRALLgPLLNKKTRVMCTHNIQAISCADMIVVMDKGK 784
Cdd:TIGR01271 546 GITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLC-KLMSNKTRILVTSKLEHLKKADKILLLHEGV 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 785 VNWSGSVTDMpKSISPTFS--------------------LTN----------------------EFDMSSPNHLTKRKET 822
Cdd:TIGR01271 625 CYFYGTFSEL-QAKRPDFSslllgleafdnfsaerrnsiLTEtlrrvsidgdstvfsgpetikqSFKQPPPEFAEKRKQS 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 823 L------SIK-----------------EDGVDEISEAAADIVKLEE---------------------RKEGRVEMMVYRN 858
Cdd:TIGR01271 704 IilnpiaSARkfsfvqmgpqkaqattiEDAVREPSERKFSLVPEDEqgeeslprgnqyhhglqhqaqRRQSVLQLMTHSN 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 859 -------------------------------YA--------------------------------VFSGW---------- 865
Cdd:TIGR01271 784 rgenrreqlqtsfrkkssitqqnelaseldiYSrrlskdsvyeiseeineedlkecfaderenvfETTTWntylryittn 863
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 866 ----FITIVILVS-AVLMQGSRNGndLWL--------SYWVDKTGKGVSHY--------STSFYLMVLCIFCIINSILTL 924
Cdd:TIGR01271 864 rnlvFVLIFCLVIfLAEVAASLLG--LWLitdnpsapNYVDQQHANASSPDvqkpviitPTSAYYIFYIYVGTADSVLAL 941
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 925 --VRAFSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFILNILLANFVGLLGIIVVLS 1002
Cdd:TIGR01271 942 gfFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVS 1021
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1003 YVQVLFLLLLLPFWYIYSKLQVFYRSTSRELRRLDSVSRSPIYASFTETLDGSSTIRAFKSEEHFVGRFieHLTLYQRTS 1082
Cdd:TIGR01271 1022 VLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLF--HKALNLHTA 1099
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1083 YSEIIASLWLSLRLQLLGSMIVLFVAVMAvlgsggnfpISFGT----PGLVGLALSYAAPLVSLLGSLLTSFTETEKEMV 1158
Cdd:TIGR01271 1100 NWFLYLSTLRWFQMRIDIIFVFFFIAVTF---------IAIGTnqdgEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMR 1170
|
....*..
gi 1063701384 1159 SVERVLQ 1165
Cdd:TIGR01271 1171 SVSRVFK 1177
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
869-1165 |
9.82e-78 |
|
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: 257.82 E-value: 9.82e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 869 IVILVSAVLMQGSRNGNDLWLSYWVDKTGKGvSHYSTSFYLMVLCIFCIINSIL-TLVRAFSFAFGGLKAAVHVHNALIS 947
Cdd:cd18580 2 LLLLLLLLLLAFLSQFSNIWLDWWSSDWSSS-PNSSSGYYLGVYAALLVLASVLlVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 948 KLINAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFILNILLANFVGLLGIIVVLSYVQVLFLLLLLPFWYIYSKLQVFYR 1027
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1028 STSRELRRLDSVSRSPIYASFTETLDGSSTIRAFKSEEHFVGRFIEHLTLYQRTSYSEIIASLWLSLRLQLLGSMIVLFV 1107
Cdd:cd18580 161 RTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALVV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063701384 1108 AVMAVLGSggnfpiSFGTPGLVGLALSYAAPLVSLLGSLLTSFTETEKEMVSVERVLQ 1165
Cdd:cd18580 241 ALLAVLLR------SSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILE 292
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
868-1163 |
8.05e-73 |
|
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: 244.31 E-value: 8.05e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 868 TIVILVSAVLMQGSRNGNDLWLSYWVDKTGKGVSHY--STSFYLMVLCIFCIINSILTLVRAFSFAFGGLKAAVHVHNAL 945
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDteQRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 946 ISKLINAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFILNILLANFVGLLGIIVVLSYVQVLFLLLLLPFWYIYSKLQVF 1025
Cdd:cd18603 81 LHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1026 YRSTSRELRRLDSVSRSPIYASFTETLDGSSTIRAFKSEEHFVGRFIEHLTLYQRTSYSEIIASLWLSLRLQLLGSMIVL 1105
Cdd:cd18603 161 YVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063701384 1106 FVAVMAVLGSGGnfpisfGTPGLVGLALSYAAPLVSLLGSLLTSFTETEKEMVSVERV 1163
Cdd:cd18603 241 FAALFAVLSRDS------LSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERI 292
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
869-1165 |
1.82e-68 |
|
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: 231.98 E-value: 1.82e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 869 IVILVSAVLMQGSRNGNDLWLSYWVDKTgkgvSHYSTSFYLMVLCIFCIINSILTLVRAFSFAFGGLKAAVHVHNALISK 948
Cdd:cd18606 2 PLLLLLLILSQFAQVFTNLWLSFWTEDF----FGLSQGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 949 LINAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFILNILLANFVGLLGIIVVLSYVQVLFLLLLLPFWYIYSKLQVFYRS 1028
Cdd:cd18606 78 VLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1029 TSRELRRLDSVSRSPIYASFTETLDGSSTIRAFKSEEHFVGRFIEHLTLYQRTSYSEIIASLWLSLRLQLLGSMIVLFVA 1108
Cdd:cd18606 158 SSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLIVA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063701384 1109 VMAVLGSggnFPISfgtPGLVGLALSYAAPLVSLLGSLLTSFTETEKEMVSVERVLQ 1165
Cdd:cd18606 238 LLCVTRR---FSIS---PSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLH 288
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
269-554 |
4.90e-66 |
|
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: 225.45 E-value: 4.90e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 269 LGLLKVFNDCIGFAGPLLLNRLIKYLEKGSGSSV--GYTLAISLGFISIFKSFLDTQYTFRLSKLKLKLRSSIMSVIYRK 346
Cdd:cd18596 2 QALLAVLSSVLSFAPPFFLNRLLRYLEDPGEDATvrPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 347 CLWV-------------------NTANRSGFSEGEIQTFMSVDADRIVNLCNSLHDLWSLPLQIGIALYLLYTQVKFAFL 407
Cdd:cd18596 82 ALRRrdksgssksseskkkdkeeDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 408 SGLAITILLIPVNKWISVLIASATEKMMKLKDERIRKTGELLTNIRTLKMYGWDNWFADWLKETRATEVTHLATRKYLDA 487
Cdd:cd18596 162 VGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDL 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063701384 488 WCVFFWATTPTLFSLCTFGLFAL-MGHQLDAATVFTCLALFNSLISPLNSFPWVINGLIDAFISTRRV 554
Cdd:cd18596 242 LLSLLWFLIPILVTVVTFATYTLvMGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
869-1165 |
3.24e-64 |
|
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: 220.03 E-value: 3.24e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 869 IVILVSAVLMQGSRNGNDLWLSYWVDKTGKGV----SHYSTSFYLMVLCIFCIINSILTLVRAFSFAFGGLKAAVHVHNA 944
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASAYETSSalppSEVSVLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 945 LISKLINAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFILNILLANFVGLLGIIVVLSYVQVLFLLLLLPFWYIYSKLQV 1024
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1025 FYRSTSRELRRLDSVSRSPIYASFTETLDGSSTIRAFKSEEHFVGRFIEHLTLYQRTSYSEIIASLWLSLRLQLLGSMIV 1104
Cdd:cd18604 162 LYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFS 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063701384 1105 LFVAVMAVLGSGGNfpisfgtPGLVGLALSYAAPLVSLLGSLLTSFTETEKEMVSVERVLQ 1165
Cdd:cd18604 242 FATAALLVYGPGID-------AGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQE 295
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
270-554 |
3.11e-59 |
|
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: 205.76 E-value: 3.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 270 GLLKVFNDCIGFAGPLLLNRLIKYLEK----GSGSSV--GYTLAISLGFISIFKSFLDTQYTFRLSKLKLKLRSSIMSVI 343
Cdd:cd18597 3 GLLKLLADVLQVLSPLLLKYLINFVEDaylgGPPPSIgyGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 344 YRKCLWVNTANRSGFSEGEIQTFMSVDADRIVNLCNSLHDLWSLPLQIGIALYLLYTQVKFAFLSGLAITILLIPVNKWI 423
Cdd:cd18597 83 YRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 424 SVLIASATEKMMKLKDERIRKTGELLTNIRTLKMYGWDNWFADWLKETRATEVTHLATRKYLDAWCVFFWATTPTLFSLC 503
Cdd:cd18597 163 MKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASML 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1063701384 504 TFGLFALMGHQLDAATVFTCLALFNSLISPLNSFPWVINGLIDAFISTRRV 554
Cdd:cd18597 243 SFITYYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
255-785 |
6.82e-58 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 210.79 E-value: 6.82e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 255 IWSIYGVYGWPYFRLGLLKVFNDCIGFAGPLLLNRLIKYLEKGSGSSVGYTLAISLGFISIFKSFLDTQYTFRLSKLKLK 334
Cdd:COG1132 12 LLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 335 LRSSIMSVIYRKCLWVNTANRSGFSEGEIQTFMSVDADRIVNLC-NSLHDLWSLPLQ-IGIALYLLYTQVKFAFLSgLAI 412
Cdd:COG1132 92 VVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLaHGLPQLVRSVVTlIGALVVLFVIDWRLALIV-LLV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 413 TILLIPVNKWISVLIASATEKMMKLKDERIRKTGELLTNIRTLKMYGwdnwfadwlKETRATEVTHLATRKYLDA----- 487
Cdd:COG1132 171 LPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFG---------REERELERFREANEELRRAnlraa 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 488 -WCVFFWATTPTLFSLCTFGLFALMGH-----QLDAATVFTCLALFNSLISPLNSFPWVINGLIDAFISTRRVSKFLccl 561
Cdd:COG1132 242 rLSALFFPLMELLGNLGLALVLLVGGLlvlsgSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELL--- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 562 ehSRDFSIDSGFTSEDL-----AVCVEDASCTWSSNVEedynlTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMR 636
Cdd:COG1132 319 --DEPPEIPDPPGAVPLppvrgEIEFENVSFSYPGDRP-----VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 637 CVHGSILLNG-------------SVAYVPQVPWLLSGTVRENILFGKP-FDSKRYFETLSACALDVDISLMVGGDMACIG 702
Cdd:COG1132 392 PTSGRILIDGvdirdltleslrrQIGVVPQDTFLFSGTIRENIRYGRPdATDEEVEEAAKAAQAHEFIEALPDGYDTVVG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 703 DKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQVGCWIlQRALLgPLLNKKTRVMCTHNIQAISCADMIVVMDK 782
Cdd:COG1132 472 ERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALI-QEALE-RLMKGRTTIVIAHRLSTIRNADRILVLDD 549
|
...
gi 1063701384 783 GKV 785
Cdd:COG1132 550 GRI 552
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
868-1165 |
8.42e-55 |
|
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: 193.59 E-value: 8.42e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 868 TIVILVSAVLMQGSRNGNDLWLSYWVDKTGKGVS-----------HYSTSFYLMVLCIFCIINSILTLVRAFSFAFGGLK 936
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWTEANHDVASvvfnitsssleDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 937 AAVHVHNALISKLINAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFILNILLANFVGLLGIIVVLSYVQVLFLLLLLPFW 1016
Cdd:cd18602 81 AARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1017 YIYSKLQVFYRSTSRELRRLDSVSRSPIYASFTETLDGSSTIRAFKSEEHFVGRFIEHLTLYQRTSYSEIIASLWLSLRL 1096
Cdd:cd18602 161 IVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063701384 1097 QLLGSMIVlFVAVMAVLGSGGNFPISfgtPGLVGLALSYAAPLVSLLGSLLTSFTETEKEMVSVERVLQ 1165
Cdd:cd18602 241 DYLGAVIV-FLAALSSLTAALAGYIS---PSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLE 305
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
270-553 |
2.57e-52 |
|
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: 186.29 E-value: 2.57e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 270 GLLKVFNDCIGFAGPLLLNRLIKYLE-----------KGSGSSV--------GYTLAISLGFISIFKSFLDTQYTFRLSK 330
Cdd:cd18591 3 GILKLLGDLLGFVGPLCISGIVDYVEentysssnstdKLSVSYVtveeffsnGYVLAVILFLALLLQATFSQASYHIVIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 331 LKLKLRSSIMSVIYRKCLWVNTANRSG--FSEGEIQTFMSVDADRIVNLCNSLHDLWSLPLQIGIALYLLYTQVKFAFLS 408
Cdd:cd18591 83 EGIRLKTALQAMIYEKALRLSSWNLSSgsMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 409 GLAITILLIPVNKWISVLIASATEKMMKLKDERIRKTGELLTNIRTLKMYGWDNWFADWLKETRATEVTHLATRKYLDAW 488
Cdd:cd18591 163 GAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063701384 489 CVFFWATTPTLFSLCTFGLFALMGHQ-LDAATVFTCLALFNSLISPLNSFPWVINGLIDAFISTRR 553
Cdd:cd18591 243 MTFLTQASPILVTLVTFGLYPYLEGEpLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRR 308
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
269-554 |
2.73e-52 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 185.50 E-value: 2.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 269 LGLLKVFNDCIGFAGPLLLNRLIKYLEKGSGS-SVGYTLAISLGFISIFKSFLDTQYTFRLSKLKLKLRSSIMSVIYRKC 347
Cdd:cd18559 2 FLLIKLVLCNHVFSGPSNLWLLLWFDDPVNGPqEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 348 LWVNTANRSGFSEGEIQTFMSVDADRIVNLCNSLHDLWSLPLQIGIALYLLYTQVKFAFLSGLAITILLIPVNKWISVLI 427
Cdd:cd18559 82 LRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 428 ASATEKMMKLKDERIRKTGELLTNIRTLKMYGWDNWFADWLKETRATEVTHLATRKYLDAWCVFFWATTPTLFSLCTFGL 507
Cdd:cd18559 162 RQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1063701384 508 FALMGH--QLDAATVFTCLALFNSLISPLNSFPWVINGLIDAFISTRRV 554
Cdd:cd18559 242 YVSRHSlaGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
864-1164 |
6.63e-52 |
|
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: 185.46 E-value: 6.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 864 GWFITIVILVSAVLMQGSRNGNDLWLSYWVDKtGKGVSHYST----------------SFYLMVLCIFCIINSILTLVRA 927
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQ-GSGNTTNNVdnstvdsgnisdnpdlNFYQLVYGGSILVILLLSLIRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 928 FSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFILNILLANFVGLLGIIVVLSYVQVL 1007
Cdd:cd18599 80 FVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1008 FLLLLLPFWYIYSKLQVFYRSTSRELRRLDSVSRSPIYASFTETLDGSSTIRAFKSEEHFVGRFIEHLTLYQRTSYSEII 1087
Cdd:cd18599 160 FLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNC 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063701384 1088 ASLWLSLRLQLLGSMIVLFVAVMAVLGSGGnfpISfgtPGLVGLALSYAAPLVSLLGSLLTSFTETEKEMVSVERVL 1164
Cdd:cd18599 240 AMRWLAVRLDILAVLITLITALLVVLLKGS---IS---PAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERIL 310
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
262-790 |
2.76e-49 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 187.73 E-value: 2.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 262 YGWPYFRLGLLKVFNDCIGFAGPLLLNRLI-KYLEKGSGSSVgYTLAISLGFISIFKSFLDTQYTFRLSKLKLKLRSSIM 340
Cdd:COG2274 154 YRRLLLQVLLASLLINLLALATPLFTQVVIdRVLPNQDLSTL-WVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLS 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 341 SVIYRKCLWVNTANRSGFSEGEIQTFMSvDADRIVN-LCNSLHDLW-SLPLQIGIALYLLYTQVKFAFLsGLAITILLIP 418
Cdd:COG2274 233 SRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREfLTGSLLTALlDLLFVLIFLIVLFFYSPPLALV-VLLLIPLYVL 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 419 VNKWISVLIASATEKMMKLKDERIRKTGELLTNIRTLKMYG--------WDNWFADWLKetratevTHLATRKYLDAwcV 490
Cdd:COG2274 311 LGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGaesrfrrrWENLLAKYLN-------ARFKLRRLSNL--L 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 491 FFWATT-PTLFSLCT--FGLFALMGHQLDAATVFTCLALFNSLISPLNSFPWVINGLIDAFISTRRVSKFLcclEHSRDF 567
Cdd:COG2274 382 STLSGLlQQLATVALlwLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDIL---DLPPER 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 568 SIDSGFTSEDL---AVCVEDASCTWSSNVEedynLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILL 644
Cdd:COG2274 459 EEGRSKLSLPRlkgDIELENVSFRYPGDSP----PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 645 NG-------------SVAYVPQVPWLLSGTVRENILFGKP-FDSKRYFETLSACALDVDISLMVGG-DMAcIGDKGLNLS 709
Cdd:COG2274 535 DGidlrqidpaslrrQIGVVLQDVFLFSGTIRENITLGDPdATDEEIIEAARLAGLHDFIEALPMGyDTV-VGEGGSNLS 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 710 GGQRARFALARAVYHGSDMYLLDDVLSAVDSQvgcwiLQRAL---LGPLLNKKTRVMCTHNIQAISCADMIVVMDKGKVN 786
Cdd:COG2274 614 GGQRQRLAIARALLRNPRILILDEATSALDAE-----TEAIIlenLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIV 688
|
....
gi 1063701384 787 WSGS 790
Cdd:COG2274 689 EDGT 692
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
580-783 |
1.04e-48 |
|
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: 172.52 E-value: 1.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 580 VCVEDASCTWSSNVEedynlTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLN-------------- 645
Cdd:cd03290 1 VQVTNGYFSWGSGLA-----TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnknesepsfeatrs 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 646 ---GSVAYVPQVPWLLSGTVRENILFGKPFDSKRYFETLSACALDVDISLMVGGDMACIGDKGLNLSGGQRARFALARAV 722
Cdd:cd03290 76 rnrYSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063701384 723 YHGSDMYLLDDVLSAVDSQVGCWILQRALLGPLL-NKKTRVMCTHNIQAISCADMIVVMDKG 783
Cdd:cd03290 156 YQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQdDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
269-554 |
5.79e-48 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 173.20 E-value: 5.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 269 LGLLKVFNDCIGFAGPLLLNRLIKYLEKGSG--SSVGYTLAISLGFISIFKSFLDTQYTFRLSKLKLKLRSSIMSVIYRK 346
Cdd:cd18594 2 LGILLFLEESLKIVQPLLLGRLVAYFVPDSTvtKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 347 CLWVNTANRSGFSEGEIQTFMSVDADRIVNLCNSLHDLWSLPLQIGIALYLLYTQVKFAFLSGLAITILLIPVNKWISVL 426
Cdd:cd18594 82 TLKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 427 IASATEKMMKLKDERIRKTGELLTNIRTLKMYGWDNWFADWLKETRATEVTHLATRKYLDAWCVFFWATTPTLFSLCTFG 506
Cdd:cd18594 162 FAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFV 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1063701384 507 LFALMGHQLDAATVFTCLALFNSL-ISPLNSFPWVINGLIDAFISTRRV 554
Cdd:cd18594 242 PYVLTGNTLTARKVFTVISLLNALrMTITRFFPESIQTLSESRVSLKRI 290
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
591-803 |
1.96e-42 |
|
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: 156.94 E-value: 1.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 591 SNVEEDYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGSVAYVPQVPWLLSGTVRENILFGK 670
Cdd:cd03291 43 SNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 671 PFDSKRYFETLSACALDVDISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQVGCWILQRA 750
Cdd:cd03291 123 SYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESC 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063701384 751 LLgPLLNKKTRVMCTHNIQAISCADMIVVMDKGKVNWSGSVTDMpKSISPTFS 803
Cdd:cd03291 203 VC-KLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL-QSLRPDFS 253
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
864-1165 |
4.54e-41 |
|
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: 154.02 E-value: 4.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 864 GWFITIVILVSAVLMQGSRNGNDLWLSYWVDKTGKG----------------VSHYSTSFYLMVLCIFCIINSILTLVRA 927
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEEKLndttdrvqgenstnvdIEDLDRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 928 FSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFILNILLANFVGLLGIIVVLSYVQVL 1007
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1008 FLLLLLPFWYIYSKLQVFYRSTSRELRRLDSVSRSPIYASFTETLDGSSTIRAFKSEEHFVGRFIEHLTLYQRTSYSEII 1087
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1088 ASLWLSLRLQLlgsMIVLFVAVMAVlgsGGNFPISFGTPGLVGLALSYAaplVSLLGSL---LTSFTETEKEMVSVERVL 1164
Cdd:cd18601 241 TSRWLAVRLDA---LCALFVTVVAF---GSLFLAESLDAGLVGLSLSYA---LTLMGTFqwcVRQSAEVENLMTSVERVL 311
|
.
gi 1063701384 1165 Q 1165
Cdd:cd18601 312 E 312
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
575-785 |
6.66e-39 |
|
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: 153.76 E-value: 6.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 575 SEDLAVCVEDASCTWssnveEDYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-------- 646
Cdd:COG4988 332 AGPPSIELEDVSFSY-----PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldp 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 647 -----SVAYVPQVPWLLSGTVRENILFGKPFDSKryfETL-----SACALDVDISLMVGGDMAcIGDKGLNLSGGQRARF 716
Cdd:COG4988 407 aswrrQIAWVPQNPYLFAGTIRENLRLGRPDASD---EELeaaleAAGLDEFVAALPDGLDTP-LGEGGRGLSGGQAQRL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063701384 717 ALARAVYHGSDMYLLDDVLSAVDSQvGCWILQRALLgPLLNKKTRVMCTHNIQAISCADMIVVMDKGKV 785
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAE-TEAEILQALR-RLAKGRTVILITHRLALLAQADRILVLDDGRI 549
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
284-554 |
5.47e-38 |
|
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: 144.29 E-value: 5.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 284 PLLLNRLIKYLEkGSGSSVGYTLAISLGFISIFKSFLDT----QYTFRLSKLKLKLRSSIMSVIYRKCLWVNTANRSGFS 359
Cdd:cd18593 17 PIFLGKLIRYFE-GNGSSISLTEAYLYAGGVSLCSFLFIithhPYFFGMQRIGMRLRVACSSLIYRKALRLSQAALGKTT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 360 EGEIQTFMSVDADRIVNLCNSLHDLWSLPLQIGIALYLLYTQVKFAFLSGLAITILLIPVNKWISVLIASATEKMMKLKD 439
Cdd:cd18593 96 VGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAARTD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 440 ERIRKTGELLTNIRTLKMYGWDNWFADWLKETRATEVTHLATRKYLDAW--CVFFWATTPTLFslCTFGLFALMGHQLDA 517
Cdd:cd18593 176 KRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALnmGLFFVSSKLILF--LTFLAYILLGNILTA 253
|
250 260 270
....*....|....*....|....*....|....*...
