|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1-1257 |
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: 864.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1 MYRAFGRPILLSSTFRYLADLLGFAGPLCISGIVQRVNETQNGTnnttgisetlsskeflENAYVLAVLLFLALILQRTF 80
Cdd:TIGR00957 311 LYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPD----------------WQGYFYTGLLFVCACLQTLI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 81 LQASYYVTIETGINLRGALLAMIYNKILRLStsNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILL 160
Cdd:TIGR00957 375 LHQYFHICFVSGMRIKTAVMGAVYRKALVIT--NSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFL 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 161 YNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSS 240
Cdd:TIGR00957 453 WLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKV 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 241 LKTFALYTSLSIFMNAAIPIAAVLATFVTHAYASGNNLKPAE-AFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKLNE 319
Cdd:TIGR00957 533 LKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNILDAEkAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRI 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 320 FLLSDEIgddswrtgesslpfesckkhtgvQPKTINRkqpgryhldsyeqstRRLRPAETEDIAIKvtNGYFSWGSGLA- 398
Cdd:TIGR00957 613 FLSHEEL-----------------------EPDSIER---------------RTIKPGEGNSITVH--NATFTWARDLPp 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 399 TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNvnesepsfeatrrnrySVAYAAQKPWLLNATVE 478
Cdd:TIGR00957 653 TLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG----------------SVAYVPQQAWIQNDSLR 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 479 ENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 558
Cdd:TIGR00957 717 ENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 559 DHLMQ-----EGILKflqddKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEHWKTLMNRQDQEle 633
Cdd:TIGR00957 797 KHIFEhvigpEGVLK-----NKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQG-- 869
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 634 kDMEADQTTL------ERKTLRRAMY-----SREAKAQMEDEDEEEEEEEDEDDNMSTVMRLRTKMP-WKTC-------- 693
Cdd:TIGR00957 870 -HLEDSWTALvsgegkEAKLIENGMLvtdvvGKQLQRQLSASSSDSGDQSRHHGSSAELQKAEAKEEtWKLMeadkaqtg 948
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 694 -------WRYLTSGGFFLLILMIFSKLLKHSVIVAIDYWLATWTSEYSINNTgKADQTYYV---AGFSILCGAGIFLclv 763
Cdd:TIGR00957 949 qvelsvyWDYMKAIGLFITFLSIFLFVCNHVSALASNYWLSLWTDDPMVNGT-QNNTSLRLsvyGALGILQGFAVFG--- 1024
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 764 TSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYAT 843
Cdd:TIGR00957 1025 YSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLAT 1104
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 844 PVFLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFL 923
Cdd:TIGR00957 1105 PIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPS 1184
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 924 SAANRWLEVRTDYLGACIVL--TASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFLTMES 1001
Cdd:TIGR00957 1185 IVANRWLAVRLECVGNCIVLfaALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEK 1264
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1002 ENyEGTMDPSQVPEHWPQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKI 1081
Cdd:TIGR00957 1265 EA-PWQIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEI 1343
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1082 VIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFS 1161
Cdd:TIGR00957 1344 IIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLS 1423
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1162 VGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTP 1241
Cdd:TIGR00957 1424 VGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAP 1503
|
1290
....*....|....*.
gi 1786986074 1242 ESLLAQEnGVFASFVR 1257
Cdd:TIGR00957 1504 SNLLQQR-GIFYSMAK 1518
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
91-1258 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 746.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 91 TGINLRGALLAMIYNKILRLStsNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSALV 170
Cdd:PLN03130 368 VGFRLRSTLVAAVFRKSLRLT--HEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLI 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 171 GAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTSL 250
Cdd:PLN03130 446 GSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAF 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 251 SIFMNAAIPIAAVLATFVTHAYASGNnLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKLNEFLLSDEigdds 330
Cdd:PLN03130 526 NSFILNSIPVLVTVVSFGVFTLLGGD-LTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEE----- 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 331 wRTGESSLPFESCkkhtgvqpktinrkQPgryhldsyeqstrrlrpaetediAIKVTNGYFSWGSGL--ATLSNIDIRIP 408
Cdd:PLN03130 600 -RVLLPNPPLEPG--------------LP-----------------------AISIKNGYFSWDSKAerPTLSNINLDVP 641
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 409 TGQLTMIVGQVGCGKSSLLLAILGEMQTLEGkvhwsnvnesepsfeATRRNRYSVAYAAQKPWLLNATVEENITFGSPFN 488
Cdd:PLN03130 642 VGSLVAIVGSTGEGKTSLISAMLGELPPRSD---------------ASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFD 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 489 KQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILK 568
Cdd:PLN03130 707 PERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKD 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 569 FLQddKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIqTKDVELYehwKTLMNR---------------QDQELE 633
Cdd:PLN03130 787 ELR--GKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEEL-SNNGPLF---QKLMENagkmeeyveengeeeDDQTSS 860
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 634 KDMEADQTTLERKTLRRAMYSREAKAQMededeeeeeeededdnMSTVMRLRTKMPWKTCWRYLTS-GGFFLLILMIFSK 712
Cdd:PLN03130 861 KPVANGNANNLKKDSSSKKKSKEGKSVL----------------IKQEERETGVVSWKVLERYKNAlGGAWVVMILFLCY 924
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 713 LLKHSVIVAIDYWLATWTSEYSINNTGKAdqtYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPI 792
Cdd:PLN03130 925 VLTEVFRVSSSTWLSEWTDQGTPKTHGPL---FYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPM 1001
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 793 RFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQ 872
Cdd:PLN03130 1002 SFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVK 1081
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 873 ELDDSTQLPLLCHFSETAEGLTTIRAFRHetrfKQRMLELTDT---NNIAYLFLS-AANRWLEVRTDYLGACIV-LTAS- 946
Cdd:PLN03130 1082 RLDSITRSPVYAQFGEALNGLSTIRAYKA----YDRMAEINGRsmdNNIRFTLVNmSSNRWLAIRLETLGGLMIwLTASf 1157
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 947 -----IASISGSSNSGLVGLGLLYALTITNYLNWVVRnLADL-EVQMGAVKKVNSFLTMESENyEGTMDPSQVPEHWPQE 1020
Cdd:PLN03130 1158 avmqnGRAENQAAFASTMGLLLSYALNITSLLTAVLR-LASLaENSLNAVERVGTYIDLPSEA-PLVIENNRPPPGWPSS 1235
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1021 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1100
Cdd:PLN03130 1236 GSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1101 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 1180
Cdd:PLN03130 1316 GIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKI 1395
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1786986074 1181 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQENGVFASFVRA 1258
Cdd:PLN03130 1396 LVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQS 1473
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-1258 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 712.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 4 AFGRPILLSSTFRYLADLLGFAGPLCISGIVQRVNEtqngtNNTTGISETLSSKEFLENAYVlavllflalilqrTFLQA 83
Cdd:PLN03232 298 SLGGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMQE-----GDPAWVGYVYAFLIFFGVTFG-------------VLCES 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 84 SYYVTI-ETGINLRGALLAMIYNKILRLStsNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYN 162
Cdd:PLN03232 360 QYFQNVgRVGFRLRSTLVAAIFHKSLRLT--HEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQ 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 163 LLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLK 242
Cdd:PLN03232 438 QLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFR 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 243 TFALYTSLSIFMNAAIPIAAVLATFVTHAYASGNnLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKLNEFLL 322
Cdd:PLN03232 518 KAQLLSAFNSFILNSIPVVVTLVSFGVFVLLGGD-LTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLL 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 323 SDEigddswRTGESSLPFesckkhtgvqpktinrkQPGRyhldsyeqstrrlrPAetediaIKVTNGYFSWGSGLA--TL 400
Cdd:PLN03232 597 SEE------RILAQNPPL-----------------QPGA--------------PA------ISIKNGYFSWDSKTSkpTL 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 401 SNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEgkvhwsnvnesepsfEATRRNRYSVAYAAQKPWLLNATVEEN 480
Cdd:PLN03232 634 SDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE---------------TSSVVIRGSVAYVPQVSWIFNATVREN 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 481 ITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDH 560
Cdd:PLN03232 699 ILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQ 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 561 LMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIqTKDVELYehwKTLM------------NRQ 628
Cdd:PLN03232 779 VFDSCMKDELKG--KTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL-SKSGSLF---KKLMenagkmdatqevNTN 852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 629 DQELEKDMEADQTTLERKTLRRAMYSREAKAQMEDEDEeeeeeededdnmstvmRLRTKMPWKTCWRYLTS-GGFFLLIL 707
Cdd:PLN03232 853 DENILKLGPTVTIDVSERNLGSTKQGKRGRSVLVKQEE----------------RETGIISWNVLMRYNKAvGGLWVVMI 916
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 708 MIFSKLLKHSVIVAIDYWLATWTSEYSINNTGKAdqtYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKI 787
Cdd:PLN03232 917 LLVCYLTTEVLRVSSSTWLSIWTDQSTPKSYSPG---FYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSI 993
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 788 ILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVA 867
Cdd:PLN03232 994 LRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQST 1073
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 868 SKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDtNNIAY-LFLSAANRWLEVRTDYLGACIV-LTA 945
Cdd:PLN03232 1074 SREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMD-NNIRFtLANTSSNRWLTIRLETLGGVMIwLTA 1152
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 946 SIASISGSSNSGLVG----LGLL--YALTITNYLNWVVRNLADLEVQMGAVKKVNSFLTMESENyEGTMDPSQVPEHWPQ 1019
Cdd:PLN03232 1153 TFAVLRNGNAENQAGfastMGLLlsYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEA-TAIIENNRPVSGWPS 1231
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1020 EGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR 1099
Cdd:PLN03232 1232 RGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV 1311
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1100 LSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 1179
Cdd:PLN03232 1312 LSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSK 1391
|
1210 1220 1230 1240 1250 1260 1270
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1786986074 1180 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQENGVFASFVRA 1258
Cdd:PLN03232 1392 ILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHS 1470
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
77-1258 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 664.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 77 QRTFLQASYYVTIETGINLRGALLAMIYNKILRLSTSNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMG 156
Cdd:PTZ00243 298 QSVCLHRFYYISIRCGLQYRSALNALIFEKCFTISSKSLAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLS 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 157 VILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMK 236
Cdd:PTZ00243 378 ILLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRAR 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 237 ELSSLKTFALYTSLSIFMNAAIPIAAVLATFVTHaYASGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQK 316
Cdd:PTZ00243 458 ELRYLRDVQLARVATSFVNNATPTLMIAVVFTVY-YLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKR 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 317 LNEFLLSDE-----IGD--DSWRTGESS----------------------LPF------------------ESCKKHTGV 349
Cdd:PTZ00243 537 ISTFLECDNatcstVQDmeEYWREQREHstacqlaavlenvdvtafvpvkLPRapkvktsllsralrmlccEQCRPTKRH 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 350 QPKTI---------------NRKQPGRYHLDSyEQSTrrlrPAETEDIAIKVTNGYFSWGSGLaTLSNIDIRIPTGQLTM 414
Cdd:PTZ00243 617 PSPSVvvedtdygspssasrHIVEGGTGGGHE-ATPT----SERSAKTPKMKTDDFFELEPKV-LLRDVSVSVPRGKLTV 690
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 415 IVGQVGCGKSSLLLAILGEMQTLEGKVhWsnvnesepsfeATRrnrySVAYAAQKPWLLNATVEENITFGSPFNKQRYKA 494
Cdd:PTZ00243 691 VLGATGSGKSTLLQSLLSQFEISEGRV-W-----------AER----SIAYVPQQAWIMNATVRGNILFFDEEDAARLAD 754
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 495 VTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDdk 574
Cdd:PTZ00243 755 AVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAG-- 832
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 575 RTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKD-IQTkdvELYEHWKT-LMNRQDQElEKDMEADQTTLER-KTLRRA 651
Cdd:PTZ00243 833 KTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADfMRT---SLYATLAAeLKENKDSK-EGDADAEVAEVDAaPGGAVD 908
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 652 MYSREAKAQMEDEDEEEEEEEDEDDNMSTVMRLRTKM-PWKTCWRYLTS-GGFFLLILMIFSKLLKHSVIVAIDYWLATW 729
Cdd:PTZ00243 909 HEPPVAKQEGNAEGGDGAALDAAAGRLMTREEKASGSvPWSTYVAYLRFcGGLHAAGFVLATFAVTELVTVSSGVWLSMW 988
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 730 TSeysiNNTGKADQTY-YV-AGFSILCGAGIFLCLVTSLTVEWMGltaAKNLHHNLLNKIILGPIRFFDTTPLGLILNRF 807
Cdd:PTZ00243 989 ST----RSFKLSAATYlYVyLGIVLLGTFSVPLRFFLSYEAMRRG---SRNMHRDLLRSVSRGTMSFFDTTPLGRILNRF 1061
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 808 SADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFS 887
Cdd:PTZ00243 1062 SRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLE 1141
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 888 ETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACIVLT------ASIASISGSSNSGLVGL 961
Cdd:PTZ00243 1142 EALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVialigvIGTMLRATSQEIGLVSL 1221
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 962 GLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSF--------------LTMESENYEGT---------MDPSQVPEHWP 1018
Cdd:PTZ00243 1222 SLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYtdevphedmpeldeEVDALERRTGMaadvtgtvvIEPASPTSAAP 1301
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1019 ---QEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHT 1095
Cdd:PTZ00243 1302 hpvQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRE 1381
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1096 LRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFV 1175
Cdd:PTZ00243 1382 LRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALL 1461
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1176 RKSSILI-MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQENGVFAS 1254
Cdd:PTZ00243 1462 KKGSGFIlMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHS 1541
|
....
gi 1786986074 1255 FVRA 1258
Cdd:PTZ00243 1542 MVEA 1545
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1021-1260 |
1.88e-174 |
|
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: 515.61 E-value: 1.88e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1021 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1100
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1101 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 1180
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1181 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQENGVFASFVRADM 1260
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVRTDK 257
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
384-600 |
3.08e-157 |
|
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: 469.12 E-value: 3.08e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATR-RNRYS 462
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 463 VAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 542
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1786986074 543 IVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGS 600
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
11-317 |
1.64e-140 |
|
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: 428.96 E-value: 1.64e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 11 LSSTFRYLADLLGFAGPLCISGIVQRVNETQNGTNNTTGISET--LSSKEFLENAYVLAVLLFLALILQRTFLQASYYVT 88
Cdd:cd18591 1 LGGILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNSTDKLSVsyVTVEEFFSNGYVLAVILFLALLLQATFSQASYHIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 89 IETGINLRGALLAMIYNKILRLSTSNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSA 168
Cdd:cd18591 81 IREGIRLKTALQAMIYEKALRLSSWNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 169 LVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYT 248
Cdd:cd18591 161 LIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYW 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1786986074 249 SLSIFMNAAIPIAAVLATFVTHAYASGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 317
Cdd:cd18591 241 SLMTFLTQASPILVTLVTFGLYPYLEGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-1247 |
1.13e-134 |
|
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: 448.21 E-value: 1.13e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 3 RAFGRPILLSSTFRYLADLLGFAGPLCISGIVQRVNEtqngtnnttgisetlSSKEFLENAYVLAVLLFLALILQRTFLQ 82
Cdd:TIGR01271 76 RCFFWRFVFYGILLYFGEATKAVQPLLLGRIIASYDP---------------FNAPEREIAYYLALGLCLLFIVRTLLLH 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 83 ASYYVTIETGINLRGALLAMIYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYN 162
Cdd:TIGR01271 141 PAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLD--KISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 163 LLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLK 242
Cdd:TIGR01271 219 LLEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTR 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 243 TFAlytSLSIFMNAAIPIAAVLATF---VTHAYASGNNLKpaEAFASLSLFHIL-VTPLFLLSTVVRFAVKAIISVQKLN 318
Cdd:TIGR01271 299 KIA---YLRYFYSSAFFFSGFFVVFlsvVPYALIKGIILR--RIFTTISYCIVLrMTVTRQFPGAIQTWYDSLGAITKIQ 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 319 EFLLSDEigddsWRTGESSLpfesckkhTGVQPKTINRKQpgryhldSYEQSTRRL-RPAETEDIAIKVTNG----YFSW 393
Cdd:TIGR01271 374 DFLCKEE-----YKTLEYNL--------TTTEVEMVNVTA-------SWDEGIGELfEKIKQNNKARKQPNGddglFFSN 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 394 GSGLAT--LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNvnesepsfeatrrnrySVAYAAQKPW 471
Cdd:TIGR01271 434 FSLYVTpvLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG----------------RISFSPQTSW 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 472 LLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 551
Cdd:TIGR01271 498 IMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 552 ALDIHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKD---------VELYEHWK 622
Cdd:TIGR01271 578 HLDVVTEKEIFESCLCKLMSN--KTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRpdfsslllgLEAFDNFS 655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 623 ----------TLM-------------------------------------------NRQDQELEKDMEADQTT------- 642
Cdd:TIGR01271 656 aerrnsilteTLRrvsidgdstvfsgpetikqsfkqpppefaekrkqsiilnpiasARKFSFVQMGPQKAQATtiedavr 735
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 643 --LERK------------TLRRA-MYSREAKAQMEDEDEEEEEEEDEDDNMSTVMRLRT---KM---------------- 688
Cdd:TIGR01271 736 epSERKfslvpedeqgeeSLPRGnQYHHGLQHQAQRRQSVLQLMTHSNRGENRREQLQTsfrKKssitqqnelaseldiy 815
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 689 ------------------------------------PWKTCWRYLTSGG--FFLLI--LMIFSKLLKHSVIVaidYWLAT 728
Cdd:TIGR01271 816 srrlskdsvyeiseeineedlkecfaderenvfettTWNTYLRYITTNRnlVFVLIfcLVIFLAEVAASLLG---LWLIT 892
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 729 WTSEYSINNTGK-ADQTYYVAGFSILCGAG-----IFLCLVTSLTVEWMG-----------LTAAKNLHHNLLNKIILGP 791
Cdd:TIGR01271 893 DNPSAPNYVDQQhANASSPDVQKPVIITPTsayyiFYIYVGTADSVLALGffrglplvhtlLTVSKRLHEQMLHSVLQAP 972
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 792 IRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDL 871
Cdd:TIGR01271 973 MAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQL 1052
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 872 QELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFK---QRMLELTDTNNIAYLflsAANRWLEVRTDYLGACIVLTASIA 948
Cdd:TIGR01271 1053 KQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFEtlfHKALNLHTANWFLYL---STLRWFQMRIDIIFVFFFIAVTFI 1129
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 949 SISGSSNSG-LVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFLTMESENYEGT-------------MDPSQVP 1014
Cdd:TIGR01271 1130 AIGTNQDGEgEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRPSggggkyqlstvlvIENPHAQ 1209
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1015 EHWPQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGIDISKLPLH 1094
Cdd:TIGR01271 1210 KCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVSWNSVTLQ 1288
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1095 TLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAF 1174
Cdd:TIGR01271 1289 TWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSI 1368
|
1370 1380 1390 1400 1410 1420 1430
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 1175 VRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1247
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1021-1241 |
2.74e-130 |
|
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: 398.41 E-value: 2.74e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1021 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1100
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1101 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 1180
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1786986074 1181 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTP 1241
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
706-997 |
3.95e-126 |
|
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: 390.81 E-value: 3.95e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 706 ILMIFSKLLKHSVIVAIDYWLATWTSE----------YSINNTGKADQTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTA 775
Cdd:cd18602 2 ALVLALALLKQGLRVATDFWLADWTEAnhdvasvvfnITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGLRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 776 AKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGV 855
Cdd:cd18602 82 ARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIII 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 856 AFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTD 935
Cdd:cd18602 162 VYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLD 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1786986074 936 YLGACIVL----TASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFL 997
Cdd:cd18602 242 YLGAVIVFlaalSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
384-600 |
2.08e-105 |
|
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: 330.97 E-value: 2.08e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGSGLA----TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNvnesepsfeatrrn 459
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 460 rySVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQ 539
Cdd:cd03250 67 --SIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1786986074 540 NTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDDKrTLVLVTHKLQYLTHADWIIAMKDGS 600
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNK-TRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
682-1258 |
1.04e-102 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 337.91 E-value: 1.04e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 682 MRLRTKMPWKTCWRYLtSGGFFLLILMIFSKLLKHSVIVAIDYWLATWTSEYSinNTGKADQTYYVAGFSILCGAGIFLC 761
Cdd:COG1132 1 MSKSPRKLLRRLLRYL-RPYRGLLILALLLLLLSALLELLLPLLLGRIIDALL--AGGDLSALLLLLLLLLGLALLRALL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 762 -LVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMIS 840
Cdd:COG1132 78 sYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 841 YATP----VFLVALLPLGVAFYFIQKYFRVASKDLQE-LDDSTQlpllcHFSETAEGLTTIRAFRHETRFKQRMLELTDT 915