gi 1063701384 518 ATVFTCLALFNSL-ISPLNSFPWVINGLIDAFISTRRV 554
Cdd:cd18593 254 ERVFVTMALYNAVrLTMTLFFPFAIQFGSELSVSIRRI 291
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
271-554 |
5.60e-38 |
|
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: 144.24 E-value: 5.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 271 LLKVFNDCIGFAGP-LLLNRLIKYLEKGSGS-SVGYTLAISLGFISIFKSFLDTQYTFRLSKLKLKLRSSIMSVIYRKCL 348
Cdd:cd18592 4 LLLLISLIFGFIGPtILIRKLLEYLEDSDSSvWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 349 WVNTANRSgfSEGEIQTFMSVDADRIVNLCNSLHDLWSLPLQIGIAL-YLLYTQVKFAFLsGLAITILLIPVNKWISVLI 427
Cdd:cd18592 84 RLRSLGDK--SVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIvYSTYLLGPWALL-GMLVFLLFYPLQAFIAKLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 428 ASATEKMMKLKDERIRKTGELLTNIRTLKMYGWDNWFADWLKETRATEVTHLATRKYLDAWCVFFWATTPTLFSLCTFGL 507
Cdd:cd18592 161 GKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFLA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1063701384 508 FALMGHQLDAATVFTCLALFNSLISPLNSFPWVINGLIDAFISTRRV 554
Cdd:cd18592 241 HVALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
594-784 |
3.97e-37 |
|
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: 137.51 E-value: 3.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 594 EEDYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQVPWLLSG 660
Cdd:cd03228 11 PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAYVPQDPFLFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 661 TVRENIlfgkpfdskryfetlsacaldvdislmvggdmacigdkglnLSGGQRARFALARAVYHGSDMYLLDDVLSAVDS 740
Cdd:cd03228 91 TIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDP 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063701384 741 ---QvgcwILQRALLGpLLNKKTRVMCTHNIQAISCADMIVVMDKGK 784
Cdd:cd03228 130 eteA----LILEALRA-LAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
325-790 |
1.62e-36 |
|
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: 146.45 E-value: 1.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 325 TFR-LSKLKLKLrssimsviYRKCLWVNTANRSGFSEGEIQTFMSVDADRIVNLcnSLHDLwsLPLQIGIALYLLYTQVk 403
Cdd:COG4987 83 TLRlLADLRVRL--------YRRLEPLAPAGLARLRSGDLLNRLVADVDALDNL--YLRVL--LPLLVALLVILAAVAF- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 404 FAFLS---------GLAITILLIPvnkWISVLIASATEKMMK-LKDERIRKTGELLTNIRTLKMYGWDNWFADWLKETRA 473
Cdd:COG4987 150 LAFFSpalalvlalGLLLAGLLLP---LLAARLGRRAGRRLAaARAALRARLTDLLQGAAELAAYGALDRALARLDAAEA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 474 TEVTHLATRKYLDAW--CVFFWATTPTLFSLCTFGLFALMGHQLD----AATVFTCLALFNslisplnsfpwVINGLIDA 547
Cdd:COG4987 227 RLAAAQRRLARLSALaqALLQLAAGLAVVAVLWLAAPLVAAGALSgpllALLVLAALALFE-----------ALAPLPAA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 548 FI-------STRRVSKflccLEHSRD---FSIDSGFTSEDLAVCVEDASCTWSSNVEEdynlTIKQVSLRVPKGSFVAVI 617
Cdd:COG4987 296 AQhlgrvraAARRLNE----LLDAPPavtEPAEPAPAPGGPSLELEDVSFRYPGAGRP----VLDGLSLTLPPGERVAIV 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 618 GEVGSGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQVPWLLSGTVRENILFGKPfDSKRyfETLSAc 684
Cdd:COG4987 368 GPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrdldeddlrrRIAVVPQRPHLFDTTLRENLRLARP-DATD--EELWA- 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 685 ALDvdislMVG-GDMAC---------IGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQVGCWILQraLLGP 754
Cdd:COG4987 444 ALE-----RVGlGDWLAalpdgldtwLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLA--DLLE 516
|
490 500 510
....*....|....*....|....*....|....*.
gi 1063701384 755 LLNKKTRVMCTHNIQAISCADMIVVMDKGKVNWSGS 790
Cdd:COG4987 517 ALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGT 552
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
592-790 |
2.13e-33 |
|
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: 128.88 E-value: 2.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 592 NVEEDYN---LTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQVP 655
Cdd:cd03254 7 NVNFSYDekkPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGVVLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 656 WLLSGTVRENILFGKPF-DSKRYFETLSACALDVDISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDV 734
Cdd:cd03254 87 FLFSGTIMENIRLGRPNaTDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063701384 735 LSAVDSQVGCwILQRALLgPLLNKKTRVMCTHNIQAISCADMIVVMDKGKVNWSGS 790
Cdd:cd03254 167 TSNIDTETEK-LIQEALE-KLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGT 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
595-785 |
3.46e-32 |
|
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: 125.01 E-value: 3.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 595 EDYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQVPWLLSGT 661
Cdd:cd03245 14 NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVPQDVTLFYGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 662 VRENILFGKPF-DSKRYFETLSACALDVDISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDS 740
Cdd:cd03245 94 LRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDM 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063701384 741 QVGCWILQRalLGPLLNKKTRVMCTHNIQAISCADMIVVMDKGKV 785
Cdd:cd03245 174 NSEERLKER--LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
594-785 |
5.27e-30 |
|
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: 119.26 E-value: 5.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 594 EEDYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNsLLGEMRCV-HGSILLNG-------------SVAYVPQVPWLLS 659
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVN-LIPRFYDVdSGRILIDGhdvrdytlaslrrQIGLVSQDVFLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 660 GTVRENILFGKPFDSKRYFETLS--ACALDVDISLMVGGDmACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSA 737
Cdd:cd03251 90 DTVAENIAYGRPGATREEVEEAAraANAHEFIMELPEGYD-TVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1063701384 738 VDSQVGCWIlQRAlLGPLLNKKTRVMCTHNIQAISCADMIVVMDKGKV 785
Cdd:cd03251 169 LDTESERLV-QAA-LERLMKNRTTFVIAHRLSTIENADRIVVLEDGKI 214
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
865-1143 |
2.97e-29 |
|
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: 118.51 E-value: 2.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 865 WFITIVILVSAVLMQGsrngNDLWLSYWVDK--TGKGVSHYSTSFYLMVLCIFCIINSILTLVRAFSFAFGGLKAAVHVH 942
Cdd:pfam00664 2 ILAILLAILSGAISPA----FPLVLGRILDVllPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 943 NALISKLINAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFILNILLANFVGLLGIIVVLSYVQVLFLLLLLPFWYIYSKL 1022
Cdd:pfam00664 78 RKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1023 QVFYRSTSRELRRLDSVSRSPIYASFTETLDGSSTIRAFKSEEHFVGRFIEHLTLYQRTSYSEIIASLWLSLRLQLLGSM 1102
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1063701384 1103 IVLFVAVMAVLGSGGNFPisfgTPGLVGLALSYAAPLVSLL 1143
Cdd:pfam00664 238 SYALALWFGAYLVISGEL----SVGDLVAFLSLFAQLFGPL 274
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
410-780 |
2.99e-29 |
|
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: 123.94 E-value: 2.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 410 LAITILLIPVnkwISVLIASATEKMMklkDERIRKTG-------ELLTNIRTLKMYGWDNWFADWLKET------RATEV 476
Cdd:TIGR02857 150 LLLTAPLIPI---FMILIGWAAQAAA---RKQWAALSrlsghflDRLRGLPTLKLFGRAKAQAAAIRRSseeyreRTMRV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 477 THLAtrkYLDAWCVFFWATTPTLFSLCTFGlFALMGHQLDAATVFTCLALfnsliSPlnsfpwvingliDAFISTRRVSK 556
Cdd:TIGR02857 224 LRIA---FLSSAVLELFATLSVALVAVYIG-FRLLAGDLDLATGLFVLLL-----AP------------EFYLPLRQLGA 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 557 FLccleHSRDFSIDS-----GFTSEDLAVCVEDASCTWS-------SNVEEDYNLT---IKQVSLRVPKGSFVAVIGEVG 621
Cdd:TIGR02857 283 QY----HARADGVAAaealfAVLDAAPRPLAGKAPVTAApasslefSGVSVAYPGRrpaLRPVSFTVPPGERVALVGPSG 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 622 SGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQVPWLLSGTVRENILFGKPFDSKRYF-ETLSACALD 687
Cdd:TIGR02857 359 AGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIAENIRLARPDASDAEIrEALERAGLD 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 688 VDISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQVGCWILQRalLGPLLNKKTRVMCTHN 767
Cdd:TIGR02857 439 EFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEA--LRALAQGRTVLLVTHR 516
|
410
....*....|...
gi 1063701384 768 IQAISCADMIVVM 780
Cdd:TIGR02857 517 LALAALADRIVVL 529
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
601-790 |
5.23e-29 |
|
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: 116.48 E-value: 5.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS-------------VAYVPQVPWLLSGTVRENIL 667
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIGLVSQEPVLFDGTIAENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 668 FGKPFDSKRyfETLSAC----ALDVDISLMVGGDMACiGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQVG 743
Cdd:cd03249 99 YGKPDATDE--EVEEAAkkanIHDFIMSLPDGYDTLV-GERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063701384 744 CWI---LQRALLGpllnkKTRVMCTHNIQAISCADMIVVMDKGKVNWSGS 790
Cdd:cd03249 176 KLVqeaLDRAMKG-----RTTIVIAHRLSTIRNADLIAVLQNGQVVEQGT 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
604-785 |
4.20e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 118.02 E-value: 4.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 604 VSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCvHGSILLNG-------------SVAYVPQVPWLLSGTVRENILFGK 670
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGielreldpeswrkHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 671 PFDSKRYFETL--SACALDVDISLMVGGDMAcIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQVGCWILQ 748
Cdd:PRK11174 448 PDASDEQLQQAleNAWVSEFLPLLPQGLDTP-IGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQ 526
|
170 180 190
....*....|....*....|....*....|....*..
gi 1063701384 749 RalLGPLLNKKTRVMCTHNIQAISCADMIVVMDKGKV 785
Cdd:PRK11174 527 A--LNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQI 561
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
598-785 |
1.51e-26 |
|
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: 107.30 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 598 NLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS-------------VAYVPQVPWLLSGTVRE 664
Cdd:cd03246 15 PPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGYLPQDDELFSGSIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 665 NIlfgkpfdskryfetlsacaldvdislmvggdmacigdkglnLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQvGC 744
Cdd:cd03246 95 NI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE-GE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1063701384 745 WILQRALLGPLLNKKTRVMCTHNIQAISCADMIVVMDKGKV 785
Cdd:cd03246 133 RALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
579-787 |
1.22e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 107.10 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 579 AVCVEDASCTWSSNVeedynlTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG--------SVAY 650
Cdd:COG1121 6 AIELENLTVSYGGRP------VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 651 VPQ---VPW---------LLSGTVRENILFGKPfdSKRYFETLSAcALDvdislMVG-GDMA--CIGDkglnLSGGQRAR 715
Cdd:COG1121 80 VPQraeVDWdfpitvrdvVLMGRYGRRGLFRRP--SRADREAVDE-ALE-----RVGlEDLAdrPIGE----LSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063701384 716 FALARAVYHGSDMYLLDDVLSAVDSQVgcwilQRALLGpLLNK-----KTRVMCTHNIQAIS-CADMIVVMDKGKVNW 787
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAAT-----EEALYE-LLRElrregKTILVVTHDLGAVReYFDRVLLLNRGLVAH 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
604-780 |
1.28e-25 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 106.40 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 604 VSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG--------SVAYVPQ----VPWLlsgTVRENILFGkp 671
Cdd:cd03293 23 ISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvtgpgpDRGYVFQqdalLPWL---TVLDNVALG-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 672 fdskryfetlsacaldVDISLMVGGD-----MACIGDKGL---------NLSGGQRARFALARAVYHGSDMYLLDDVLSA 737
Cdd:cd03293 98 ----------------LELQGVPKAEareraEELLELVGLsgfenayphQLSGGMRQRVALARALAVDPDVLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063701384 738 VDSQVgcwilqRALLGPLL------NKKTRVMCTHNI-QAISCADMIVVM 780
Cdd:cd03293 162 LDALT------REQLQEELldiwreTGKTVLLVTHDIdEAVFLADRVVVL 205
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
887-1165 |
1.44e-25 |
|
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: 108.07 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 887 LWLSYWVDKTGKGvSHYSTSFYLMVLCIFCIINSILTLVRAFSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRIL 966
Cdd:cd18559 20 LWLLLWFDDPVNG-PQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 967 NRFSSDLYTIDDSLPFILNILLANFVGLLGIIVVLSYVQVlFLLLLLPFWYIYSKLQVFYRSTSRELRRLDSVSRSPIYA 1046
Cdd:cd18559 99 NLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGP-MAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1047 SFTETLDGSSTIRAFKSEEHFvGRFIEHLTLYQRTSYSEIIASLWLSLRLQLLGSMIVLFVAVMAVLGSGGNfpisfgtP 1126
Cdd:cd18559 178 LFNETLLGISVIKAFEWEEAF-IRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHSL-------A 249
|
250 260 270
....*....|....*....|....*....|....*....
gi 1063701384 1127 GLVGLALSYAAPLVSLLGSLLTSFTETEKEMVSVERVLQ 1165
Cdd:cd18559 250 GLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLE 288
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
595-785 |
2.12e-25 |
|
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: 105.65 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 595 EDYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQVPWLLSGT 661
Cdd:cd03244 14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISIIPQDPVLFSGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 662 VRENI-LFGKPFDSKRYfETLSACALDVDISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDS 740
Cdd:cd03244 94 IRSNLdPFGEYSDEELW-QALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063701384 741 QVGCwILQRALLGPLLNkKTRVMCTHNIQAISCADMIVVMDKGKV 785
Cdd:cd03244 173 ETDA-LIQKTIREAFKD-CTVLTIAHRLDTIIDSDRILVLDKGRV 215
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
601-785 |
6.13e-25 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 104.62 E-value: 6.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQVPWLLSGTVRENIL 667
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVVPQDTVLFNDTIGYNIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 668 FGKPFDSK-RYFETLSACALDVDISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQVGCWI 746
Cdd:cd03253 97 YGRPDATDeEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREI 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 1063701384 747 LQRalLGPLLNKKTRVMCTHNIQAISCADMIVVMDKGKV 785
Cdd:cd03253 177 QAA--LRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRI 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
601-783 |
7.45e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 105.17 E-value: 7.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG--------SVAYVPQ----VPWLlsgTVRENILF 668
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpDRGVVFQepalLPWL---TVLDNVAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 669 GKPFD--SKRYFETLSACALDvdislMVGgdmacigdkgL---------NLSGGQRARFALARAVYHGSDMYLLDDVLSA 737
Cdd:COG1116 104 GLELRgvPKAERRERARELLE-----LVG----------LagfedayphQLSGGMRQRVAIARALANDPEVLLMDEPFGA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063701384 738 VDSQVgcwilqRALLGPLL------NKKTRVMCTHNIQ-AISCADMIVVMDKG 783
Cdd:COG1116 169 LDALT------RERLQDELlrlwqeTGKTVLFVTHDVDeAVFLADRVVVLSAR 215
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
304-767 |
1.13e-24 |
|
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: 109.76 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 304 YTLAISLGFISIFKSFLdtQYTFRLSKLKLKLRS--SIMSVIYRKCLWVNTANRSGFSEGEIQTFMSVDADrivnlcnSL 381
Cdd:TIGR02868 53 SVAAVAVRAFGIGRAVF--RYLERLVGHDAALRSlgALRVRVYERLARQALAGRRRLRRGDLLGRLGADVD-------AL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 382 HDLWS---LPLQIGIALYLLYTQVKFAFLS--------GLAITILLIPvnkWISVLIASATEKMMK-LKDERIRKTGELL 449
Cdd:TIGR02868 124 QDLYVrviVPAGVALVVGAAAVAAIAVLSVpaalilaaGLLLAGFVAP---LVSLRAARAAEQALArLRGELAAQLTDAL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 450 TNIRTLKMYGWDNWF--------ADWLK-ETRATEVTHLATrkyldawCVFFWATTPTLFSLCTFGLFALMGHQLDAAT- 519
Cdd:TIGR02868 201 DGAAELVASGALPAAlaqveeadRELTRaERRAAAATALGA-------ALTLLAAGLAVLGALWAGGPAVADGRLAPVTl 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 520 ---VFTCLALFNslisPLNSFPWVINGLIDAFISTRRVSKFLcclEHSRDFSIDSGFTSEDLAV-----CVEDASCTWss 591
Cdd:TIGR02868 274 avlVLLPLAAFE----AFAALPAAAQQLTRVRAAAERIVEVL---DAAGPVAEGSAPAAGAVGLgkptlELRDLSAGY-- 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 592 nveEDYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS-------------VAYVPQVPWLL 658
Cdd:TIGR02868 345 ---PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVpvssldqdevrrrVSVCAQDAHLF 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 659 SGTVRENILFGKP-FDSKRYFETLSACALDVDISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSA 737
Cdd:TIGR02868 422 DTTVRENLRLARPdATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEH 501
|
490 500 510
....*....|....*....|....*....|
gi 1063701384 738 VDSQVGCWILqRALLGPlLNKKTRVMCTHN 767
Cdd:TIGR02868 502 LDAETADELL-EDLLAA-LSGRTVVLITHH 529
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
601-794 |
1.14e-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: 104.36 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQ---VPWLLsgTVRE 664
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAYVPQeppAPFGL--TVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 665 NILFG-KPFdsKRYFETLSAC-------ALD-VDISlmvggDMAcigDKGLN-LSGGQRARFALARAVYHGSDMYLLDDV 734
Cdd:COG1120 95 LVALGrYPH--LGLFGRPSAEdreaveeALErTGLE-----HLA---DRPVDeLSGGERQRVLIARALAQEPPLLLLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063701384 735 LSAVD--SQVGCW-ILQRallgplLNK---KTRVMCTHNI-QAISCADMIVVMDKGKVNWSGSVTDM 794
Cdd:COG1120 165 TSHLDlaHQLEVLeLLRR------LARergRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
598-785 |
1.37e-24 |
|
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: 109.84 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 598 NLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQVPWLLSGTVRE 664
Cdd:COG4618 345 RPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGadlsqwdreelgrHIGYLPQDVELFDGTIAE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 665 NI-LFGKPfDSKRYFETlsACALDVDislmvggDMAC---------IGDKGLNLSGGQRARFALARAVYHGSDMYLLDDV 734
Cdd:COG4618 425 NIaRFGDA-DPEKVVAA--AKLAGVH-------EMILrlpdgydtrIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1063701384 735 LSAVDSQvGCWILQRALLGPLLNKKTRVMCTHNIQAISCADMIVVMDKGKV 785
Cdd:COG4618 495 NSNLDDE-GEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
596-790 |
4.56e-24 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 102.18 E-value: 4.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 596 DYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQVPWLLSGTV 662
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 663 RENILFGKPFDSKRYFETLSACALDVD-ISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQ 741
Cdd:cd03252 93 RDNIALADPGMSMERVIEAAKLAGAHDfISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063701384 742 VGCWILQRalLGPLLNKKTRVMCTHNIQAISCADMIVVMDKGKVNWSGS 790
Cdd:cd03252 173 SEHAIMRN--MHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGS 219
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
601-789 |
1.50e-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: 99.90 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-----------SVAYVPQ----VPWLlsgTVREN 665
Cdd:cd03259 16 LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvtgvpperrNIGMVFQdyalFPHL---TVAEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 666 ILFG-----KPFDSKRyfETLSACALDVDISLMvggdmacIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDS 740
Cdd:cd03259 93 IAFGlklrgVPKAEIR--ARVRELLELVGLEGL-------LNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063701384 741 QvgcwiLQRALLGPLLN-----KKTRVMCTHNIQ-AISCADMIVVMDKGKVNWSG 789
Cdd:cd03259 164 K-----LREELREELKElqrelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
601-787 |
1.55e-23 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 99.92 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG--------SVAYVPQ---VPWLLSGTVRENILFG 669
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQrrsIDRDFPISVRDVVLMG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 670 kPFDSKRYFETLS-ACALDVDISL-MVG-GDMA--CIGdkglNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQVgc 744
Cdd:cd03235 95 -LYGHKGLFRRLSkADKAKVDEALeRVGlSELAdrQIG----ELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKT-- 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063701384 745 wilQRALLGpLLNK-----KTRVMCTHNIQAIS-CADMIVVMDKGKVNW 787
Cdd:cd03235 168 ---QEDIYE-LLRElrregMTILVVTHDLGLVLeYFDRVLLLNRTVVAS 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
601-733 |
5.75e-23 |
|
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: 96.18 E-value: 5.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQVPWLLSG-TVRENI 666
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063701384 667 LFGKPFdsKRYFETLSACALDVDISLMVGGDMA--CIGDKGLNLSGGQRARFALARAVYHGSDMYLLDD 733
Cdd:pfam00005 81 RLGLLL--KGLSKREKDARAEEALEKLGLGDLAdrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
601-790 |
2.30e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 102.98 E-value: 2.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQVPWLLSGTVRENIL 667
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiadyseaalrqAISVVSQRVHLFSATLRDNLL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 668 FGKPFDSKryfETLSACALDVDISLMVGGDM---ACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQVGC 744
Cdd:PRK11160 436 LAAPNASD---EALIEVLQQVGLEKLLEDDKglnAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETER 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063701384 745 WILQrallgpLLNK----KTRVMCTHNIQAISCADMIVVMDKGKVNWSGS 790
Cdd:PRK11160 513 QILE------LLAEhaqnKTVLMITHRLTGLEQFDRICVMDNGQIIEQGT 556
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
907-1167 |
6.24e-22 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 101.78 E-value: 6.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 907 FYLMVLCIFCIINSILTLVRAFSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFILNI 986
Cdd:COG1132 62 LLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 987 LLANFVGLLGIIVVLSYVQVL----FLLLLLPFWYIYSKLQVFYRSTSRELRRldsvSRSPIYASFTETLDGSSTIRAFK 1062
Cdd:COG1132 142 LVRSVVTLIGALVVLFVIDWRlaliVLLVLPLLLLVLRLFGRRLRKLFRRVQE----ALAELNGRLQESLSGIRVVKAFG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1063 SEEHFVGRFIEHLTLYQRTSYSEIIASlwlslRLQLLGSMIVLFVAVMAVLGSGGNFpISFG--TPGLVGLALSYAAPLV 1140
Cdd:COG1132 218 REERELERFREANEELRRANLRAARLS-----ALFFPLMELLGNLGLALVLLVGGLL-VLSGslTVGDLVAFILYLLRLF 291
|
250 260
....*....|....*....|....*..
gi 1063701384 1141 SLLGSLLTSFTETEKEMVSVERVLQVM 1167
Cdd:COG1132 292 GPLRQLANVLNQLQRALASAERIFELL 318
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
601-794 |
6.65e-22 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 95.90 E-value: 6.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG------------SVAYVPQVPWLLSG-TVRENI- 666
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALYPDlTVRENLr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 667 ----LFGKPFDS--KRYFETLSACALDVDISLMVGgdmacigdkglNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDS 740
Cdd:COG1131 96 ffarLYGLPRKEarERIDELLELFGLTDAADRKVG-----------TLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063701384 741 QVGCWIlqRALLGPLLNK-KTRVMCTHNIQ-AISCADMIVVMDKGKVNWSGSVTDM 794
Cdd:COG1131 165 EARREL--WELLRELAAEgKTVLLSTHYLEeAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
594-789 |
1.86e-21 |
|
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: 92.76 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 594 EEDYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS------------VAYVPQVPWLLSGT 661
Cdd:cd03247 11 PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVLNQRPYLFDTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 662 VRENIlfgkpfdskryfetlsacaldvdislmvggdmacigdkGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSq 741
Cdd:cd03247 91 LRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDP- 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1063701384 742 vgcwILQRALLGPL---LNKKTRVMCTHNIQAISCADMIVVMDKGKVNWSG 789
Cdd:cd03247 132 ----ITERQLLSLIfevLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
599-785 |
2.48e-21 |
|
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: 94.07 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 599 LTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS-------------VAYVPQVPWLLSGTVREN 665
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVSLVGQEPVLFARSLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 666 ILFG---KPFDskRYFETLSACALDVDISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQV 742
Cdd:cd03248 108 IAYGlqsCSFE--CVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1063701384 743 GCWILQRALLGPllNKKTRVMCTHNIQAISCADMIVVMDKGKV 785
Cdd:cd03248 186 EQQVQQALYDWP--ERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
601-785 |
4.53e-21 |
|
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: 91.73 E-value: 4.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS-------------VAYVPQVpwllsgtvrenil 667
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaslspkelarkIAYVPQA------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 668 fgkpfdskryfetLSACaldvdislmvggDMACIGDKGLN-LSGGQRARFALARAVYHGSDMYLLDDVLSAVDsqVGCwi 746
Cdd:cd03214 82 -------------LELL------------GLAHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLD--IAH-- 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063701384 747 lQRALLGPL--LNK---KTRVMCTHNI-QAISCADMIVVMDKGKV 785
Cdd:cd03214 133 -QIELLELLrrLARergKTVVMVLHDLnLAARYADRVILLKDGRI 176
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
598-793 |
6.38e-21 |
|
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: 93.38 E-value: 6.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 598 NLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG------------SVAYVPQVPWLLSG-TVRE 664
Cdd:COG4555 14 VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPDERGLYDRlTVRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 665 NIlfgkpfdskRYFETL-----SACALDVD--ISLMvggDMACIGDKGL-NLSGGQRARFALARAVYHGSDMYLLDDVLS 736
Cdd:COG4555 94 NI---------RYFAELyglfdEELKKRIEelIELL---GLEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 737 AVDSQVGCWILQ--RALLGPllnKKTRVMCTHNIQAISC-ADMIVVMDKGKVNWSGSVTD 793
Cdd:COG4555 162 GLDVMARRLLREilRALKKE---GKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDE 218
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
897-1167 |
1.10e-20 |
|
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: 94.48 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 897 GKGVSHYSTSFYLMVLCIFCIINSILTL--VRAFSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFSSDLY 974
Cdd:cd18600 59 TYAVIVTFTSSYYVFYIYVGVADSLLAMgfFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 975 TIDDSLPFILNILLANFVGLLGIIVVLSYVQVLFLLLLLPFWYIYSKLQVFYRSTSRELRRLDSVSRSPIYASFTETLDG 1054
Cdd:cd18600 139 ILDDLLPLTIFDFIQLFLIVIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1055 SSTIRAFKSEEHFVGRFIEHLTLYQRTSYSEIIASLWLSLRLQLLGSMIVLFVAVMAVLGSGGNfpisfgtPGLVGLALS 1134
Cdd:cd18600 219 LWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIGTTGDG-------EGRVGIILT 291
|
250 260 270
....*....|....*....|....*....|...
gi 1063701384 1135 YAAPLVSLLGSLLTSFTETEKEMVSVERVLQVM 1167
Cdd:cd18600 292 LAMNIMSTLQWAVNTSIDVDSLMRSVSRIFKFI 324
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
601-785 |
1.70e-20 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 91.47 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSL-----LGEMRCVHGSILLNGS---------------VAYVPQVPWLLSG 660
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKdiydldvdvlelrrrVGMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 661 TVRENILFGKPF---DSKRYFETLSACALDvdislMVG-----GDMAcigdKGLNLSGGQRARFALARAVYHGSDMYLLD 732
Cdd:cd03260 96 SIYDNVAYGLRLhgiKLKEELDERVEEALR-----KAAlwdevKDRL----HALGLSGGQQQRLCLARALANEPEVLLLD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063701384 733 DVLSAVDSqvgcwILQRA---LLGPLLNKKTRVMCTHNI-QAISCADMIVVMDKGKV 785
Cdd:cd03260 167 EPTSALDP-----ISTAKieeLIAELKKEYTIVIVTHNMqQAARVADRTAFLLNGRL 218
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
576-785 |
3.31e-20 |
|
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: 90.16 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 576 EDLAVCVEDASCTWSSNVEEdynlTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG--------- 646
Cdd:cd03369 3 EHGEIEVENLSVRYAPDLPP----VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistiple 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 647 ----SVAYVPQVPWLLSGTVRENI-LFGKpFDSKRYFETLSacaldvdislmvggdmacIGDKGLNLSGGQRARFALARA 721
Cdd:cd03369 79 dlrsSLTIIPQDPTLFSGTIRSNLdPFDE-YSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063701384 722 VYHGSDMYLLDDVLSAVDSQVGCWIlQRALLgPLLNKKTRVMCTHNIQAISCADMIVVMDKGKV 785
Cdd:cd03369 140 LLKRPRVLVLDEATASIDYATDALI-QKTIR-EEFTNSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
591-784 |
6.33e-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: 88.40 E-value: 6.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 591 SNVEEDYN--LTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG---------------SVAYVPQ 653
Cdd:cd03229 4 KNVSKRYGqkTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelpplrrRIGMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 654 VPWLLSG-TVRENILFGkpfdskryfetlsacaldvdislmvggdmacigdkglnLSGGQRARFALARAVYHGSDMYLLD 732
Cdd:cd03229 84 DFALFPHlTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063701384 733 DVLSAVDSQVgcwilqRALLGPLLNK------KTRVMCTHNI-QAISCADMIVVMDKGK 784
Cdd:cd03229 126 EPTSALDPIT------RREVRALLKSlqaqlgITVVLVTHDLdEAARLADRVVVLRDGK 178
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
601-785 |
6.98e-20 |
|
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: 89.47 E-value: 6.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-----------------SVAYVPQVPWLLSG-TV 662
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdisklsekelaafrrrHIGFVFQSFNLLPDlTA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 663 RENILFGKPFDSKRYFEtlsacALDVDISLMvggDMACIGDKgLN-----LSGGQRARFALARAVYHGSDMYLLDDVLSA 737
Cdd:cd03255 100 LENVELPLLLAGVPKKE-----RRERAEELL---ERVGLGDR-LNhypseLSGGQQQRVAIARALANDPKIILADEPTGN 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063701384 738 VDSQVGCWILQraLLGPLLNK--KTRVMCTHNIQAISCADMIVVMDKGKV 785
Cdd:cd03255 171 LDSETGKEVME--LLRELNKEagTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
893-1163 |
8.04e-20 |
|
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: 91.08 E-value: 8.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 893 VDKTGKGVSHYSTSFYLMVLCIFCIINSILTLVRAFSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFSSD 972
Cdd:cd18557 23 IDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 973 LYTIDDSLPFILNILLANF---VGLLGIIVVLSYVQVLFLLLLLPfwyIYSKLQVFYRSTSRELRR--LDSVSRSPIYAS 1047
Cdd:cd18557 103 TSVLQSAVTDNLSQLLRNIlqvIGGLIILFILSWKLTLVLLLVIP---LLLIASKIYGRYIRKLSKevQDALAKAGQVAE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1048 ftETLDGSSTIRAFKSEEHFVGRFIEHLTLYQRTSYSEIIASlwlslRLQLLGSMIVLFVAVMAVLGSGGNFpISFG--T 1125
Cdd:cd18557 180 --ESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALAN-----ALFQGITSLLIYLSLLLVLWYGGYL-VLSGqlT 251
|
250 260 270
....*....|....*....|....*....|....*....
gi 1063701384 1126 PG-LVGLALsYAAPLVSLLGSLLTSFTETEKEMVSVERV 1163
Cdd:cd18557 252 VGeLTSFIL-YTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
270-534 |
1.08e-19 |
|
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: 90.39 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 270 GLLKVFNDCIGFAGPLLLNRLIKYLEKGSGSSVGYTLAISLGFIS--IFKSFLDTQYTFRLSKLKLKLRSSIMSVIYRKC 347
Cdd:pfam00664 5 ILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLlgLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 348 LWVNTANRSGFSEGEIQTFMSVDADRIVNLCNSLHDLWSLPLQIGIALYLL--YTQVKFAfLSGLAITILLIPVNKWISV 425
Cdd:pfam00664 85 LRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVmfYYGWKLT-LVLLAVLPLYILVSAVFAK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 426 LIASATEKMMKLKDERIRKTGELLTNIRTLKMYGWDNWFADWLKEtrATEVTHLATRKYLDAWCVFF---WATTPTLFSL 502
Cdd:pfam00664 164 ILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDK--ALEEALKAGIKKAVANGLSFgitQFIGYLSYAL 241
|
250 260 270
....*....|....*....|....*....|...
gi 1063701384 503 CT-FGLFALMGHQLDAATVFTCLALFNSLISPL 534
Cdd:pfam00664 242 ALwFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
601-739 |
1.15e-19 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 88.72 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQVPWLLSGTVRENIL 667
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYVPQEPALWGGTVRDNLP 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063701384 668 F-----GKPFDSKRYFETLSACALDVDIsLmvggdmacigDKGL-NLSGGQRARFALARAVYHGSDMYLLDDVLSAVD 739
Cdd:COG4619 96 FpfqlrERKFDRERALELLERLGLPPDI-L----------DKPVeRLSGGERQRLALIRALLLQPDVLLLDEPTSALD 162
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
598-785 |
3.20e-19 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 93.24 E-value: 3.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 598 NLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQVPWLLSGTVRE 664
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsslshsvlrqGVAMVQQDPVVLADTFLA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 665 NILFGKPFDSKRYFETLSACALDVDISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQVGC 744
Cdd:PRK10790 434 NVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQ 513
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1063701384 745 WIlQRAlLGPLLNKKTRVMCTHNIQAISCADMIVVMDKGKV 785
Cdd:PRK10790 514 AI-QQA-LAAVREHTTLVVIAHRLSTIVEADTILVLHRGQA 552
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
598-785 |
4.49e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 92.77 E-value: 4.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 598 NLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQVPWLLSGTVRE 664
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlaslrnQVALVSQNVHLFNDTIAN 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 665 NILFG-KPFDSKRYFETLS--ACALDVdISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQ 741
Cdd:PRK11176 436 NIAYArTEQYSREQIEEAArmAYAMDF-INKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTE 514
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063701384 742 VGCWIlQRAlLGPLLNKKTRVMCTHNIQAISCADMIVVMDKGKV 785
Cdd:PRK11176 515 SERAI-QAA-LDELQKNRTSLVIAHRLSTIEKADEILVVEDGEI 556
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
250-785 |
7.41e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 92.48 E-value: 7.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 250 STPSLIWSIYGVYG--WPYFRLGLLKVFNDCIG-FAGPLLLNRLIKYLeKGSGSSVGYTLAI-SLGFISIFKSFL----D 321
Cdd:TIGR00958 144 ETADLLFRLLGLSGrdWPWLISAFVFLTLSSLGeMFIPFYTGRVIDTL-GGDKGPPALASAIfFMCLLSIASSVSaglrG 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 322 TQYTFRLSKLKLKLRSSIMSVIYRKCLWVNTANRSGfsegEIQTFMSVDADrivNLCNSLHD-----LWSLPLQIGIALY 396
Cdd:TIGR00958 223 GSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTG----ELTSRLSSDTQ---TMSRSLSLnvnvlLRNLVMLLGLLGF 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 397 LLYTQVKFAFLSGLAITILLIpVNKWISVLIASATEKMmklkDERIRKTG----ELLTNIRTLKMYGWDNWFADWLKEtR 472
Cdd:TIGR00958 296 MLWLSPRLTMVTLINLPLVFL-AEKVFGKRYQLLSEEL----QEAVAKANqvaeEALSGMRTVRSFAAEEGEASRFKE-A 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 473 ATEVTHLATRKYLdAWCVFFWATtptlfSLCTFGLFALM----GHQLDAATV----FTCLALFN-SLISPLNSFPWVING 543
Cdd:TIGR00958 370 LEETLQLNKRKAL-AYAGYLWTT-----SVLGMLIQVLVlyygGQLVLTGKVssgnLVSFLLYQeQLGEAVRVLSYVYSG 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 544 LIDAFISTRRVSKFLcclEHSRDFSIDSGFTSEDLAVCVE--DASCTWSSNVEedyNLTIKQVSLRVPKGSFVAVIGEVG 621
Cdd:TIGR00958 444 MMQAVGASEKVFEYL---DRKPNIPLTGTLAPLNLEGLIEfqDVSFSYPNRPD---VPVLKGLTFTLHPGEVVALVGPSG 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 622 SGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQVPWLLSGTVRENILFGKPF--DSKRYFETLSACAL 686
Cdd:TIGR00958 518 SGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVALVGQEPVLFSGSVRENIAYGLTDtpDEEIMAAAKAANAH 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 687 DVdISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQVgcwilqRALLGPLLNKKTR--VMC 764
Cdd:TIGR00958 598 DF-IMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC------EQLLQESRSRASRtvLLI 670
|
570 580
....*....|....*....|.
gi 1063701384 765 THNIQAISCADMIVVMDKGKV 785
Cdd:TIGR00958 671 AHRLSTVERADQILVLKKGSV 691
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
601-784 |
1.69e-18 |
|
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: 83.83 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGsvayvpqvpwllsgtvrENILFGKPFDSKRyfet 680
Cdd:cd00267 15 LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG-----------------KDIAKLPLEELRR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 681 lsacaldvDISLMVGgdmacigdkglnLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQVGcWILQRALLGPLLNKKT 760
Cdd:cd00267 74 --------RIGYVPQ------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR-ERLLELLRELAEEGRT 132
|
170 180
....*....|....*....|....*
gi 1063701384 761 RVMCTHNI-QAISCADMIVVMDKGK 784
Cdd:cd00267 133 VIIVTHDPeLAELAADRVIVLKDGK 157
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
601-785 |
2.60e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 90.16 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLL-------GEMRcVHGSIL-------LNGSVAYVPQVPWLLSGTVRENI 666
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQrhfdvseGDIR-FHDIPLtklqldsWRSRLAVVSQTPFLFSDTVANNI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 667 LFGKPFDSKRYFETLS--ACALDvDISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQVGC 744
Cdd:PRK10789 410 ALGRPDATQQEIEHVArlASVHD-DILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEH 488
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1063701384 745 WILQRalLGPLLNKKTRVMCTHNIQAISCADMIVVMDKGKV 785
Cdd:PRK10789 489 QILHN--LRQWGEGRTVIISAHRLSALTEASEILVMQHGHI 527
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
601-785 |
3.33e-18 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 83.22 E-value: 3.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG------------SVAYVPQVPWLLSG-TVRENil 667
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGkdikkepeevkrRIGYLPEEPSLYENlTVREN-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 668 fgkpfdskryfetlsacaldvdislmvggdmacigdkgLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDsqvgcwIL 747
Cdd:cd03230 94 --------------------------------------LKLSGGMKQRLALAQALLHDPELLILDEPTSGLD------PE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063701384 748 QRALLGPLLNK-----KTRVMCTHNIQ-AISCADMIVVMDKGKV 785
Cdd:cd03230 130 SRREFWELLRElkkegKTILLSSHILEeAERLCDRVAILNNGRI 173
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
602-785 |
8.57e-18 |
|
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: 84.08 E-value: 8.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 602 KQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS-------------VAYVPQVPwLLS----GTVRE 664
Cdd:COG1124 22 KDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRpvtrrrrkafrrrVQMVFQDP-YASlhprHTVDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 665 NI-----LFGKPFDSKRYFETLSACALDVDIslmvggdmacigdkgLN-----LSGGQRARFALARAVYHGSDMYLLDDV 734
Cdd:COG1124 101 ILaeplrIHGLPDREERIAELLEQVGLPPSF---------------LDryphqLSGGQRQRVAIARALILEPELLLLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063701384 735 LSAVDSqvgcwILQRALLGpLLN--KKTR----VMCTHNIQAISC-ADMIVVMDKGKV 785
Cdd:COG1124 166 TSALDV-----SVQAEILN-LLKdlREERgltyLFVSHDLAVVAHlCDRVAVMQNGRI 217
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
601-785 |
1.83e-17 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 85.53 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-----------SVAYVPQ----VPWLlsgTVREN 665
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGrdvtglppekrNVGMVFQdyalFPHL---TVAEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 666 ILFG-------KPFDSKRYFETLSacaldvdislMVG-GDMAciGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSA 737
Cdd:COG3842 98 VAFGlrmrgvpKAEIRARVAELLE----------LVGlEGLA--DRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063701384 738 VD----SQVGCWI--LQRALlgpllnKKTRVMCTHNiQ--AISCADMIVVMDKGKV 785
Cdd:COG3842 166 LDaklrEEMREELrrLQREL------GITFIYVTHD-QeeALALADRIAVMNDGRI 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
602-793 |
3.22e-17 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 84.43 E-value: 3.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 602 KQVSLRVPKGSFVAVIGEVGSGKTSLLnsllgemRCV-------HGSILLNG------------SVAYVPQ----VPWLl 658
Cdd:COG1118 19 DDVSLEIASGELVALLGPSGSGKTTLL-------RIIagletpdSGRIVLNGrdlftnlpprerRVGFVFQhyalFPHM- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 659 sgTVRENILFG----KPFDS---KRYFETLSAcaldVDISlmvggdmacigdkGL------NLSGGQRARFALARAVYHG 725
Cdd:COG1118 91 --TVAENIAFGlrvrPPSKAeirARVEELLEL----VQLE-------------GLadrypsQLSGGQRQRVALARALAVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063701384 726 SDMYLLDDVLSAVDSQVGcWILqRALLGPLLNK--KTRVMCTHNIQ-AISCADMIVVMDKGKVNWSGSVTD 793
Cdd:COG1118 152 PEVLLLDEPFGALDAKVR-KEL-RRWLRRLHDElgGTTVFVTHDQEeALELADRVVVMNQGRIEQVGTPDE 220
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
579-789 |
4.93e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 82.62 E-value: 4.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 579 AVCVEDASCTWSSNveedyNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS----------V 648
Cdd:PRK15056 6 GIVVNDVTVTWRNG-----HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 649 AYVPQ---VPWLLSGTVRENILFGK-------PFDSKRYFETLSACALDVDislMVGGDMACIGDkglnLSGGQRARFAL 718
Cdd:PRK15056 81 AYVPQseeVDWSFPVLVEDVVMMGRyghmgwlRRAKKRDRQIVTAALARVD---MVEFRHRQIGE----LSGGQKKRVFL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063701384 719 ARAVYHGSDMYLLDDVLSAVDSQVGCWILqrALLGPLLNK-KTRVMCTHNIQAISCADMIVVMDKGKVNWSG 789
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTEARII--SLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
601-785 |
4.99e-17 |
|
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: 81.40 E-value: 4.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG----------------SVAYVPQ------VPWLl 658
Cdd:cd03257 21 LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirrkEIQMVFQdpmsslNPRM- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 659 sgTVRENILfgKPF-----DSKRYFETLSACALDVdislMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDD 733
Cdd:cd03257 100 --TIGEQIA--EPLrihgkLSKKEARKEAVLLLLV----GVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063701384 734 VLSAVDSqvgcwILQRALLgPLLNK------KTRVMCTHNIQAIS-CADMIVVMDKGKV 785
Cdd:cd03257 172 PTSALDV-----SVQAQIL-DLLKKlqeelgLTLLFITHDLGVVAkIADRVAVMYAGKI 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
591-797 |
5.24e-17 |
|
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: 81.51 E-value: 5.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 591 SNVEEDYN--LTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-SVAYVP----QV--------- 654
Cdd:cd03300 4 ENVSKFYGgfVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkDITNLPphkrPVntvfqnyal 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 655 -PWLlsgTVRENILFG-----KPFDS--KRYFETLSacaldvdislMVGgdMACIGDKGLN-LSGGQRARFALARAVYHG 725
Cdd:cd03300 84 fPHL---TVFENIAFGlrlkkLPKAEikERVAEALD----------LVQ--LEGYANRKPSqLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 726 SDMYLLDDVLSAVDSQVGCWI------LQRALlgpllnKKTRVMCTHNIQ-AISCADMIVVMDKGKVNWSGS---VTDMP 795
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMqlelkrLQKEL------GITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTpeeIYEEP 222
|
..
gi 1063701384 796 KS 797
Cdd:cd03300 223 AN 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
601-785 |
7.38e-17 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 80.86 E-value: 7.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-----------------SVAYVPQ----VPWLls 659
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdisslserelarlrrrHIGFVFQffnlLPEL-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 660 gTVRENILF-----GKPF--DSKRYFETLSacaldvdislMVGgdmacIGDKgLN-----LSGGQRARFALARAVYHGSD 727
Cdd:COG1136 102 -TALENVALplllaGVSRkeRRERARELLE----------RVG-----LGDR-LDhrpsqLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063701384 728 MYLLDDVLSAVDSQVGCWILQrALLGplLNK---KTRVMCTHNIQAISCADMIVVMDKGKV 785
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLE-LLRE--LNRelgTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
908-1075 |
1.42e-16 |
|
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: 81.44 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 908 YLMVLCIFCIINSILTLVRAFSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFILNIL 987
Cdd:cd18572 38 AVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 988 LANFVGLLGIIVVLSYVQ----VLFLLLLLPFWYIYSKLQVFYRSTSRELRrlDSVSRSPIYAsfTETLDGSSTIRAFKS 1063
Cdd:cd18572 118 LRNLVQLVGGLAFMFSLSwrltLLAFITVPVIALITKVYGRYYRKLSKEIQ--DALAEANQVA--EEALSNIRTVRSFAT 193
|
170
....*....|..
gi 1063701384 1064 EEHFVGRFIEHL 1075
Cdd:cd18572 194 EEREARRYERAL 205
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
908-1163 |
1.55e-16 |
|
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: 81.44 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 908 YLMVLCIFCIINSILTLVRAFSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFILNIL 987
Cdd:cd07346 41 IALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 988 LANFVGLLGIIVVLSYVQVL---FLLLLLPF-WYIYSKLQVFYRSTSRELRRldsvSRSPIYASFTETLDGSSTIRAFKS 1063
Cdd:cd07346 121 LSDVLTLIGALVILFYLNWKltlVALLLLPLyVLILRYFRRRIRKASREVRE----SLAELSAFLQESLSGIRVVKAFAA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1064 EEHFVGRFIEHLTLYQRTSYSEIIASLWLSLRlqllgSMIVLFVAVMAVLGSGGNFPISfG--TPGLVGLALSYAAPLVS 1141
Cdd:cd07346 197 EEREIERFREANRDLRDANLRAARLSALFSPL-----IGLLTALGTALVLLYGGYLVLQ-GslTIGELVAFLAYLGMLFG 270
|
250 260
....*....|....*....|..