Cdd:COG1132 158 VIDWrlalIVLLVLPLLLLVLRLFGRRLRKLFRRVQEaLAELNG-----RLQESLSGIRVVKAFGREERELERFREANEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 916 NNIAYLFLSAANRWLEVRTDYLGACIVLTasiasisgssnsgLVGLG-----------------LLYALTITNYLNWVVR 978
Cdd:COG1132 233 LRRANLRAARLSALFFPLMELLGNLGLAL-------------VLLVGgllvlsgsltvgdlvafILYLLRLFGPLRQLAN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 979 NLADLEVQMGAVKKVNSFLTMESENYEGTmDPSQVPehwPQEGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGR 1058
Cdd:COG1132 300 VLNQLQRALASAERIFELLDEPPEIPDPP-GAVPLP---PVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1059 TGSGKSSL-SLaFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPECkcTDDRLWEALE 1134
Cdd:COG1132 375 SGSGKSTLvNL-LLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRPDA--TDEEVEEAAK 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1135 IAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTI 1214
Cdd:COG1132 452 AAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVI 531
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1786986074 1215 AHRVHTILTADLVIVMKRGNILEYDTPESLLAQeNGVFASFVRA 1258
Cdd:COG1132 532 AHRLSTIRNADRILVLDDGRIVEQGTHEELLAR-GGLYARLYRL 574
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1017-1241 |
2.95e-90 |
|
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: 289.70 E-value: 2.95e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1017 WPQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL 1096
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1097 RSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEiaqlknmvkslpggldavVTEGGENFSVGQRQLFCLARAFVR 1176
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1786986074 1177 KSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTP 1241
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
701-996 |
6.03e-83 |
|
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: 273.23 E-value: 6.03e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 701 GFFLLILMIFSKLLKHSVIVAIDYWLATWTSEYSINNTgkadqTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLH 780
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSG-----YYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 781 HNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFI 860
Cdd:cd18580 76 DKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 861 QKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGAC 940
Cdd:cd18580 156 QRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGAL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1786986074 941 IV--LTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSF 996
Cdd:cd18580 236 LAlvVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEY 293
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
747-1257 |
2.02e-81 |
|
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: 282.49 E-value: 2.02e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 747 VAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSaDTNIIDQHIP-PTLESL 825
Cdd:COG2274 199 AIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTgSLLTAL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 826 TRSTLLCLSAIGMISYATPVFLVALLPLGVAF---YFIQKYFRVASKDLQELDDSTQLpllcHFSETAEGLTTIRAFRHE 902
Cdd:COG2274 278 LDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVllgLLFQPRLRRLSREESEASAKRQS----LLVETLRGIETIKALGAE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 903 TRFKQRMLELTdtnnIAYLFLSAANRWLEVRTDYLGACIvltasiasisgssnSGLVGLGLLYA---------LTI---- 969
Cdd:COG2274 354 SRFRRRWENLL----AKYLNARFKLRRLSNLLSTLSGLL--------------QQLATVALLWLgaylvidgqLTLgqli 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 970 -TNYLNWV----VRNLADL--EVQM--GAVKKVNSFLTMESENYEGTmDPSQVPEhwpQEGEIKIHDLCVRYENNLKPVL 1040
Cdd:COG2274 416 aFNILSGRflapVAQLIGLlqRFQDakIALERLDDILDLPPEREEGR-SKLSLPR---LKGDIELENVSFRYPGDSPPVL 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1041 KHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL-- 1118
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItl 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1119 -DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENI 1197
Cdd:COG2274 572 gDPDA--TDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAI 649
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1198 LQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQeNGVFASFVR 1257
Cdd:COG2274 650 ILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR-KGLYAELVQ 708
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
703-984 |
1.92e-78 |
|
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: 260.49 E-value: 1.92e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 703 FLLILMIFskLLKHSVIVAIDYWLATWTSEYSINNTGKADQT-YYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHH 781
Cdd:cd18603 1 SLLILLLY--LLSQAFSVGSNIWLSEWSDDPALNGTQDTEQRdYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 782 NLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQ 861
Cdd:cd18603 79 KLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 862 KYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACI 941
Cdd:cd18603 159 RFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLI 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1786986074 942 VLTASIASISGSSNSG--LVGLGLLYALTITNYLNWVVRNLADLE 984
Cdd:cd18603 239 VLFAALFAVLSRDSLSpgLVGLSISYALQITQTLNWLVRMTSELE 283
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
706-997 |
7.06e-73 |
|
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: 244.68 E-value: 7.06e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 706 ILMIFSKLLKHSVIVAIDYWLATWTSEYSINNTGKADQ---TYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHN 782
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEvsvLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 783 LLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQK 862
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 863 YFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACIV 942
Cdd:cd18604 162 LYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFS 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1786986074 943 L-TASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFL 997
Cdd:cd18604 242 FaTAALLVYGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1021-1247 |
9.45e-72 |
|
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: 239.05 E-value: 9.45e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1021 GEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1100
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1101 SIILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 1177
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIrlgRPNA--TDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1178 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1247
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
11-317 |
1.16e-69 |
|
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: 235.46 E-value: 1.16e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 11 LSSTFRYLADLLGFAGPLCISGIVQRVNETQNgtnnttgisetlsskEFLENAYVLAVLLFLALILQRTFLQASYYVTIE 90
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPD---------------EPLSEGYLLALALFLVSLLQSLLLHQYFFLSFR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 91 TGINLRGALLAMIYNKILRLSTSnlSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSALV 170
Cdd:cd18579 66 LGMRVRSALSSLIYRKALRLSSS--ARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 171 GAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTSL 250
Cdd:cd18579 144 GLGVLLLLIPLQAFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRAL 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 251 SIFMNAAIPIAAVLATFVTHAYaSGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 317
Cdd:cd18579 224 NSFLFFSTPVLVSLATFATYVL-LGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
829-1248 |
3.38e-69 |
|
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: 243.51 E-value: 3.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 829 TLLCLSAIGMISYATPVFLVALLPLGVAF-YFIQKYFRVASKD----LQELDDstqlpllcHFSETAEGLTTIRAFRHET 903
Cdd:COG4988 146 PLLILVAVFPLDWLSGLILLVTAPLIPLFmILVGKGAAKASRRqwraLARLSG--------HFLDRLRGLTTLKLFGRAK 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 904 RFKQRMLELTDTNNIAYL------FLSAANrwLEVRTdYLGACIVLtasiasisgssnsGLVGLGLLYA-LTITN----- 971
Cdd:COG4988 218 AEAERIAEASEDFRKRTMkvlrvaFLSSAV--LEFFA-SLSIALVA-------------VYIGFRLLGGsLTLFAalfvl 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 972 ------YLNwvVRNLAdleVQ-------MGAVKKVNSFLTMESEnyegTMDPSQVPEHWPQEGEIKIHDLCVRYENNlKP 1038
Cdd:COG4988 282 llapefFLP--LRDLG---SFyharangIAAAEKIFALLDAPEP----AAPAGTAPLPAAGPPSIELEDVSFSYPGG-RP 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1039 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 1118
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1119 ---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 1195
Cdd:COG4988 432 rlgRPDA--SDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETE 509
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 1196 NILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQE 1248
Cdd:COG4988 510 AEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
702-997 |
4.76e-67 |
|
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: 228.57 E-value: 4.76e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 702 FFLLILMIFSKllkhsviVAIDYWLATWTSEYSIN--NTGKADQTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNL 779
Cdd:cd18605 5 LLSLILMQASR-------NLIDFWLSYWVSHSNNSffNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 780 HHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYF 859
Cdd:cd18605 78 HNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 860 IQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGA 939
Cdd:cd18605 158 IQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 940 CIV-----LTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFL 997
Cdd:cd18605 238 LIVtfvalTAVVQHFFGLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
702-990 |
1.99e-63 |
|
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: 217.73 E-value: 1.99e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 702 FFLLILMIFSKllkhsviVAIDYWLATWTSeysinNTGKADQTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHH 781
Cdd:cd18606 5 LLLLILSQFAQ-------VFTNLWLSFWTE-----DFFGLSQGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 782 NLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQ 861
Cdd:cd18606 73 KALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 862 KYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACI 941
Cdd:cd18606 153 NYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1786986074 942 VL--TASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAV 990
Cdd:cd18606 233 VLivALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSV 283
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1023-1233 |
8.29e-63 |
|
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: 211.09 E-value: 8.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1102
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1103 ILQDPILFSGSIRFNLdpeckctddrlwealeiaqlknmvkslpggldavvteggenFSVGQRQLFCLARAFVRKSSILI 1182
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1786986074 1183 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRG 1233
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
77-317 |
8.93e-62 |
|
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: 213.10 E-value: 8.93e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 77 QRTFLQASYYVTIETGINLRGALLAMIYNKILRLStsNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMG 156
Cdd:cd18595 51 QSLLLHQYFHRCFRLGMRIRTALTSAIYRKALRLS--NSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 157 VILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMK 236
Cdd:cd18595 129 LYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 237 ELSSLKTFALYTSLSIFMNAAIPIAAVLATFVTHAYASGNN-LKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQ 315
Cdd:cd18595 209 ELKLLKKAAYLNAVSSFLWTCAPFLVSLATFATYVLSDPDNvLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLK 288
|
..
gi 1786986074 316 KL 317
Cdd:cd18595 289 RL 290
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
701-997 |
1.70e-61 |
|
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: 213.19 E-value: 1.70e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 701 GFFLLILMIFSKLLKHSVIVAIDYWLATW--------------TSEYSINNTGKADQTYYVAGFSILCGAGIFLCLVTSL 766
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWlkqgsgnttnnvdnSTVDSGNISDNPDLNFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 767 TVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVF 846
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 847 LVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAA 926
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 927 NRWLEVRTDYLGACIVLTASIASISGSSNS--GLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFL 997
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSIspAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1023-1254 |
5.45e-58 |
|
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: 200.15 E-value: 5.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1102
Cdd:cd03253 1 IEFENVTFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1103 ILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 1179
Cdd:cd03253 80 VPQDTVLFNDTIGYNIrygRPDA--TDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1786986074 1180 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAqENGVFAS 1254
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLA-KGGLYAE 231
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
747-1254 |
2.57e-57 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 208.80 E-value: 2.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 747 VAGFSILCGAGIFlclVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLT 826
Cdd:TIGR02203 60 VIGLAVLRGICSF---VSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 827 RSTLLCLSAIGMI---SYATPVFLVALLPL-GVAFYFIQKYFRVASKDLQELD-DSTQLpllchFSETAEGLTTIRAFRH 901
Cdd:TIGR02203 137 RETLTVIGLFIVLlyySWQLTLIVVVMLPVlSILMRRVSKRLRRISKEIQNSMgQVTTV-----AEETLQGYRVVKLFGG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 902 ETRFKQRmleltdtnniaYLFLSAANRWLEVRTDYLGAciVLTASIASISGSSNSGLVGLGLLYA----LTITNYLNWVV 977
Cdd:TIGR02203 212 QAYETRR-----------FDAVSNRNRRLAMKMTSAGS--ISSPITQLIASLALAVVLFIALFQAqagsLTAGDFTAFIT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 978 ---------RNLADLEVQM----GAVKKVNSFLTMESENYEGTMDPSQVpehwpqEGEIKIHDLCVRYENNLKPVLKHVK 1044
Cdd:TIGR02203 279 amialirplKSLTNVNAPMqrglAAAESLFTLLDSPPEKDTGTRAIERA------RGDVEFRNVTFRYPGRDRPALDSIS 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1045 AYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPE 1121
Cdd:TIGR02203 353 LVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRTE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1122 cKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKV 1201
Cdd:TIGR02203 433 -QADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAA 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 1202 VMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQeNGVFAS 1254
Cdd:TIGR02203 512 LERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLAR-NGLYAQ 563
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1023-1253 |
3.37e-57 |
|
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: 197.84 E-value: 3.37e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1102
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1103 ILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 1179
Cdd:cd03251 81 VSQDVFLFNDTVAENIaygRPGA--TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786986074 1180 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQeNGVFA 1253
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ-GGVYA 231
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
83-606 |
4.24e-56 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 205.40 E-value: 4.24e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 83 ASYYVTIETGINLRGALLAMIYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFL-FLCPNLWAMPVQIIMGVILLY 161
Cdd:COG1132 80 LQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLaHGLPQLVRSVVTLIGALVVLF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 162 NLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWE----HIFCKSVEETRMKE 237
Cdd:COG1132 158 VIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREerelERFREANEELRRAN 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 238 LSSLKTFALYTSLSIFMNAAIpIAAVLAtFVTHAYASGNnLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 317
Cdd:COG1132 238 LRAARLSALFFPLMELLGNLG-LALVLL-VGGLLVLSGS-LTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERI 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 318 NEFL-LSDEIGDdswrtGESSLPFesckkhtgvqpktinrkqpgryhldsyeqstrrlrPAETEDIAIK-VTngyFSWGS 395
Cdd:COG1132 315 FELLdEPPEIPD-----PPGAVPL-----------------------------------PPVRGEIEFEnVS---FSYPG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 396 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNrysVAYAAQKPWLLNA 475
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ---IGVVPQDTFLFSG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 476 TVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 554
Cdd:COG1132 429 TIRENIRYGRPdATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALD 508
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 555 IHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 606
Cdd:COG1132 509 TE-TEALIQEALERLMKG--RTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
80-317 |
8.49e-56 |
|
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: 195.75 E-value: 8.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 80 FLQASYYVTIETGINLRGALLAMIYNKILRLSTSnlSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVIL 159
Cdd:cd18597 59 LLNHFFYRSMLTGAQVRAALTKAIYRKSLRLSGK--SRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIAL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 160 LYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELS 239
Cdd:cd18597 137 LIVNLGPSALVGIGVLILSIPLQGFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELK 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1786986074 240 SLKTFALYTSLSIFMNAAIPIAAVLATFVThAYASGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 317
Cdd:cd18597 217 YVRKLQILRSILTAVAFSLPVLASMLSFIT-YYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1038-1258 |
8.24e-55 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 190.83 E-value: 8.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1038 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN 1117
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1118 L---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 1194
Cdd:cd03249 97 IrygKPDA--TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786986074 1195 ENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQEnGVFASFVRA 1258
Cdd:cd03249 175 EKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK-GVYAKLVKA 237
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
79-622 |
2.82e-54 |
|
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: 203.14 E-value: 2.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 79 TFLQASYYVTIETGINLRgaLLAMIYNKILRLSTSNL---SMGEMtLGQINNLVAIE---TNQLMWFLFLCPNLWampvq 152
Cdd:COG2274 213 RLLRSYLLLRLGQRIDLR--LSSRFFRHLLRLPLSFFesrSVGDL-ASRFRDVESIReflTGSLLTALLDLLFVL----- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 153 IIMGVILLYNllGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYA--------WEH 224
Cdd:COG2274 285 IFLIVLFFYS--PPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGaesrfrrrWEN 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 225 IFCKSVEetrmKELSSLKTFALYTSLSIFMNAAIPIAAVL--ATFVTHayasgNNLKPAEAFASLSLFHILVTPLF-LLS 301
Cdd:COG2274 363 LLAKYLN----ARFKLRRLSNLLSTLSGLLQQLATVALLWlgAYLVID-----GQLTLGQLIAFNILSGRFLAPVAqLIG 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 302 TVVRFAvKAIISVQKLNEFLlsdeigddswrtgesSLPFEsckkhtgvqpktinrkqpgryhldsyEQSTRRLRPAETED 381
Cdd:COG2274 434 LLQRFQ-DAKIALERLDDIL---------------DLPPE--------------------------REEGRSKLSLPRLK 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 382 IAIKVTNGYFSW-GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNr 460
Cdd:COG2274 472 GDIELENVSFRYpGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ- 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 461 ysVAYAAQKPWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQ 539
Cdd:COG2274 551 --IGVVLQDVFLFSGTIRENITLGDPdATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLR 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 540 NTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYE 619
Cdd:COG2274 629 NPRILILDEATSALDAE-TEAIILENLRRLLKG--RTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAE 705
|
...
gi 1786986074 620 HWK 622
Cdd:COG2274 706 LVQ 708
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
79-315 |
1.79e-52 |
|
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: 186.93 E-value: 1.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 79 TFLQASYYVTIETGINLRGALLAMIYNKILRL-----------------STSNLSMGEMTLGQINNLVAIETN---QLMW 138
Cdd:cd18596 54 LLDQQYLWIGRRLSVRLRAILTQLIFEKALRRrdksgssksseskkkdkEEDEDEKSSASVGKINNLMSVDANrisEFAA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 139 FLFLcpnLWAMPVQIIMGVILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLK 218
Cdd:cd18596 134 FLHL---LVSAPLQIVIAIVFLYRLLGWSALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIK 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 219 LYAWEHIFCKSVEETRMKELSSLKTFALYTSLSIFMNAAIPIAAVLATFVTHAYASGNNLKPAEAFASLSLFHILVTPLF 298
Cdd:cd18596 211 FFAWERKWEERILEAREEELKWLRKRFLLDLLLSLLWFLIPILVTVVTFATYTLVMGQELTASVAFTSLALFNMLRGPLN 290
|
250
....*....|....*..
gi 1786986074 299 LLSTVVRFAVKAIISVQ 315
Cdd:cd18596 291 VLPELITQLLQAKVSLD 307
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
701-993 |
1.85e-52 |
|
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: 187.14 E-value: 1.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 701 GFFLLILMIFSKLLKHSVIVAIDYWLATWTSEY---------------SINNTGKADQTYYVAGFSILCGAGIFLCLVTS 765
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEeklndttdrvqgensTNVDIEDLDRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 766 LTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPV 845
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 846 FLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAY-LFLs 924
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWfLFL- 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1786986074 925 AANRWLEVRTDYLGA--CIVLTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKV 993
Cdd:cd18601 240 ATSRWLAVRLDALCAlfVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERV 310
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
694-1256 |
6.42e-52 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 195.71 E-value: 6.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 694 WRYLTSGGFFLLILMIFSKLLKHSVIVAIDYWLATWTSEYSINNTGKADQTYYVAGFSILCGAGIFLCLvtsltvewMGL 773
Cdd:TIGR00958 160 WPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYT--------MAR 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 774 TAAKnLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRS--TLLCLSAIgMIS---YATPVFLV 848
Cdd:TIGR00958 232 INLR-IREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNlvMLLGLLGF-MLWlspRLTMVTLI 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 849 ALLPLGVAFYFIQKYFRVASKDLQE-LDDSTQLPLlchfsETAEGLTTIRAFRHE----TRFKQ---RMLELTDTNNIAY 920
Cdd:TIGR00958 310 NLPLVFLAEKVFGKRYQLLSEELQEaVAKANQVAE-----EALSGMRTVRSFAAEegeaSRFKEaleETLQLNKRKALAY 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 921 LFLSAANRWLE----VRTDYLGACIVLTASIASISgssnsgLVGLgLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSF 996
Cdd:TIGR00958 385 AGYLWTTSVLGmliqVLVLYYGGQLVLTGKVSSGN------LVSF-LLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEY 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 997 L--TMESENyEGTMDPSQVpehwpqEGEIKIHDLCVRYENNL-KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRM 1073
Cdd:TIGR00958 458 LdrKPNIPL-TGTLAPLNL------EGLIEFQDVSFSYPNRPdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1074 VDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAV 1152
Cdd:TIGR00958 531 YQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLtDTPDEEIMAAAKAANAHDFIMEFPNGYDTE 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1153 VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKvvMTAFADRTVVTIAHRVHTILTADLVIVMKR 1232
Cdd:TIGR00958 611 VGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKK 688
|
570 580
....*....|....*....|....