gi 1063701384 1142 LLGSLLTSFTETEKEMVSVERV 1163
Cdd:cd07346 271 PIQRLANLYNQLQQALASLERI 292
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
601-785 |
2.09e-16 |
|
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: 79.68 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQVPW--LLSGTVREN 665
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknlrelrrKVGLVFQNPDdqLFAPTVEED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 666 ILFG-----KPFD--SKRYFETLSACALDvdislmvggDMAcigDKG-LNLSGGQRARFALARAVYHGSDMYLLDDVLSA 737
Cdd:COG1122 97 VAFGpenlgLPREeiRERVEEALELVGLE---------HLA---DRPpHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063701384 738 VDSQVGCWILQrallgpLLNK-----KTRVMCTHNIQ-AISCADMIVVMDKGKV 785
Cdd:COG1122 165 LDPRGRRELLE------LLKRlnkegKTVIIVTHDLDlVAELADRVIVLDDGRI 212
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
591-797 |
2.28e-16 |
|
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: 80.08 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 591 SNVEEDYN--LTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-----------SVAYVPQVPWL 657
Cdd:cd03296 6 RNVSKRFGdfVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatdvpvqerNVGFVFQHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 658 LSG-TVRENILFGkpFDSKRYFETLSACALD---VDISLMVGGDMacIGDKGLN-LSGGQRARFALARAVYHGSDMYLLD 732
Cdd:cd03296 86 FRHmTVFDNVAFG--LRVKPRSERPPEAEIRakvHELLKLVQLDW--LADRYPAqLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063701384 733 DVLSAVDSQVgcwilqRALLGPLLNK------KTRVMCTHNI-QAISCADMIVVMDKGKVNWSGS---VTDMPKS 797
Cdd:cd03296 162 EPFGALDAKV------RKELRRWLRRlhdelhVTTVFVTHDQeEALEVADRVVVMNKGRIEQVGTpdeVYDHPAS 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
600-794 |
2.47e-16 |
|
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: 83.41 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 600 TIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRC---VHGSILLNG-------------SVAYVPQVPW--LLSGT 661
Cdd:COG1123 21 AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGrdllelsealrgrRIGMVFQDPMtqLNPVT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 662 VRENILFGkpfdsKRYFETLSACALDVDISLMVGGDMACIGDKGLN-LSGGQRARFALARAVYHGSDMYLLDDVLSAVDS 740
Cdd:COG1123 101 VGDQIAEA-----LENLGLSRAEARARVLELLEAVGLERRLDRYPHqLSGGQRQRVAIAMALALDPDLLIADEPTTALDV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063701384 741 QVGCWILqrALLGPLLNK--KTRVMCTHNIQAISC-ADMIVVMDKGKVNWSGSVTDM 794
Cdd:COG1123 176 TTQAEIL--DLLRELQRErgTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEI 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
601-785 |
3.10e-16 |
|
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: 83.41 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG----------------SVAYVPQ------VPWLl 658
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkdltklsrrslrelrrRVQMVFQdpysslNPRM- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 659 sgTVRENILFG----KPFDS----KRYFETLSACALDVDIslmvggdmacigdkgLN-----LSGGQRARFALARAVYHG 725
Cdd:COG1123 360 --TVGDIIAEPlrlhGLLSRaerrERVAELLERVGLPPDL---------------ADrypheLSGGQRQRVAIARALALE 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063701384 726 SDMYLLDDVLSAVDSQVgcwilQRALLGpLLNK------KTRVMCTHNIQAISC-ADMIVVMDKGKV 785
Cdd:COG1123 423 PKLLILDEPTSALDVSV-----QAQILN-LLRDlqrelgLTYLFISHDLAVVRYiADRVAVMYDGRI 483
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
582-784 |
3.30e-16 |
|
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: 78.66 E-value: 3.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 582 VEDASCTWSSNVEEdynlTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-------------SV 648
Cdd:cd03225 2 LKNLSFSYPDGARP----ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelrrKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 649 AYVPQVP--WLLSGTVRENILFG-------KPFDSKRYFETLSACAL----DVDISlmvggdmacigdkglNLSGGQRAR 715
Cdd:cd03225 78 GLVFQNPddQFFGPTVEEEVAFGlenlglpEEEIEERVEEALELVGLeglrDRSPF---------------TLSGGQKQR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063701384 716 FALARAVYHGSDMYLLDDVLSAVDSQvGCWILQRALLGplLNK--KTRVMCTHNIQ-AISCADMIVVMDKGK 784
Cdd:cd03225 143 VAIAGVLAMDPDILLLDEPTAGLDPA-GRRELLELLKK--LKAegKTIIIVTHDLDlLLELADRVIVLEDGK 211
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
601-780 |
3.45e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.04 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG--SVAYVPQ---VPWLLSGTVRENILFGKpFDSK 675
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQrseVPDSLPLTVRDLVAMGR-WARR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 676 RYFETLSACA-LDVDISLM-VGgdMACIGDKGLN-LSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQVGCWIlqRALL 752
Cdd:NF040873 87 GLWRRLTRDDrAAVDDALErVG--LADLAGRQLGeLSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI--IALL 162
|
170 180
....*....|....*....|....*....
gi 1063701384 753 GPLLNKKTRVMC-THNIQAISCADMIVVM 780
Cdd:NF040873 163 AEEHARGATVVVvTHDLELVRRADPCVLL 191
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
602-785 |
6.49e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 78.17 E-value: 6.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 602 KQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG---------SVAY-------VPQVPWLLSG-TVRE 664
Cdd:COG2884 19 SDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlkrrEIPYlrrrigvVFQDFRLLPDrTVYE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 665 NILF-----GKPfdSKRYFETLSAcALDvdislMVGgdmacIGDKG----LNLSGGQRARFALARAVYHGSDMYLLDDVL 735
Cdd:COG2884 99 NVALplrvtGKS--RKEIRRRVRE-VLD-----LVG-----LSDKAkalpHELSGGEQQRVAIARALVNRPELLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063701384 736 SAVDSQVGCWILQrallgpLL---NK--KTRVMCTHNIQAI-SCADMIVVMDKGKV 785
Cdd:COG2884 166 GNLDPETSWEIME------LLeeiNRrgTTVLIATHDLELVdRMPKRVLELEDGRL 215
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
603-794 |
2.06e-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: 79.37 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 603 QVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGSV-----------------AYVPQ----VPWLlsgT 661
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargiflpphrrriGYVFQearlFPHL---S 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 662 VRENILFGkpfdSKRYFETLSACALDvDISLMVGgdmacIGD----KGLNLSGGQRARFALARAVYHGSDMYLLDDVLSA 737
Cdd:COG4148 94 VRGNLLYG----RKRAPRAERRISFD-EVVELLG-----IGHlldrRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063701384 738 VDSQvgcwiLQRALLgPLLNKKTR------VMCTHNIQAIS-CADMIVVMDKGKVNWSGSVTDM 794
Cdd:COG4148 164 LDLA-----RKAEIL-PYLERLRDeldipiLYVSHSLDEVArLADHVVLLEQGRVVASGPLAEV 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
602-800 |
2.91e-15 |
|
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: 76.39 E-value: 2.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 602 KQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS----------------VAYVPQVPWLLSG-TVRE 664
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrrMGMLFQSGALFDSlTVFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 665 NILFgkPFdskRYFETLSACALDvDISLMvggdmaCIGDKGL---------NLSGGQRARFALARAVYHGSDMYLLDDVL 735
Cdd:cd03261 97 NVAF--PL---REHTRLSEEEIR-EIVLE------KLEAVGLrgaedlypaELSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063701384 736 SAVD----SQVGCWI--LQRALlgpllnKKTRVMCTHNIQAI-SCADMIVVMDKGKVNWSGSVTDMPKSISP 800
Cdd:cd03261 165 AGLDpiasGVIDDLIrsLKKEL------GLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRASDDP 230
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
601-798 |
3.19e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 78.84 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-SVAYVP----QV----------PWLlsgTVREN 665
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqDITHVPaenrHVntvfqsyalfPHM---TVFEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 666 ILFG-----KPFD--SKRYFETLSACALDvdislmvggDMAciGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAV 738
Cdd:PRK09452 107 VAFGlrmqkTPAAeiTPRVMEALRMVQLE---------EFA--QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063701384 739 DS------QVGCWILQRALlgpllnKKTRVMCTHNI-QAISCADMIVVMDKGKVNWSGSvtdmPKSI 798
Cdd:PRK09452 176 DYklrkqmQNELKALQRKL------GITFVFVTHDQeEALTMSDRIVVMRDGRIEQDGT----PREI 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
594-791 |
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: 75.62 E-value: 3.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 594 EEDYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG------------SVAYVPQ---VPWLL 658
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYCPQfdaLFDEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 659 sgTVRENILF-----GKPfdskryfetLSACALDVDISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDD 733
Cdd:cd03263 91 --TVREHLRFyarlkGLP---------KSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063701384 734 VLSAVDSqvgcwILQRALLGPLLNKKTR---VMCTHNIQAIS-CADMIVVMDKGKVNWSGSV 791
Cdd:cd03263 160 PTSGLDP-----ASRRAIWDLILEVRKGrsiILTTHSMDEAEaLCDRIAIMSDGKLRCIGSP 216
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
601-790 |
4.55e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.01 E-value: 4.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQVPWLLSGTVRENIL 667
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtvtraslrrNIAVVFQDAGLFNRSIEDNIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 668 FGKP--FDSKRYFETLSACALDVdISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQVGCw 745
Cdd:PRK13657 431 VGRPdaTDEEMRAAAERAQAHDF-IERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEA- 508
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063701384 746 ILQRALLGPLLNKKTRVMcTHNIQAISCADMIVVMDKGKVNWSGS 790
Cdd:PRK13657 509 KVKAALDELMKGRTTFII-AHRLSTVRNADRILVFDNGRVVESGS 552
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
895-1076 |
8.07e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 79.38 E-value: 8.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 895 KTGKGVSHYSTSFYLMvlCIFCIINSILTLVRAFSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFSSDLY 974
Cdd:TIGR00958 192 GGDKGPPALASAIFFM--CLLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 975 TIDDSLPFILNILLANFV---GLLGIIVVLSYVQVLFLLLLLPFWYIYSK-LQVFYRSTSRELRrlDSVSRSPIYASftE 1050
Cdd:TIGR00958 270 TMSRSLSLNVNVLLRNLVmllGLLGFMLWLSPRLTMVTLINLPLVFLAEKvFGKRYQLLSEELQ--EAVAKANQVAE--E 345
|
170 180
....*....|....*....|....*.
gi 1063701384 1051 TLDGSSTIRAFKSEEHFVGRFIEHLT 1076
Cdd:TIGR00958 346 ALSGMRTVRSFAAEEGEASRFKEALE 371
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
601-793 |
8.74e-15 |
|
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: 74.93 E-value: 8.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLnsllgemRCVH-------GSILLNG----------------SVAYVPQVPWL 657
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLI-------RCINglerptsGSVLVDGtdltllsgkelrkarrRIGMIFQHFNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 658 LSG-TVRENILF-------GKPFDSKRYFETLSacaldvdislMVGgdmacIGDKG----LNLSGGQRARFALARAVYHG 725
Cdd:cd03258 94 LSSrTVFENVALpleiagvPKAEIEERVLELLE----------LVG-----LEDKAdaypAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063701384 726 SDMYLLDDVLSAVDSQVGCWILQRaLLGplLNKK---TRVMCTHNIQAI-SCADMIVVMDKGKVNWSGSVTD 793
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILAL-LRD--INRElglTIVLITHEMEVVkRICDRVAVMEKGEVVEEGTVEE 227
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
595-804 |
1.10e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 75.79 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 595 EDYNLTIKqvslrvpKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS--------------VAYVPQVP--WLL 658
Cdd:PRK13644 19 ENINLVIK-------KGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgdfsklqgirklVGIVFQNPetQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 659 SGTVRENILFGKpfdskryfETLsaCALDVDISLMVggDMAcIGDKGL---------NLSGGQRARFALARAVYHGSDMY 729
Cdd:PRK13644 92 GRTVEEDLAFGP--------ENL--CLPPIEIRKRV--DRA-LAEIGLekyrhrspkTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063701384 730 LLDDVLSAVDSQVGCWILQRalLGPLLNK-KTRVMCTHNIQAISCADMIVVMDKGKVNWSGSvtdmPKSISPTFSL 804
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLER--IKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGE----PENVLSDVSL 228
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
600-785 |
1.10e-14 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 74.21 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 600 TIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS-VAYVPQ--------------VPWLlsgTVRE 664
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdVTDLPPkdrdiamvfqnyalYPHM---TVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 665 NILFG-------KPFDSKRYFETlsACALDVDISLmvggdmaciGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSA 737
Cdd:cd03301 92 NIAFGlklrkvpKDEIDERVREV--AELLQIEHLL---------DRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063701384 738 VDSQVGCWI------LQRALlgpllnKKTRVMCTHN-IQAISCADMIVVMDKGKV 785
Cdd:cd03301 161 LDAKLRVQMraelkrLQQRL------GTTTIYVTHDqVEAMTMADRIAVMNDGQI 209
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
601-785 |
1.17e-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: 75.03 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLL---NSLLGEmrcVHGSILLNG-------------SVAYVPQVPWLLSG-TVR 663
Cdd:cd03295 17 VNNLNLEIAKGEFLVLIGPSGSGKTTTMkmiNRLIEP---TSGEIFIDGedireqdpvelrrKIGYVIQQIGLFPHmTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 664 ENI-----LFG--KPFDSKRYFETLSacaldvdislMVGGDMACIGDK-GLNLSGGQRARFALARAVYHGSDMYLLDDVL 735
Cdd:cd03295 94 ENIalvpkLLKwpKEKIRERADELLA----------LVGLDPAEFADRyPHELSGGQQQRVGVARALAADPPLLLMDEPF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063701384 736 SAVDSqvgcwILQRALLGPLLN-----KKTRVMCTHNIQ-AISCADMIVVMDKGKV 785
Cdd:cd03295 164 GALDP-----ITRDQLQEEFKRlqqelGKTIVFVTHDIDeAFRLADRIAIMKNGEI 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
604-781 |
1.87e-14 |
|
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: 73.28 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 604 VSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG------------SVAYVPQVPWLLSG-TVRENILF-- 668
Cdd:COG4133 21 LSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYLGHADGLKPElTVRENLRFwa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 669 ---GKPFDSKRYFETLSACALDVDISLMVGgdmacigdkglNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQvgcw 745
Cdd:COG4133 101 alyGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA---- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1063701384 746 ilQRALLGPLLNKKTR-----VMCTHNIQAISCADMIVVMD 781
Cdd:COG4133 166 --GVALLAELIAAHLArggavLLTTHQPLELAAARVLDLGD 204
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
604-790 |
2.61e-14 |
|
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: 73.24 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 604 VSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS--------------VAYVPQVPWLLSG-TVRENILF 668
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEGRRIFPElTVEENLLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 669 GkpfdskryFETLSACALDVDISLMVG-----GDMAciGDKGLNLSGGQRARFALARAVYHGSDMYLLDDV---LS-AVD 739
Cdd:cd03224 99 G--------AYARRRAKRKARLERVYElfprlKERR--KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPsegLApKIV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063701384 740 SQVGcwilqRALLGplLNKK--TRVMCTHNI-QAISCADMIVVMDKGKVNWSGS 790
Cdd:cd03224 169 EEIF-----EAIRE--LRDEgvTILLVEQNArFALEIADRAYVLERGRVVLEGT 215
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
602-793 |
2.82e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 73.96 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 602 KQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGSVAyvpqvpWLL---SG-----TVRENILFG---- 669
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVS------ALLelgAGfhpelTGRENIYLNgrll 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 670 --KPFDSKRYFEtlsacaldvDISlmvggDMACIGD------KglNLSGGQRAR--FALARAVYHgsDMYLLDDVLSAVD 739
Cdd:COG1134 117 glSRKEIDEKFD---------EIV-----EFAELGDfidqpvK--TYSSGMRARlaFAVATAVDP--DILLVDEVLAVGD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063701384 740 S--QVGCwilqRALLGPLLNK-KTRVMCTHNIQAIS--CaDMIVVMDKGKVNWSGSVTD 793
Cdd:COG1134 179 AafQKKC----LARIRELRESgRTVIFVSHSMGAVRrlC-DRAIWLEKGRLVMDGDPEE 232
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
605-789 |
3.15e-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: 72.91 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 605 SLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-SVAYVPQVPWLLSGTVRENILFgkpfdSKRYFETLSA 683
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvDVTAAPPADRPVSMLFQENNLF-----AHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 684 CALDVDISL------MVGGDMACIGDKGL------NLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSqvgcwILQRAL 751
Cdd:cd03298 93 LGLSPGLKLtaedrqAIEVALARVGLAGLekrlpgELSGGERQRVALARVLVRDKPVLLLDEPFAALDP-----ALRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063701384 752 LGPLLN-----KKTRVMCTHNIQ-AISCADMIVVMDKGKVNWSG 789
Cdd:cd03298 168 LDLVLDlhaetKMTVLMVTHQPEdAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
592-802 |
3.17e-14 |
|
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: 73.52 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 592 NVEEDY-NLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS-----------VAYVPQVPWLLS 659
Cdd:cd03299 5 NLSKDWkEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNYALFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 660 G-TVRENILFG-------KPFDSKRYFEtlsacaldvdISLMVGGDmACIGDKGLNLSGGQRARFALARAVYHGSDMYLL 731
Cdd:cd03299 85 HmTVYKNIAYGlkkrkvdKKEIERKVLE----------IAEMLGID-HLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063701384 732 DDVLSAVDSQvgcwiLQRALLGPL-----LNKKTRVMCTHN-IQAISCADMIVVMDKGKVNWSGSVTDMPKSISPTF 802
Cdd:cd03299 154 DEPFSALDVR-----TKEKLREELkkirkEFGVTVLHVTHDfEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEF 225
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
582-785 |
5.78e-14 |
|
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: 72.99 E-value: 5.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 582 VEDASCTWSSNVEedynlTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS-------------- 647
Cdd:cd03256 3 VENLSKTYPNGKK-----ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 648 --VAYVPQ----VPWLlsgTVRENILFGK---------------PFDSKRYFETLSACALDVDISLMVGgdmacigdkgl 706
Cdd:cd03256 78 rqIGMIFQqfnlIERL---SVLENVLSGRlgrrstwrslfglfpKEEKQRALAALERVGLLDKAYQRAD----------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 707 NLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSqvgcwILQRALLGPLLNK-----KTRVMCTHNIQ-AISCADMIVVM 780
Cdd:cd03256 144 QLSGGQQQRVAIARALMQQPKLILADEPVASLDP-----ASSRQVMDLLKRInreegITVIVSLHQVDlAREYADRIVGL 218
|
....*
gi 1063701384 781 DKGKV 785
Cdd:cd03256 219 KDGRI 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
601-785 |
6.18e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 74.72 E-value: 6.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-----------SVAYVPQVPWLL-SGTVRENILF 668
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGrdvtdlppkdrNIAMVFQSYALYpHMTVYENIAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 669 GkpfdskryfetLSACALD-------VD-ISLMVGgdmacIGD----KGLNLSGGQRARFALARAVYHGSDMYLLDDVLS 736
Cdd:COG3839 99 P-----------LKLRKVPkaeidrrVReAAELLG-----LEDlldrKPKQLSGGQRQRVALGRALVREPKVFLLDEPLS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063701384 737 AVD-----------SQvgcwiLQRALlgpllnKKTRVMCTHN-IQAISCADMIVVMDKGKV 785
Cdd:COG3839 163 NLDaklrvemraeiKR-----LHRRL------GTTTIYVTHDqVEAMTLADRIAVMNDGRI 212
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
601-785 |
7.61e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 72.81 E-value: 7.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQVPwlLSGT-----V 662
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkdvtklpeykrakYIGRVFQDP--MMGTapsmtI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 663 RENILF----GKPF---------DSKRYFETLSACALDVDISLmvggdmaciGDK-GLnLSGGQRARFALARAVYHGSDM 728
Cdd:COG1101 100 EENLALayrrGKRRglrrgltkkRRELFRELLATLGLGLENRL---------DTKvGL-LSGGQRQALSLLMATLTKPKL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063701384 729 YLLDDVLSAVDSQVGCWILQrallgplLNKK-------TRVMCTHNI-QAISCADMIVVMDKGKV 785
Cdd:COG1101 170 LLLDEHTAALDPKTAALVLE-------LTEKiveennlTTLMVTHNMeQALDYGNRLIMMHEGRI 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
601-789 |
8.35e-14 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 72.18 E-value: 8.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGSVAyvpqvpWLL---SG-----TVRENILFG--- 669
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS------SLLglgGGfnpelTGRENIYLNgrl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 670 ----KPFDSKRYFETLSACALDVDISLMVGgdmacigdkglNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDS--QVG 743
Cdd:cd03220 112 lglsRKEIDEKIDEIIEFSELGDFIDLPVK-----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAafQEK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1063701384 744 CwilQRALLGPLLNKKTRVMCTHNIQAIS--CaDMIVVMDKGKVNWSG 789
Cdd:cd03220 181 C---QRRLRELLKQGKTVILVSHDPSSIKrlC-DRALVLEKGKIRFDG 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
604-816 |
9.78e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 73.96 E-value: 9.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 604 VSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS-----------VAYVPQVPWLLSG-TVRENILFGKP 671
Cdd:PRK10851 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHYALFRHmTVFDNIAFGLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 672 FDSKRyfETLSACALDVDISLMVggDMACIGDKG----LNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQVGC--- 744
Cdd:PRK10851 101 VLPRR--ERPNAAAIKAKVTQLL--EMVQLAHLAdrypAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKelr 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063701384 745 -WIlqRALLGPLlnKKTRVMCTHNIQ-AISCADMIVVMDKGKVNWSGSVTDMPKSISPTFSLtnEFdMSSPNHL 816
Cdd:PRK10851 177 rWL--RQLHEEL--KFTSVFVTHDQEeAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVL--EF-MGEVNRL 243
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
568-783 |
1.23e-13 |
|
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: 72.25 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 568 SIDSGFTSEDLAVCVEDASCTWSSNVEEdynlTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG- 646
Cdd:cd03288 8 SSNSGLVGLGGEIKIHDLCVRYENNLKP----VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 647 SVAYVP------------QVPWLLSGTVRENILFGKPFDSKRYFETLSACALDVDISLMVGGDMACIGDKGLNLSGGQRA 714
Cdd:cd03288 84 DISKLPlhtlrsrlsiilQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQ 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063701384 715 RFALARAVYHGSDMYLLDDVLSAVDSQVGCwILQRALLGPLLNkKTRVMCTHNIQAISCADMIVVMDKG 783
Cdd:cd03288 164 LFCLARAFVRKSSILIMDEATASIDMATEN-ILQKVVMTAFAD-RTVVTIAHRVSTILDADLVLVLSRG 230
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
601-785 |
5.01e-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: 70.16 E-value: 5.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-SVAYVP-------------QVPWLLSG-TVREN 665
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeDITGLPpheiarlgigrtfQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 666 ILFGKPFDSKRYFETLSACALDVDIslmVGGDMACIGDKGL---------NLSGGQRARFALARAVYHGSDMYLLDDV-- 734
Cdd:cd03219 96 VMVAAQARTGSGLLLARARREEREA---RERAEELLERVGLadladrpagELSYGQQRRLEIARALATDPKLLLLDEPaa 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063701384 735 -LSAVDSQVGCWILQRallgplLNKK--TRVMCTHNIQAI-SCADMIVVMDKGKV 785
Cdd:cd03219 173 gLNPEETEELAELIRE------LRERgiTVLLVEHDMDVVmSLADRVTVLDQGRV 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
595-794 |
6.79e-13 |
|
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: 73.44 E-value: 6.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 595 EDYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQVPWLLSGT 661
Cdd:TIGR00957 1296 EDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniakiglhdlrfKITIIPQDPVLFSGS 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 662 VRENIlfgKPFDSKRYFETLSACAL----DVDISLMVGGDMACiGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSA 737
Cdd:TIGR00957 1376 LRMNL---DPFSQYSDEEVWWALELahlkTFVSALPDKLDHEC-AEGGENLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063701384 738 VDSQVGCWIlqRALLGPLLNKKTRVMCTHNIQAISCADMIVVMDKGKVNWSGSVTDM 794
Cdd:TIGR00957 1452 VDLETDNLI--QSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNL 1506
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
592-793 |
7.02e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 69.40 E-value: 7.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 592 NVEEDYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-SVAYVP--QVP-----------WL 657
Cdd:COG3840 6 DLTYRYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqDLTALPpaERPvsmlfqennlfPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 658 LsgTVRENILFG-----KPFDSKRyfETLSACALDVDISlmvggdmACIGDKGLNLSGGQRARFALARAVYHGSDMYLLD 732
Cdd:COG3840 86 L--TVAQNIGLGlrpglKLTAEQR--AQVEQALERVGLA-------GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063701384 733 DVLSAvdsqvgcwilqralLGP--------LLNKKTR------VMCTHNIQ-AISCADMIVVMDKGKVNWSGSVTD 793
Cdd:COG3840 155 EPFSA--------------LDPalrqemldLVDELCRergltvLMVTHDPEdAARIADRVLLVADGRIAADGPTAA 216
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
596-789 |
1.41e-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: 68.09 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 596 DYNLtikQVSLRVPkGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS-----------------VAYVPQ----V 654
Cdd:cd03297 12 DFTL---KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkkinlppqqrkIGLVFQqyalF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 655 PWLlsgTVRENILFGKPFDS---KRYFETLSACALDVDISLmvggdmaciGDKGLNLSGGQRARFALARAVYHGSDMYLL 731
Cdd:cd03297 88 PHL---NVRENLAFGLKRKRnreDRISVDELLDLLGLDHLL---------NRYPAQLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063701384 732 DDVLSAVDSQVgcwilqRALLGPLLNK-KTR-----VMCTHNI-QAISCADMIVVMDKGKVNWSG 789
Cdd:cd03297 156 DEPFSALDRAL------RLQLLPELKQiKKNlnipvIFVTHDLsEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
597-740 |
2.23e-12 |
|
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: 68.07 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 597 YNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRC---VHGSILLNG----------SVAYVPQVPWLLSG-TV 662
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGqprkpdqfqkCVAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063701384 663 RENILFGKPFDSKRYFETLSACALDVDISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDS 740
Cdd:cd03234 99 RETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
601-785 |
2.57e-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: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSillngSVAYVPQVPWLLSGTVRENILFGKPFDSKryFET 680
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA-----GCVDVPDNQFGREASLIDAIGRKGDFKDA--VEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 681 LSACALdVDISLMVGgdmacigdKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVD---SQVGCWILQRALLGpllN 757
Cdd:COG2401 119 LNAVGL-SDAVLWLR--------RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQKLARR---A 186
|
170 180 190
....*....|....*....|....*....|.
gi 1063701384 758 KKTRVMCTHN---IQAIScADMIVVMDKGKV 785
Cdd:COG2401 187 GITLVVATHHydvIDDLQ-PDLLIFVGYGGV 216
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
601-789 |
2.61e-12 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 67.39 E-value: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-SVAYVPQ---------------VPWLlsgTVRE 664
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAearrrlgfvsdstglYDRL---TARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 665 NIL-FGKPFDSKRyfETLSAcALDVDISLMvggDMACIGDK-GLNLSGGQRARFALARAVYHGSDMYLLD------DVLS 736
Cdd:cd03266 98 NLEyFAGLYGLKG--DELTA-RLEELADRL---GMEELLDRrVGGFSTGMRQKVAIARALVHDPPVLLLDepttglDVMA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063701384 737 AvdsqvgcwilqRALLGPLLNK----KTRVMCTHNIQAI-SCADMIVVMDKGKVNWSG 789
Cdd:cd03266 172 T-----------RALREFIRQLralgKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
602-808 |
2.66e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 69.34 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 602 KQVSLRVPKGSFVAVIGEVGSGKTSLLnsllgemRCV-------HGSILLNG----------------SVAYVPQVPWLL 658
Cdd:COG1135 22 DDVSLTIEKGEIFGIIGYSGAGKSTLI-------RCInllerptSGSVLVDGvdltalserelraarrKIGMIFQHFNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 659 SG-TVRENILF-------GKPFDSKRYFETLSacaldvdislMVGgdmacIGDKGL----NLSGGQRARFALARAVYHGS 726
Cdd:COG1135 95 SSrTVAENVALpleiagvPKAEIRKRVAELLE----------LVG-----LSDKADaypsQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 727 DMYLLDDVLSAVDSQVGCWILQrallgpLL---NKK---TRVMCTHN---IQAIscADMIVVMDKGKVNWSGSVTDM--- 794
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILD------LLkdiNRElglTIVLITHEmdvVRRI--CDRVAVLENGRIVEQGPVLDVfan 231
|
250
....*....|....
gi 1063701384 795 PKSisptfSLTNEF 808
Cdd:COG1135 232 PQS-----ELTRRF 240
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
601-848 |
2.80e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 68.92 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG---------------SVAYVPQVP--WLLSGTVR 663
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 664 ENILFGkPFD--------SKRYFETLSacaldvdislMVGGDMACIGDKG-LNLSGGQRARFALARAVYHGSDMYLLDDV 734
Cdd:PRK13637 103 KDIAFG-PINlglseeeiENRVKRAMN----------IVGLDYEDYKDKSpFELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 735 LSAVDSQVGCWILQRAllgPLLNKK---TRVMCTHNIQAIS-CADMIVVMDKGKVNWSGSVTDMPKSIsptfSLTNEFDM 810
Cdd:PRK13637 172 TAGLDPKGRDEILNKI---KELHKEynmTIILVSHSMEDVAkLADRIIVMNKGKCELQGTPREVFKEV----ETLESIGL 244
|
250 260 270
....*....|....*....|....*....|....*...
gi 1063701384 811 SSPNHLTKRKEtlsIKEDGVDeISEaaaDIVKLEERKE 848
Cdd:PRK13637 245 AVPQVTYLVRK---LRKKGFN-IPD---DIFTIEEAKE 275
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
269-554 |
3.07e-12 |
|
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: 68.73 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 269 LGLLKVFndcIGFAGPLLLNRLIKYLEKGSGSSVGYTLAISLGFISIFKSFLDTQYTFRLSKLKLKLRSSIMSVIYRKCL 348
Cdd:cd07346 7 LLLLATA---LGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 349 WVNTANRSGFSEGEIQTFMSVDADRIVNLCNS-LHDLWSLPLQ-IGIALYLLYTQVKFAFLSgLAITILLIPVNKWISVL 426
Cdd:cd07346 84 RLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSgLLQLLSDVLTlIGALVILFYLNWKLTLVA-LLLLPLYVLILRYFRRR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 427 IASATEKMMKLKDERIRKTGELLTNIRTLKMYGwdnwfadwlKETRATEVTHLATRKYLDA------WCVFFWATTPTLF 500
Cdd:cd07346 163 IRKASREVRESLAELSAFLQESLSGIRVVKAFA---------AEEREIERFREANRDLRDAnlraarLSALFSPLIGLLT 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063701384 501 SLCTFGLFAL-----MGHQLDAATVFTCLALFNSLISPLNSFPWVINGLIDAFISTRRV 554
Cdd:cd07346 234 ALGTALVLLYggylvLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
909-1167 |
3.23e-12 |
|
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: 71.02 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 909 LMVLCI----FCIINSILTLVRAFSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFsSDLYTIDDSLP-FI 983
Cdd:COG2274 195 LWVLAIglllALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTgSL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 984 LNILLANFVGLLGIIVVLSY-------VQVLFLLLLLPFWYIYSKLqvfyRSTSRELRRLDSVsrspIYASFTETLDGSS 1056
Cdd:COG2274 274 LTALLDLLFVLIFLIVLFFYspplalvVLLLIPLYVLLGLLFQPRL----RRLSREESEASAK----RQSLLVETLRGIE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1057 TIRAFKSEEHFVGRFIEHLTLYQRTSYSEIIASLWLSLRLQ---LLGSMIVLFVAVMAVLGSGgnfpISFGTpgLV---G 1130
Cdd:COG2274 346 TIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGllqQLATVALLWLGAYLVIDGQ----LTLGQ--LIafnI 419
|
250 260 270
....*....|....*....|....*....|....*..
gi 1063701384 1131 LALSYAAPLVSLLGsLLTSFTETekeMVSVERVLQVM 1167
Cdd:COG2274 420 LSGRFLAPVAQLIG-LLQRFQDA---KIALERLDDIL 452
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
593-741 |
4.68e-12 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 66.36 E-value: 4.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 593 VEEDYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS---------------VAYVPQVPWL 657
Cdd:cd03231 8 CERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldfqrdsiargllyLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 658 LSgtVRENILFGKPFDSKRYFETlsacALDvDISLMVGGDMACIgdkglNLSGGQRARFALARAVYHGSDMYLLDDVLSA 737
Cdd:cd03231 88 LS--VLENLRFWHADHSDEQVEE----ALA-RVGLNGFEDRPVA-----QLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
....
gi 1063701384 738 VDSQ 741
Cdd:cd03231 156 LDKA 159
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
601-781 |
9.59e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 65.58 E-value: 9.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMR---CVHGSILLNGS-----------VAYVPQVPWL---LSgtVR 663
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRrltalpaeqrrIGILFQDDLLfphLS--VG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 664 ENILFGKPFD-SKRYFETLSACALDvDISLmvgGDMAcigDKGLN-LSGGQRARFALARAVYHGSDMYLLDDVLSAVD-- 739
Cdd:COG4136 95 ENLAFALPPTiGRAQRRARVEQALE-EAGL---AGFA---DRDPAtLSGGQRARVALLRALLAEPRALLLDEPFSKLDaa 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1063701384 740 --SQVGCWILQRAllgpllnkKTR----VMCTHNIQAISCADMIVVMD 781
Cdd:COG4136 168 lrAQFREFVFEQI--------RQRgipaLLVTHDEEDAPAAGRVLDLG 207
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
599-803 |
1.15e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.42 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 599 LTIKQVSLRVPKGSFVAVIGEVGSGKTSLLnslLGEMRCVH---GSILLNGS--VAY-----------VPQVPWLLSGTV 662
Cdd:PTZ00243 1324 LVLRGVSFRIAPREKVGIVGRTGSGKSTLL---LTFMRMVEvcgGEIRVNGReiGAYglrelrrqfsmIPQDPVLFDGTV 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 663 RENIlfgKPF---DSKRYFETLSACALDVDISLMVGGDMACIGDKGLNLSGGQRARFALARAVY-HGSDMYLLDDVLS-- 736
Cdd:PTZ00243 1401 RQNV---DPFleaSSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATAni 1477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063701384 737 --AVDSQVgcwilqRALLGPLLNKKTRVMCTHNIQAISCADMIVVMDKGKVNWSGSVTDMPKSISPTFS 803
Cdd:PTZ00243 1478 dpALDRQI------QATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFH 1540
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
614-785 |
1.24e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 69.62 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 614 VAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQVPWLLSGTVRENIlfgKPF---DSKRY 677
Cdd:PLN03232 1265 VGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcdvakfgltdlrrVLSIIPQSPVLFSGTVRFNI---DPFsehNDADL 1341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 678 FETLSACALDVDISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQVGCWIlQRALLGPlLN 757
Cdd:PLN03232 1342 WEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLI-QRTIREE-FK 1419
|
170 180
....*....|....*....|....*...
gi 1063701384 758 KKTRVMCTHNIQAISCADMIVVMDKGKV 785
Cdd:PLN03232 1420 SCTMLVIAHRLNTIIDCDKILVLSSGQV 1447
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
596-742 |
1.27e-11 |
|
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: 64.10 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 596 DYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSI--LLNGSVAYVPQVPWLLSGTVRENILFgkPFD 673
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgmPEGEDLLFLPQRPYLPLGTLREQLIY--PWD 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063701384 674 SKryfetlsacaldvdislmvggdmacigdkglnLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQV 742
Cdd:cd03223 90 DV--------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
592-776 |
1.80e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 65.96 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 592 NVEEDYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLL------NSLLGEMRcVHGSILLNGSVAYVPQVPwllSGTVREN 665
Cdd:PRK14243 17 NVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlNDLIPGFR-VEGKVTFHGKNLYAPDVD---PVEVRRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 666 I--LFGKPFD-SKRYFETLSACA--------LD--VDISLMVGGDMACIGDK----GLNLSGGQRARFALARAVYHGSDM 728
Cdd:PRK14243 93 IgmVFQKPNPfPKSIYDNIAYGAringykgdMDelVERSLRQAALWDEVKDKlkqsGLSLSGGQQQRLCIARAIAVQPEV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063701384 729 YLLDDVLSAVDSQVGCWIlqRALLGPLLNKKTRVMCTHNI-QAISCADM 776
Cdd:PRK14243 173 ILMDEPCSALDPISTLRI--EELMHELKEQYTIIIVTHNMqQAARVSDM 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
596-808 |
2.09e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 67.17 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 596 DYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-SVAYVP--QVPWLL---------SGTVR 663
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvDLSHVPpyQRPINMmfqsyalfpHMTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 664 ENILFGKPFD-------SKRYFETLSacaldvdisLMVGGDMAciGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLS 736
Cdd:PRK11607 110 QNIAFGLKQDklpkaeiASRVNEMLG---------LVHMQEFA--KRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 737 AVDSQVG-------CWILQRAllgpllnKKTRVMCTHNI-QAISCADMIVVMDKGKVNWSGSvtdmPKSI--SPTFSLTN 806
Cdd:PRK11607 179 ALDKKLRdrmqlevVDILERV-------GVTCVMVTHDQeEAMTMAGRIAIMNRGKFVQIGE----PEEIyeHPTTRYSA 247
|
..
gi 1063701384 807 EF 808
Cdd:PRK11607 248 EF 249
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
595-798 |
2.25e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 65.78 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 595 EDYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQVP--WLLS 659
Cdd:PRK13632 19 NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskenlkeirkKIGIIFQNPdnQFIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 660 GTVRENILFG---KPFDSKRYFETLSACALDVDislmvggdMACIGDK-GLNLSGGQRARFALARAVYHGSDMYLLDDVL 735
Cdd:PRK13632 99 ATVEDDIAFGlenKKVPPKKMKDIIDDLAKKVG--------MEDYLDKePQNLSGGQKQRVAIASVLALNPEIIIFDEST 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063701384 736 SAVDSQVGCWILQraLLGPLLNK--KTRVMCTHNIQAISCADMIVVMDKGKVNWSGSvtdmPKSI 798
Cdd:PRK13632 171 SMLDPKGKREIKK--IMVDLRKTrkKTLISITHDMDEAILADKVIVFSEGKLIAQGK----PKEI 229
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
601-796 |
3.39e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 65.08 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSiLLNGSvAYVPQV--------------PWllsGTVRENI 666
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGT-APLAEAredtrlmfqdarllPW---KKVIDNV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 667 ---LFGKPFDSKRyfETLSACALdvdislmvgGDMAciGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSqvg 743
Cdd:PRK11247 103 glgLKGQWRDAAL--QALAAVGL---------ADRA--NEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA--- 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 744 cwiLQRALLGPLLNKK------TRVMCTHNI-QAISCADMIVVMDKGKVNWSGSVtDMPK 796
Cdd:PRK11247 167 ---LTRIEMQDLIESLwqqhgfTVLLVTHDVsEAVAMADRVLLIEEGKIGLDLTV-DLPR 222
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
602-819 |
3.96e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 65.98 E-value: 3.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 602 KQVSLRVPKGSFVAVIGEVGSGKTSLLnsllgemRCVH-------GSILLNG----------------SVAYVPQVPWLL 658
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLI-------RCINllerptsGRVLVDGqdltalsekelrkarrQIGMIFQHFNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 659 SG-TVRENILF-----GKPFDS--KRYFETLSacaldvdislMVGgdmacIGDKGL----NLSGGQRARFALARAVYHGS 726
Cdd:PRK11153 95 SSrTVFDNVALplelaGTPKAEikARVTELLE----------LVG-----LSDKADrypaQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 727 DMYLLDDVLSAVDSQVGCWILQrallgpLL---NKK---TRVMCTHNIQAI-SCADMIVVMDKGKVNWSGSVTDM---PK 796
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILE------LLkdiNRElglTIVLITHEMDVVkRICDRVAVIDAGRLVEQGTVSEVfshPK 233
|
250 260
....*....|....*....|....*...
gi 1063701384 797 SisptfSLTNEFDMSS-----PNHLTKR 819
Cdd:PRK11153 234 H-----PLTREFIQSTlhldlPEDYLAR 256
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
604-809 |
4.67e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 66.40 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 604 VSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQVPWL-LSGTVRENILFG 669
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASVPQDTSLsFEFDVRQVVEMG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 670 KPFDSKRYFETLSACALDVDiSLMVGGDMACIGDKGL-NLSGGQRARFALARAVYHGSDMYLLDDVLSAVD--SQVGCWI 746
Cdd:PRK09536 102 RTPHRSRFDTWTETDRAAVE-RAMERTGVAQFADRPVtSLSGGERQRVLLARALAQATPVLLLDEPTASLDinHQVRTLE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063701384 747 LQRALLGpllNKKTRVMCTH--NIQAISCaDMIVVMDKGKVNWSGSvtdmPKSISPTFSLTNEFD 809
Cdd:PRK09536 181 LVRRLVD---DGKTAVAAIHdlDLAARYC-DELVLLADGRVRAAGP----PADVLTADTLRAAFD 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
602-732 |
5.33e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 66.63 E-value: 5.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 602 KQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG--SVAYVPQVPWLLSG-TVRENIL--FGKPFDSKR 676
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDDDlTVLDTVLdgDAELRALEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 677 YFETLSACALDVDISLM----VGGDMACIGD-----------KGL------------NLSGGQRARFALARAVYHGSDMY 729
Cdd:COG0488 95 ELEELEAKLAEPDEDLErlaeLQEEFEALGGweaearaeeilSGLgfpeedldrpvsELSGGWRRRVALARALLSEPDLL 174
|
...
gi 1063701384 730 LLD 732
Cdd:COG0488 175 LLD 177
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
596-739 |
8.06e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 65.98 E-value: 8.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 596 DYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILL--NGSVAYVPQVPWLLSGTVRENILFGKP-- 671
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQRPYLPLGTLREALLYPATae 453
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063701384 672 -FDSKRYFETLSACALD-----VDISLmvggdmacigDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVD 739
Cdd:COG4178 454 aFSDAELREALEAVGLGhlaerLDEEA----------DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
601-732 |
1.19e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.47 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILL--NGSVAYVPQVPWLLSG--TVRENIlfgkpfdsKR 676
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgeTVKIGYFDQHQEELDPdkTVLDEL--------RD 402
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063701384 677 YFETLSacalDVDISLMVG-----GDMAC--IGDkglnLSGGQRARFALARAVYHGSDMYLLD 732
Cdd:COG0488 403 GAPGGT----EQEVRGYLGrflfsGDDAFkpVGV----LSGGEKARLALAKLLLSPPNVLLLD 457
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
575-794 |
1.23e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 63.67 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 575 SEDLAVCVEDASCTWSSNVEEdynlTIKQVSLRVPKGSFVAVIGEVGSGKTS---LLNSLLGEMRCVHGSILLNG----- 646
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKP----ALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGitlta 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 647 --------SVAYVPQVP--WLLSGTVRENILFG-------KPFDSKRYFETLSacalDVDISLMVGGDMAcigdkglNLS 709
Cdd:PRK13640 77 ktvwdireKVGIVFQNPdnQFVGATVGDDVAFGlenravpRPEMIKIVRDVLA----DVGMLDYIDSEPA-------NLS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 710 GGQRARFALARAVYHGSDMYLLDDVLSAVDSQVGCWILQraLLGPLLNKK--TRVMCTHNIQAISCADMIVVMDKGKVNW 787
Cdd:PRK13640 146 GGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILK--LIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLA 223
|
....*..
gi 1063701384 788 SGSVTDM 794
Cdd:PRK13640 224 QGSPVEI 230
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
591-794 |
1.82e-10 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 62.18 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 591 SNVEEDYNLT--IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG--------------SVAYVPQV 654
Cdd:cd03218 4 ENLSKRYGKRkvVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmhkrarlGIGYLPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 655 PWLLSG-TVRENI---LFGKPFDSKRYFETLSACALDVDISlmvggdmACIGDKGLNLSGGQRARFALARAVYHGSDMYL 730
Cdd:cd03218 84 ASIFRKlTVEENIlavLEIRGLSKKEREEKLEELLEEFHIT-------HLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063701384 731 LDDVLSAVDSQVGCWIlqRALLGPLLNKKTRVMCT-HNI-QAISCADMIVVMDKGKVNWSGSVTDM 794
Cdd:cd03218 157 LDEPFAGVDPIAVQDI--QKIIKILKDRGIGVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
598-732 |
2.57e-10 |
|
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: 59.77 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 598 NLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILL--NGSVAYVPQvpwllsgtvrenilfgkpfdsk 675
Cdd:cd03221 13 KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWgsTVKIGYFEQ---------------------- 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063701384 676 ryfetlsacaldvdislmvggdmacigdkglnLSGGQRARFALARAVYHGSDMYLLD 732
Cdd:cd03221 71 --------------------------------LSGGEKMRLALAKLLLENPNLLLLD 95
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
605-790 |
4.56e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 61.14 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 605 SLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS-----------VAYVPQVPWLLSG-TVRENILFG--- 669
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsrrpVSMLFQENNLFSHlTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 670 --KPFDSKRyfETLSACALDVDISlmvggdmACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQVGCWIL 747
Cdd:PRK10771 99 glKLNAAQR--EKLHAIARQMGIE-------DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEML 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063701384 748 QraLLGPLLNKK--TRVMCTHNIQ-AISCADMIVVMDKGKVNWSGS 790
Cdd:PRK10771 170 T--LVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGP 213
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
601-790 |
6.39e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 61.18 E-value: 6.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQVPWLLSG-TVRENI 666
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTPEGiTVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 667 LFGK-PFDSkrYFETLSacalDVDISL----MVGGDMACIGDKGL-NLSGGQRARFALARAVYHGSDMYLLDDVLSAVD- 739
Cdd:PRK11231 98 AYGRsPWLS--LWGRLS----AEDNARvnqaMEQTRINHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDi 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063701384 740 -SQVGcwiLQRaLLGPLLNK-KTRVMCTHNI-QAISCADMIVVMDKGKVNWSGS 790
Cdd:PRK11231 172 nHQVE---LMR-LMRELNTQgKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGT 221
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
907-1125 |
6.42e-10 |
|
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: 61.63 E-value: 6.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 907 FYLMVLcifcIINSILTLVRAFSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFILNI 986
Cdd:cd18544 46 LYLGLL----LLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 987 LLANFVGLLGIIVVLSYVQV---LFLLLLLPFWYIYSKL-QVFYRSTSRELRRLdsVSRspIYASFTETLDGSSTIRAFK 1062
Cdd:cd18544 122 LIGDLLLLIGILIAMFLLNWrlaLISLLVLPLLLLATYLfRKKSRKAYREVREK--LSR--LNAFLQESISGMSVIQLFN 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063701384 1063 SEEHFVGRFIEHLTLYQRTSYSEIIASLWLSlrlqllgSMIVLF--VAVMAVLGSGGNF----PISFGT 1125
Cdd:cd18544 198 REKREFEEFDEINQEYRKANLKSIKLFALFR-------PLVELLssLALALVLWYGGGQvlsgAVTLGV 259
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
614-785 |
6.95e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.60 E-value: 6.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 614 VAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQVPWLLSGTVRENIlfgKPFDSKR---Y 677
Cdd:PLN03130 1268 VGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiskfglmdlrkVLGIIPQAPVLFSGTVRFNL---DPFNEHNdadL 1344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 678 FETLSACALDVDISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDsqVGCWILQRALLGPLLN 757
Cdd:PLN03130 1345 WESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD--VRTDALIQKTIREEFK 1422
|
170 180
....*....|....*....|....*...