gi 1786986074 1233 GNILEYDTPESLLAQEnGVFASFV 1256
Cdd:TIGR00958 689 GSVVEMGTHKQLMEDQ-GCYKHLV 711
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
379-614 |
1.01e-51 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 192.28 E-value: 1.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 379 TEDIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRR 458
Cdd:COG4988 332 AGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 459 NrysVAYAAQKPWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARAL 537
Cdd:COG4988 412 Q---IAWVPQNPYLFAGTIRENLRLGRPdASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARAL 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 538 YQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKD 614
Cdd:COG4988 489 LRDAPLLLLDEPTAHLDAE-TEAEILQALRRLAKG--RTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1021-1249 |
1.66e-51 |
|
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: 182.75 E-value: 1.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1021 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGIDISKLPLHTLRSRL 1100
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1101 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 1180
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1786986074 1181 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQEN 1249
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKS 228
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
760-1248 |
3.06e-51 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 191.47 E-value: 3.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 760 LCLVTSLTVEWMGLTA-AKNLHHN---LLNKIILG----------------PIRFFDTTPLGLILNRFSADTNIIDQHIP 819
Cdd:PRK10790 61 LGLVAGLAAAYVGLQLlAAGLHYAqslLFNRAAVGvvqqlrtdvmdaalrqPLSAFDTQPVGQLISRVTNDTEVIRDLYV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 820 PTLESLTRSTLLcLSA--IGMISYATPVFLVALL--PLGVAFYFIQKYF------RVASKdLQELDDStqlpllchFSET 889
Cdd:PRK10790 141 TVVATVLRSAAL-IGAmlVAMFSLDWRMALVAIMifPAVLVVMVIYQRYstpivrRVRAY-LADINDG--------FNEV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 890 AEGLTTIRAFRHETRFKQRMLELTDTNNIAylflsaanRWLEVRTD--------YLGACIVLTASIASISGSSNSGlVGL 961
Cdd:PRK10790 211 INGMSVIQQFRQQARFGERMGEASRSHYMA--------RMQTLRLDgfllrpllSLFSALILCGLLMLFGFSASGT-IEV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 962 GLLYALTitNYLNWVVRNLADLE-----VQMGAVKKVNSFLTMESENYEGTMDPSQVpehwpQEGEIKIHDLCVRYENNl 1036
Cdd:PRK10790 282 GVLYAFI--SYLGRLNEPLIELTtqqsmLQQAVVAGERVFELMDGPRQQYGNDDRPL-----QSGRIDIDNVSFAYRDD- 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1037 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRF 1116
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLA 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1117 NLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEN 1196
Cdd:PRK10790 434 NVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQ 513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 1197 ILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQE 1248
Cdd:PRK10790 514 AIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1021-1235 |
5.32e-49 |
|
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: 173.54 E-value: 5.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1021 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1100
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1101 SIILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 1177
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAPLA--DDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1786986074 1178 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNI 1235
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
971-1254 |
1.38e-48 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 183.87 E-value: 1.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 971 NYLNWVVR----NLADLEvQMGAVkkvnsfLTMESEnyegTMDPSQVPEHWPQEGEIKIHDLCVRYENNlKPVLKHVKAY 1046
Cdd:COG5265 313 NFLGFVYReirqALADME-RMFDL------LDQPPE----VADAPDAPPLVVGGGEVRFENVSFGYDPE-RPILKGVSFE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1047 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPECk 1123
Cdd:COG5265 381 VPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIaygRPDA- 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1124 cTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVM 1203
Cdd:COG5265 460 -SEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALR 538
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1786986074 1204 TAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQeNGVFAS 1254
Cdd:COG5265 539 EVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQ-GGLYAQ 588
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
997-1260 |
3.48e-48 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 184.00 E-value: 3.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 997 LTMESENYEGTMDPSQVpehwpqEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDI 1076
Cdd:TIGR03797 432 LEALPEVDEAKTDPGKL------SGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTL----LRLLLG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1077 FD----GKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAV 1152
Cdd:TIGR03797 502 FEtpesGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTV 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1153 VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDmateNILQKVVMTAFA--DRTVVTIAHRVHTILTADLVIVM 1230
Cdd:TIGR03797 582 ISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALD----NRTQAIVSESLErlKVTRIVIAHRLSTIRNADRIYVL 657
|
250 260 270
....*....|....*....|....*....|
gi 1786986074 1231 KRGNILEYDTPESLLAQEnGVFASFVRADM 1260
Cdd:TIGR03797 658 DAGRVVQQGTYDELMARE-GLFAQLARRQL 686
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
15-317 |
8.33e-48 |
|
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: 172.74 E-value: 8.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 15 FRYLADLLGFAGPLCISGIVQRVNETQNGTNNTTGISETLSSKEFLenayvlavllflalilqRTFLQASY-YVTIETGI 93
Cdd:cd18598 5 LKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLL-----------------GALLSSHYnFQMNKVSL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 94 NLRGALLAMIYNKILRLSTSnlSMGEMTLGQINNLVAIETNQLMWFlflCPNL---WAMPVQIIMGVILLYNLLGSSALV 170
Cdd:cd18598 68 KVRAALVTAVYRKALRVRSS--SLSKFSTGEIVNLMSTDADRIVNF---CPSFhdlWSLPLQIIVALYLLYQQVGVAFLA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 171 GAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTSL 250
Cdd:cd18598 143 GLVFALVLIPINKWIAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDAL 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 251 SIFMNAAIPIAAVLATFVTHAYaSGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 317
Cdd:cd18598 223 CVYFWATTPVLISILTFATYVL-MGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1031-1256 |
4.55e-47 |
|
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: 168.82 E-value: 4.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1031 RYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILF 1110
Cdd:cd03252 9 RYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1111 SGSIRFNL---DPECKCtdDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEAT 1187
Cdd:cd03252 89 NRSIRDNIalaDPGMSM--ERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1786986074 1188 ASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAqENGVFASFV 1256
Cdd:cd03252 167 SALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA-ENGLYAYLY 234
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
1005-1257 |
2.69e-46 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 178.60 E-value: 2.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1005 EGTMDPSQVPEHWPQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVID 1084
Cdd:TIGR03796 460 EPEGSAATSEPPRRLSGYVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFD 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1085 GIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPecKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFS 1161
Cdd:TIGR03796 540 GIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLtlwDP--TIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLS 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1162 VGQRQLFCLARAFVRKSSILIMDEATASIDMATEnilqKVVMTAFADR--TVVTIAHRVHTILTADLVIVMKRGNILEYD 1239
Cdd:TIGR03796 618 GGQRQRLEIARALVRNPSILILDEATSALDPETE----KIIDDNLRRRgcTCIIVAHRLSTIRDCDEIIVLERGKVVQRG 693
|
250
....*....|....*...
gi 1786986074 1240 TPESLLAQEnGVFASFVR 1257
Cdd:TIGR03796 694 THEELWAVG-GAYARLIR 710
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
80-317 |
4.29e-45 |
|
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: 164.66 E-value: 4.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 80 FLQASYYVTIETGINLRGALLAMIYNKILRLStsnlSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVIL 159
Cdd:cd18592 55 FFSLTWAISYRTGIRLRGAVLGLLYKKILRLR----SLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 160 LYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELS 239
Cdd:cd18592 131 STYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERK 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1786986074 240 SLKTFALYTSLSIFMNAAIPIAAVLATFVTHaYASGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 317
Cdd:cd18592 211 ILEKAGYLQSISISLAPIVPVIASVVTFLAH-VALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
987-1253 |
1.87e-44 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 170.97 E-value: 1.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 987 MGAVKKVNSFLTMESENYEGTMDPSQVpehwpqEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSL 1066
Cdd:PRK11176 312 MAACQTLFAILDLEQEKDEGKRVIERA------KGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTI 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1067 SLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPEC--KCTDDRLWEALEIAQLKNMVKS 1144
Cdd:PRK11176 386 ANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARteQYSREQIEEAARMAYAMDFINK 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1145 LPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTA 1224
Cdd:PRK11176 466 MDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKA 545
|
250 260
....*....|....*....|....*....
gi 1786986074 1225 DLVIVMKRGNILEYDTPESLLAQeNGVFA 1253
Cdd:PRK11176 546 DEILVVEDGEIVERGTHAELLAQ-NGVYA 573
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
384-599 |
1.92e-44 |
|
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: 158.70 E-value: 1.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGSGLA-TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNrys 462
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 463 VAYAAQKPWLLNATVEENItfgspfnkqrykavtdacslqpdidllpfgdqteigerginLSGGQRQRICVARALYQNTN 542
Cdd:cd03228 78 IAYVPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 543 IVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDG 599
Cdd:cd03228 117 ILILDEATSALDPE-TEALILEALRALAKG--KTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
992-1258 |
1.08e-43 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 168.99 E-value: 1.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 992 KVNSFLTME-----SENYEGTMDPSQVpehwpqEGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSL 1066
Cdd:PRK13657 305 KLEEFFEVEdavpdVRDPPGAIDLGRV------KGAVEFDDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1067 SLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVK 1143
Cdd:PRK13657 378 INLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIrvgRPDA--TDEEMRAAAERAQAHDFIE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1144 SLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILT 1223
Cdd:PRK13657 456 RKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRN 535
|
250 260 270
....*....|....*....|....*....|....*
gi 1786986074 1224 ADLVIVMKRGNILEYDTPESLLAQeNGVFASFVRA 1258
Cdd:PRK13657 536 ADRILVFDNGRVVESGSFDELVAR-GGRFAALLRA 569
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
363-606 |
8.05e-43 |
|
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: 165.71 E-value: 8.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 363 HLDSYEQSTRRL------RPAETE---------DIAIKVTNGYFSW-GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSL 426
Cdd:COG4987 298 HLGRVRAAARRLnelldaPPAVTEpaepapapgGPSLELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 427 LLAILGEMQTLEGKVHWSNVNESEPSFEATRRNrysVAYAAQKPWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPDI 505
Cdd:COG4987 378 LALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR---IAVVPQRPHLFDTTLRENLRLARPdATDEELWAALERVGLGDWL 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 506 DLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDdkRTLVLVTHKLQ 585
Cdd:COG4987 455 AALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAG--RTVLLITHRLA 531
|
250 260
....*....|....*....|.
gi 1786986074 586 YLTHADWIIAMKDGSVLREGT 606
Cdd:COG4987 532 GLERMDRILVLEDGRIVEQGT 552
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
400-611 |
1.48e-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: 157.33 E-value: 1.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNvnesepsfeatrrnrySVAYAAQKPWLLNATVEE 479
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG----------------RISFSSQFSWIMPGTIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 480 NITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD 559
Cdd:cd03291 117 NIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 560 HLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQ 611
Cdd:cd03291 197 EIFESCVCKLMAN--KTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQ 246
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
829-1230 |
2.43e-41 |
|
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: 160.53 E-value: 2.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 829 TLLCLSAIGMISYATPVFLVALLPLgVAFYFIQKYFRVASKDLQELDDSTQLPllCHFSETAEGLTTIRAFRHETRFKQR 908
Cdd:TIGR02857 132 PLAILAAVFPQDWISGLILLLTAPL-IPIFMILIGWAAQAAARKQWAALSRLS--GHFLDRLRGLPTLKLFGRAKAQAAA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 909 MLELTD--------TNNIAylFLSAANrwLEVRTDyLGACIVLTAsiasisgssnsglVGLGLLY-------ALTI---- 969
Cdd:TIGR02857 209 IRRSSEeyrertmrVLRIA--FLSSAV--LELFAT-LSVALVAVY-------------IGFRLLAgdldlatGLFVllla 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 970 -TNYLNwvVRNL-ADLEVQMGAVKKVNSFLTMESENyeGTMDPSQVPEHWPQEGEIKIHDLCVRYENNlKPVLKHVKAYI 1047
Cdd:TIGR02857 271 pEFYLP--LRQLgAQYHARADGVAAAEALFAVLDAA--PRPLAGKAPVTAAPASSLEFSGVSVAYPGR-RPALRPVSFTV 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1048 KPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPECkc 1124
Cdd:TIGR02857 346 PPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRPDA-- 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1125 TDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMT 1204
Cdd:TIGR02857 424 SDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRA 503
|
410 420
....*....|....*....|....*.
gi 1786986074 1205 AFADRTVVTIAHRVHTILTADLVIVM 1230
Cdd:TIGR02857 504 LAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
80-318 |
6.90e-41 |
|
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: 152.79 E-value: 6.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 80 FLQASYYVTIETGINLRGALLAMIYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVIL 159
Cdd:cd18594 55 LHHPYFFGLHRYGMQLRIALSSLIYKKTLKLSSSALS--KITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 160 LYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELS 239
Cdd:cd18594 133 LWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 240 SLKTFALYTSLSIFMNAAIPIAAVLATFVTHAyASGNNLKPAEAFASLSLFHILVTPL-FLLSTVVRFAVKAIISVQKLN 318
Cdd:cd18594 213 LIRKAAYIRAFNMAFFFFSPTLVSFATFVPYV-LTGNTLTARKVFTVISLLNALRMTItRFFPESIQTLSESRVSLKRIQ 291
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
384-622 |
2.11e-40 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 149.30 E-value: 2.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRnrySV 463
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRR---AI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 464 AYAAQKPWLLNATVEENITFGSP--FNKQRYKAVTDACsLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 541
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGRPdaTDEEVIEAAKAAQ-IHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 542 NIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEHW 621
Cdd:cd03253 157 PILLLDEATSALDTH-TEREIQAALRDVSKG--RTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMW 233
|
.
gi 1786986074 622 K 622
Cdd:cd03253 234 K 234
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
779-1258 |
4.33e-39 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 156.44 E-value: 4.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 779 LHHNLLNKIILG--------PIRFFDTTPLGLILNRFSADTNIIDqhippTLESLTRSTLLCLSAIGMISYA-----TPV 845
Cdd:TIGR01193 223 LGQRLSIDIILSyikhlfelPMSFFSTRRTGEIVSRFTDASSIID-----ALASTILSLFLDMWILVIVGLFlvrqnMLL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 846 FLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLpLLCHFSETAEGLTTIRAFRHE-TRFKQ----------RMLELTD 914
Cdd:TIGR01193 298 FLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAV-LNSSIIEDLNGIETIKSLTSEaERYSKidsefgdylnKSFKYQK 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 915 TNNIAYLFLSAANRWLEVRTDYLGACIVLTASIAsisgssnsglVGLGLLYALTITNYLNwVVRNLADLEVQMGAVK--- 991
Cdd:TIGR01193 377 ADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLT----------LGQLITFNALLSYFLT-PLENIINLQPKLQAARvan 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 992 -KVNSFLTMESE-NYEGTMDPSQVPEhwpqeGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLA 1069
Cdd:TIGR01193 446 nRLNEVYLVDSEfINKKKRTELNNLN-----GDIVINDVSYSYGYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1070 FFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL--DPECKCTDDRLWEALEIAQLKNMVKSLPG 1147
Cdd:TIGR01193 520 LVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLllGAKENVSQDEIWAACEIAEIKDDIENMPL 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1148 GLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEnilQKVV--MTAFADRTVVTIAHRVHTILTAD 1225
Cdd:TIGR01193 600 GYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVnnLLNLQDKTIIFVAHRLSVAKQSD 676
|
490 500 510
....*....|....*....|....*....|...
gi 1786986074 1226 LVIVMKRGNILEYDTPESLLAQeNGVFASFVRA 1258
Cdd:TIGR01193 677 KIIVLDHGKIIEQGSHDELLDR-NGFYASLIHN 708
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
384-606 |
8.74e-39 |
|
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: 144.68 E-value: 8.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRnrySV 463
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRS---MI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 464 AYAAQKPWLLNATVEENITFGSPFNKQ-RYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 542
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDeEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786986074 543 IVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 606
Cdd:cd03254 160 ILILDEATSNIDTE-TEKLIQEALEKLMKG--RTSIIIAHRLSTIKNADKILVLDDGKIIEEGT 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
398-605 |
5.44e-38 |
|
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: 141.96 E-value: 5.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 398 ATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNrysVAYAAQKPWLLNATV 477
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN---IGYVPQDVTLFYGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 478 EENITFGSPF-NKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 556
Cdd:cd03245 95 RDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMN 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1786986074 557 LSDHLMQEgiLKFLQDDKrTLVLVTHKLQYLTHADWIIAMKDGSVLREG 605
Cdd:cd03245 175 SEERLKER--LRQLLGDK-TLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1018-1217 |
7.30e-38 |
|
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: 150.20 E-value: 7.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1018 PQEGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 1097
Cdd:TIGR02868 330 LGKPTLELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1098 SRLSIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVR 1176
Cdd:TIGR02868 409 RRVSVCAQDAHLFDTTVRENLRLARPdATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1786986074 1177 KSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR 1217
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
394-606 |
8.08e-37 |
|
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: 138.90 E-value: 8.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 394 GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNrysVAYAAQKPWLL 473
Cdd:cd03251 12 GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ---IGLVSQDVFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 474 NATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 552
Cdd:cd03251 89 NDTVAENIAYGRPgATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1786986074 553 LDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 606
Cdd:cd03251 169 LDTE-SERLVQAALERLMKN--RTTFVIAHRLSTIENADRIVVLEDGKIVERGT 219
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
988-1258 |
1.02e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 147.68 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 988 GAVKKVNSFLTMESEnyegTMDPSQVPEHWPQEGEIKIHDLCVrYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLS 1067
Cdd:PRK11174 319 GAAESLVTFLETPLA----HPQQGEKELASNDPVTIEAEDLEI-LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1068 ---LAFFRmvdiFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNM 1141
Cdd:PRK11174 394 nalLGFLP----YQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllgNPDA--SDEQLQQALENAWVSEF 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1142 VKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTI 1221
Cdd:PRK11174 468 LPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDL 547
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1786986074 1222 LTADLVIVMKRGNILE---YDTpeslLAQENGVFASFVRA 1258
Cdd:PRK11174 548 AQWDQIWVMQDGQIVQqgdYAE----LSQAGGLFATLLAH 583
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1018-1253 |
1.74e-35 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 143.81 E-value: 1.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1018 PQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 1097
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1098 SRLSIILQDPILFSGSIRFNL---DPEckCTDDRLWEALEIAQLKNMVKSlPGGLDAVVTEGGENFSVGQRQLFCLARAF 1174
Cdd:PRK11160 414 QAISVVSQRVHLFSATLRDNLllaAPN--ASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1175 VRKSSILIMDEATASIDMATEN-ILQkVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQENGVFA 1253
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERqILE-LLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQ 569
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
400-606 |
5.30e-35 |
|
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: 133.82 E-value: 5.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNrysVAYAAQKPWLLNATVEE 479
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ---IGLVSQEPVLFDGTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 480 NITFGSPFNKQryKAVTDACSL---QPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 556
Cdd:cd03249 96 NIRYGKPDATD--EEVEEAAKKaniHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1786986074 557 lSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 606
Cdd:cd03249 174 -SEKLVQEALDRAMKG--RTTIVIAHRLSTIRNADLIAVLQNGQVVEQGT 220
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
84-291 |
3.02e-34 |
|
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: 133.50 E-value: 3.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 84 SYYVTIETGINLRGALLAMIYNKILRLSTSnlSMGEMTLGQINNLVAIETNQL-MWFLFLcPNLWAMPVQIIMGVILLYN 162
Cdd:cd18593 60 YFFGMQRIGMRLRVACSSLIYRKALRLSQA--ALGKTTVGQIVNLLSNDVNRFdQAVLFL-HYLWVAPLQLIAVIYILWF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 163 LLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLK 242
Cdd:cd18593 137 EIGWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVR 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 243 TFALYTSlsifMNAAIPIAA----VLATFVTHAYaSGNNLKPAEAFASLSLFH 291
Cdd:cd18593 217 RTSFLRA----LNMGLFFVSskliLFLTFLAYIL-LGNILTAERVFVTMALYN 264
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
364-596 |
3.21e-34 |
|
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: 138.96 E-value: 3.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 364 LDSYEQSTRRLRPA-ETEDIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH 442
Cdd:TIGR02857 301 LDAAPRPLAGKAPVtAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIA 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 443 WSNVNESEPSfEATRRNRysVAYAAQKPWLLNATVEENITFGSPFNKQ-RYKAVTDACSLQPDIDLLPFGDQTEIGERGI 521
Cdd:TIGR02857 381 VNGVPLADAD-ADSWRDQ--IAWVPQHPFLFAGTIAENIRLARPDASDaEIREALERAGLDEFVAALPQGLDTPIGEGGA 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1786986074 522 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAM 596
Cdd:TIGR02857 458 GLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAE-TEAEVLEALRALAQG--RTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1011-1235 |
4.03e-34 |
|
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: 131.05 E-value: 4.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1011 SQVPEHWpqEGEIKIHDLCVRYENNL-KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIS 1089
Cdd:cd03248 2 SLAPDHL--KGIVKFQNVTFAYPTRPdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1090 KLPLHTLRSRLSIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLF 1168
Cdd:cd03248 80 QYEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQsCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 1169 CLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNI 1235
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
379-620 |
4.97e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 131.36 E-value: 4.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 379 TEDIAIKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNesepsfeaTRR 458
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPV-LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP--------PRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 459 NRYSVAYAAQK---PWLLNATVEE--------NITFGSPFNKQRYKAVTDACSLqpdIDLLPFGDQTeIGErginLSGGQ 527
Cdd:COG1121 73 ARRRIGYVPQRaevDWDFPITVRDvvlmgrygRRGLFRRPSRADREAVDEALER---VGLEDLADRP-IGE----LSGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 528 RQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYL-THADWIIAMKDGsVLREGT 606
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYE--LLRELRREGKTILVVTHDLGAVrEYFDRVLLLNRG-LVAHGP 221
|
250
....*....|....*.
gi 1786986074 607 LKDIQTKDV--ELYEH 620
Cdd:COG1121 222 PEEVLTPENlsRAYGG 237
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
385-599 |
1.51e-33 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 128.74 E-value: 1.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 385 KVTNGYFSWGSGL-ATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNrysV 463
Cdd:cd03225 1 ELKNLSFSYPDGArPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK---V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 464 AYAAQKP--WLLNATVEENITFGsPFN--------KQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICV 533
Cdd:cd03225 78 GLVFQNPddQFFGPTVEEEVAFG-LENlglpeeeiEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 534 ARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYL-THADWIIAMKDG 599
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLE--LLKKLKAEGKTIIIVTHDLDLLlELADRVIVLEDG 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1023-1235 |
1.79e-33 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 127.33 E-value: 1.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAffrMVDIF---DGKIVIDGIDISKLPLHTLRSR 1099
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARL---ILGLLrptSGRVRLDGADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1100 LSIILQDPILFSGSIRFNLdpeckctddrlwealeiaqlknmvkslpggldavvteggenFSVGQRQLFCLARAFVRKSS 1179
Cdd:cd03246 78 VGYLPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 1180 ILIMDEATASIDMATEN-ILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNI 1235
Cdd:cd03246 117 ILVLDEPNSHLDVEGERaLNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1023-1247 |
3.62e-33 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 136.77 E-value: 3.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCvrYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1102
Cdd:PRK10789 316 VNIRQFT--YPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1103 ILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSIL 1181
Cdd:PRK10789 394 VSQTPFLFSDTVANNIALGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 1182 IMDEATASIDMATE-NILQKVVMTAfADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1247
Cdd:PRK10789 474 ILDDALSAVDGRTEhQILHNLRQWG-EGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQ 539
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
400-618 |
9.24e-32 |
|
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: 125.16 E-value: 9.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNrysVAYAAQK---PWLLnaT 476
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR---IAYVPQEppaPFGL--T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 477 VEENITFG--------SPFNKQRYKAVTDACslqpdidllpfgDQTEIG---ERGIN-LSGGQRQRICVARALYQNTNIV 544
Cdd:COG1120 92 VRELVALGryphlglfGRPSAEDREAVEEAL------------ERTGLEhlaDRPVDeLSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 545 FLDDPFSALDIHlsdHlmQEGILKFLQD----DKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDIQTKDV--EL 617
Cdd:COG1120 160 LLDEPTSHLDLA---H--QLEVLELLRRlareRGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEVLTPELleEV 234
|
.