gi 1063701384 758 KKTRVMCTHNIQAISCADMIVVMDKGKV 785
Cdd:PLN03130 1423 SCTMLIIAHRLNTIIDCDRILVLDAGRV 1450
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
596-799 |
8.20e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 60.92 E-value: 8.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 596 DYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS-------------VAYVPQVP--WLLSG 660
Cdd:PRK13648 20 DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQaitddnfeklrkhIGIVFQNPdnQFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 661 TVRENILFG-----KPFDS--KRYFETLSacalDVDISlmvggDMAciGDKGLNLSGGQRARFALARAVYHGSDMYLLDD 733
Cdd:PRK13648 100 IVKYDVAFGlenhaVPYDEmhRRVSEALK----QVDML-----ERA--DYEPNALSGGQKQRVAIAGVLALNPSVIILDE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063701384 734 VLSAVDSQvgcwilQRALLGPLLNkktRVMCTHNIQAISC---------ADMIVVMDKGKVNWSGSVTDMPKSIS 799
Cdd:PRK13648 169 ATSMLDPD------ARQNLLDLVR---KVKSEHNITIISIthdlseameADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
601-789 |
1.32e-09 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 59.51 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFvAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS------------VAYVPQ-VPWLLSGTVRENIl 667
Cdd:cd03264 16 LDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrIGYLPQeFGVYPNFTVREFL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 668 fgkpfdskRYFETLSACA---LDVDISLMVGG-DMACIGDKGLN-LSGGQRARFALARAVYHGSDMYLLDDVLSAVDsqV 742
Cdd:cd03264 94 --------DYIAWLKGIPskeVKARVDEVLELvNLGDRAKKKIGsLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD--P 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1063701384 743 GCWILQRALLGPLLNKKTRVMCTHNIQAI-SCADMIVVMDKGKVNWSG 789
Cdd:cd03264 164 EERIRFRNLLSELGEDRIVILSTHIVEDVeSLCNQVAVLNKGKLVFEG 211
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
909-1075 |
1.63e-09 |
|
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: 60.40 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 909 LMVLCIFCIINSILTLVRA--FSFAFGGLKaaVHVHNALISKLINAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFILNI 986
Cdd:cd18784 39 IIIMGLLAIASSVAAGIRGglFTLAMARLN--IRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 987 LLANFVGLLGIIV---VLSYVQVLFLLLLLPFWYIYSKLQ-VFYRSTSRELRrlDSVSRSPIYASftETLDGSSTIRAFK 1062
Cdd:cd18784 117 FLRSLVKAIGVIVfmfKLSWQLSLVTLIGLPLIAIVSKVYgDYYKKLSKAVQ--DSLAKANEVAE--ETISSIRTVRSFA 192
|
170
....*....|...
gi 1063701384 1063 SEEHFVGRFIEHL 1075
Cdd:cd18784 193 NEDGEANRYSEKL 205
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
601-785 |
1.64e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 59.76 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSL-------LGEMRCvhGSILLNGSVAYVPQ----------VPWLLSG--- 660
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIRV--GDITIDTARSLSQQkglirqlrqhVGFVFQNfnl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 661 ----TVRENILFGKPFDSKRYFETLSACALDVdislmvggdMACIGDKG------LNLSGGQRARFALARAVYHGSDMYL 730
Cdd:PRK11264 97 fphrTVLENIIEGPVIVKGEPKEEATARAREL---------LAKVGLAGketsypRRLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063701384 731 LDDVLSAVDSQvgcwilqraLLGPLLN--------KKTRVMCTHNIQ-AISCADMIVVMDKGKV 785
Cdd:PRK11264 168 FDEPTSALDPE---------LVGEVLNtirqlaqeKRTMVIVTHEMSfARDVADRAIFMDQGRI 222
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
601-738 |
1.79e-09 |
|
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: 62.07 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNsLLGEMRCVHGSILL---NGSVAYVPQVPWLLSGTVRENILF-GKPFDSKR 676
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGGRLTkpaKGKLFYVPQRPYMTLGTLRDQIIYpDSSEDMKR 546
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063701384 677 YF---ETLSACALDVDISLMV--GGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAV 738
Cdd:TIGR00954 547 RGlsdKDLEQILDNVQLTHILerEGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
594-798 |
3.15e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 59.26 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 594 EEDYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQVP--WLL 658
Cdd:PRK13635 16 PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseetvwdvrrQVGMVFQNPdnQFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 659 SGTVRENILF-----GKPFDS--KRyfetlsacaldVDISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLL 731
Cdd:PRK13635 96 GATVQDDVAFgleniGVPREEmvER-----------VDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIIL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063701384 732 DDVLSAVDSQvGcwilQRALLGPL--LNKKTRVMC---THNIQAISCADMIVVMDKGKVNWSGSvtdmPKSI 798
Cdd:PRK13635 165 DEATSMLDPR-G----RREVLETVrqLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEEGT----PEEI 227
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
593-790 |
3.43e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 59.26 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 593 VEEDYN-------LTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSIL-----------------LNGSV 648
Cdd:PRK13634 8 VEHRYQyktpferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTigervitagkknkklkpLRKKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 649 AYVPQVP--WLLSGTVRENILFGkPFD---SKRYFETLSACALDvdislMVGGDMACIGDKGLNLSGGQRARFALARAVY 723
Cdd:PRK13634 88 GIVFQFPehQLFEETVEKDICFG-PMNfgvSEEDAKQKAREMIE-----LVGLPEELLARSPFELSGGQMRRVAIAGVLA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 724 HGSDMYLLDDVLSAVDSQVGCWILQraLLGPLLNKK--TRVMCTHNIQ-AISCADMIVVMDKGKVNWSGS 790
Cdd:PRK13634 162 MEPEVLVLDEPTAGLDPKGRKEMME--MFYKLHKEKglTTVLVTHSMEdAARYADQIVVMHKGTVFLQGT 229
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
592-784 |
3.63e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 59.43 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 592 NVEEDY--NLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS------------VAYVPQVPWL 657
Cdd:PRK13537 12 NVEKRYgdKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharqrVGVVPQFDNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 658 LSG-TVRENIL-FGkpfdskRYFETLSACALDVDISLMVGGDMACIGDKGL-NLSGGQRARFALARAVYHGSDMYLLDDV 734
Cdd:PRK13537 92 DPDfTVRENLLvFG------RYFGLSAAAARALVPPLLEFAKLENKADAKVgELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1063701384 735 LSAVDSQVGCWILQRaLLGPLLNKKTRVMCTHNI-QAISCADMIVVMDKGK 784
Cdd:PRK13537 166 TTGLDPQARHLMWER-LRSLLARGKTILLTTHFMeEAERLCDRLCVIEEGR 215
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
602-740 |
3.71e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 57.96 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 602 KQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGSVAYVPQVPWLL-----------SGTVRENILFGK 670
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAChylghrnamkpALTVAENLEFWA 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063701384 671 PFdskryfetLSACALDVDISLmvggdmACIGDKGL------NLSGGQRARFALARAVYHGSDMYLLDDVLSAVDS 740
Cdd:PRK13539 99 AF--------LGGEELDIAAAL------EAVGLAPLahlpfgYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
602-785 |
4.36e-09 |
|
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: 56.67 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 602 KQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGsvayvpqvpwllsgtvrENILFGKPFDskryfetl 681
Cdd:cd03216 17 DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-----------------KEVSFASPRD-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 682 sacALDVDISlMVggdmacigdkgLNLSGGQRARFALARAVYHGSDMYLLDD---VLSAVDSQvgcwilqrALLGPLLNK 758
Cdd:cd03216 72 ---ARRAGIA-MV-----------YQLSVGERQMVEIARALARNARLLILDEptaALTPAEVE--------RLFKVIRRL 128
|
170 180 190
....*....|....*....|....*....|....
gi 1063701384 759 KTR----VMCTHN---IQAIscADMIVVMDKGKV 785
Cdd:cd03216 129 RAQgvavIFISHRldeVFEI--ADRVTVLRDGRV 160
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
893-1076 |
5.07e-09 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 58.89 E-value: 5.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 893 VDKTGKGVSHYSTSFYLMVLCIFCIINSILTLVRAFSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFSSD 972
Cdd:cd18590 23 IDILGGEYQHNAFTSAIGLMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 973 LYTIDDSLPFILNILLANFV---GLLGIIVVLSYVQVLFLLLLLPFWYIYSKLqvfYRSTSRELRR--LDSVSRSPIYAs 1047
Cdd:cd18590 103 TTLMSRSVALNANVLLRSLVktlGMLGFMLSLSWQLTLLTLIEMPLTAIAQKV---YNTYHQKLSQavQDSIAKAGELA- 178
|
170 180
....*....|....*....|....*....
gi 1063701384 1048 fTETLDGSSTIRAFKSEEHFVGRFIEHLT 1076
Cdd:cd18590 179 -REAVSSIRTVRSFKAEEEEACRYSEALE 206
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
590-835 |
5.33e-09 |
|
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: 58.71 E-value: 5.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 590 SSNVEEDYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLgEMRCVHGSILLNG-------------SVAYVPQVPW 656
Cdd:cd03289 9 TAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwrkAFGVIPQKVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 657 LLSGTVRENI-LFGKPFDskryfETLSACALDVDISLMV----GGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLL 731
Cdd:cd03289 88 IFSGTFRKNLdPYGKWSD-----EEIWKVAEEVGLKSVIeqfpGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 732 DDV---LSAVDSQVGCWILQRALLGPllnkkTRVMCTHNIQAISCADMIVVMDKGKVNWSGSV-------TDMPKSISPT 801
Cdd:cd03289 163 DEPsahLDPITYQVIRKTLKQAFADC-----TVILSEHRIEAMLECQRFLVIEENKVRQYDSIqkllnekSHFKQAISPS 237
|
250 260 270
....*....|....*....|....*....|....*
gi 1063701384 802 FSLTNEFDMSSPNHLTK-RKETLSIKEDGVDEISE 835
Cdd:cd03289 238 DRLKLFPRRNSSKSKRKpRPQIQALQEETEEEVQD 272
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
601-785 |
5.68e-09 |
|
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: 57.18 E-value: 5.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVH--GSILLNG----------SVAYVPQVPWLLSG-TVRENIL 667
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGrpldkrsfrkIIGYVPQDDILHPTlTVRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 668 FgkpfdskryfetlSACAldvdislmvggdmacigdKGlnLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSqVGCWIL 747
Cdd:cd03213 105 F-------------AAKL------------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDS-SSALQV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1063701384 748 QRALLGPLLNKKTRVMCTH--NIQAISCADMIVVMDKGKV 785
Cdd:cd03213 151 MSLLRRLADTGRTIICSIHqpSSEIFELFDKLLLLSQGRV 190
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
603-741 |
1.12e-08 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 56.21 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 603 QVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS------VAYVPQVPWL--LSG-----TVRENILFG 669
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeqrDEPHENILYLghLPGlkpelSALENLHFW 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063701384 670 KPFdskryfetLSACALDVDISLmvggdmACIGDKGLN------LSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQ 741
Cdd:TIGR01189 98 AAI--------HGGAQRTIEDAL------AAVGLTGFEdlpaaqLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
605-781 |
1.16e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 57.42 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 605 SLRVPKGSF-----VAVIGEVGSGKTSLLNSLLGEMRCVHGSILL-NGSVAYVPQ-VPWLLSGTVREnILFGKP--FDSK 675
Cdd:cd03237 14 TLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIeLDTVSYKPQyIKADYEGTVRD-LLSSITkdFYTH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 676 RYFETLSACALDVDiSLMvggdmacigDKGLN-LSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQvgcwilQRALLGP 754
Cdd:cd03237 93 PYFKTEIAKPLQIE-QIL---------DREVPeLSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE------QRLMASK 156
|
170 180 190
....*....|....*....|....*....|....
gi 1063701384 755 LL------NKKTRVMCTHNIQAIS-CADMIVVMD 781
Cdd:cd03237 157 VIrrfaenNEKTAFVVEHDIIMIDyLADRLIVFE 190
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
603-793 |
1.88e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 57.58 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 603 QVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGSV-----------------AYVPQVPWLLSG-TVRE 664
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgiclppekrriGYVFQDARLFPHyKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 665 NILFG-KPFDsKRYFETLsacaldvdISLMvggdmaciGDKGL------NLSGGQRARFALARAVYHGSDMYLLDDVLSA 737
Cdd:PRK11144 96 NLRYGmAKSM-VAQFDKI--------VALL--------GIEPLldrypgSLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063701384 738 VDsqvgcwiL--QRALLgPLLNKKTR------VMCTHNIQAI-SCADMIVVMDKGKVNWSGSVTD 793
Cdd:PRK11144 159 LD-------LprKRELL-PYLERLAReinipiLYVSHSLDEIlRLADRVVVLEQGKVKAFGPLEE 215
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
601-733 |
2.11e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.43 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG--------------SVAYVPQVPWLLSG-TVREN 665
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditdwqtakimreAVAIVPEGRRVFSRmTVEEN 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063701384 666 ILFGKPFDSKRYFETLSACALDVDISLMV-----GGDMacigdkglnlSGGQRARFALARAVYHGSDMYLLDD 733
Cdd:PRK11614 101 LAMGGFFAERDQFQERIKWVYELFPRLHErriqrAGTM----------SGGEQQMLAIGRALMSQPRLLLLDE 163
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
602-785 |
2.63e-08 |
|
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: 55.61 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 602 KQVSLRVPKGSFVAVIGEVGSGKTSLLnsllgemRCVH-------GSILLNG---------------SVAYVPQ----VP 655
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLL-------RCINlleepdsGTIIIDGlkltddkkninelrqKVGMVFQqfnlFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 656 WLlsgTVRENILFGkPFD----SKRYFETLSACALDVdislmVGgdmacIGDKG----LNLSGGQRARFALARAVYHGSD 727
Cdd:cd03262 90 HL---TVLENITLA-PIKvkgmSKAEAEERALELLEK-----VG-----LADKAdaypAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063701384 728 MYLLDDVLSAVDSQvgcwilqraLLGPLLN--------KKTRVMCTHNIQ-AISCADMIVVMDKGKV 785
Cdd:cd03262 156 VMLFDEPTSALDPE---------LVGEVLDvmkdlaeeGMTMVVVTHEMGfAREVADRVIFMDDGRI 213
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
909-1071 |
3.75e-08 |
|
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: 56.28 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 909 LMVLCIFcIINSILTLVRAFSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFILNILL 988
Cdd:cd18552 43 LAIIGLF-LLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 989 ANFVGLLGIIVVLSYVQ--------VLFLLLLLPFWYIYSKLqvfyRSTSRelRRLDSVSRspIYASFTETLDGSSTIRA 1060
Cdd:cd18552 122 RDPLTVIGLLGVLFYLDwkltlialVVLPLAALPIRRIGKRL----RKISR--RSQESMGD--LTSVLQETLSGIRVVKA 193
|
170
....*....|.
gi 1063701384 1061 FKSEEHFVGRF 1071
Cdd:cd18552 194 FGAEDYEIKRF 204
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
583-836 |
4.16e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 55.86 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 583 EDASCTWSSNVEEDYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSL---LNSLLGEMRcvhGSILLNG------------- 646
Cdd:PRK13633 8 KNVSYKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALLIPSE---GKVYVDGldtsdeenlwdir 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 647 -SVAYVPQVP--WLLSGTVRENILFGKpfdskryfETLSACALD----VDISLmvggdmacigdKGLN-----------L 708
Cdd:PRK13633 85 nKAGMVFQNPdnQIVATIVEEDVAFGP--------ENLGIPPEEirerVDESL-----------KKVGmyeyrrhaphlL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 709 SGGQRARFALARAVYHGSDMYLLDDVLSAVDSqvgcwILQRALLGPL--LNKK---TRVMCTHNIQAISCADMIVVMDKG 783
Cdd:PRK13633 146 SGGQKQRVAIAGILAMRPECIIFDEPTAMLDP-----SGRREVVNTIkeLNKKygiTIILITHYMEEAVEADRIIVMDSG 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 784 KVNWSGSvtdmPKSISPTFSLTNEFDMSSPnHLTK-----RKETLSIKED--GVDEISEA 836
Cdd:PRK13633 221 KVVMEGT----PKEIFKEVEMMKKIGLDVP-QVTElayelKKEGVDIPSDilTIDEMVNE 275
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
600-772 |
4.87e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 55.55 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 600 TIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSL--LGEMR---CVHGSILLNGSVAYVP---------------QVPWLLS 659
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNpevTITGSIVYNGHNIYSPrtdtvdlrkeigmvfQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 660 GTVRENILFGKPFDSKRYFETLSACaldVDISLMvggdMACIGDK--------GLNLSGGQRARFALARAVYHGSDMYLL 731
Cdd:PRK14239 100 MSIYENVVYGLRLKGIKDKQVLDEA---VEKSLK----GASIWDEvkdrlhdsALGLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1063701384 732 DDVLSAVDSqVGCWILQRALLGpLLNKKTRVMCTHNIQAIS 772
Cdd:PRK14239 173 DEPTSALDP-ISAGKIEETLLG-LKDDYTMLLVTRSMQQAS 211
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
592-739 |
5.17e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.57 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 592 NVEEDYN--LTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS------VAYVPQV--------- 654
Cdd:PRK13540 6 ELDFDYHdqPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlCTYQKQLcfvghrsgi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 655 -PWLlsgTVRENILFGKPFDSKRyFETLSACALdvdISLMVGGDMACigdkGLnLSGGQRARFALARAVYHGSDMYLLDD 733
Cdd:PRK13540 86 nPYL---TLRENCLYDIHFSPGA-VGITELCRL---FSLEHLIDYPC----GL-LSSGQKRQVALLRLWMSKAKLWLLDE 153
|
....*.
gi 1063701384 734 VLSAVD 739
Cdd:PRK13540 154 PLVALD 159
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
604-767 |
5.45e-08 |
|
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: 54.72 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 604 VSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-SVAYVP--QVPWLlsgtvRENIlfGKPFDSKRYFET 680
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqDVSDLRgrAIPYL-----RRKI--GVVFQDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 681 LS-----ACALDV------DISLMVGGDMACIGDKG------LNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQVG 743
Cdd:cd03292 93 RNvyenvAFALEVtgvpprEIRKRVPAALELVGLSHkhralpAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180
....*....|....*....|....*....
gi 1063701384 744 CWILQrallgpLLNK-----KTRVMCTHN 767
Cdd:cd03292 173 WEIMN------LLKKinkagTTVVVATHA 195
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
601-721 |
5.51e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 55.16 E-value: 5.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-------------SVAYVPQV-----PWllsgTV 662
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHsslsfPF----TV 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063701384 663 RENILFGK-PF-DSKRYFETLSACALD-VDISLMVGGDMacigdkgLNLSGGQRARFALARA 721
Cdd:PRK13548 94 EEVVAMGRaPHgLSRAEDDALVAAALAqVDLAHLAGRDY-------PQLSGGEQQRVQLARV 148
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
577-785 |
7.41e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 55.13 E-value: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 577 DLAVCVEDASCTWssnveEDYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS--------- 647
Cdd:PRK13647 2 DNIIEVEDLHFRY-----KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRevnaenekw 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 648 ----VAYVPQVP--WLLSGTVRENILFGkPFD--------SKRYFETLSACaldvdislmvggDMACIGDKG-LNLSGGQ 712
Cdd:PRK13647 77 vrskVGLVFQDPddQVFSSTVWDDVAFG-PVNmgldkdevERRVEEALKAV------------RMWDFRDKPpYHLSYGQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063701384 713 RARFALARAVYHGSDMYLLDDVLSAVDSQvGCWILQRALLGPLLNKKTRVMCTHNIQ-AISCADMIVVMDKGKV 785
Cdd:PRK13647 144 KKRVAIAGVLAMDPDVIVLDEPMAYLDPR-GQETLMEILDRLHNQGKTVIVATHDVDlAAEWADQVIVLKEGRV 216
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
598-797 |
9.53e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.50 E-value: 9.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 598 NLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG------------------SVAYVPQVpwlls 659
Cdd:PRK11432 19 NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedvthrsiqqrdicmvfqSYALFPHM----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 660 gTVRENILFG-------KPFDSKRYFETLSacaldvdislMVggDMACIGDKGLN-LSGGQRARFALARAVYHGSDMYLL 731
Cdd:PRK11432 94 -SLGENVGYGlkmlgvpKEERKQRVKEALE----------LV--DLAGFEDRYVDqISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063701384 732 DDVLSAVDSQvgcwiLQRAL------LGPLLNkKTRVMCTHN-IQAISCADMIVVMDKGKVNWSGSVTDM---PKS 797
Cdd:PRK11432 161 DEPLSNLDAN-----LRRSMrekireLQQQFN-ITSLYVTHDqSEAFAVSDTVIVMNKGKIMQIGSPQELyrqPAS 230
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
604-819 |
1.10e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 54.74 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 604 VSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-----------------SVAYVPQVP--WLLSGTVRE 664
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstskqkeikpvrkKVGVVFQFPesQLFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 665 NILFG-KPFD-SKRYFETLSACALDvdislMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQV 742
Cdd:PRK13643 105 DVAFGpQNFGiPKEKAEKIAAEKLE-----MVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063701384 743 GCWILQraLLGPLLNK-KTRVMCTHNIQAIS-CADMIVVMDKGKVNWSGSVTDMPKSISptFSLTNEFDMSSPNHLTKR 819
Cdd:PRK13643 180 RIEMMQ--LFESIHQSgQTVVLVTHLMDDVAdYADYVYLLEKGHIISCGTPSDVFQEVD--FLKAHELGVPKATHFADQ 254
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
603-785 |
1.10e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 54.84 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 603 QVSLRVPKGSFVAVIGEVGSGKTSLL---NSLL----GEMRCVHGSILLNGS----------VAYVPQVP--WLLSGTVR 663
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMqhfNALLkpssGTITIAGYHITPETGnknlkklrkkVSLVFQFPeaQLFENTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 664 ENILFGkpfdsKRYFETLSACALDVDISLM--VGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQ 741
Cdd:PRK13641 105 KDVEFG-----PKNFGFSEDEAKEKALKWLkkVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063701384 742 VgcwilQRALLGPLLNKK----TRVMCTHNIQAIS-CADMIVVMDKGKV 785
Cdd:PRK13641 180 G-----RKEMMQLFKDYQkaghTVILVTHNMDDVAeYADDVLVLEHGKL 223
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
598-785 |
1.28e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 54.08 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 598 NLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSL-----LGEMRCVHGSILLNGSVAYVPQV-PWLLSGTVRENILFGKP 671
Cdd:PRK14267 17 NHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVdPIEVRREVGMVFQYPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 672 FDSKRYFETLsacALDVDISLMVGGDMAC--------------------IGDKGLNLSGGQRARFALARAVYHGSDMYLL 731
Cdd:PRK14267 97 FPHLTIYDNV---AIGVKLNGLVKSKKELdervewalkkaalwdevkdrLNDYPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063701384 732 DDVLSAVDSqVGCWILQRaLLGPLLNKKTRVMCTHN-IQAISCADMIVVMDKGKV 785
Cdd:PRK14267 174 DEPTANIDP-VGTAKIEE-LLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKL 226
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
610-772 |
1.77e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.61 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 610 KGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGSVAYVPQVPWLLSGTVrenilfgkpfdskryfetlsacaldvd 689
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 690 islmvggdmacIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQVGCWILQ----RALLGPLLNKKTRVMCT 765
Cdd:smart00382 54 -----------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelRLLLLLKSEKNLTVILT 122
|
....*..
gi 1063701384 766 HNIQAIS 772
Cdd:smart00382 123 TNDEKDL 129
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
909-1071 |
1.85e-07 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 54.03 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 909 LMVLCIFcIINSILTLVRAFSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFILNILL 988
Cdd:cd18576 40 LLLLGLF-LLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 989 ANFVGLLGIIVVLSYVQV---LFLLLLLPFWYIYSKLqvfyrsTSRELRRL-----DSVSRSPIYAsfTETLDGSSTIRA 1060
Cdd:cd18576 119 RQILTLIGGVVLLFFISWkltLLMLATVPVVVLVAVL------FGRRIRKLskkvqDELAEANTIV--EETLQGIRVVKA 190
|
170
....*....|.