gi 1786986074 618 Y 618
Cdd:COG1120 235 Y 235
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
384-610 |
1.66e-31 |
|
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: 123.60 E-value: 1.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNrysV 463
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK---V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 464 AYAAQKPW--LLNATVEENITFGsPFN--------KQRYKAVTDACSLQpdiDLL---PFgdqteigergiNLSGGQRQR 530
Cdd:COG1122 78 GLVFQNPDdqLFAPTVEEDVAFG-PENlglpreeiRERVEEALELVGLE---HLAdrpPH-----------ELSGGQKQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 531 ICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKD 609
Cdd:COG1122 143 VAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLE--LLKRLNKEGKTVIIVTHDLDLVAeLADRVIVLDDGRIVADGTPRE 220
|
.
gi 1786986074 610 I 610
Cdd:COG1122 221 V 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1023-1237 |
2.56e-31 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 121.27 E-value: 2.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPlHTLRSRLSI 1102
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1103 ILQDPILFSGSIRFNLdpeckctddrlwealeiaqlknmvkslpggldavvtegGENFSVGQRQLFCLARAFVRKSSILI 1182
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1786986074 1183 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILE 1237
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
400-631 |
3.25e-31 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 130.74 E-value: 3.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMqTLEGKVHWSNVNESEPSFEATRRNrysVAYAAQKPWLLNATVEE 479
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKH---LSWVGQNPQLPHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 480 NITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlS 558
Cdd:PRK11174 442 NVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH-S 520
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 559 DHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEhwktlMNRQDQE 631
Cdd:PRK11174 521 EQLVMQALNAASRR--QTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFAT-----LLAHRQE 586
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
705-943 |
6.38e-31 |
|
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: 123.52 E-value: 6.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 705 LILMIFSKLLKHSVIVAIDYWLATWTSEYS-INNTGKADQTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNL 783
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLpDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 784 LNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKY 863
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 864 FRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACIVL 943
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
394-614 |
7.56e-31 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 129.45 E-value: 7.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 394 GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNrysVAYAAQKPWLL 473
Cdd:TIGR02203 342 GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQ---VALVSQDVVLF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 474 NATVEENITFGSP--FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 551
Cdd:TIGR02203 419 NDTIANNIAYGRTeqADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATS 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 552 ALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKD 614
Cdd:TIGR02203 499 ALDNE-SERLVQAALERLMQG--RTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARN 558
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
384-610 |
8.84e-31 |
|
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: 121.82 E-value: 8.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGS-GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNrys 462
Cdd:cd03252 1 ITFEHVRFRYKPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 463 VAYAAQKPWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 541
Cdd:cd03252 78 VGVVLQENVLFNRSIRDNIALADPgMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1786986074 542 NIVFLDDPFSALDIHlSDHLMQEGILKFLqdDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDI 610
Cdd:cd03252 158 RILIFDEATSALDYE-SEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
384-619 |
1.40e-30 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 121.73 E-value: 1.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI--LGEMQtlEGKVHWSNVNESE-PSFEATRRnr 460
Cdd:COG4604 2 IEIKNVSKRYG-GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMIsrLLPPD--SGEVLVDGLDVATtPSRELAKR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 461 ysVAYAAQKPWL-LNATVEENITFGS-PFNKQR-----YKAVTDAcslqpdIDLLpfgDQTEIGERGIN-LSGGQRQRIC 532
Cdd:COG4604 77 --LAILRQENHInSRLTVRELVAFGRfPYSKGRltaedREIIDEA------IAYL---DLEDLADRYLDeLSGGQRQRAF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 533 VARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDK-RTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 610
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMKHSVQMMK--LLRRLADELgKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPEEI 223
|
250
....*....|.
gi 1786986074 611 QTKDV--ELYE 619
Cdd:COG4604 224 ITPEVlsDIYD 234
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1023-1248 |
1.58e-30 |
|
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: 120.90 E-value: 1.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1102
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1103 ILQDPI--LFSGSIR---------FNLDPECkcTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLA 1171
Cdd:COG1122 80 VFQNPDdqLFAPTVEedvafgpenLGLPREE--IRERVEEALELVGLEHLADRPPHEL-----------SGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1786986074 1172 RAFVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLAQE 1248
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDpRGRRELLELLKRLNKEGKTVIIVTHDLDLVAeLADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
384-606 |
1.65e-30 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 120.29 E-value: 1.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGSGLAT-LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRnryS 462
Cdd:cd03244 3 IEFKNVSLRYRPNLPPvLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS---R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 463 VAYAAQKPWLLNATVEENItfgSPFNK----QRYKAVtDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALY 538
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNL---DPFGEysdeELWQAL-ERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1786986074 539 QNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 606
Cdd:cd03244 156 RKSKILVLDEATASVDPE-TDALIQKTIREAFKD--CTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1024-1233 |
2.96e-30 |
|
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: 117.35 E-value: 2.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1024 KIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSII 1103
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1104 LQdpilfsgsirfnldpeckctddrlwealeiaqlknmvkslpggldavvteggenFSVGQRQLFCLARAFVRKSSILIM 1183
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 1184 DEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTILTA-DLVIVMKRG 1233
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1023-1233 |
3.59e-30 |
|
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: 118.73 E-value: 3.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENN---LKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIvidgidisklplhTLRSR 1099
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1100 LSIILQDPILFSGSIRFN------LDPEckctddRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARA 1173
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENilfgkpFDEE------RYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 1174 FVRKSSILIMDEATASIDMATEN-ILQKVVMTAFAD-RTVVTIAHRVHTILTADLVIVMKRG 1233
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRhIFENCILGLLLNnKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
379-604 |
4.93e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 120.19 E-value: 4.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 379 TEDIAIKVTN---GYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEa 455
Cdd:COG1116 3 AAAPALELRGvskRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 456 trrnrysVAYAAQK----PWLlnaTVEENITFGSPFN----KQRYKAVTDACSLqpdIDLLPFGD----QteigerginL 523
Cdd:COG1116 82 -------RGVVFQEpallPWL---TVLDNVALGLELRgvpkAERRERARELLEL---VGLAGFEDayphQ---------L 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 524 SGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQ---YLthADWIIAMKD-- 598
Cdd:COG1116 140 SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDE-LLRLWQETGKTVLFVTHDVDeavFL--ADRVVVLSArp 216
|
....*.
gi 1786986074 599 GSVLRE 604
Cdd:COG1116 217 GRIVEE 222
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
400-606 |
8.68e-30 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 126.37 E-value: 8.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRnRYSVAyaAQKPWLLNATVEE 479
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRS-RLAVV--SQTPFLFSDTVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 480 NITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlS 558
Cdd:PRK10789 408 NIALGRPdATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGR-T 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1786986074 559 DHlmqeGILKFLQD--DKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 606
Cdd:PRK10789 487 EH----QILHNLRQwgEGRTVIISAHRLSALTEASEILVMQHGHIAQRGN 532
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
399-613 |
1.94e-29 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 124.77 E-value: 1.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 399 TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRnrySVAYAAQKPWLLNATVE 478
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK---HIGYLPQDVELFPGTVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 479 ENIT-FGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 557
Cdd:TIGR01842 410 ENIArFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEG 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1786986074 558 SDHLMQEgiLKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTK 613
Cdd:TIGR01842 490 EQALANA--IKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
193-1257 |
2.95e-29 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 127.07 E-value: 2.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 193 QKSTLDYSTERLKKTNEILKGIKLLKLYAWEHifcksveeTRMKELS-SLKTFALYTSLSIFMNAaIPIAaVLATFVTHA 271
Cdd:PTZ00265 225 KKTSLLYNNNTMSIIEEALVGIRTVVSYCGEK--------TILKKFNlSEKLYSKYILKANFMES-LHIG-MINGFILAS 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 272 YASG------------NNLKPAEAFASLSLFHILV---TPLFLLSTV---VRFAVKAIISVQKLNEFLLSDEIGDDSwRT 333
Cdd:PTZ00265 295 YAFGfwygtriiisdlSNQQPNNDFHGGSVISILLgvlISMFMLTIIlpnITEYMKSLEATNSLYEIINRKPLVENN-DD 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 334 GESslpFESCKKhtgVQPKTInrkqpgRYHLDsyeqsTRRlrpaeteDIAIkvtngyfswgsglatLSNIDIRIPTGQLT 413
Cdd:PTZ00265 374 GKK---LKDIKK---IQFKNV------RFHYD-----TRK-------DVEI---------------YKDLNFTLTEGKTY 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 414 MIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnVNESEPSFEATRRN-RYSVAYAAQKPWLLNATVEENITFG-------- 484
Cdd:PTZ00265 415 AFVGESGCGKSTILKLIERLYDPTEGDII---INDSHNLKDINLKWwRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdle 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 485 --------SPFNKQRYKAVTDACSLQPDIDL------------------------------------------LPFGDQT 514
Cdd:PTZ00265 492 alsnyyneDGNDSQENKNKRNSCRAKCAGDLndmsnttdsneliemrknyqtikdsevvdvskkvlihdfvsaLPDKYET 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 515 EIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWII 594
Cdd:PTZ00265 572 LVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIF 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 595 AMK--------DGSVLREGTLKDIQTKD--------------------------VELYEH----------WKTLMNRQ-- 628
Cdd:PTZ00265 651 VLSnrergstvDVDIIGEDPTKDNKENNnknnkddnnnnnnnnnnkinnagsyiIEQGTHdalmknkngiYYTMINNQkv 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 629 --------DQELEKDM------------EADQTTLERKTLRRAMySREAKAQMEDEDEEEEEEEDEDDNMSTVMRLRTKM 688
Cdd:PTZ00265 731 sskkssnnDNDKDSDMkssaykdsergyDPDEMNGNSKHENESA-SNKKSCKMSDENASENNAGGKLPFLRNLFKRKPKA 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 689 P------WKTCWRY-----------LTSGGFFLLILMIFSKLlkhsVIVAIDYW-LATWTSEYSInntgkadqtyyvagF 750
Cdd:PTZ00265 810 PnnlrivYREIFSYkkdvtiialsiLVAGGLYPVFALLYAKY----VSTLFDFAnLEANSNKYSL--------------Y 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 751 SILCGAGIFLC-LVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDT---TPlGLILNRFSADTNIIDQHIPPTLESLT 826
Cdd:PTZ00265 872 ILVIAIAMFISeTLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINRDVHLLKTGLVNNIVIFT 950
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 827 RSTLLCLSAIGMISYATPVflVALLPLGVAFYFIqKYFRV-----ASKDLQELDDSTQLPLLCHFS-------------E 888
Cdd:PTZ00265 951 HFIVLFLVSMVMSFYFCPI--VAAVLTGTYFIFM-RVFAIrarltANKDVEKKEINQPGTVFAYNSddeifkdpsfliqE 1027
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 889 TAEGLTTIRAFRHETRFKQRMLELTDTNN------------------IAYLFLSAANRW----------LEVrTDYLGAc 940
Cdd:PTZ00265 1028 AFYNMNTVIIYGLEDYFCNLIEKAIDYSNkgqkrktlvnsmlwgfsqSAQLFINSFAYWfgsflirrgtILV-DDFMKS- 1105
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 941 iVLTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNlADLEVQ-MGAVKKVNSFLTmesenyegtmdpsqvpehwpq 1019
Cdd:PTZ00265 1106 -LFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRK-SNIDVRdNGGIRIKNKNDI--------------------- 1162
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1020 EGEIKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFD-------------------- 1078
Cdd:PTZ00265 1163 KGKIEIMDVNFRYISRPNvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtneqdy 1242
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1079 ----------------------------------GKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLD-PECK 1123
Cdd:PTZ00265 1243 qgdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKfGKED 1322
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1124 CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVV- 1202
Cdd:PTZ00265 1323 ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIv 1402
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1786986074 1203 -MTAFADRTVVTIAHRVHTILTADLVIVM----KRGNILE-YDTPESLLAQENGVFASFVR 1257
Cdd:PTZ00265 1403 dIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELLSVQDGVYKKYVK 1463
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
394-601 |
3.49e-29 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 124.09 E-value: 3.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 394 GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV--------HWsnvnesepsfEATRRNRYsVAY 465
Cdd:COG4618 342 GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsQW----------DREELGRH-IGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 466 AAQKPWLLNATVEENIT-FGSPfNKQrykAVTDACSLQpD----IDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 540
Cdd:COG4618 411 LPQDVELFDGTIAENIArFGDA-DPE---KVVAAAKLA-GvhemILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGD 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1786986074 541 TNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSV 601
Cdd:COG4618 486 PRLVVLDEPNSNLDDEGEAALAA--AIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
15-317 |
3.71e-29 |
|
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: 118.86 E-value: 3.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 15 FRYLADLLGFAGPLCISGIVQRVNETQngtnnttgisetlsskEFLENAYVLAVLLFLALILQRTFLQASYYVTIETGIN 94
Cdd:cd18559 5 IKLVLCNHVFSGPSNLWLLLWFDDPVN----------------GPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 95 LRGALLAMIYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSALVGAAV 174
Cdd:cd18559 69 ASRAVHLDLYHKALRSPISFFE--RTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 175 IVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTSLSIFM 254
Cdd:cd18559 147 GLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786986074 255 NAAIPIAAVLATFVTHAYASGNN-LKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 317
Cdd:cd18559 227 WCVGPCIVLFASFFAYVSRHSLAgLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
97-584 |
1.03e-28 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 122.47 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 97 GALLAMIYNKILRLS---TSNLSMGEMtlgqINNLVA-IETNQLMWFLFLCPNLWAMPVQII--MGVILLYNLLGSSALV 170
Cdd:TIGR02868 86 GALRVRVYERLARQAlagRRRLRRGDL----LGRLGAdVDALQDLYVRVIVPAGVALVVGAAavAAIAVLSVPAALILAA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 171 GAAVIVLLAPiqyFIATKLAEAQKSTLDYS-TERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTS 249
Cdd:TIGR02868 162 GLLLAGFVAP---LVSLRAARAAEQALARLrGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 250 LSIFMNAAIPIAAVLATFVTHAYASGNNLKPAEAFASLSLFHILVT-PLFLLSTVVRFAVKAIISVQKLNEFLlsdeigD 328
Cdd:TIGR02868 239 LGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFeAFAALPAAAQQLTRVRAAAERIVEVL------D 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 329 DSWRTGESSLPfesckkhtgvQPKTINRKQPGRyhldsyeqstrrlrpaETEDIAikvtngyFSWGSGLATLSNIDIRIP 408
Cdd:TIGR02868 313 AAGPVAEGSAP----------AAGAVGLGKPTL----------------ELRDLS-------AGYPGAPPVLDGVSLDLP 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 409 TGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRnrySVAYAAQKPWLLNATVEENITFGSP-F 487
Cdd:TIGR02868 360 PGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRR---RVSVCAQDAHLFDTTVRENLRLARPdA 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 488 NKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMqEGIL 567
Cdd:TIGR02868 437 TDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELL-EDLL 515
|
490
....*....|....*..
gi 1786986074 568 KflQDDKRTLVLVTHKL 584
Cdd:TIGR02868 516 A--ALSGRTVVLITHHL 530
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
391-597 |
2.10e-28 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 114.17 E-value: 2.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 391 FSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnVNESEPsfeatRRNRYSVAYAAQK- 469
Cdd:cd03235 7 VSYGGHPV-LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIR---VFGKPL-----EKERKRIGYVPQRr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 470 --PWLLNATVEE--------NITFGSPFNKQRYKAVTDAcslqpdidlLPFGDQTEIGERGI-NLSGGQRQRICVARALY 538
Cdd:cd03235 78 siDRDFPISVRDvvlmglygHKGLFRRLSKADKAKVDEA---------LERVGLSELADRQIgELSGGQQQRVLLARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 539 QNTNIVFLDDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMK 597
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIY--ELLRELRREGMTILVVTHDLGLVLeYFDRVLLLN 206
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
400-551 |
3.48e-28 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 111.20 E-value: 3.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNrysVAYAAQKPWLLNA-TVE 478
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKE---IGYVFQDPQLFPRlTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1786986074 479 ENITFGSPFnkQRYKAVTDACSLQPDIDLLPFGDQ--TEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 551
Cdd:pfam00005 78 ENLRLGLLL--KGLSKREKDARAEEALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
385-605 |
6.19e-28 |
|
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: 111.76 E-value: 6.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 385 KVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNrysVA 464
Cdd:cd03214 1 EVENLSVGYGGRTV-LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK---IA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 465 YAAQkpwLLNATveenitfgspfnkqrykavtdacslqpdiDLLPFGDqteigeRGIN-LSGGQRQRICVARALYQNTNI 543
Cdd:cd03214 77 YVPQ---ALELL-----------------------------GLAHLAD------RPFNeLSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786986074 544 VFLDDPFSALDIHLSDHLMQegILKFLQDDK-RTLVLVTHKL-QYLTHADWIIAMKDGSVLREG 605
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLE--LLRRLARERgKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
386-604 |
7.44e-28 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 112.57 E-value: 7.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 386 VTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEatrrnrysVAY 465
Cdd:cd03293 6 VSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD--------RGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 466 AAQK----PWLlnaTVEENITFGSPFN----KQRYKAVTDACSLqpdIDLLPFGDQTeIGErginLSGGQRQRICVARAL 537
Cdd:cd03293 78 VFQQdallPWL---TVLDNVALGLELQgvpkAEARERAEELLEL---VGLSGFENAY-PHQ----LSGGMRQRVALARAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 538 YQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQ---YLthADWIIAM--KDGSVLRE 604
Cdd:cd03293 147 AVDPDVLLLDEPFSALD-ALTREQLQEELLDIWRETGKTVLLVTHDIDeavFL--ADRVVVLsaRPGRIVAE 215
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
385-599 |
7.50e-28 |
|
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: 110.41 E-value: 7.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 385 KVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNrysVA 464
Cdd:cd00267 1 EIENLSFRYGGRTA-LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRR---IG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 465 YAAQkpwllnatveenitfgspfnkqrykavtdacslqpdidllpfgdqteigerginLSGGQRQRICVARALYQNTNIV 544
Cdd:cd00267 77 YVPQ------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1786986074 545 FLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTHA-DWIIAMKDG 599
Cdd:cd00267 103 LLDEPTSGLDPASRERLLE--LLRELAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1024-1233 |
2.08e-27 |
|
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: 111.02 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1024 KIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSII 1103
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1104 LQDP--ILFSGSIR----FNLDPECKCTDD---RLWEALEIAQLKNMVKSLPggldavvteggENFSVGQRQLFCLARAF 1174
Cdd:cd03225 81 FQNPddQFFGPTVEeevaFGLENLGLPEEEieeRVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 1175 VRKSSILIMDEATASIDMATENILQKVVmTAFADR--TVVTIAHRVHTILT-ADLVIVMKRG 1233
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELL-KKLKAEgkTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1023-1247 |
2.25e-27 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 118.08 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI---FDGKIVIDGIDISKLPLHTLRSR 1099
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1100 LSIILQDPI--LFSGSIRFNLD--PECKCTD-----DRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCL 1170
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQIAeaLENLGLSraearARVLELLEAVGLERRLDRYPHQL-----------SGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1171 ARAFVRKSSILIMDEATASIDMATenilQKVVMTAFAD------RTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPES 1243
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTT----QAEILDLLRElqrergTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEE 229
|
....
gi 1786986074 1244 LLAQ 1247
Cdd:COG1123 230 ILAA 233
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1023-1238 |
2.75e-27 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 111.44 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL---R 1097
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1098 SRLSIILQDPILfsgsirfNLDP------------ECKCTDDRLWEALEIAQLKNMVKSLPGG-LDAVVTEggenFSVGQ 1164
Cdd:cd03257 82 KEIQMVFQDPMS-------SLNPrmtigeqiaeplRIHGKLSKKEARKEAVLLLLVGVGLPEEvLNRYPHE----LSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1786986074 1165 RQLFCLARAFVRKSSILIMDEATASIDMATE-NILQkvVMTAFADR---TVVTIAHRVHTIL-TADLVIVMKRGNILEY 1238
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQaQILD--LLKKLQEElglTLLFITHDLGVVAkIADRVAVMYAGKIVEE 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
392-605 |
5.79e-27 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 109.92 E-value: 5.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 392 SWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSfeATRRNrysVAYAAQK-- 469
Cdd:cd03259 9 TYGSVRA-LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP--PERRN---IGMVFQDya 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 470 --PWLlnaTVEENITFGSPFNKQRYKAVTDACSLqpdidLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFL 546
Cdd:cd03259 83 lfPHL---TVAENIAFGLKLRGVPKAEIRARVRE-----LLELVGLEGLLNRYPHeLSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 547 DDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQ-YLTHADWIIAMKDGSVLREG 605
Cdd:cd03259 155 DEPLSALDAKLREELREE-LKELQRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
400-624 |
6.49e-27 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 117.49 E-value: 6.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRnrySVAYAAQKPWLLNATVEE 479
Cdd:TIGR02204 356 LDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRA---RMALVPQDPVLFAASVME 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 480 NITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLS 558
Cdd:TIGR02204 433 NIRYGRPdATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDA-ES 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1786986074 559 DHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDvELYEHWKTL 624
Cdd:TIGR02204 512 EQLVQQALETLMKG--RTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKG-GLYARLARL 574
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1020-1247 |
9.54e-27 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 116.77 E-value: 9.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1020 EGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAffrMVDIFD---GKIVIDGIDISKLPlhtl 1096
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARL---LVGVWPptaGSVRLDGADLSQWD---- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1097 RSRLSIIL----QDPILFSGSI-----RFNlDPeckcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQL 1167
Cdd:COG4618 401 REELGRHIgylpQDVELFDGTIaeniaRFG-DA----DPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1168 FCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLA 1246
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
.
gi 1786986074 1247 Q 1247
Cdd:COG4618 556 R 556
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
83-297 |
1.10e-26 |
|
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: 111.20 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 83 ASYYVTIETGINLRGALLAMIYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYN 162
Cdd:pfam00664 60 LQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 163 LLG-SSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSL 241
Cdd:pfam00664 138 YYGwKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAG 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 242 KTFALYTSLSI-FMNAAIPIAAVLATFVTHAYASGNNLKPAEAFASLSLFHILVTPL 297
Cdd:pfam00664 218 IKKAVANGLSFgITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
384-599 |
1.76e-26 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 108.73 E-value: 1.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGSG---LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTL-EGKVHWSNVNESEPSfEATR-- 457
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLL-NILGGLDRPtSGEVRVDGTDISKLS-EKELaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 458 -RNRySVAYAAQKPWLLNA-TVEENITFGSPFNKQRYKAVTDACslqpdIDLLpfgDQTEIGERgIN-----LSGGQRQR 530
Cdd:cd03255 79 fRRR-HIGFVFQSFNLLPDlTALENVELPLLLAGVPKKERRERA-----EELL---ERVGLGDR-LNhypseLSGGQQQR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1786986074 531 ICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDG 599
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMEL-LRELNKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
378-599 |
1.76e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 108.36 E-value: 1.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 378 ETEDIAIKVTNGYFswgsglatLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATR 457
Cdd:COG4619 2 ELEGLSFRVGGKPI--------LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 458 RnrySVAYAAQKPWLLNATVEENITFGSPFNKQRYkavtdacSLQPDIDLLP-FGDQTEIGERGI-NLSGGQRQRICVAR 535
Cdd:COG4619 74 R---QVAYVPQEPALWGGTVRDNLPFPFQLRERKF-------DRERALELLErLGLPPDILDKPVeRLSGGERQRLALIR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1786986074 536 ALYQNTNIVFLDDPFSALDIHLSDHLmQEGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDG 599
Cdd:COG4619 144 ALLLQPDVLLLDEPTSALDPENTRRV-EELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAG 207
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
724-991 |
1.80e-26 |
|
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: 110.77 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 724 YWLATWTSEysiNNTGKADQTY-YVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGL 802
Cdd:cd18559 20 LWLLLWFDD---PVNGPQEHGQvYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 803 ILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVAlLPLGVAFYFIQKYFRVASKDLQELDDSTQLPL 882
Cdd:cd18559 97 LVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVG-IPLGLLYVPVNRVYAASSRQLKRLESVSKDPR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 883 LCHFSETAEGLTTIRAFRHETRFKQRMLELTDtNNIAYLFLSAANRWLEVRTDYLGACIV-LTASIASISGSSNSGLVGL 961
Cdd:cd18559 176 YKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIVlFASFFAYVSRHSLAGLVAL 254
|
250 260 270
....*....|....*....|....*....|
gi 1786986074 962 GLLYALTITNYLNWVVRNLADLEVQMGAVK 991
Cdd:cd18559 255 KVFYSLALTTYLNWPLNMSPEVITNIVAAE 284
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1023-1244 |
3.80e-26 |
|
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: 108.04 E-value: 3.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIF-----DGKIVIDGIDISKLPLH--T 1095
Cdd:cd03260 1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1096 LRSRLSIILQDPILFSGSIRFNLD--------PECKCTDDRLWEALEIAQLKNMVKSLPGGLDavvteggenFSVGQRQL 1167
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAyglrlhgiKLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1786986074 1168 FCLARAFVRKSSILIMDEATASID-MATENIlQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESL 1244
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDpISTAKI-EELIAELKKEYTIVIVTHNMQQAArVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
400-601 |
5.71e-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: 105.76 E-value: 5.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNrysVAYAAQKPWLLNATVEE 479
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH---VGYLPQDDELFSGSIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 480 NItfgspfnkqrykavtdacslqpdidllpfgdqteigerginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD 559
Cdd:cd03246 95 NI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1786986074 560 HLMQegILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSV 601
Cdd:cd03246 134 ALNQ--AIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
380-601 |
1.01e-25 |
|
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: 106.34 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 380 EDIAIKVTNGYFSWGSGLA-TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRR 458
Cdd:cd03369 3 EHGEIEVENLSVRYAPDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 459 nrySVAYAAQKPWLLNATVEENItfgSPFNKQRYKAVTDACSlqpdidllpfgdqteIGERGINLSGGQRQRICVARALY 538
Cdd:cd03369 83 ---SLTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGALR---------------VSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 539 QNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDDkrTLVLVTHKLQYLTHADWIIAMKDGSV 601
Cdd:cd03369 142 KRPRVLVLDEATASIDYA-TDALIQKTIREEFTNS--TILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
690-997 |
1.62e-25 |
|
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350044 [Multi-domain] Cd Length: 324 Bit Score: 109.12 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 690 WKTCWRYLTSGGFFLLILmIFSKLLKHSVIVAIDYWLATWTSEYSINNTGKAD---QTY---------------YVAGFS 751
Cdd:cd18600 3 WNTYLRYITSHKSLIFVL-ILCLVIFAIEVAASLVGLWLLRSQADRVNTTRPEsssNTYavivtftssyyvfyiYVGVAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 752 ILCGAGIF--LCLVTSLtvewmgLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRST 829
Cdd:cd18600 82 SLLAMGFFrgLPLVHTL------ITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 830 LLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRM 909
Cdd:cd18600 156 LIVIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 910 LELTDTNNIAYLFLSAANRWLEVRTDYLGAC-IVLTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMG 988
Cdd:cd18600 236 HKALNLHTANWFLYLSTLRWFQMRIEMIFVIfFTAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMR 315
|
....*....
gi 1786986074 989 AVKKVNSFL 997
Cdd:cd18600 316 SVSRIFKFI 324
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
362-610 |
2.64e-25 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 113.30 E-value: 2.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 362 YHLDSYEQSTRRLRPAETEDIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV 441
Cdd:TIGR01193 452 YLVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEI 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 442 HWSNVNESEPSFEATRRnrySVAYAAQKPWLLNATVEENITFGSPFN--KQRYKAVTDACSLQPDIDLLPFGDQTEIGER 519
Cdd:TIGR01193 532 LLNGFSLKDIDRHTLRQ---FINYLPQEPYIFSGSILENLLLGAKENvsQDEIWAACEIAEIKDDIENMPLGYQTELSEE 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 520 GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLSDHLMQEGILkFLQDdkRTLVLVTHKLQYLTHADWIIAMKDG 599
Cdd:TIGR01193 609 GSSISGGQKQRIALARALLTDSKVLILDESTSNLDT-ITEKKIVNNLL-NLQD--KTIIFVAHRLSVAKQSDKIIVLDHG 684
|
250
....*....|.
gi 1786986074 600 SVLREGTLKDI 610
Cdd:TIGR01193 685 KIIEQGSHDEL 695
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
381-604 |
2.67e-25 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 105.51 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 381 DIAIKVTNGYFSWGSGLAT---LSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTL-EGKVHWSNVNESEPSfEAT 456
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEvtaLRGVSLSIEAGEFVAIVGPSGSGKSTLL-NILGGLDRPtSGEVLIDGQDISSLS-ERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 457 R---RNRYsVAYAAQKPWLL-NATVEENITFGSPFNKQRYKAVTDACslqpdIDLLpfgDQTEIGERgIN-----LSGGQ 527
Cdd:COG1136 80 LarlRRRH-IGFVFQFFNLLpELTALENVALPLLLAGVSRKERRERA-----RELL---ERVGLGDR-LDhrpsqLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1786986074 528 RQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFL-QDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLRE 604
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLE--LLRELnRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
384-617 |
2.90e-25 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 105.66 E-value: 2.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNRYSV 463
Cdd:cd03261 1 IELRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 464 AYAAQKPWLLNA-TVEENITFG----SPFNKQRYKAVT----DACSLQPDIDLLPfgdqteigergINLSGGQRQRICVA 534
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVAFPlrehTRLSEEEIREIVleklEAVGLRGAEDLYP-----------AELSGGMKKRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 535 RALYQNTNIVFLDDPFSALDIHLSDhLMQEGILKfLQDDKR-TLVLVTHKLQ-YLTHADWIIAMKDGSVLREGTLKDIQT 612
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASG-VIDDLIRS-LKKELGlTSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
....*
gi 1786986074 613 KDVEL 617
Cdd:cd03261 227 SDDPL 231
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
400-610 |
3.15e-25 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 112.91 E-value: 3.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSL--LLAILGEMQTLEGKVHWSNVNESEPSFeaTRRNrysVAYAAQKPWLLNATV 477
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLtkLLQRLYTPQHGQVLVDGVDLAIADPAW--LRRQ---MGVVLQENVLFSRSI 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 478 EENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 556
Cdd:TIGR01846 548 RDNIALCNPgAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYE 627
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1786986074 557 lSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDI 610
Cdd:TIGR01846 628 -SEALIMRNMREICRG--RTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
384-618 |
3.99e-25 |
|
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: 105.34 E-value: 3.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNRYSV 463
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 464 AYAAQKPWLLN-ATVEENITFG------------SPFNKQRYKAvtdACSLQPDIDLLPFGDQteigeRGINLSGGQRQR 530
Cdd:cd03256 81 GMIFQQFNLIErLSVLENVLSGrlgrrstwrslfGLFPKEEKQR---ALAALERVGLLDKAYQ-----RADQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 531 ICVARALYQNTNIVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQY-LTHADWIIAMKDGSVLREGTLKD 609
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVM-DLLKRINREEGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAE 231
|
250
....*....|
gi 1786986074 610 IQTKDV-ELY 618
Cdd:cd03256 232 LTDEVLdEIY 241
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
384-610 |
6.31e-25 |
|
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: 105.08 E-value: 6.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNrysV 463
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRK---I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 464 AYAAQKPWLL-NATVEENITFGSPFNK-QRYKAVTDACSLQPDIDLLPfgdqTEIGER-GINLSGGQRQRICVARALYQN 540
Cdd:cd03295 78 GYVIQQIGLFpHMTVEENIALVPKLLKwPKEKIRERADELLALVGLDP----AEFADRyPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1786986074 541 TNIVFLDDPFSALDIHLSDHLmQEGILKFLQDDKRTLVLVTHKLQ-YLTHADWIIAMKDGSVLREGTLKDI 610
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQL-QEEFKRLQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1040-1188 |
8.18e-25 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 101.57 E-value: 8.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1040 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSG-SIRFNL 1118
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 1119 DPECKCT-------DDRLWEALEiaQLknmvkSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA 1188
Cdd:pfam00005 81 RLGLLLKglskrekDARAEEALE--KL-----GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
383-610 |
1.00e-24 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 104.50 E-value: 1.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 383 AIKVTN---GYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWsnvNESEPSFEATRRN 459
Cdd:COG1124 1 MLEVRNlsvSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTF---DGRPVTRRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 460 RYSVAYAAQKPWL-LNA--TVEENIT-----FGSPFNKQRYKAVTDACSLQPDI-DLLPfgDQteigerginLSGGQRQR 530
Cdd:COG1124 78 RRRVQMVFQDPYAsLHPrhTVDRILAeplriHGLPDREERIAELLEQVGLPPSFlDRYP--HQ---------LSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 531 ICVARALYQNTNIVFLDDPFSALDIHlsdhlMQEGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMKDGSVLREG 605
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVS-----VQAEILNLLKDLREerglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEEL 221
|
....*
gi 1786986074 606 TLKDI 610
Cdd:COG1124 222 TVADL 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
369-618 |
1.01e-24 |
|
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: 109.99 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 369 QSTRRLRPAETEDIAIKVTN---GYFSWGSGLAT-LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS 444
Cdd:COG1123 246 ARGRAAPAAAAAEPLLEVRNlskRYPVRGKGGVRaVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 445 NVNESEPSFEATRRNRYSVAYAAQKPWL-LNA--TVEENITFG-------SPfnKQRYKAVT---DACSLQPD-IDLLPF 510
Cdd:COG1123 326 GKDLTKLSRRSLRELRRRVQMVFQDPYSsLNPrmTVGDIIAEPlrlhgllSR--AERRERVAellERVGLPPDlADRYPH 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 511 GdqteigerginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKL-- 584
Cdd:COG1123 404 E-----------LSGGQRQRVAIARALALEPKLLILDEPTSALDVSV-----QAQILNLLRDLQRelglTYLFISHDLav 467
|
250 260 270
....*....|....*....|....*....|....*
gi 1786986074 585 -QYLthADWIIAMKDGSVLREGTLKDIQTKDVELY 618
Cdd:COG1123 468 vRYI--ADRVAVMYDGRIVEDGPTEEVFANPQHPY 500
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
400-605 |
1.01e-24 |
|
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: 102.39 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnVNESEPS-FEATRRNRYSVAyaAQKPWLLNATVE 478
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT---LDGVPVSdLEKALSSLISVL--NQRPYLFDTTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 479 ENItfgspfnkqrykavtdacslqpdidllpfgdqteigerGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 558
Cdd:cd03247 93 NNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1786986074 559 DHLMqEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREG 605
Cdd:cd03247 135 RQLL-SLIFEVLKD--KTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1023-1249 |
1.19e-24 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 104.17 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHtLRSRLSI 1102
Cdd:COG4555 2 IEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1103 ILQDPILFSG-SIRFNLDPECKCTDDRLWEALEIAQlkNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSIL 1181
Cdd:COG4555 79 LPDERGLYDRlTVRENIRYFAELYGLFDEELKKRIE--ELIELL--GLEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1182 IMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLAQEN 1249
Cdd:COG4555 155 LLDEPTNGLDvMARRLLREILRALKKEGKTVLFSSHIMQEVEaLCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
384-614 |
1.79e-24 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 109.72 E-value: 1.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSW-GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSL--LLAILGEMQtlEGKVHWSNVNESEPSFEATRRNr 460
Cdd:PRK11176 342 IEFRNVTFTYpGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIanLLTRFYDID--EGEILLDGHDLRDYTLASLRNQ- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 461 ysVAYAAQKPWLLNATVEENITFGSpfnKQRY------KAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICVA 534
Cdd:PRK11176 419 --VALVSQNVHLFNDTIANNIAYAR---TEQYsreqieEAARMAYAMD-FINKMDNGLDTVIGENGVLLSGGQRQRIAIA 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 535 RALYQNTNIVFLDDPFSALDIHlSDHLMQEGiLKFLQDDKRTLVlVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKD 614
Cdd:PRK11176 493 RALLRDSPILILDEATSALDTE-SERAIQAA-LDELQKNRTSLV-IAHRLSTIEKADEILVVEDGEIVERGTHAELLAQN 569
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
384-616 |
1.97e-24 |
|
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: 103.40 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRnrysV 463
Cdd:COG4555 2 IEVENLSKKYGKVPA-LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ----I 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 464 AYAAQKPWL-LNATVEENITFGSPFN---KQRYKAVTDacSLQPDIDLLPFGDQTeIGErginLSGGQRQRICVARALYQ 539
Cdd:COG4555 77 GVLPDERGLyDRLTVRENIRYFAELYglfDEELKKRIE--ELIELLGLEEFLDRR-VGE----LSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1786986074 540 NTNIVFLDDPFSALDIhLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKDVE 616
Cdd:COG4555 150 DPKVLLLDEPTNGLDV-MARRLLRE-ILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
89-628 |
3.01e-24 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 109.66 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 89 IETGINlrGALLAMIYNKILRL--------STSNLSMGEMTLGQINNLVAIET-NQLMWFLFLCPNLWAMpvqiimgviL 159
Cdd:TIGR03797 203 LETRMD--ASLQAAVWDRLLRLpvsffrqySTGDLASRAMGISQIRRILSGSTlTTLLSGIFALLNLGLM---------F 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 160 LYNLlgSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLK--------LYAWEHIFCKSVE 231
Cdd:TIGR03797 272 YYSW--KLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRvagaenraFARWAKLFSRQRK 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 232 ---ETRMKE--LSSLKT-FALYTSLSIFMNAAIPIAAV---LATFVTHAYASGNNLKPAEAFASlSLFHIL-VTPLFlls 301
Cdd:TIGR03797 350 lelSAQRIEnlLTVFNAvLPVLTSAALFAAAISLLGGAglsLGSFLAFNTAFGSFSGAVTQLSN-TLISILaVIPLW--- 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 302 tvvrfavkaiisvqklnefllsdeigddswrtgESSLP-FESckkhtgvQPKT-INRKQPGRYHLdsyeqstrrlrpaet 379
Cdd:TIGR03797 426 ---------------------------------ERAKPiLEA-------LPEVdEAKTDPGKLSG--------------- 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 380 ediAIKVTNGYFSWG-SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRR 458
Cdd:TIGR03797 451 ---AIEVDRVTFRYRpDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRR 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 459 NRYSVAYAAQkpwLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALY 538
Cdd:TIGR03797 528 QLGVVLQNGR---LMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALV 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 539 QNTNIVFLDDPFSALdihlsDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELY 618
Cdd:TIGR03797 605 RKPRILLFDEATSAL-----DNRTQAIVSESLERLKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFA 679
|
570
....*....|
gi 1786986074 619 EhwktLMNRQ 628
Cdd:TIGR03797 680 Q----LARRQ 685
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1023-1246 |
6.27e-24 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 102.19 E-value: 6.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYE--NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1100
Cdd:COG1124 2 LEVRNLSVSYGqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1101 SIILQDPIlfsGSI--RFNLDpeckctdDRLWEALEIAQLKNMVKSLPGGLDAVvteG-GENF--------SVGQRQLFC 1169
Cdd:COG1124 82 QMVFQDPY---ASLhpRHTVD-------RILAEPLRIHGLPDREERIAELLEQV---GlPPSFldryphqlSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1170 LARAFVRKSSILIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESL 1244
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQaeilNLLKD--LREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADL 226
|
..
gi 1786986074 1245 LA 1246
Cdd:COG1124 227 LA 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
400-601 |
6.73e-24 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 101.39 E-value: 6.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnVNESEPSFEATRRNRYSVAYAAQKPWLLNATVEE 479
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVL---LDGKPISQYEHKYLHSKVSLVGQEPVLFARSLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 480 NITFG---SPFnkQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 556
Cdd:cd03248 107 NIAYGlqsCSF--ECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1786986074 557 lSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSV 601
Cdd:cd03248 185 -SEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1023-1247 |
6.73e-24 |
|
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: 107.30 E-value: 6.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNLK---PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTL 1096
Cdd:COG1123 261 LEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1097 RSRLSIILQDPilfSGSirfnLDPECKCTDDrLWEALEI------AQLKNMVKSLpggLDAVvteG----------GEnF 1160
Cdd:COG1123 341 RRRVQMVFQDP---YSS----LNPRMTVGDI-IAEPLRLhgllsrAERRERVAEL---LERV---GlppdladrypHE-L 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1161 SVGQRQLFCLARAFVRKSSILIMDEATASIDMATenilQKVVMTAFAD------RTVVTIAHRVHTILT-ADLVIVMKRG 1233
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDVSV----QAQILNLLRDlqrelgLTYLFISHDLAVVRYiADRVAVMYDG 481
|
250
....*....|....