gi 1063701384 1061 FKSEEHFVGRF 1071
Cdd:cd18576 191 FTREDYEIERY 201
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
601-785 |
1.91e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 54.02 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-----------------SVAYVPQVP--WLLSGT 661
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrkRIGMVFQFPesQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 662 VRENILFGkPFDSKRYFETLSACALDVDISLMVGGDMacIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQ 741
Cdd:PRK13646 103 VEREIIFG-PKNFKMNLDEVKNYAHRLLMDLGFSRDV--MSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063701384 742 VGCWILQRALLGPLLNKKTRVMCTHNIQAISC-ADMIVVMDKGKV 785
Cdd:PRK13646 180 SKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSI 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
575-790 |
2.17e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 54.09 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 575 SEDLAVCVEDASCTWSSNVEEDYnLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSIL----------- 643
Cdd:PRK13631 17 SDDIILRVKNLYCVFDEKQENEL-VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiyigdkkn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 644 ------------------LNGSVAYVPQVP--WLLSGTVRENILFGkPFD---SKRYFETLSACALDvdislMVGGDMAC 700
Cdd:PRK13631 96 nhelitnpyskkiknfkeLRRRVSMVFQFPeyQLFKDTIEKDIMFG-PVAlgvKKSEAKKLAKFYLN-----KMGLDDSY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 701 IGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQvGCWILQRALLGPLLNKKTRVMCTHNI-QAISCADMIVV 779
Cdd:PRK13631 170 LERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK-GEHEMMQLILDAKANNKTVFVITHTMeHVLEVADEVIV 248
|
250
....*....|.
gi 1063701384 780 MDKGKVNWSGS 790
Cdd:PRK13631 249 MDKGKILKTGT 259
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
604-739 |
2.31e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.18 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 604 VSLRVPKGSFVAVIGEVGSGKTSLLN---SLLGEMRcvhGSILLNGS-------------VAYVPQVPWLLSGTVRENIL 667
Cdd:PRK10247 26 ISFSLRAGEFKLITGPSGCGKSTLLKivaSLISPTS---GTLLFEGEdistlkpeiyrqqVSYCAQTPTLFGDTVYDNLI 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063701384 668 F-----GKPFDSKRYFETLSACALDVDISlmvggdmacigDKGLN-LSGGQRARFALARAVYHGSDMYLLDDVLSAVD 739
Cdd:PRK10247 103 FpwqirNQQPDPAIFLDDLERFALPDTIL-----------TKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
604-740 |
2.59e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 53.16 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 604 VSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGSVAYVPQ------------VPWLlsgTVRENILFGkp 671
Cdd:PRK11248 20 INLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGaergvvfqneglLPWR---NVQDNVAFG-- 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063701384 672 fdskryfetLSACALDVDISLMVGGDM-ACIGDKGL------NLSGGQRARFALARAVYHGSDMYLLDDVLSAVDS 740
Cdd:PRK11248 95 ---------LQLAGVEKMQRLEIAHQMlKKVGLEGAekryiwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
596-798 |
2.74e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 53.54 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 596 DYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG---------------SVAYVPQVP--WLL 658
Cdd:PRK13639 13 DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkksllevrkTVGIVFQNPddQLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 659 SGTVRENILFGkPFD--------SKRYFETLSAcaldvdislmVGgdMACIGDKG-LNLSGGQRARFALARAVYHGSDMY 729
Cdd:PRK13639 93 APTVEEDVAFG-PLNlglskeevEKRVKEALKA----------VG--MEGFENKPpHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063701384 730 LLDDVLSAVDSQVGCWILQraLLGPlLNKK--TRVMCTHNIQAISC-ADMIVVMDKGKVNWSGSvtdmPKSI 798
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMK--LLYD-LNKEgiTIIISTHDVDLVPVyADKVYVMSDGKIIKEGT----PKEV 224
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
601-796 |
2.93e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 54.67 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRC---VHGSILLNGSV----------AYVPQVPWLL-SGTVRENI 666
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPidakemraisAYVQQDDLFIpTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 667 LFGKPFDSKRYFeTLSACALDVDISLMVGGDMAC----IGDKGL--NLSGGQRARFALARAVYHGSDMYLLDDVLSAVDS 740
Cdd:TIGR00955 121 MFQAHLRMPRRV-TKKEKRERVDEVLQALGLRKCantrIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063701384 741 QVGCWILQraLLGPLLNKKTRVMCT-H--NIQAISCADMIVVMDKGKVNWSGSVTDMPK 796
Cdd:TIGR00955 200 FMAYSVVQ--VLKGLAQKGKTIICTiHqpSSELFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
604-798 |
3.16e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.21 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 604 VSLRVPKGSFVAVIGEVGSGKTS---LLNSLL----GEMRcVHGSILLNGS-----------VAYVPQVP--WLLSGTVR 663
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTimqLLNGLHvptqGSVR-VDDTLITSTSknkdikqirkkVGLVFQFPesQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 664 ENILFG-KPFD-SKRYFETLSACALdvdisLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQ 741
Cdd:PRK13649 105 KDVAFGpQNFGvSQEEAEALAREKL-----ALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063701384 742 vgcwilQRALLGPLLNK-----KTRVMCTHNIQAIS-CADMIVVMDKGKVNWSGSvtdmPKSI 798
Cdd:PRK13649 180 ------GRKELMTLFKKlhqsgMTIVLVTHLMDDVAnYADFVYVLEKGKLVLSGK----PKDI 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
601-785 |
3.23e-07 |
|
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: 53.03 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG------------------------SVAYVPQVpw 656
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrelrrkkismvfqSFALLPHR-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 657 llsgTVRENILFG-------KPFDSKRYFETLSACALDVDISLMVGgdmacigdkglNLSGGQRARFALARAVYHGSDMY 729
Cdd:cd03294 118 ----TVLENVAFGlevqgvpRAEREERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDIL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063701384 730 LLDDVLSAVDS------QVGCWILQRALlgpllnKKTRVMCTHN-IQAISCADMIVVMDKGKV 785
Cdd:cd03294 183 LMDEAFSALDPlirremQDELLRLQAEL------QKTIVFITHDlDEALRLGDRIAIMKDGRL 239
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
588-783 |
3.70e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 51.86 E-value: 3.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 588 TWSS-----NVEEDYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLG--EMRCVHGSILLNG---------SVAYV 651
Cdd:cd03232 5 TWKNlnytvPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGrpldknfqrSTGYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 652 PQVPWLLSG-TVRENILFgkpfdskryfetlSACAldvdislmvggdmacigdKGLNLSggQRARFALARAVYHGSDMYL 730
Cdd:cd03232 85 EQQDVHSPNlTVREALRF-------------SALL------------------RGLSVE--QRKRLTIGVELAAKPSILF 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063701384 731 LDDVLSAVDSQvGCWILQRaLLGPLLNKKTRVMCT-H--NIQAISCADMIVVMDKG 783
Cdd:cd03232 132 LDEPTSGLDSQ-AAYNIVR-FLKKLADSGQAILCTiHqpSASIFEKFDRLLLLKRG 185
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
651-781 |
4.85e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.26 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 651 VPQVPWLLSGTVRENILFGKPfDSKRYfETLSAC---ALDVDISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSD 727
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGKE-DATRE-DVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPK 1378
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1063701384 728 MYLLDDVLSAVDSQVGCWILQRALLGPLLNKKTRVMCTHNIQAISCADMIVVMD 781
Cdd:PTZ00265 1379 ILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFN 1432
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
448-779 |
4.98e-07 |
|
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: 54.53 E-value: 4.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 448 LLTNIR---TLKMYG----WDNWFADWLKETRATEVTHLATRKYLDAWC----VFFwattptlFSLCTFglFALMGHQLD 516
Cdd:TIGR01271 1067 LITSLKglwTIRAFGrqsyFETLFHKALNLHTANWFLYLSTLRWFQMRIdiifVFF-------FIAVTF--IAIGTNQDG 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 517 AATVFTCLALFNSLISplnSFPWVINGLIDAFISTRRVSKFLCCLEHSRDFSIDSGFT-----SEDLAVCVEDASCTWSS 591
Cdd:TIGR01271 1138 EGEVGIILTLAMNILS---TLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRPSGGGgkyqlSTVLVIENPHAQKCWPS 1214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 592 NVEEDY-NLTIK----------QVSLRVPKGSFVAVIGEVGSGKTSLLNSLLgEMRCVHGSILLNG-------------S 647
Cdd:TIGR01271 1215 GGQMDVqGLTAKyteagravlqDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGvswnsvtlqtwrkA 1293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 648 VAYVPQVPWLLSGTVRENILFGKPFDSKRYFETLSACALDVDISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSD 727
Cdd:TIGR01271 1294 FGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAK 1373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1063701384 728 MYLLDDVLSAVDSqVGCWILQRALLGPLLNkKTRVMCTHNIQA-ISCADMIVV 779
Cdd:TIGR01271 1374 ILLLDEPSAHLDP-VTLQIIRKTLKQSFSN-CTVILSEHRVEAlLECQQFLVI 1424
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
908-1071 |
5.55e-07 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 52.64 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 908 YLMVLCIFcIINSILTLVRAFSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFILNIL 987
Cdd:cd18780 45 VLILLGVV-LIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSML 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 988 LANFVGLLGIIVVLSYVQVLFLLLLLPFWYIYSKLQVFYRSTSRELRRL--DSVSRSPIYASftETLDGSSTIRAFKSEE 1065
Cdd:cd18780 124 LRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKfqDALAAASTVAE--ESISNIRTVRSFAKET 201
|
....*.
gi 1063701384 1066 HFVGRF 1071
Cdd:cd18780 202 KEVSRY 207
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
605-766 |
5.58e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 51.34 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 605 SLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS------VAYVPQVPWL--LSG-----TVRENIlfgkp 671
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEpirrqrDEYHQDLLYLghQPGiktelTALENL----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 672 fdskRYFETLSACALDVDI--SL-MVG--G--DMACigdkgLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQvGC 744
Cdd:PRK13538 96 ----RFYQRLHGPGDDEALweALaQVGlaGfeDVPV-----RQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ-GV 165
|
170 180
....*....|....*....|..
gi 1063701384 745 WILQRALLGPLLNKKTRVMCTH 766
Cdd:PRK13538 166 ARLEALLAQHAEQGGMVILTTH 187
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
601-789 |
6.96e-07 |
|
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: 51.56 E-value: 6.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGsvaYVP-------------------QVPWLLSgt 661
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG---LVPwkrrkkflrrigvvfgqktQLWWDLP-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 662 VRENILFGKP---FDSKRYFETLSACAldvdiSLMvggDMACIGDKGL-NLSGGQRARFALARAVYHGSDMYLLD----- 732
Cdd:cd03267 112 VIDSFYLLAAiydLPPARFKKRLDELS-----ELL---DLEELLDTPVrQLSLGQRMRAEIAAALLHEPEILFLDeptig 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063701384 733 -DVLSavdsqvgcwilQRALLGPL--LNK--KTRVMCT-HNIQAI-SCADMIVVMDKGKVNWSG 789
Cdd:cd03267 184 lDVVA-----------QENIRNFLkeYNRerGTTVLLTsHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
591-794 |
8.11e-07 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 51.62 E-value: 8.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 591 SNVEEDYN--LTIKQVSLRVPKGSFVAVIGEVGSGKTSLLnSLLGE-MRCVHGSILLNG-------------SVAYVPQV 654
Cdd:COG4604 5 KNVSKRYGgkVVLDDVSLTIPKGGITALIGPNGAGKSTLL-SMISRlLPPDSGEVLVDGldvattpsrelakRLAILRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 655 PWLLSG-TVRENILFGK-PFDSKRyfetLSACalD---VD--ISLMvggDMACIGDKGLN-LSGGQRARFALARAVYHGS 726
Cdd:COG4604 84 NHINSRlTVRELVAFGRfPYSKGR----LTAE--DreiIDeaIAYL---DLEDLADRYLDeLSGGQRQRAFIAMVLAQDT 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063701384 727 DMYLLDDVLSAVD---SQVGCWILQRAL--LGpllnkKTRVMCTHNIQAISC-ADMIVVMDKGKVNWSGSVTDM 794
Cdd:COG4604 155 DYVLLDEPLNNLDmkhSVQMMKLLRRLAdeLG-----KTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPEEI 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
601-794 |
1.15e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 51.77 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG---------------SVAYVPQVP--WLLSGTVR 663
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpidysrkglmklreSVGMVFQDPdnQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 664 ENILFGK-----PFDSKRYfetlsacalDVDISLMVGGdMACIGDKGLN-LSGGQRARFALARAVYHGSDMYLLDDVLSA 737
Cdd:PRK13636 102 QDVSFGAvnlklPEDEVRK---------RVDNALKRTG-IEHLKDKPTHcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063701384 738 VDSQVGCWILQraLLGPLLNKK--TRVMCTHNIQ--AISCaDMIVVMDKGKVNWSGSVTDM 794
Cdd:PRK13636 172 LDPMGVSEIMK--LLVEMQKELglTIIIATHDIDivPLYC-DNVFVMKEGRVILQGNPKEV 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
602-785 |
1.16e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.72 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 602 KQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS--------------VAYVPQ----VPWLlsgTVR 663
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvrirsprdaialgIGMVHQhfmlVPNL---TVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 664 ENILFGKPfDSKRYFETLSACA-----------LDVDISLMVGgdmacigdkglNLSGGQRARFALARAVYHGSDMYLLD 732
Cdd:COG3845 99 ENIVLGLE-PTKGGRLDRKAARarirelserygLDVDPDAKVE-----------DLSVGEQQRVEILKALYRGARILILD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063701384 733 D---VLS--AVDsqvgcwilqrALLGpLLNK-----KTRVMCTHN---IQAIscADMIVVMDKGKV 785
Cdd:COG3845 167 EptaVLTpqEAD----------ELFE-ILRRlaaegKSIIFITHKlreVMAI--ADRVTVLRRGKV 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
602-732 |
1.20e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 52.71 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 602 KQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGemrcVH----GSILLNGS--------------VAYVPQ----VPWLls 659
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSG----VYqpdsGEILLDGEpvrfrsprdaqaagIAIIHQelnlVPNL-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 660 gTVRENILFGKPF-------------DSKRYFETLSacaLDVDISLMVGgdmacigdkglNLSGGQRARFALARAVYHGS 726
Cdd:COG1129 95 -SVAENIFLGREPrrgglidwramrrRARELLARLG---LDIDPDTPVG-----------DLSVAQQQLVEIARALSRDA 159
|
....*.
gi 1063701384 727 DMYLLD 732
Cdd:COG1129 160 RVLILD 165
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
598-790 |
2.69e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 51.19 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 598 NLTIKQVSLRVPKGSFVAVIGEVGSGKTS---LLNSLLGEMRcvhGSILLNG-----------------SVAYVPQVPWL 657
Cdd:PRK10070 41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTmvrLLNRLIEPTR---GQVLIDGvdiakisdaelrevrrkKIAMVFQSFAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 658 LSG-TVRENILFGKPFDSKRYFETLSACaldVDISLMVGGDMACIGDKGlNLSGGQRARFALARAVYHGSDMYLLDDVLS 736
Cdd:PRK10070 118 MPHmTVLDNTAFGMELAGINAEERREKA---LDALRQVGLENYAHSYPD-ELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063701384 737 AVDSQVGCWILQRALLGPLLNKKTRVMCTHNI-QAISCADMIVVMDKGKVNWSGS 790
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
592-733 |
3.21e-06 |
|
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: 51.09 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 592 NVEEDYN--LTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGSV--AYVPQvpwllsgtVRENIL 667
Cdd:TIGR03719 327 NLTKAFGdkLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVklAYVDQ--------SRDALD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 668 fgkpfDSKRYFETLSAcALDVdisLMVGG-DM---ACIGD---KGL-------NLSGGQRARFALARAVYHGSDMYLLDD 733
Cdd:TIGR03719 399 -----PNKTVWEEISG-GLDI---IKLGKrEIpsrAYVGRfnfKGSdqqkkvgQLSGGERNRVHLAKTLKSGGNVLLLDE 469
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
592-785 |
3.84e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 50.41 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 592 NVEEDYNLTI--KQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG-----------SVAYVPQ----V 654
Cdd:PRK11000 8 NVTKAYGDVVisKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmndvppaerGVGMVFQsyalY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 655 PWLlsgTVRENILFG-------KPFDSKRY---FETLSACALdvdislmvggdmacIGDKGLNLSGGQRARFALARAVYH 724
Cdd:PRK11000 88 PHL---SVAENMSFGlklagakKEEINQRVnqvAEVLQLAHL--------------LDRKPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063701384 725 GSDMYLLDDVLSAVDS----QVGCWI--LQRALlgpllnKKTRVMCTHN-IQAISCADMIVVMDKGKV 785
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAalrvQMRIEIsrLHKRL------GRTMIYVTHDqVEAMTLADKIVVLDAGRV 212
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
904-1146 |
6.22e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 49.43 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 904 STSFYLMVLCIFCIINSILTLVRAFSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFSSDLYT-------- 975
Cdd:cd18555 40 LLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRANSNVYIrqilsnqv 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 976 ----IDDSLPFILNILLANFVGLLGIIVVLSYVqvlflllllpfwyIYSKLQVFYRSTSRELRRLDSVSRSPIYASFTET 1051
Cdd:cd18555 120 isliIDLLLLVIYLIYMLYYSPLLTLIVLLLGL-------------LIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTET 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1052 LDGSSTIRAFKSEEHFV----GRFIEHLTLYQRTSYSEIIASlWLSLRLQLLGSMIVLFVAVMAVLgsGGNfpISFGTpg 1127
Cdd:cd18555 187 LYGIETIKSLGSEKNIYkkweNLFKKQLKAFKKKERLSNILN-SISSSIQFIAPLLILWIGAYLVI--NGE--LTLGE-- 259
|
250 260
....*....|....*....|..
gi 1063701384 1128 LVG---LALSYAAPLVSLLGSL 1146
Cdd:cd18555 260 LIAfssLAGSFLTPIVSLINSY 281
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
908-1074 |
6.67e-06 |
|
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: 49.32 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 908 YLMVLCIFCIINSILTLVRAFSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFILNIL 987
Cdd:cd18547 47 ILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 988 LANFVGLLGIIV---VLSYVQVLFLLLLLPFWYIYSKL-----QVFYRSTSRELRRLDSvsrspiYAsfTETLDGSSTIR 1059
Cdd:cd18547 127 ISSILTIVGTLImmlYISPLLTLIVLVTVPLSLLVTKFiakrsQKYFRKQQKALGELNG------YI--EEMISGQKVVK 198
|
170
....*....|....*
gi 1063701384 1060 AFKSEEHFVGRFIEH 1074
Cdd:cd18547 199 AFNREEEAIEEFDEI 213
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
907-1163 |
1.08e-05 |
|
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: 48.58 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 907 FYLMVLCIFCIINSILTLVRAFSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFILNI 986
Cdd:cd18542 40 LLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 987 LLANFVGLLGIIVVLSYVQVL---FLLLLLPF-----WYIYSKLQVFYRSTSRELRRLDSVsrspiyasFTETLDGSSTI 1058
Cdd:cd18542 120 LVRAVLLFIGALIIMFSINWKltlISLAIIPFialfsYVFFKKVRPAFEEIREQEGELNTV--------LQENLTGVRVV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1059 RAFKSEEHFVGRFIEHLTLYQRTSYSEIIASLWLSLRlqllgSMIVLFVAVMAVLGSGGNF----PISFGTpgLVGLaLS 1134
Cdd:cd18542 192 KAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPL-----MDFLSGLQIVLVLWVGGYLvingEITLGE--LVAF-IS 263
|
250 260 270
....*....|....*....|....*....|..
gi 1063701384 1135 YAAPL---VSLLGSLLTSFTETekeMVSVERV 1163
Cdd:cd18542 264 YLWMLiwpVRQLGRLINDMSRA---SASAERI 292
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
905-1163 |
1.12e-05 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 48.66 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 905 TSFYLMVLCIFCIiNSILTLVRAFSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFIL 984
Cdd:cd18573 41 KTFALALLGVFVV-GAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 985 NILLANFVGLLGIIVVLSYVQV---LFLLLLLP----FWYIYSKLQvfyRSTSRELrrLDSVSRSPIYAsfTETLDGSST 1057
Cdd:cd18573 120 SDGLRSLVSGVGGIGMMLYISPkltLVMLLVVPpiavGAVFYGRYV---RKLSKQV--QDALADATKVA--EERLSNIRT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1058 IRAFKSEEHFVGRFIEHLTLYQRTSYSEIIASLWLSLRLQLLGSMIVLfvavmAVLGSGGNF----PISFGtpGLVGLAL 1133
Cdd:cd18573 193 VRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLL-----SVLYYGGSLvasgELTVG--DLTSFLM 265
|
250 260 270
....*....|....*....|....*....|
gi 1063701384 1134 sYAAPLVSLLGSLLTSFTETEKEMVSVERV 1163
Cdd:cd18573 266 -YAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
615-854 |
1.21e-05 |
|
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: 50.01 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 615 AVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG------------SVAYVPQVPWLLSG-TVRENILFGKPFDSKRYFETl 681
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldavrqSLGMCPQHNILFHHlTVAEHILFYAQLKGRSWEEA- 1038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 682 sacALDVDISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVD--SQVGCWilqrALLGPLLNKK 759
Cdd:TIGR01257 1039 ---QLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDpySRRSIW----DLLLKYRSGR 1111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 760 TRVMCTHNI-QAISCADMIVVMDKGKVNWSGSVTDMPKSISPTFSLTNEFDMSSPNHLTKRKE-TLSIKEDGVDEISEAA 837
Cdd:TIGR01257 1112 TIIMSTHHMdEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIQSQRGGCEgTCSCTSKGFSTRCPAR 1191
|
250
....*....|....*...