gi 1786986074 1234 NILEYDTPESLLAQ 1247
Cdd:COG1123 482 RIVEDGPTEEVFAN 495
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1023-1249 |
1.12e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 102.38 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1102
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1103 ILQDPI-LFSGS-----IRFNLdpECKCTD-----DRLWEALEIAQLKNMVKSLPggldavvteggENFSVGQRQLFCLA 1171
Cdd:PRK13632 88 IFQNPDnQFIGAtveddIAFGL--ENKKVPpkkmkDIIDDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1172 RAFVRKSSILIMDEATASID-MATENILQKVV-MTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQEN 1249
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDpKGKREIKKIMVdLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
384-599 |
1.82e-23 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 98.80 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEaTRRNRYSV 463
Cdd:cd03229 1 LELKNVSKRYGQKTV-LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDE-LPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 464 AYAAQKPWLL-NATVEENITFGspfnkqrykavtdacslqpdidllpfgdqteigerginLSGGQRQRICVARALYQNTN 542
Cdd:cd03229 79 GMVFQDFALFpHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 543 IVFLDDPFSALDIhlsdhLMQEGILKFLQD----DKRTLVLVTHKLQYLTH-ADWIIAMKDG 599
Cdd:cd03229 121 VLLLDEPTSALDP-----ITRREVRALLKSlqaqLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
400-620 |
4.44e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 105.96 E-value: 4.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNrysVAYAAQKPWLLNATVEE 479
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQ---VALVGQEPVLFSGSVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 480 NITFGSPF-NKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlS 558
Cdd:TIGR00958 574 NIAYGLTDtPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE-C 652
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 559 DHLMQEgiLKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTkDVELYEH 620
Cdd:TIGR00958 653 EQLLQE--SRSRAS--RTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLME-DQGCYKH 709
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
384-610 |
6.06e-23 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 98.79 E-value: 6.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLL-----LAILGEMQTLEGKVHW--SNVNESEPSFEAT 456
Cdd:cd03260 1 IELRDLNVYYGDKHA-LKDISLDIPKGEITALIGPSGCGKSTLLrllnrLNDLIPGAPDEGEVLLdgKDIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 457 RRNrysVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDAC---SLQpDIDLLP-FGDQTEIGErginLSGGQRQRIC 532
Cdd:cd03260 80 RRR---VGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERveeALR-KAALWDeVKDRLHALG----LSGGQQQRLC 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1786986074 533 VARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFlqDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 610
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPI-STAKIEELIAEL--KKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
400-610 |
6.43e-23 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 98.98 E-value: 6.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRnrysVAYAAQKPWL-LNATVE 478
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR----IGYVPQEPALyPDLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 479 ENITF-------GSPFNKQRYKAVTDACSLQPDIDllpfgdqteigERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 551
Cdd:COG1131 92 ENLRFfarlyglPRKEARERIDELLELFGLTDAAD-----------RKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 552 ALDIHLSDHLMQegILKFLQDDKRTLVLVTHklqYLTHA----DWIIAMKDGSVLREGTLKDI 610
Cdd:COG1131 161 GLDPEARRELWE--LLRELAAEGKTVLLSTH---YLEEAerlcDRVAIIDKGRIVADGTPDEL 218
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
396-591 |
7.11e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 97.30 E-value: 7.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 396 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnvnesepsfeatRRNRYSVAYAAQK---PWL 472
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR--------------RAGGARVAYVPQRsevPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 473 LNATVEENITFG--------SPFNKQRYKAVTDACSlqpDIDLLPFGDQtEIGErginLSGGQRQRICVARALYQNTNIV 544
Cdd:NF040873 70 LPLTVRDLVAMGrwarrglwRRLTRDDRAAVDDALE---RVGLADLAGR-QLGE----LSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1786986074 545 FLDDPFSALDIHLSDHLmqEGILKFLQDDKRTLVLVTHKLQYLTHAD 591
Cdd:NF040873 142 LLDEPTTGLDAESRERI--IALLAEEHARGATVVVVTHDLELVRRAD 186
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1023-1249 |
7.44e-23 |
|
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: 99.35 E-value: 7.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAffRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1100
Cdd:COG1120 2 LEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLlrALA--GLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1101 SIILQDPIL-FSGSIR--------------FNLDPEckctDDRL-WEALE---IAQLKN-MVKSLPGGldavvteggenf 1160
Cdd:COG1120 78 AYVPQEPPApFGLTVRelvalgryphlglfGRPSAE----DREAvEEALErtgLEHLADrPVDELSGG------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1161 svgQRQLFCLARAFVRKSSILIMDEATASIDMA----TENILQKvvMTAFADRTVVTIAHRV-HTILTADLVIVMKRGNI 1235
Cdd:COG1120 142 ---ERQRVLIARALAQEPPLLLLDEPTSHLDLAhqleVLELLRR--LARERGRTVVMVLHDLnLAARYADRLVLLKDGRI 216
|
250
....*....|....
gi 1786986074 1236 LEYDTPESLLAQEN 1249
Cdd:COG1120 217 VAQGPPEEVLTPEL 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
383-620 |
1.35e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 100.92 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 383 AIKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG-EMQTlEGKVHW--SNVNESEPSfeatRRN 459
Cdd:COG3839 3 SLELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGlEDPT-SGEILIggRDVTDLPPK----DRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 460 rysVAYAAQKPWLL-NATVEENITFG------SPfnKQRYKAVTDACSLqpdIDLLPFGDQteigeRGINLSGGQRQRIC 532
Cdd:COG3839 77 ---IAMVFQSYALYpHMTVYENIAFPlklrkvPK--AEIDRRVREAAEL---LGLEDLLDR-----KPKQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 533 VARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKdiq 611
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKLRVEMRAE-IKRLHRRLGTTTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPE--- 219
|
....*....
gi 1786986074 612 tkdvELYEH 620
Cdd:COG3839 220 ----ELYDR 224
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
400-605 |
1.70e-22 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 97.58 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNRYSVAYAAQKPWL-LNA--T 476
Cdd:cd03257 21 LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRKEIQMVFQDPMSsLNPrmT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 477 VEENIT-----FGSPFNKQRYKAVT--DACSLQPDIDLL---PFGdqteigerginLSGGQRQRICVARALYQNTNIVFL 546
Cdd:cd03257 101 IGEQIAeplriHGKLSKKEARKEAVllLLVGVGLPEEVLnryPHE-----------LSGGQRQRVAIARALALNPKLLIA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 547 DDPFSALDIHLSDHLMQegILKFLQDDK-RTLVLVTHKL---QYLthADWIIAMKDGSVLREG 605
Cdd:cd03257 170 DEPTSALDVSVQAQILD--LLKKLQEELgLTLLFITHDLgvvAKI--ADRVAVMYAGKIVEEG 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
378-619 |
8.84e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 96.74 E-value: 8.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 378 ETEDIAIKVTNGYFSWGSGLA-TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEAT 456
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 457 RRNrysVAYAAQKP--WLLNATVEENITFG-----SPFNKQRYKaVTDACSlqpDIDLLPFGDQTEigergINLSGGQRQ 529
Cdd:PRK13648 82 RKH---IGIVFQNPdnQFVGSIVKYDVAFGlenhaVPYDEMHRR-VSEALK---QVDMLERADYEP-----NALSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 530 RICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKR-TLVLVTHKLQYLTHADWIIAMKDGSVLREGTLK 608
Cdd:PRK13648 150 RVAIAGVLALNPSVIILDEATSMLDPDARQNLLD--LVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKGTVYKEGTPT 227
|
250
....*....|.
gi 1786986074 609 DIQTKDVELYE 619
Cdd:PRK13648 228 EIFDHAEELTR 238
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
384-601 |
1.15e-21 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 93.23 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRnrysV 463
Cdd:cd03230 1 IEVRNLSKRYGKKTA-LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR----I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 464 AYAAQKPWLL-NATVEENItfgspfnkqrykavtdacslqpdidllpfgdqteigergiNLSGGQRQRICVARALYQNTN 542
Cdd:cd03230 76 GYLPEEPSLYeNLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 543 IVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYL-THADWIIAMKDGSV 601
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWE--LLRELKKEGKTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
379-617 |
1.83e-21 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 95.05 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 379 TEDIAIKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRR 458
Cdd:COG1127 1 MSEPMIEVRNLTKSFG-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 459 NRYSVAYAAQKPWLLNA-TVEENITFG-------SPfnKQRYKAVT---DACSLQPDIDLLPfgdqteiGErginLSGGQ 527
Cdd:COG1127 80 LRRRIGMLFQGGALFDSlTVFENVAFPlrehtdlSE--AEIRELVLeklELVGLPGAADKMP-------SE----LSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 528 RQRICVARALYQNTNIVFLDDPFSALDIHLS---DHLMQEgilkfLQDD-KRTLVLVTHKLQYL-THADWIIAMKDGSVL 602
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDPITSaviDELIRE-----LRDElGLTSVVVTHDLDSAfAIADRVAVLADGKII 221
|
250
....*....|....*
gi 1786986074 603 REGTLKDIQTKDVEL 617
Cdd:COG1127 222 AEGTPEELLASDDPW 236
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
402-610 |
2.67e-21 |
|
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: 95.02 E-value: 2.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 402 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW-----SNVNESEpsFEATRRNRYSVAYaaQKPWLL-NA 475
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIdgqdiAAMSRKE--LRELRRKKISMVF--QSFALLpHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 476 TVEENITFGSPFN----KQRYKAVTDACSLqpdIDLLPFGDQtEIGErginLSGGQRQRICVARALYQNTNIVFLDDPFS 551
Cdd:cd03294 118 TVLENVAFGLEVQgvprAEREERAAEALEL---VGLEGWEHK-YPDE----LSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 552 ALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDI 610
Cdd:cd03294 190 ALD-PLIRREMQDELLRLQAELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
400-610 |
5.40e-21 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 95.98 E-value: 5.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGemqtLE----GKVHW------SNVnesepsfEATRRNrysVAYAAQK 469
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAG----LEtpdsGRIVLngrdlfTNL-------PPRERR---VGFVFQH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 470 PWLL-NATVEENITFG---SPFNKQRYKA-VTDACSLqpdIDLLPFGD----QteigerginLSGGQRQRICVARALYQN 540
Cdd:COG1118 84 YALFpHMTVAENIAFGlrvRPPSKAEIRArVEELLEL---VQLEGLADrypsQ---------LSGGQRQRVALARALAVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1786986074 541 TNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQ-YLTHADWIIAMKDGSVLREGTLKDI 610
Cdd:COG1118 152 PEVLLLDEPFGALDAKVRKELRRW-LRRLHDELGGTTVFVTHDQEeALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
400-612 |
5.80e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 93.93 E-value: 5.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNvnESEPSFEATRRNRYsVAYAAQKPWLLNA-TVE 478
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGD--KPISMLSSRQLARR-LALLPQHHLTPEGiTVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 479 ENITFG-SPFNK------QRYKAVTDACSLQPDIDllpfgdqtEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPF 550
Cdd:PRK11231 95 ELVAYGrSPWLSlwgrlsAEDNARVNQAMEQTRIN--------HLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 551 SALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDIQT 612
Cdd:PRK11231 167 TYLDINHQVELM--RLMRELNTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
376-606 |
6.66e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 98.36 E-value: 6.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 376 PAETEDIAIKVTNGYFSW-GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSfE 454
Cdd:PRK11160 331 TAAADQVSLTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS-E 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 455 ATRRNRYSVAyaAQKPWLLNATVEENITFGSP-FNKQRYKAVTDACSLQpdiDLLPfGDQ---TEIGERGINLSGGQRQR 530
Cdd:PRK11160 410 AALRQAISVV--SQRVHLFSATLRDNLLLAAPnASDEALIEVLQQVGLE---KLLE-DDKglnAWLGEGGRQLSGGEQRR 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1786986074 531 ICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 606
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILEL-LAEHAQN--KTVLMITHRLTGLEQFDRICVMDNGQIIEQGT 556
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
400-606 |
1.67e-20 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 97.71 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRnrySVAYAAQKPWLLNATVEE 479
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLAN---SVAMVDQDIFLFEGTVRD 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 480 NITFGSPF--NKQRYKAVTDACsLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD--- 554
Cdd:TIGR03796 572 NLTLWDPTipDADLVRACKDAA-IHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDpet 650
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 555 -IHLSDHLMQEGIlkflqddkrTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 606
Cdd:TIGR03796 651 eKIIDDNLRRRGC---------TCIIVAHRLSTIRDCDEIIVLERGKVVQRGT 694
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1023-1239 |
1.77e-20 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 91.04 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHtlRS 1098
Cdd:cd03259 1 LELKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTL----LRLIAGLErpdsGEILIDGRDVTGVPPE--RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1099 RLSIILQDPILFS-----GSIRFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCL 1170
Cdd:cd03259 73 NIGMVFQDYALFPhltvaENIAFGLKLRGVPKAEiraRVRELLELVGLEGLLNRYPHEL-----------SGGQQQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 1171 ARAFVRKSSILIMDEATASIDMAT-ENILQKVV-MTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYD 1239
Cdd:cd03259 142 ARALAREPSLLLLDEPLSALDAKLrEELREELKeLQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1024-1236 |
2.28e-20 |
|
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: 89.80 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1024 KIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSII 1103
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1104 LQdpILfsgsirfnldpeckctddrlwEALEIAQLKN-MVKSLPGGldavvteggenfsvgQRQLFCLARAFVRKSSILI 1182
Cdd:cd03214 79 PQ--AL---------------------ELLGLAHLADrPFNELSGG---------------ERQRVLLARALAQEPPILL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 1183 MDEATASIDMATE-NILQKVV-MTAFADRTVVTIAHRV-HTILTADLVIVMKRGNIL 1236
Cdd:cd03214 121 LDEPTSHLDIAHQiELLELLRrLARERGKTVVMVLHDLnLAARYADRVILLKDGRIV 177
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
415-624 |
2.80e-20 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 93.33 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 415 IVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNRYSVAYAAqkpwLLNATVEENITFGSPFNK----Q 490
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYAL----FPHMTVEENVAFGLKMRKvpraE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 491 RYKAVTDACSLqpdIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgiLKFL 570
Cdd:TIGR01187 77 IKPRVLEALRL---VQLEEFADR-----KPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLE--LKTI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1786986074 571 QDD-KRTLVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKdiqtkdvELYEHWKTL 624
Cdd:TIGR01187 147 QEQlGITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPE-------EIYEEPANL 195
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
400-582 |
4.43e-20 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 89.85 E-value: 4.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRnrysVAYAAQKPWLLNA-TVE 478
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR----LAYLGHADGLKPElTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 479 ENITF-----GSPFNKQRYKAVTDACSLQPDIDLlPFGdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSAL 553
Cdd:COG4133 94 ENLRFwaalyGLRADREAIDEALEAVGLAGLADL-PVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 1786986074 554 DI--------HLSDHLMQEGIlkflqddkrtLVLVTH 582
Cdd:COG4133 163 DAagvallaeLIAAHLARGGA----------VLLTTH 189
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
400-606 |
4.82e-20 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 93.24 E-value: 4.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG-EMQTlEGKVHWS--NVNESEPSfeatRRNrysVAYAAQK----PWL 472
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfETPD-SGRILLDgrDVTGLPPE----KRN---VGMVFQDyalfPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 473 lnaTVEENITFG------SPfnKQRYKAVTDACSLqpdIDLLPFGDqteigeRGIN-LSGGQRQRICVARALYQNTNIVF 545
Cdd:COG3842 93 ---TVAENVAFGlrmrgvPK--AEIRARVAELLEL---VGLEGLAD------RYPHqLSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786986074 546 LDDPFSALDIHLSDHLMQEgiLKFLQDD-KRTLVLVTHKlQY--LTHADWIIAMKDGSVLREGT 606
Cdd:COG3842 159 LDEPLSALDAKLREEMREE--LRRLQRElGITFIYVTHD-QEeaLALADRIAVMNDGRIEQVGT 219
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
383-588 |
5.18e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 91.25 E-value: 5.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 383 AIKVTNGYFSWGSGlATLSNIDIRIPTGQLTMIVGQVGCGKSSLL--LAILGEMQT---LEGKVHWSNVNESEPSFEATR 457
Cdd:PRK14258 7 AIKVNNLSFYYDTQ-KILEGVSMEIYQSKVTAIIGPSGCGKSTFLkcLNRMNELESevrVEGRVEFFNQNIYERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 458 RNRySVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDAC--SLQPDIDLLpfgDQTE--IGERGINLSGGQRQRICV 533
Cdd:PRK14258 86 LRR-QVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIveSALKDADLW---DEIKhkIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1786986074 534 ARALYQNTNIVFLDDPFSALDIHLS---DHLMQEGILKflqdDKRTLVLVTHKLQYLT 588
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASmkvESLIQSLRLR----SELTMVIVSHNLHQVS 215
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
402-605 |
6.63e-20 |
|
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: 89.66 E-value: 6.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 402 NIDIRIPtGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNV--NESEPSFEATRRNRySVAYAAQKPWLL-NATVE 478
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlFDSRKKINLPPQQR-KIGLVFQQYALFpHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 479 ENITFGSPFN-----KQRYKAVTDACSLQPdidllpfgdqteIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFSA 552
Cdd:cd03297 94 ENLAFGLKRKrnredRISVDELLDLLGLDH------------LLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1786986074 553 LDIHLSDHLMQEgILKFLQDDKRTLVLVTHKL---QYLthADWIIAMKDGSVLREG 605
Cdd:cd03297 162 LDRALRLQLLPE-LKQIKKNLNIPVIFVTHDLseaEYL--ADRIVVMEDGRLQYIG 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
399-610 |
1.10e-19 |
|
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: 94.20 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 399 TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG---EMQTLEGKVHWSNVNESEPSfEATRRNRysVAYAAQKPW--LL 473
Cdd:COG1123 21 AVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELS-EALRGRR--IGMVFQDPMtqLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 474 NATVEENITFGSpfnkqRYKAVTDACSLQPDIDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSA 552
Cdd:COG1123 98 PVTVGDQIAEAL-----ENLGLSRAEARARVLELLEAVGLERRLDRYPHqLSGGQRQRVAIAMALALDPDLLIADEPTTA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 553 LDIHLSDHLMQegILKFLQDDK-RTLVLVTHKLQY-LTHADWIIAMKDGSVLREGTLKDI 610
Cdd:COG1123 173 LDVTTQAEILD--LLRELQRERgTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
375-606 |
1.22e-19 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 94.78 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 375 RPAETEDIAIKvtNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFE 454
Cdd:PRK10790 334 RPLQSGRIDID--NVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 455 ATRRnrySVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVA 534
Cdd:PRK10790 412 VLRQ---GVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786986074 535 RALYQNTNIVFLDDPFSALDIHlsdhlMQEGILKFLQ--DDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 606
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSG-----TEQAIQQALAavREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGT 557
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1010-1247 |
1.28e-19 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 93.98 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1010 PSQVPEHWPQEGE--IKIHDLCVRYENN---LKPVLKHVKAY------IKPGQKVGICGRTGSGKSSLSLAFFRMVDiFD 1078
Cdd:COG4172 261 PRGDPRPVPPDAPplLEARDLKVWFPIKrglFRRTVGHVKAVdgvsltLRRGETLGLVGESGSGKSTLGLALLRLIP-SE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1079 GKIVIDGIDISKLP---LHTLRSRLSIILQDPilFsGSirfnLDPeckctddRL------WEALEI-------AQLKNMV 1142
Cdd:COG4172 340 GEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--F-GS----LSP-------RMtvgqiiAEGLRVhgpglsaAERRARV 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1143 KSLPG--GLDAVV-----TEggenFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATenilQKVVMTAFA-------- 1207
Cdd:COG4172 406 AEALEevGLDPAArhrypHE----FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV----QAQILDLLRdlqrehgl 477
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1786986074 1208 -------DRTVV-TIAHRvhtiltadlVIVMKRGNILEYDTPESLLAQ 1247
Cdd:COG4172 478 aylfishDLAVVrALAHR---------VMVMKDGKVVEQGPTEQVFDA 516
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
390-582 |
1.58e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 89.92 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 390 YFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSfeATRrnrysvAYAAQK 469
Cdd:COG4525 13 YPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG--ADR------GVVFQK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 470 ----PWLlnaTVEENITFGSPFNK----QRYKAVTDACSLqpdIDLLPFGDQTeIGErginLSGGQRQRICVARALYQNT 541
Cdd:COG4525 85 dallPWL---NVLDNVAFGLRLRGvpkaERRARAEELLAL---VGLADFARRR-IWQ----LSGGMRQRVGIARALAADP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1786986074 542 NIVFLDDPFSALDIhLSDHLMQEGILKFLQDDKRTLVLVTH 582
Cdd:COG4525 154 RFLLMDEPFGALDA-LTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
376-585 |
2.98e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 89.07 E-value: 2.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 376 PAETEDIAIKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLL-----LAILGEMQTLEGKV--HWSNVNE 448
Cdd:PRK14243 3 TLNGTETVLRTENLNVYYGSFLA-VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrLNDLIPGFRVEGKVtfHGKNLYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 449 SEPSFEATRRNrysVAYAAQKPWLLNATVEENITFGSPFNKqrYKavtdacslqpdidllpfGDQTEIGER--------- 519
Cdd:PRK14243 82 PDVDPVEVRRR---IGMVFQKPNPFPKSIYDNIAYGARING--YK-----------------GDMDELVERslrqaalwd 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1786986074 520 ---------GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDiHLSDhLMQEGILKFLQDDkRTLVLVTHKLQ 585
Cdd:PRK14243 140 evkdklkqsGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALD-PIST-LRIEELMHELKEQ-YTIIIVTHNMQ 211
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
394-615 |
3.43e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.89 E-value: 3.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 394 GSGLATLS-NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhWsnvnesepsFEATRRNRYSVAYAAQKPWL 472
Cdd:PRK10253 16 GYGKYTVAeNLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-W---------LDGEHIQHYASKEVARRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 473 L--NATVEENITFGSPFNKQRYKAvtdacslQP--------DIDLLPFGDQ----TEIGERGIN-LSGGQRQRICVARAL 537
Cdd:PRK10253 86 LaqNATTPGDITVQELVARGRYPH-------QPlftrwrkeDEEAVTKAMQatgiTHLADQSVDtLSGGQRQRAWIAMVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 538 YQNTNIVFLDDPFSALDIhlsDHlmQEGILKFLQDDKR----TLVLVTHKL----QYLTHadwIIAMKDGSVLREGTLKD 609
Cdd:PRK10253 159 AQETAIMLLDEPTTWLDI---SH--QIDLLELLSELNRekgyTLAAVLHDLnqacRYASH---LIALREGKIVAQGAPKE 230
|
....*.
gi 1786986074 610 IQTKDV 615
Cdd:PRK10253 231 IVTAEL 236
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
384-601 |
3.62e-19 |
|
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: 87.31 E-value: 3.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS--NVNESEPSfeatRRNry 461
Cdd:cd03301 1 VELENVTKRFGNVTA-LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrDVTDLPPK----DRD-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 462 sVAYAAQKPWLL-NATVEENITFGSPFNKQRY----KAVTDACSLQpDIDLLpfgdqteIGERGINLSGGQRQRICVARA 536
Cdd:cd03301 74 -IAMVFQNYALYpHMTVYDNIAFGLKLRKVPKdeidERVREVAELL-QIEHL-------LDRKPKQLSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1786986074 537 LYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTH-KLQYLTHADWIIAMKDGSV 601
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQMRAE-LKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
402-638 |
4.44e-19 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 92.64 E-value: 4.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 402 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRnrySVAYAAQKPWLLNATVEENI 481
Cdd:TIGR01192 353 DVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRK---SIATVFQDAGLFNRSIRENI 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 482 TFG--SPFNKQRYKAvTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSD 559
Cdd:TIGR01192 430 RLGreGATDEEVYEA-AKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVE-TE 507
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1786986074 560 HLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEHWKTLMNRQDQELEKDMEA 638
Cdd:TIGR01192 508 ARVKNAIDALRKN--RTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRRSGLLTNQPATKPLRK 584
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1023-1247 |
5.45e-19 |
|
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: 87.64 E-value: 5.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNLK--PVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLP---L 1093
Cdd:cd03258 2 IELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTL----IRCINGLErptsGSVLVDGTDLTLLSgkeL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1094 HTLRSRLSIILQDPILFS-----GSIRFNLD---PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQR 1165
Cdd:cd03258 78 RKARRRIGMIFQHFNLLSsrtvfENVALPLEiagVPKAEIEERVLELLELVGLEDKADAYPAQL-----------SGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1166 QLFCLARAFVRKSSILIMDEATASIDMA-TENILQ--KVVMTAFaDRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTP 1241
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPEtTQSILAllRDINREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTV 225
|
....*.
gi 1786986074 1242 ESLLAQ 1247
Cdd:cd03258 226 EEVFAN 231
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1023-1235 |
5.61e-19 |
|
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: 87.16 E-value: 5.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYEN--NLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHTL 1096
Cdd:cd03255 1 IELKNLSKTYGGggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTL----LNILGGLDrptsGEVRVDGTDISKLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1097 ----RSRLSIILQD---------------PILFSGSIRfnldPECKctdDRLWEALEIAQLKNMVKSLPGGLdavvtegg 1157
Cdd:cd03255 77 aafrRRHIGFVFQSfnllpdltalenvelPLLLAGVPK----KERR---ERAEELLERVGLGDRLNHYPSEL-------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1158 enfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHRVHTILTADLVIVMKRG 1233
Cdd:cd03255 142 ---SGGQQQRVAIARALANDPKIILADEPTGNLDSETGkevmELLRE--LNKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
..
gi 1786986074 1234 NI 1235
Cdd:cd03255 217 KI 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
400-610 |
9.64e-19 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 86.87 E-value: 9.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG-EMQTlEGKVHWSNVNESEPSFEATRRNRYSVAYAAQKPWLLNA-TV 477
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGlERPT-SGSVLVDGTDLTLLSGKELRKARRRIGMIFQHFNLLSSrTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 478 EENITF-----GSPfNKQRYKAVTDacslqpdidLLPFGDQTEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFS 551
Cdd:cd03258 100 FENVALpleiaGVP-KAEIEERVLE---------LLELVGLEDKADAYPaQLSGGQKQRVGIARALANNPKVLLCDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786986074 552 ALDIHLSDhlmqeGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 610
Cdd:cd03258 170 ALDPETTQ-----SILALLRDINRelglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
379-610 |
1.06e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 87.74 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 379 TEDIAIKVTNGYFSWGSG-LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATR 457
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 458 RNrysVAYAAQKP--WLLNATVEENITFG---SPFNKQRYKAVTDACSLQPDI-DLLPFGDQteigergiNLSGGQRQRI 531
Cdd:PRK13632 83 KK---IGIIFQNPdnQFIGATVEDDIAFGlenKKVPPKKMKDIIDDLAKKVGMeDYLDKEPQ--------NLSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 532 CVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDD-KRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDI 610
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIKK--IMVDLRKTrKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1038-1246 |
1.53e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 87.35 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1038 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGI---DISKLPlhTLRSRLSIILQDP-ILFSG- 1112
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgDFSKLQ--GIRKLVGIVFQNPeTQFVGr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1113 SIRFNL--DPECKCTddrlwEALEIAQLKNMVKSlPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASI 1190
Cdd:PRK13644 94 TVEEDLafGPENLCL-----PPIEIRKRVDRALA-EIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 1191 DMAT-ENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLA 1246
Cdd:PRK13644 168 DPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1023-1237 |
2.10e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.12 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIF-----DGKIVIDGIDISKLPLHTLR 1097
Cdd:PRK14247 4 IEIRDLKVSFGQ--VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1098 SRLSIILQ--DPI----LFSG---SIRFN-LDPECKCTDDRLWEALEIAQLKNMVKSLpggLDAVVTEggenFSVGQRQL 1167
Cdd:PRK14247 82 RRVQMVFQipNPIpnlsIFENvalGLKLNrLVKSKKELQERVRWALEKAQLWDEVKDR---LDAPAGK----LSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1786986074 1168 FCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAH------RVhtiltADLVIVMKRGNILE 1237
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVE 225
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
375-585 |
2.78e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 85.86 E-value: 2.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 375 RPAETEDIAIKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI-----LGEMQTLEGKVHWSNVNES 449
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQA-LKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndLIPGARVEGEILLDGEDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 450 EPSFEAT--RRNrysVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDacslqpdidllpfgdqtEIGER-------- 519
Cdd:COG1117 82 DPDVDVVelRRR---VGMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSELD-----------------EIVEEslrkaalw 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1786986074 520 ----------GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDH---LMQEgiLKflqdDKRTLVLVTHKLQ 585
Cdd:COG1117 142 devkdrlkksALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKieeLILE--LK----KDYTIVIVTHNMQ 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1023-1233 |
2.86e-18 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 83.78 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYenNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHT--L 1096
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTL----LRCIAGLEepdsGSILIDGEDLTDLEDELppL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1097 RSRLSIILQDPILFSGsirfnldpeckctddrlweaLEIAQlkNMVKSLPGGldavvteggenfsvgQRQLFCLARAFVR 1176
Cdd:cd03229 75 RRRIGMVFQDFALFPH--------------------LTVLE--NIALGLSGG---------------QQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1177 KSSILIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTILT-ADLVIVMKRG 1233
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
396-585 |
2.92e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.91 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 396 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEatrrnRYSV-AYAAQKPWLln 474
Cdd:PRK11248 13 GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE-----RGVVfQNEGLLPWR-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 475 aTVEENITFGspfnkQRYKAVTDACSLQPDIDLLPFGDQTEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFSAL 553
Cdd:PRK11248 86 -NVQDNVAFG-----LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190
....*....|....*....|....*....|..
gi 1786986074 554 DIHLSDHlMQEGILKFLQDDKRTLVLVTHKLQ 585
Cdd:PRK11248 160 DAFTREQ-MQTLLLKLWQETGKQVLLITHDIE 190
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
400-596 |
3.07e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 85.15 E-value: 3.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNrysVAYAAQKPWLLNATVEE 479
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQ---VSYCAQTPTLFGDTVYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 480 NITFGSPFNKQRykavtdacsLQPDI---DLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDI 555
Cdd:PRK10247 100 NLIFPWQIRNQQ---------PDPAIfldDLERFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1786986074 556 HlSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAM 596
Cdd:PRK10247 171 S-NKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
384-624 |
3.10e-18 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 85.37 E-value: 3.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESepSFEATRRNRYSV 463
Cdd:cd03300 1 IELENVSKFYGGFVA-LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT--NLPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 464 --AYAaqkpwLL-NATVEENITFG---SPFNKQRYKA-VTDACSLqpdIDLLPFGDqteigeRGIN-LSGGQRQRICVAR 535
Cdd:cd03300 78 fqNYA-----LFpHLTVFENIAFGlrlKKLPKAEIKErVAEALDL---VQLEGYAN------RKPSqLSGGQQQRVAIAR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 536 ALYQNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDD-KRTLVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKDIqtk 613
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLKLRKDMQLE--LKRLQKElGITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEI--- 218
|
250
....*....|.
gi 1786986074 614 dvelYEHWKTL 624
Cdd:cd03300 219 ----YEEPANR 225
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1038-1233 |
4.34e-18 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 84.69 E-value: 4.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1038 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR----LSIILQDPILFSGS 1113
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1114 IRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDM- 1192
Cdd:cd03290 95 VEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIh 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1786986074 1193 ATENILQKVVMTAFAD--RTVVTIAHRVHTILTADLVIVMKRG 1233
Cdd:cd03290 175 LSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
383-610 |
6.30e-18 |
|
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: 84.70 E-value: 6.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 383 AIKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhWSNvNESEPSFEATRRNrys 462
Cdd:cd03296 2 SIEVRNVSKRFGDFVA-LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTI-LFG-GEDATDVPVQERN--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 463 VAYAAQKPWLL-NATVEENITFGSPFNKQRYKAVTDACSLQPDiDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQN 540
Cdd:cd03296 76 VGFVFQHYALFrHMTVFDNVAFGLRVKPRSERPPEAEIRAKVH-ELLKLVQLDWLADRYPAqLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 541 TNIVFLDDPFSALDIHLSDHLmqEGILKFLQDDKR-TLVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKDI 610
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKEL--RRWLRRLHDELHvTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
404-605 |
6.93e-18 |
|
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: 83.70 E-value: 6.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 404 DIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV--HWSNVNESEPSfeatrrnRYSVAYAAQKPWLL-NATVEEN 480
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVliNGVDVTAAPPA-------DRPVSMLFQENNLFaHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 481 ITFG-SP---FNKQRYKAVTDAcslqpdidLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 556
Cdd:cd03298 91 VGLGlSPglkLTAEDRQAIEVA--------LARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1786986074 557 LSDHlMQEGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREG 605
Cdd:cd03298 163 LRAE-MLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1023-1249 |
7.25e-18 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 84.37 E-value: 7.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidiskLPLHTLRSRLSI 1102
Cdd:COG1121 7 IELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG-----KPPRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1103 ILQD-------PIL--------FSGSIRF--NLDPECKctdDRLWEALE---IAQLKN-MVKSLpggldavvteggenfS 1161
Cdd:COG1121 80 VPQRaevdwdfPITvrdvvlmgRYGRRGLfrRPSRADR---EAVDEALErvgLEDLADrPIGEL---------------S 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1162 VGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVHTILT-ADLVIVMKRGnILEYD 1239
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRG-LVAHG 220
|
250
....*....|
gi 1786986074 1240 TPESLLAQEN 1249
Cdd:COG1121 221 PPEEVLTPEN 230
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
400-606 |
8.12e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 88.72 E-value: 8.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSL--LLAILGEMQtlEGKVHWSNVNESEPSFEATRRnrySVAYAAQKPWLLNATV 477
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLarLLFRFYDVT--SGRILIDGQDIRDVTQASLRA---AIGIVPQDTVLFNDTI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 478 EENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 556
Cdd:COG5265 449 AYNIAYGRPdASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSR 528
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1786986074 557 lSDHLMQEGiLKFLQDDKRTLVlVTHKLQYLTHADWIIAMKDGSVLREGT 606
Cdd:COG5265 529 -TERAIQAA-LREVARGRTTLV-IAHRLSTIVDADEILVLEAGRIVERGT 575
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
399-633 |
8.76e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 84.44 E-value: 8.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 399 TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI--LGEMQ---TLEGKVHWSNVNESEPSFEaTRRNRYSVAYAAQKPWLL 473
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNpevTITGSIVYNGHNIYSPRTD-TVDLRKEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 474 NATVEENITFGSPFNKQRYKAVTDAcSLQPDIDLLPFGDQTE--IGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 551
Cdd:PRK14239 99 PMSIYENVVYGLRLKGIKDKQVLDE-AVEKSLKGASIWDEVKdrLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 552 ALDiHLSDHLMQEGILKFlqDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIqtkdvelyehwktLMNRQDQ 630
Cdd:PRK14239 178 ALD-PISAGKIEETLLGL--KDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQM-------------FMNPKHK 241
|
...
gi 1786986074 631 ELE 633
Cdd:PRK14239 242 ETE 244
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
400-610 |
1.02e-17 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 83.92 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEatRRNrysVAYAAQKPWLL-NATVE 478
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRD---ISYVPQNYALFpHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 479 ENITFGspFNKQRYKAVTDACSLQpdidllpfgdqtEIGER-GIN---------LSGGQRQRICVARALYQNTNIVFLDD 548
Cdd:cd03299 90 KNIAYG--LKKRKVDKKEIERKVL------------EIAEMlGIDhllnrkpetLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786986074 549 PFSALDIHLSDHLMQEgiLKFLQDDKRTLVL-VTHKL-QYLTHADWIIAMKDGSVLREGTLKDI 610
Cdd:cd03299 156 PFSALDVRTKEKLREE--LKKIRKEFGVTVLhVTHDFeEAWALADKVAIMLNGKLIQVGKPEEV 217
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
402-614 |
1.17e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 83.65 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 402 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNesepsfeatrrnrYSVAYAAQKP----------- 470
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD-------------LTALPPAERPvsmlfqennlf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 471 WLLnaTVEENITFG-------SPFNKQRYKAVTDACSLQPDIDLLPfgDQteigerginLSGGQRQRICVARALYQNTNI 543
Cdd:COG3840 84 PHL--TVAQNIGLGlrpglklTAEQRAQVEQALERVGLAGLLDRLP--GQ---------LSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 544 VFLDDPFSALDIHLSDHLMQegILKFLQDD-KRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKD 614
Cdd:COG3840 151 LLLDEPFSALDPALRQEMLD--LVDELCRErGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1018-1217 |
1.18e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 88.33 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1018 PQEGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVI-DGIDISKLP 1092
Cdd:COG4178 358 SEDGALALEDLTLRTPDG-RPLLEDLSLSLKPGERLLITGPSGSGKSTL----LRAIaglwPYGSGRIARpAGARVLFLP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1093 lhtlrsrlsiilQDPILFSGSIRFNL---DPECKCTDDRLWEALEIAQLKNmvksLPGGLDaVVTEGGENFSVGQRQLFC 1169
Cdd:COG4178 433 ------------QRPYLPLGTLREALlypATAEAFSDAELREALEAVGLGH----LAERLD-EEADWDQVLSLGEQQRLA 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1786986074 1170 LARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR 1217
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
391-606 |
1.27e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 88.09 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 391 FSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKVHWSNVNESEPSFEATRRNrysVAYAAQK 469
Cdd:PRK13657 342 FSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI-NLLQRVFDpQSGRILIDGTDIRTVTRASLRRN---IAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 470 PWLLNATVEENITFGSP--FNKQRYKAVTDACSLqpD-IDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFL 546
Cdd:PRK13657 418 AGLFNRSIEDNIRVGRPdaTDEEMRAAAERAQAH--DfIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILIL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 547 DDPFSALDIHLSDHLmQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 606
Cdd:PRK13657 496 DEATSALDVETEAKV-KAALDELMKG--RTTFIIAHRLSTVRNADRILVFDNGRVVESGS 552
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
403-620 |
1.44e-17 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 85.93 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 403 IDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNV--NESEPSFEATRRNRySVAYAAQKPWLL-NATVEE 479
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlFDSRKGIFLPPEKR-RIGYVFQEARLFpHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 480 NITFG-----SPFNKQRYKAVTDACSLQPDIDLLPfGDqteigerginLSGGQRQRICVARALYQNTNIVFLDDPFSALD 554
Cdd:TIGR02142 95 NLRYGmkrarPSERRISFERVIELLGIGHLLGRLP-GR----------LSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 555 IHLSDHlmqegILKFLQDDKRTL----VLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQ-TKDVELYEH 620
Cdd:TIGR02142 164 DPRKYE-----ILPYLERLHAEFgipiLYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWaSPDLPWLAR 230
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
393-583 |
1.56e-17 |
|
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: 83.09 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 393 WGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ---TLEGKVHwsnVNESEPSFEATRrnrYSVAYAAQK 469
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQIL---FNGQPRKPDQFQ---KCVAYVRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 470 PWLL-NATVEENITFGSPF-----NKQRYKAVTDACSLQPDIDLLPFGdqteiGERGINLSGGQRQRICVARALYQNTNI 543
Cdd:cd03234 90 DILLpGLTVRETLTYTAILrlprkSSDAIRKKRVEDVLLRDLALTRIG-----GNLVKGISGGERRRVSIAVQLLWDPKV 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1786986074 544 VFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHK 583
Cdd:cd03234 165 LILDEPTSGLDSFTALNLVS--TLSQLARRNRIVILTIHQ 202
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
383-605 |
1.82e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 84.16 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 383 AIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnvneSEPSFEATRRNRys 462
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIL----GQPTRQALQKNL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 463 VAYAAQKP---WLLNATVEENITFGS---------PFNKQRyKAVTDACSlqpDIDLLPFgDQTEIGErginLSGGQRQR 530
Cdd:PRK15056 80 VAYVPQSEevdWSFPVLVEDVVMMGRyghmgwlrrAKKRDR-QIVTAALA---RVDMVEF-RHRQIGE----LSGGQKKR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1786986074 531 ICVARALYQNTNIVFLDDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKdGSVLREG 605
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARII--SLLRELRDEGKTMLVSTHNLGSVTEfCDYTVMVK-GTVLASG 223
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1023-1235 |
2.05e-17 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 81.29 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRM----VDIFDGKIVIDGIDISKLPlHTLRS 1098
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTL----IKIilglLKPDSGEIKVLGKDIKKEP-EEVKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1099 RLSIILQDPILFSG-SIRFNLDpeckctddrlwealeiaqlknmvkslpggldavvteggenFSVGQRQLFCLARAFVRK 1177
Cdd:cd03230 74 RIGYLPEEPSLYENlTVRENLK----------------------------------------LSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1178 SSILIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVHTILT-ADLVIVMKRGNI 1235
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
384-614 |
2.29e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.05 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVN-ESEPSFEATRRnrys 462
Cdd:PRK09536 4 IDVSDLSVEFG-DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDvEALSARAASRR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 463 VAYAAQKPWL-LNATVEENITFGSPFNKQRYKAVTDACSLQPDiDLLPFGDQTEIGERGI-NLSGGQRQRICVARALYQN 540
Cdd:PRK09536 79 VASVPQDTSLsFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVE-RAMERTGVAQFADRPVtSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1786986074 541 TNIVFLDDPFSALDIHlsdHLMQE-GILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDIQTKD 614
Cdd:PRK09536 158 TPVLLLDEPTASLDIN---HQVRTlELVRRLVDDGKTAVAAIHDLDLAArYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1023-1237 |
2.94e-17 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 82.40 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYE--NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAffrMVDIFD-GKIVIDGIDISKLP---LH 1094
Cdd:COG1136 5 LELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLlnILG---GLDRPTsGEVLIDGQDISSLSereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1095 TLRSR-LSIILQDpilfsgsirFNLDPE-----------------CKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteg 1156
Cdd:COG1136 82 RLRRRhIGFVFQF---------FNLLPEltalenvalplllagvsRKERRERARELLERVGLGDRLDHRPSQL------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1157 genfSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT-ENILQkvVMTAFAD---RTVVTIAHRVHTILTADLVIVMKR 1232
Cdd:COG1136 146 ----SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgEEVLE--LLRELNRelgTTIVMVTHDPELAARADRVIRLRD 219
|
....*
gi 1786986074 1233 GNILE 1237
Cdd:COG1136 220 GRIVS 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1023-1249 |
3.39e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 82.11 E-value: 3.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYEN-----NLKpvlkhvkayIKPGQKVGICGRTGSGKSSLS--LAFFRMVDifDGKIVIDGIDISKLPLHT 1095
Cdd:COG3840 2 LRLDDLTYRYGDfplrfDLT---------IAAGERVAILGPSGAGKSTLLnlIAGFLPPD--SGRILWNGQDLTALPPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1096 lrsR-LSIILQDPILFSG-SIRFN----LDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQ 1166
Cdd:COG3840 71 ---RpVSMLFQENNLFPHlTVAQNiglgLRPGLKLTAEqraQVEQALERVGLAGLLDRLPGQL-----------SGGQRQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1167 LFCLARAFVRKSSILIMDEATASIDMA-TENILQKVV-MTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPES 1243
Cdd:COG3840 137 RVALARCLVRKRPILLLDEPFSALDPAlRQEMLDLVDeLCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAA 216
|
....*.