gi 1063701384 838 ADIVKLEERKEGRV-EMM 854
Cdd:TIGR01257 1192 VDEITPEQVLDGDVnELM 1209
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
601-797 |
1.36e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 48.04 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLnsllgemRCVH-------GSILLNGS-------------VAYVPQVPWLLSG 660
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFL-------RCINflekpseGSIVVNGQtinlvrdkdgqlkVADKNQLRLLRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 661 --------------TVRENILfGKPFD----SKRYFETLSACALDvdislMVGGDMACIGDKGLNLSGGQRARFALARAV 722
Cdd:PRK10619 94 ltmvfqhfnlwshmTVLENVM-EAPIQvlglSKQEARERAVKYLA-----KVGIDERAQGKYPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063701384 723 YHGSDMYLLDDVLSAVDSQVGCWILqRALLGPLLNKKTRVMCTHNIQ-AISCADMIVVMDKGKVNWSGSVTDM---PKS 797
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVL-RIMQQLAEEGKTMVVVTHEMGfARHVSSHVIFLHQGKIEEEGAPEQLfgnPQS 245
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
893-1163 |
1.37e-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: 48.20 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 893 VDKTGKGVSHYSTsfyLMVLCIFCIINSILTLVRAFSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFSSD 972
Cdd:cd18551 26 IDALSAGGSSGGL---LALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTND 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 973 LYTIDDSLPFILNILLANFVGLLGIIVVLSY--------VQVLFLLLLLPFWYIYSKLQVFYRSTSRELRRLDSVsrspi 1044
Cdd:cd18551 103 TTLLRELITSGLPQLVTGVLTVVGAVVLMFLldwvltlvTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAA----- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1045 yasFTETLDGSSTIRAFKSEEHFVGRFIEHLT-LYQ---RTSYSEIIASLWlslrlqllgSMIVLFVAVMAVLGSGG--- 1117
Cdd:cd18551 178 ---LERALSAIRTVKASNAEERETKRGGEAAErLYRaglKAAKIEALIGPL---------MGLAVQLALLVVLGVGGarv 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1063701384 1118 -NFPISFGTpgLVGLALsYAAPLVSLLGSLLTSFTETEKEMVSVERV 1163
Cdd:cd18551 246 aSGALTVGT--LVAFLL-YLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
601-785 |
1.41e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 49.34 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSL-------LGEMRcVHGSIL--LNGSVayvpqvpwlLSGTVRENilFGKP 671
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptSGTYR-VAGQDVatLDADA---------LAQLRREH--FGFI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 672 FDSKRYFETLSAcALDVDISLMVGG---------DMACIGDKGL---------NLSGGQRARFALARAVYHGSDMYLLDD 733
Cdd:PRK10535 92 FQRYHLLSHLTA-AQNVEVPAVYAGlerkqrllrAQELLQRLGLedrveyqpsQLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063701384 734 VLSAVDSQVGCWILqrALLGPLLNK-KTRVMCTHNIQAISCADMIVVMDKGKV 785
Cdd:PRK10535 171 PTGALDSHSGEEVM--AILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
580-831 |
1.68e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 48.08 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 580 VCVEDASCTWSSNVEEDYNlTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSIL---------------- 643
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEFK-ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIvgdyaipanlkkikev 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 644 --LNGSVAYVPQVP--WLLSGTVRENILFG-------KPFDSKRYFETLSACALDVDIslmvggdmacIGDKGLNLSGGQ 712
Cdd:PRK13645 86 krLRKEIGLVFQFPeyQLFQETIEKDIAFGpvnlgenKQEAYKKVPELLKLVQLPEDY----------VKRSPFELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 713 RARFALARAVYHGSDMYLLDDVLSAVDSQVGCWILQralLGPLLNK---KTRVMCTHNI-QAISCADMIVVMDKGKVNWS 788
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFIN---LFERLNKeykKRIIMVTHNMdQVLRIADEVIVMHEGKVISI 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1063701384 789 GSvtdmPKSISPTFSLTNEFDMSSPNHLtkrKETLSIKEDGVD 831
Cdd:PRK13645 233 GS----PFEIFSNQELLTKIEIDPPKLY---QLMYKLKNKGID 268
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
595-732 |
1.70e-05 |
|
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: 49.01 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 595 EDYNLTIKQVSLRvpKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGSVAYVPQ-VPWLLSGTVRENI--LFGKP 671
Cdd:COG1245 352 GGFSLEVEGGEIR--EGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQyISPDYDGTVEEFLrsANTDD 429
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063701384 672 FDSKrYFETLSACALDVDiSLMvggdmacigDKGL-NLSGGQRARFALARAVYHGSDMYLLD 732
Cdd:COG1245 430 FGSS-YYKTEIIKPLGLE-KLL---------DKNVkDLSGGELQRVAIAACLSRDADLYLLD 480
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
578-653 |
2.09e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.73 E-value: 2.09e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063701384 578 LAVCVEDASCTWssnveeDYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILL--NGSVAYVPQ 653
Cdd:PRK15064 318 NALEVENLTKGF------DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWseNANIGYYAQ 389
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
591-784 |
2.84e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 47.52 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 591 SNVEEDY--NLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS------------VAYVPQVPW 656
Cdd:PRK13536 45 AGVSKSYgdKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVpvpararlararIGVVPQFDN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 657 L-LSGTVRENIL-FGkpfdskRYFEtLSACALDVDISLMVggDMACIGDKG----LNLSGGQRARFALARAVYHGSDMYL 730
Cdd:PRK13536 125 LdLEFTVRENLLvFG------RYFG-MSTREIEAVIPSLL--EFARLESKAdarvSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063701384 731 LDDVLSAVDSQVGCWILQRalLGPLLNK-KTRVMCTHNI-QAISCADMIVVMDKGK 784
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWER--LRSLLARgKTILLTTHFMeEAERLCDRLCVLEAGR 249
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
601-785 |
2.85e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.92 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGSV-----------AYVPQ----VPWLlsgTVREN 665
Cdd:PRK11650 20 IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVvnelepadrdiAMVFQnyalYPHM---SVREN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 666 ILFG-------KPFDSKRYFETlsACALDVDISLmvggdmacigD-KGLNLSGGQRARFALARAVYHGSDMYLLDDVLSA 737
Cdd:PRK11650 97 MAYGlkirgmpKAEIEERVAEA--ARILELEPLL----------DrKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSN 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063701384 738 VDS----QVGCWI--LQRALlgpllnKKTRVMCTHN-IQAISCADMIVVMDKGKV 785
Cdd:PRK11650 165 LDAklrvQMRLEIqrLHRRL------KTTSLYVTHDqVEAMTLADRVVVMNGGVA 213
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
576-646 |
2.94e-05 |
|
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: 46.37 E-value: 2.94e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063701384 576 EDLAVCVEDasctwssnveedyNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEM--RCVHGSILLNG 646
Cdd:cd03217 4 KDLHVSVGG-------------KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKG 63
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
865-1118 |
3.57e-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: 47.09 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 865 WFITIVILVSAVLMQGsrngndLWLSYWVDKTGKGVSHYSTSFYLMVLCIFCIINSILTLVRAFSFAFGGLKAAVHVHNA 944
Cdd:cd18575 1 ALIALLIAAAATLALG------QGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 945 LISKLINAPTQFFDQTPSGRILNRFSSD---LYT-IDDSLPFIL-NILLanFVGLLGIIVVLS-----YVQVLFLLLLLP 1014
Cdd:cd18575 75 VFAHLLRLSPSFFETTRTGEVLSRLTTDttlIQTvVGSSLSIALrNLLL--LIGGLVMLFITSpkltlLVLLVIPLVVLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1015 FWYIysklqvfyrstSRELRRL-----DSVSRSPIYASftETLDGSSTIRAFKSEEHFVGRFIEHLTLYQRTSYSEIIAS 1089
Cdd:cd18575 153 IILF-----------GRRVRRLsrasqDRLADLSAFAE--ETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRAR 219
|
250 260
....*....|....*....|....*....
gi 1063701384 1090 LWLSLRlqllgSMIVLFVAVMAVLGSGGN 1118
Cdd:cd18575 220 ALLTAL-----VIFLVFGAIVFVLWLGAH 243
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
601-802 |
4.06e-05 |
|
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: 46.62 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHG---SIL-----------LNGSVAYV-PQVPWLLSG--TVR 663
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFgerrggedvweLRKRIGLVsPALQLRFPRdeTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 664 ENILFGKpFDSKRYFETLSacalDVDISL------MVGgdMACIGDKGLN-LSGGQRARFALARAVYHGSDMYLLDDVLS 736
Cdd:COG1119 99 DVVLSGF-FDSIGLYREPT----DEQRERarelleLLG--LAHLADRPFGtLSQGEQRRVLIARALVKDPELLILDEPTA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063701384 737 AVDsqvgcwILQRALLGPLLNK------KTRVMCTHNIQAI-SCADMIVVMDKGKVNWSGSVTDM--PKSISPTF 802
Cdd:COG1119 172 GLD------LGARELLLALLDKlaaegaPTLVLVTHHVEEIpPGITHVLLLKDGRVVAAGPKEEVltSENLSEAF 240
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
611-793 |
4.21e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.95 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 611 GSFVAVIGEVGSGKTSLLNSLLGEMR--CVHGSILLNGS---------VAYVPQVPWLLSG-TVRENILFGK----PFDS 674
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQgnNFTGTILANNRkptkqilkrTGFVTQDDILYPHlTVRETLVFCSllrlPKSL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 675 KRYFETLSACALDVDISLMVGGDmACIGDKGL-NLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQVGCWILQRalLG 753
Cdd:PLN03211 174 TKQEKILVAESVISELGLTKCEN-TIIGNSFIrGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLT--LG 250
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1063701384 754 PLLNK-KTRVMCTH--NIQAISCADMIVVMDKGKVNWSGSVTD 793
Cdd:PLN03211 251 SLAQKgKTIVTSMHqpSSRVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
598-733 |
4.22e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 47.71 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 598 NLT----IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS--------------VAYVPQ------ 653
Cdd:COG1129 261 GLSvggvVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVPEdrkgeg 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 654 VpwLLSGTVRENI-------LFGKPF--------DSKRYFEtlsacALDV---DISLMVGgdmacigdkglNLSGG--QR 713
Cdd:COG1129 341 L--VLDLSIRENItlasldrLSRGGLldrrreraLAEEYIK-----RLRIktpSPEQPVG-----------NLSGGnqQK 402
|
170 180
....*....|....*....|
gi 1063701384 714 ArfALARAVYHGSDMYLLDD 733
Cdd:COG1129 403 V--VLAKWLATDPKVLILDE 420
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
594-785 |
8.26e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 45.85 E-value: 8.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 594 EEDYNlTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS-------------VAYVPQVP--WLL 658
Cdd:PRK13642 17 ESDVN-QLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGElltaenvwnlrrkIGMVFQNPdnQFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 659 SGTVRENILFGKPFDSKRYFETLSAcaldVDISLMVGGDMACIGDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAV 738
Cdd:PRK13642 96 GATVEDDVAFGMENQGIPREEMIKR----VDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063701384 739 DSQVGCWILQraLLGPLLNKK--TRVMCTHNIQAISCADMIVVMDKGKV 785
Cdd:PRK13642 172 DPTGRQEIMR--VIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
596-732 |
1.39e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.96 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 596 DYNLTIKQVSLRvpKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGSVAYVPQvpWLLS---GTVRENILF-GKP 671
Cdd:PRK13409 352 DFSLEVEGGEIY--EGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQ--YIKPdydGTVEDLLRSiTDD 427
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063701384 672 FDSKrYFETLSACALDVDiSLMvggdmacigDKGLN-LSGGQRARFALARAVYHGSDMYLLD 732
Cdd:PRK13409 428 LGSS-YYKSEIIKPLQLE-RLL---------DKNVKdLSGGELQRVAIAACLSRDADLYLLD 478
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
602-798 |
1.57e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 44.98 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 602 KQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG------SVAYVPQVPWLLSG--------TVRENIL 667
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqhyASKEVARRIGLLAQnattpgdiTVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 668 FGK----PFDSKRYFETLSACAldvdiSLMVGGDMACIGDKGLN-LSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQV 742
Cdd:PRK10253 104 RGRyphqPLFTRWRKEDEEAVT-----KAMQATGITHLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063701384 743 GCWILQraLLGPLLNKK--TRVMCTHNI-QAISCADMIVVMDKGKVNWSGSvtdmPKSI 798
Cdd:PRK10253 179 QIDLLE--LLSELNREKgyTLAAVLHDLnQACRYASHLIALREGKIVAQGA----PKEI 231
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
601-794 |
1.61e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 44.69 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKT----SLLNSLLGEMRCVHGSILLNGsvayVPQVPWLLSG----TVRENilfgkP- 671
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDG----KPVAPCALRGrkiaTIMQN-----Pr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 672 --FDSKRYF-----ETLSACALDVDISLMvggdMACIGDKGL------------NLSGGQRARFALARAVYHGSDMYLLD 732
Cdd:PRK10418 90 saFNPLHTMhtharETCLALGKPADDATL----TAALEAVGLenaarvlklypfEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063701384 733 DVLSAVDSQVGCWIL--------QRAlLGPLLnkktrvmCTHNIQAIS-CADMIVVMDKGKVNWSGSVTDM 794
Cdd:PRK10418 166 EPTTDLDVVAQARILdllesivqKRA-LGMLL-------VTHDMGVVArLADDVAVMSHGRIVEQGDVETL 228
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
601-789 |
2.36e-04 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 43.79 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSL---LGEMRCVHGSILLNG------------SVAYVPQ----VPWLlsgT 661
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGipykefaekypgEIIYVSEedvhFPTL---T 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 662 VRENILFgkpfdskryfeTLSACALDvdislMVGGdmacigdkglnLSGGQRARFALARAVYHGSDMYLLDDVLSAVDSQ 741
Cdd:cd03233 100 VRETLDF-----------ALRCKGNE-----FVRG-----------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063701384 742 VGCWILQRallgplLNKKTRVMCTHNIQAISCA--------DMIVVMDKGKVNWSG 789
Cdd:cd03233 153 TALEILKC------IRTMADVLKTTTFVSLYQAsdeiydlfDKVLVLYEGRQIYYG 202
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
592-802 |
2.60e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.43 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 592 NVEEDYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMR--------CVHGSILLNGSV-------------AY 650
Cdd:PRK13547 8 HVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPlaaidaprlarlrAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 651 VPQVPW-LLSGTVRENILFGKPFDSKRYFETLSACALDVDISLMVGGDMACIGDKGLNLSGGQRARFALARAVYH----- 724
Cdd:PRK13547 88 LPQAAQpAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpph 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 725 ----GSDMYLLDDVLSAVDSQVGCWILQ--RAL-----LGPLlnkktrvMCTHNIQ-AISCADMIVVMDKGKVNWSGSVT 792
Cdd:PRK13547 168 daaqPPRYLLLDEPTAALDLAHQHRLLDtvRRLardwnLGVL-------AIVHDPNlAARHADRIAMLADGAIVAHGAPA 240
|
250
....*....|..
gi 1063701384 793 DM--PKSISPTF 802
Cdd:PRK13547 241 DVltPAHIARCY 252
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
917-1163 |
2.82e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 44.43 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 917 IINSILTLVRAFSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFILNILLANFVGLLG 996
Cdd:cd18564 65 LLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 997 IIVVLSYVQ----VLFLLLLLPFWYIYSKLQVFYRSTSRELRRLDSVsrspIYASFTETLDGSSTIRAFKSEEHFVGRF- 1071
Cdd:cd18564 145 MLGVMFWLDwqlaLIALAVAPLLLLAARRFSRRIKEASREQRRREGA----LASVAQESLSAIRVVQAFGREEHEERRFa 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1072 ---IEHLTLYQRTS-----YS---EIIASlwlslrlqlLGSMIVLFVAVMAVLGsggnfpisfG--TPG--LVGLA-LSY 1135
Cdd:cd18564 221 renRKSLRAGLRAArlqalLSpvvDVLVA---------VGTALVLWFGAWLVLA---------GrlTPGdlLVFLAyLKN 282
|
250 260
....*....|....*....|....*...
gi 1063701384 1136 AAPLVSLLGSLLTSFTeteKEMVSVERV 1163
Cdd:cd18564 283 LYKPVRDLAKLTGRIA---KASASAERV 307
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
602-785 |
3.89e-04 |
|
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: 44.68 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 602 KQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCvHGSILLNGSvayvpqvPWL-LSGT----VREN--ILFGKPFDS 674
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQ-------DLDgLSRRalrpLRRRmqVVFQDPFGS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 675 ----------------------------KRYFETLSACALDVDIslmvggdmacigdkgLN-----LSGGQRARFALARA 721
Cdd:COG4172 375 lsprmtvgqiiaeglrvhgpglsaaerrARVAEALEEVGLDPAA---------------RHrypheFSGGQRQRIAIARA 439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063701384 722 VYHGSDMYLLDDVLSAVDSQVGCWILQraLLGpLLNKKTRVMC---THNIQAI-SCADMIVVMDKGKV 785
Cdd:COG4172 440 LILEPKLLVLDEPTSALDVSVQAQILD--LLR-DLQREHGLAYlfiSHDLAVVrALAHRVMVMKDGKV 504
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
603-733 |
3.96e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 43.60 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 603 QVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGSvayvpQVPWLLSG---TVRE--NILF--GKPFDSK 675
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGE-----NIPAMSRSrlyTVRKrmSMLFqsGALFTDM 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063701384 676 RYFETLsACALDVDISL-------MVGGDMACIGDKGL------NLSGGQRARFALARAVYHGSDMYLLDD 733
Cdd:PRK11831 100 NVFDNV-AYPLREHTQLpapllhsTVMMKLEAVGLRGAaklmpsELSGGMARRAALARAIALEPDLIMFDE 169
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
909-1113 |
4.03e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 43.73 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 909 LMVLCI----FCIINSILTLVRAFSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFsSDLYTIDDSL--PF 982
Cdd:cd18566 41 LQVLVIgvviAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIREFLtgQA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 983 ILNILLANFVGL-LGIIVVLSYVQVLFLLLLLPFWYIYSKLQ-VFYRSTSRELRRLDSVSRSPIyasfTETLDGSSTIRA 1060
Cdd:cd18566 120 LLALLDLPFVLIfLGLIWYLGGKLVLVPLVLLGLFVLVAILLgPILRRALKERSRADERRQNFL----IETLTGIHTIKA 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063701384 1061 FKSEEHFVGRFIEhltLYQRTSYSE----IIASLWLSLRLQLLGSMIVLFVAVMAVL 1113
Cdd:cd18566 196 MAMEPQMLRRYER---LQANAAYAGfkvaKINAVAQTLGQLFSQVSMVAVVAFGALL 249
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
940-1075 |
4.25e-04 |
|
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: 43.61 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 940 HVHNALISKLINAPTQFFDQTPSGRILNRFSSDLYTIDDSLPFILNILL---ANFVGLLGIIVVLSYVQVLFLLLLLPF- 1015
Cdd:cd18589 70 RLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMwylARGLFLFIFMLWLSPKLALLTALGLPLl 149
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 1016 WYIYSKLQVFYRSTSRELRrlDSVSRSPIYAsfTETLDGSSTIRAFKSEEHFVGRFIEHL 1075
Cdd:cd18589 150 LLVPKFVGKFQQSLAVQVQ--KSLARANQVA--VETFSAMKTVRSFANEEGEAQRYRQRL 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
602-646 |
4.47e-04 |
|
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: 44.29 E-value: 4.47e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1063701384 602 KQVSLRVPKGSFVAVIGEVGSGKT----SLLNSLLGEMRCVHGSILLNG 646
Cdd:COG4172 27 KGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDG 75
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
601-815 |
5.93e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 43.16 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSL------LGEMRcVHGSILLNGS--------------VAYVPQVPWLLSG 660
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkVSGYR-YSGDVLLGGRsifnyrdvlefrrrVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 661 TVRENILFG----KPFDSKRYFETLSACALDVDISLMVGGDMAcigDKGLNLSGGQRARFALARAVYHGSDMYLLDDVLS 736
Cdd:PRK14271 116 SIMDNVLAGvrahKLVPRKEFRGVAQARLTEVGLWDAVKDRLS---DSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 737 AVDSQVGCWIlqRALLGPLLNKKTRVMCTHNI-QAISCADMIVVMDKGKVNWSGsvtdmpksisPTFSLtnefdMSSPNH 815
Cdd:PRK14271 193 ALDPTTTEKI--EEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEG----------PTEQL-----FSSPKH 255
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
601-739 |
7.20e-04 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 42.71 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS--------------VAYVPQVPWLLSG-TVREN 665
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIGYLPQEASIFRKlTVEDN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063701384 666 I---LFGKPFDSKRYFETLSACALDVDISLmvggdmacIGD-KGLNLSGGQRARFALARAVYHGSDMYLLDDVLSAVD 739
Cdd:COG1137 99 IlavLELRKLSKKEREERLEELLEEFGITH--------LRKsKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
601-677 |
1.26e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 42.71 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 601 IKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS--------------VAYVPQ-------VPwllS 659
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsprerrrlgVAYIPEdrlgrglVP---D 350
|
90
....*....|....*...
gi 1063701384 660 GTVRENILFGKpFDSKRY 677
Cdd:COG3845 351 MSVAENLILGR-YRRPPF 367
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
900-1089 |
2.37e-03 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 41.28 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 900 VSHYSTSFYLMVLCIFC--IINSILTLVRAFSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFSsDLYTID 977
Cdd:cd18570 34 PSGDINLLNIISIGLILlyLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN-DANKIR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 978 D-----SLPFILNILLANFVGL--------LGIIVVLS---YVQVLflllllpfwYIYSKlqvFYRSTSRELRRLDSVSR 1041
Cdd:cd18570 113 EaisstTISLFLDLLMVIISGIilffynwkLFLITLLIiplYILII---------LLFNK---PFKKKNREVMESNAELN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1063701384 1042 SpiyaSFTETLDGSSTIRAFKSEEHFVGRFIEHLTLYQRTSYSEIIAS 1089
Cdd:cd18570 181 S----YLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLS 224
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
898-1001 |
2.80e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 41.34 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 898 KGVSHYSTSFYLMVLCIFC--IINSILTLVRAFSFAFGGLKAAVHVHNALISKLINAPTQFFDQTPSGRILNRFSSDLYT 975
Cdd:cd18563 33 LGPGGNTSLLLLLVLGLAGayVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDR 112
|
90 100
....*....|....*....|....*.
gi 1063701384 976 IDDSLPFILNILLANFVGLLGIIVVL 1001
Cdd:cd18563 113 LQDFLSDGLPDFLTNILMIIGIGVVL 138
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
604-643 |
3.00e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 40.68 E-value: 3.00e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1063701384 604 VSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSIL 643
Cdd:PRK11701 25 VSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH 64
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
614-635 |
4.00e-03 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 39.58 E-value: 4.00e-03
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
599-646 |
4.18e-03 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 40.36 E-value: 4.18e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1063701384 599 LTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNG 646
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRG 66
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
615-642 |
5.04e-03 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 38.98 E-value: 5.04e-03
10 20
....*....|....*....|....*...
gi 1063701384 615 AVIGEVGSGKTSLLNSLLGEMRCVHGSI 642
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEVGEVSDV 28
|
|
| Dynamin_N |
pfam00350 |
Dynamin family; |
614-634 |
5.21e-03 |
|
Dynamin family;
Pssm-ID: 459775 [Multi-domain] Cd Length: 168 Bit Score: 39.14 E-value: 5.21e-03
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
602-691 |
5.59e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.80 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 602 KQVS-LRVPKG-SFVAVIGEV-------GSGKTSLLNSLLGEMRCVHGSILLNGS--------------VAYVPQVPWLL 658
Cdd:PRK15439 19 KQYSgVEVLKGiDFTLHAGEVhallggnGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLF 98
|
90 100 110
....*....|....*....|....*....|....*....
gi 1063701384 659 SG-TVRENILFG--KPFDSKRYFETLSA---CALDVDIS 691
Cdd:PRK15439 99 PNlSVKENILFGlpKRQASMQKMKQLLAalgCQLDLDSS 137
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
603-722 |
6.77e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 40.28 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 603 QVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGS--------------VAYVPQ----VPWLlsgTVRE 664
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttaalaagVAIIYQelhlVPEM---TVAE 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063701384 665 NILFGKpFDSKRYF-----------ETLSACALDVDISLMVGgdmacigdkglNLSGGQRARFALARAV 722
Cdd:PRK11288 99 NLYLGQ-LPHKGGIvnrrllnyearEQLEHLGVDIDPDTPLK-----------YLSIGQRQMVEIAKAL 155
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
596-651 |
8.08e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 40.26 E-value: 8.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063701384 596 DYNLTIKQVSLRVPKGSFVAVIGEVGSGKTSLLNSLLGEMRCVHGSILLNGSVAYV 651
Cdd:PRK13545 35 EYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALI 90
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
614-637 |
8.14e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 39.75 E-value: 8.14e-03
10 20
....*....|....*....|....
gi 1063701384 614 VAVIGEVGSGKTSLLNSLLGEMRC 637
Cdd:COG3596 42 IALVGKTGAGKSSLINALFGAEVA 65
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
908-1006 |
8.58e-03 |
|
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: 39.78 E-value: 8.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063701384 908 YLMVLCIFciinsILTLVRAFSFA---FGGLKAAVHVHNALIS----KLINAPTQFFDQTPSGRILNRFSSDLYTIDDSL 980
Cdd:cd18579 39 YLLALALF-----LVSLLQSLLLHqyfFLSFRLGMRVRSALSSliyrKALRLSSSARQETSTGEIVNLMSVDVQRIEDFF 113
|
90 100
....*....|....*....|....*.
gi 1063701384 981 PFILNILLANFvgLLGIIVVLSYVQV 1006
Cdd:cd18579 114 LFLHYLWSAPL--QIIVALYLLYRLL 137
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
610-635 |
8.68e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 39.39 E-value: 8.68e-03
10 20
....*....|....*....|....*.
gi 1063701384 610 KGSFVAVIGEVGSGKTSLLNSLLGEM 635
Cdd:COG3267 42 GGGFVVLTGEVGTGKTTLLRRLLERL 67
|
|
| |