gi 1786986074 1244 LLAQEN 1249
Cdd:COG3840 217 LLDGEP 222
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
400-630 |
4.25e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 82.75 E-value: 4.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEM---QTLEGKVHW--SNVNESEPSFEATRRNRYSVAYAAQKPWLLN 474
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELlgRTVQREGRLARDIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 475 A-TVEENITFG---------------SPFNKQR-YKAVTDacslqpdIDLLPFGDQteigeRGINLSGGQRQRICVARAL 537
Cdd:PRK09984 100 RlSVLENVLIGalgstpfwrtcfswfTREQKQRaLQALTR-------VGMVHFAHQ-----RVSTLSGGQQQRVAIARAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 538 YQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDDKRTLVLVTHKLQY-LTHADWIIAMKDGSVLREGTlkdIQTKDVE 616
Cdd:PRK09984 168 MQQAKVILADEPIASLDPE-SARIVMDTLRDINQNDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGS---SQQFDNE 243
|
250
....*....|....
gi 1786986074 617 LYEHWKTLMNRQDQ 630
Cdd:PRK09984 244 RFDHLYRSINRVEE 257
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
400-620 |
4.80e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.15 E-value: 4.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWsnvneSEPSFEATRRN------RYSVAYAAQKP--W 471
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-----GERVITAGKKNkklkplRKKVGIVFQFPehQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 472 LLNATVEENITFGsPFN--------KQRYKAVTDACSLQPDI-DLLPFgdqteigergiNLSGGQRQRICVARALYQNTN 542
Cdd:PRK13634 98 LFEETVEKDICFG-PMNfgvseedaKQKAREMIELVGLPEELlARSPF-----------ELSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1786986074 543 IVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKDVELYEH 620
Cdd:PRK13634 166 VLVLDEPTAGLDPKGRKEMM-EMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADPDELEAI 243
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
389-604 |
4.85e-17 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 82.55 E-value: 4.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 389 GYFSWGSG-LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNRYSVAYAA 467
Cdd:TIGR02769 15 GGLFGAKQrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRRDVQLVF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 468 QK-PWLLNA--TVEENItfGSPF----------NKQRYKAVTDACSLQPDI-DLLPfgdqteigergINLSGGQRQRICV 533
Cdd:TIGR02769 95 QDsPSAVNPrmTVRQII--GEPLrhltsldeseQKARIAELLDMVGLRSEDaDKLP-----------RQLSGGQLQRINI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1786986074 534 ARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMKDGSVLRE 604
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVL-----QAVILELLRKLQQafgtAYLFITHDLRLVQSfCQRVAVMDKGQIVEE 232
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1023-1244 |
5.01e-17 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 81.85 E-value: 5.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSR 1099
Cdd:cd03256 1 IEVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1100 LSIILQDpilfsgsirFNLDPECKCTDDRLWEALeiAQlKNMVKSLPG-----------------GLDAVVTEGGENFSV 1162
Cdd:cd03256 80 IGMIFQQ---------FNLIERLSVLENVLSGRL--GR-RSTWRSLFGlfpkeekqralaalervGLLDKAYQRADQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1163 GQRQLFCLARAFVRKSSILIMDEATASIDMATENIlqkvVMTAFAD------RTVVTIAHRVHTILT-ADLVIVMKRGNI 1235
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQ----VMDLLKRinreegITVIVSLHQVDLAREyADRIVGLKDGRI 223
|
....*....
gi 1786986074 1236 LEYDTPESL 1244
Cdd:cd03256 224 VFDGPPAEL 232
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
400-601 |
6.20e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.03 E-value: 6.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnVNESEPSFEATRRNRYSVAYAAQKPWllnATVEE 479
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL----LAGTAPLAEAREDTRLMFQDARLLPW---KKVID 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 480 NITFGSPFN-KQRYKAVTDACSLQPdidllpfgdqtEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLS 558
Cdd:PRK11247 101 NVGLGLKGQwRDAALQALAAVGLAD-----------RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA-LT 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1786986074 559 DHLMQEGILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSV 601
Cdd:PRK11247 169 RIEMQDLIESLWQQHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
402-612 |
7.32e-17 |
|
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: 83.61 E-value: 7.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 402 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH-----WsnVNESEPSFEATRRNRysVAYAAQK----PWL 472
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevL--QDSARGIFLPPHRRR--IGYVFQEarlfPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 473 lnaTVEENITFGSPFNKQRYKAVtdacslQPD--IDLLpfgdqtEIG---ERGI-NLSGGQRQRICVARALYQNTNIVFL 546
Cdd:COG4148 93 ---SVRGNLLYGRKRAPRAERRI------SFDevVELL------GIGhllDRRPaTLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1786986074 547 DDPFSALDIHLSDHLMQegILKFLQDDKRTLVL-VTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQT 612
Cdd:COG4148 158 DEPLAALDLARKAEILP--YLERLRDELDIPILyVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLS 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
384-617 |
7.49e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 82.34 E-value: 7.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNRYSV 463
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 464 AYAAQKPWLLNATVEENITFGsPFNkqrykavtdACslQPDIDLLPFGDQTeIGERGI---------NLSGGQRQRICVA 534
Cdd:PRK13644 82 VFQNPETQFVGRTVEEDLAFG-PEN---------LC--LPPIEIRKRVDRA-LAEIGLekyrhrspkTLSGGQGQCVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 535 RALYQNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT----LKDI 610
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLER--IKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEpenvLSDV 226
|
....*..
gi 1786986074 611 QTKDVEL 617
Cdd:PRK13644 227 SLQTLGL 233
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
392-603 |
8.34e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 85.93 E-value: 8.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 392 SWGSG---LATLSNIDIRIPTGQLTMIVGQVGCGKSSLL--LAILGEMQTLEGKVHWSNVNESEP-SFEATRRNRYSVAY 465
Cdd:PRK10535 13 SYPSGeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMniLGCLDKPTSGTYRVAGQDVATLDAdALAQLRREHFGFIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 466 aaQKPWLL-NATVEENITF-----GSPFNKQRYKAVTDacslqpdidLLPFGDQTEIGERGINLSGGQRQRICVARALYQ 539
Cdd:PRK10535 93 --QRYHLLsHLTAAQNVEVpavyaGLERKQRLLRAQEL---------LQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786986074 540 NTNIVFLDDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLR 603
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVM--AILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
400-610 |
1.08e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 83.46 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESepSFEATRRNRYSV--AYAaqkpwLL-NAT 476
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVNTVfqSYA-----LFpHMT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 477 VEENITFG-----SPfNKQRYKAVTDACSLqpdIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPFS 551
Cdd:PRK09452 103 VFENVAFGlrmqkTP-AAEITPRVMEALRM---VQLEEFAQR-----KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786986074 552 ALDIHLSDHLMQEgiLKFLQddkRTL----VLVTH-KLQYLTHADWIIAMKDGSVLREGTLKDI 610
Cdd:PRK09452 174 ALDYKLRKQMQNE--LKALQ---RKLgitfVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1023-1249 |
1.09e-16 |
|
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: 80.62 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFR-MVDIF---DGKIVIDGIDISKL---PLHT 1095
Cdd:cd03261 1 IELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTL----LRlIVGLLrpdSGEVLIDGEDISGLseaELYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1096 LRSRLSIILQDPILFSG-----SIRFNLDPECKCTDdrlWEALEIAQLK-NMVkSLPGGLDAVVTEggenFSVGQRQLFC 1169
Cdd:cd03261 75 LRRRMGMLFQSGALFDSltvfeNVAFPLREHTRLSE---EEIREIVLEKlEAV-GLRGAEDLYPAE----LSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1170 LARAFVRKSSILIMDEATASIDMATENILQKVVMT--AFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLA 1246
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFaIADRIAVLYDGKIVAEGTPEELRA 226
|
...
gi 1786986074 1247 QEN 1249
Cdd:cd03261 227 SDD 229
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1023-1232 |
1.13e-16 |
|
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: 80.21 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENN--LKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGidiskLPLHTL 1096
Cdd:cd03293 1 LEVRNVSKTYGGGggAVTALEDISLSVEEGEFVALVGPSGCGKSTL----LRIIAGLErptsGEVLVDG-----EPVTGP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1097 RSRLSIILQDPILFS-GSIRFN--LDPECKCTDDRLW-----EALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1168
Cdd:cd03293 72 GPDRGYVFQQDALLPwLTVLDNvaLGLELQGVPKAEAreraeELLELVGLSGFENAYPHQL-----------SGGMRQRV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 1169 CLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVH-TILTADLVIVMKR 1232
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDeAVFLADRVVVLSA 207
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1023-1259 |
1.21e-16 |
|
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: 80.81 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYeNNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1102
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1103 ILQDPILFSG-SIRFNLD--------PECKcTDDRLWEALEIAQL--KNMVKSLPGGLdavvteggenfSVGQRQLFCLA 1171
Cdd:cd03295 80 VIQQIGLFPHmTVEENIAlvpkllkwPKEK-IRERADELLALVGLdpAEFADRYPHEL-----------SGGQQQRVGVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1172 RAFVRKSSILIMDEATASIDMATENILQKvvmtAFAD------RTVVTIAHRV-HTILTADLVIVMKRGNILEYDTPESL 1244
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQE----EFKRlqqelgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
250
....*....|....*.
gi 1786986074 1245 LA-QENGVFASFVRAD 1259
Cdd:cd03295 224 LRsPANDFVAEFVGAD 239
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
384-601 |
1.25e-16 |
|
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: 80.14 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYfswGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNRYSV 463
Cdd:cd03292 4 INVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 464 AYAAQKPWLL-NATVEENITF-----GSPFN--KQRYKAVTDACSLQPDIDLLPFGdqteigerginLSGGQRQRICVAR 535
Cdd:cd03292 81 GVVFQDFRLLpDRNVYENVAFalevtGVPPReiRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 536 ALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTH-KLQYLTHADWIIAMKDGSV 601
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMN--LLKKINKAGTTVVVATHaKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1019-1247 |
1.49e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 81.60 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1019 QEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS 1098
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1099 RLSIILQDPI-LFSGS-----IRFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 1169
Cdd:PRK13635 82 QVGMVFQNPDnQFVGAtvqddVAFGLENIGVPREEmveRVDQALRQVGMEDFLNREPHRL-----------SGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1170 LARAFVRKSSILIMDEATASID-MATENILQKV-VMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1247
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDpRGRREVLETVrQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
396-566 |
1.66e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.53 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 396 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFeatrrnRYSVAYA----AQKPW 471
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV------AEACHYLghrnAMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 472 LlnaTVEENITFGSPFNKQRYKAVTDACS---LQPDIDLlPFGdqteigergiNLSGGQRQRICVARALYQNTNIVFLDD 548
Cdd:PRK13539 88 L---TVAENLEFWAAFLGGEELDIAAALEavgLAPLAHL-PFG----------YLSAGQKRRVALARLLVSNRPIWILDE 153
|
170 180
....*....|....*....|....*.
gi 1786986074 549 PFSALDIH--------LSDHLMQEGI 566
Cdd:PRK13539 154 PTAALDAAavalfaelIRAHLAQGGI 179
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
400-610 |
1.73e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 81.36 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNV---NESEPSFEATRRNRYSVAYAAQKPWLLNAT 476
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDItitHKTKDKYIRPVRKRIGMVFQFPESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 477 VEENITFGSP-FNKQRYKAVTDACSLqpdidLLPFGDQTEIGERG-INLSGGQRQRICVARALYQNTNIVFLDDPFSALD 554
Cdd:PRK13646 103 VEREIIFGPKnFKMNLDEVKNYAHRL-----LMDLGFSRDVMSQSpFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1786986074 555 IHLSDHLMQegILKFLQ-DDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDI 610
Cdd:PRK13646 178 PQSKRQVMR--LLKSLQtDENKTIILVSHDMNEVArYADEVIVMKEGSIVSQTSPKEL 233
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
400-602 |
1.75e-16 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 80.72 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEaTRRNRYSVAYaaQKPWLLNATVEE 479
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLH-TLRSRLSIIL--QDPILFSGSIRF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 480 NITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLSD 559
Cdd:cd03288 114 NLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDM-ATE 192
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1786986074 560 HLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVL 602
Cdd:cd03288 193 NILQKVVMTAFAD--RTVVTIAHRVSTILDADLVLVLSRGILV 233
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
384-601 |
1.89e-16 |
|
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: 78.24 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnvnesepsfeatrrnrysv 463
Cdd:cd03216 1 LELRGITKRFGGVKA-LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 464 ayaaqkpwllnatvEENITFGSPFNKQRykavtdacslqpdidllpfgdqteigeRGIN----LSGGQRQRICVARALYQ 539
Cdd:cd03216 61 --------------GKEVSFASPRDARR---------------------------AGIAmvyqLSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 540 NTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQ-YLTHADWIIAMKDGSV 601
Cdd:cd03216 100 NARLLILDEPTAALTPAEVERLFK--VIRRLRAQGVAVIFISHRLDeVFEIADRVTVLRDGRV 160
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
381-605 |
1.96e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 80.94 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 381 DIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnVNESEPSFEATRRNR 460
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVK---VMGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 461 YSVAYAAQKP--WLLNATVEENITFGsPFN--------KQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQR 530
Cdd:PRK13647 79 SKVGLVFQDPddQVFSSTVWDDVAFG-PVNmgldkdevERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1786986074 531 ICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQY-LTHADWIIAMKDGSVLREG 605
Cdd:PRK13647 147 VAIAGVLAMDPDVIVLDEPMAYLDPRGQETLME--ILDRLHNQGKTVIVATHDVDLaAEWADQVIVLKEGRVLAEG 220
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1040-1257 |
2.33e-16 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 80.77 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1040 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRS-RLSIILQDPILFS---- 1111
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRkKISMVFQSFALLPhrtv 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1112 -GSIRFNLDPECKCTDDRL---WEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEAT 1187
Cdd:cd03294 120 lENVAFGLEVQGVPRAEREeraAEALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786986074 1188 ASIDMATENILQKVVMTAFAD--RTVVTIAHRV-HTILTADLVIVMKRGNILEYDTPESLLAQ-ENGVFASFVR 1257
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAElqKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILTNpANDYVREFFR 262
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1023-1246 |
2.96e-16 |
|
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: 79.02 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTlRSRLSI 1102
Cdd:cd03224 1 LEVENLNAGYGKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1103 IL--QDPILFSG-SIRFNLD-PECKCTDDRLWEALEIA-----QLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARA 1173
Cdd:cd03224 78 GYvpEGRRIFPElTVEENLLlGAYARRRAKRKARLERVyelfpRLKERRKQLAGTL-----------SGGEQQMLAIARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1786986074 1174 FVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLA 1246
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLApKIVEEIFEAIRELRDEGVTILLVEQNARFALeIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1050-1235 |
3.60e-16 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 78.69 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1050 GQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPlhTLRSRLSIILQDPILFS-----GSIRFNLDP 1120
Cdd:cd03298 24 GEITAIVGPSGSGKSTL----LNLIAGFEtpqsGRVLINGVDVTAAP--PADRPVSMLFQENNLFAhltveQNVGLGLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1121 ECKCT-DDRlwEALEIAQ----LKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 1195
Cdd:cd03298 98 GLKLTaEDR--QAIEVALarvgLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1786986074 1196 NILQKVVMTAFADR--TVVTIAHRVHTILT-ADLVIVMKRGNI 1235
Cdd:cd03298 165 AEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1024-1235 |
4.46e-16 |
|
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: 78.34 E-value: 4.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1024 KIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidiskLPLHTLRSRL--- 1100
Cdd:cd03235 1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIgyv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1101 ---SIILQD-PILFSGSIRFNLDPEC------KCTD-DRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 1169
Cdd:cd03235 74 pqrRSIDRDfPISVRDVVLMGLYGHKglfrrlSKADkAKVDEALERVGLSELADRQIGEL-----------SGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1786986074 1170 LARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTILT-ADLVIVMKRGNI 1235
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEyFDRVLLLNRTVV 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1023-1256 |
4.52e-16 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 78.92 E-value: 4.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNlkpVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDifDGKIVIDGIDISKLPlhTLRSRL 1100
Cdd:cd03299 1 LKVENLSKDWKEF---KLKNVSLEVERGDYFVILGPTGSGKSVLleTIAGFIKPD--SGKILLNGKDITNLP--PEKRDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1101 SIILQDPILFSG-SIRFNLDPECKctdDRLWEALEI-AQLKNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 1178
Cdd:cd03299 74 SYVPQNYALFPHmTVYKNIAYGLK---KRKVDKKEIeRKVLEIAEML--GIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1179 SILIMDEATASIDMATENILQKVVMTAF--ADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQ-ENGVFAS 1254
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRkeFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKpKNEFVAE 228
|
..
gi 1786986074 1255 FV 1256
Cdd:cd03299 229 FL 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
380-605 |
5.62e-16 |
|
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: 77.59 E-value: 5.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 380 EDIAIKVTNGyfSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG--EMQTLEGKVHWSNVNESEPSFeatr 457
Cdd:cd03213 7 RNLTVTVKSS--PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSF---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 458 rnRYSVAYAAQKPWLL-NATVEENITFgspfnkqrykavtdACSLQpdidllpfgdqteigergiNLSGGQRQRICVARA 536
Cdd:cd03213 81 --RKIIGYVPQDDILHpTLTVRETLMF--------------AAKLR-------------------GLSGGERKRVSIALE 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1786986074 537 LYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTHA--DWIIAMKDGSVLREG 605
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMS--LLRRLADTGRTIICSIHQPSSEIFElfDKLLLLSQGRVIYFG 194
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
400-610 |
6.28e-16 |
|
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: 78.24 E-value: 6.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVN-ESEPSFEatrRNRYSVAYAAQKPWLL-NATV 477
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDiTGLPPHE---RARAGIGYVPEGRRIFpELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 478 EENITFG-SPFNKQRYKAVTDACslqpdIDLLPfgdqtEIGER----GINLSGGQRQRICVARALYQNTNIVFLDDPFSA 552
Cdd:cd03224 93 EENLLLGaYARRRAKRKARLERV-----YELFP-----RLKERrkqlAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1786986074 553 LDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQY-LTHADWIIAMKDGSVLREGTLKDI 610
Cdd:cd03224 163 LAPKIVEEIFE--AIRELRDEGVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAEL 219
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
1055-1256 |
7.45e-16 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 80.23 E-value: 7.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1055 ICGRTGSGKSSL--SLAFFRMVDifDGKIVIDGIDISKLPLHtLRSrLSIILQDPILF-----SGSIRFNL--DPECKCT 1125
Cdd:TIGR01187 1 LLGPSGCGKTTLlrLLAGFEQPD--SGSIMLDGEDVTNVPPH-LRH-INMVFQSYALFphmtvEENVAFGLkmRKVPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1126 -DDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASID------MATE--N 1196
Cdd:TIGR01187 77 iKPRVLEALRLVQLEEFADRKPHQL-----------SGGQQQRVALARALVFKPKILLLDEPLSALDkklrdqMQLElkT 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 1197 ILQKVVMtafadrTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQENGVF-ASFV 1256
Cdd:TIGR01187 146 IQEQLGI------TFVFVTHDQEEAMTmSDRIAIMRKGKIAQIGTPEEIYEEPANLFvARFI 201
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
400-606 |
8.28e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 78.66 E-value: 8.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV--------HWSnvnesePSFEATRRnrysvAYAAQK-- 469
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVrlngrplaDWS------PAELARRR-----AVLPQHss 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 470 ---PWllnaTVEENITFG-SPF--NKQRYKAVTDACSLQpdIDLLPFGD---QTeigerginLSGGQRQRICVARALYQN 540
Cdd:PRK13548 87 lsfPF----TVEEVVAMGrAPHglSRAEDDALVAAALAQ--VDLAHLAGrdyPQ--------LSGGEQQRVQLARVLAQL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 541 TN------IVFLDDPFSALDIHLSDHLMQegILK-FLQDDKRTLVLVTHKL----QYlthADWIIAMKDGSVLREGT 606
Cdd:PRK13548 153 WEpdgpprWLLLDEPTSALDLAHQHHVLR--LARqLAHERGLAVIVVLHDLnlaaRY---ADRIVLLHQGRLVADGT 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1023-1247 |
8.79e-16 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 79.71 E-value: 8.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNLKPVlkhvKA------YIKPGQKVGICGRTGSGKSSLSLAFFRMVD---IFDGKIVIDGIDISKLPL 1093
Cdd:COG0444 2 LEVRNLKVYFPTRRGVV----KAvdgvsfDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1094 HTLRS----RLSIILQDPIlfsGSirfnLDPeCKCTDDRLWEALEI------AQLKNMVKSLpggLDAV-VTEGGE---- 1158
Cdd:COG0444 78 KELRKirgrEIQMIFQDPM---TS----LNP-VMTVGDQIAEPLRIhgglskAEARERAIEL---LERVgLPDPERrldr 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1159 ---NFSVGQRQLFCLARAFVRKSSILIMDEATASIDmATeniLQKVVMTAFADR------TVVTIAHRVHTIL-TADLVI 1228
Cdd:COG0444 147 yphELSGGMRQRVMIARALALEPKLLIADEPTTALD-VT---IQAQILNLLKDLqrelglAILFITHDLGVVAeIADRVA 222
|
250
....*....|....*....
gi 1786986074 1229 VMKRGNILEYDTPESLLAQ 1247
Cdd:COG0444 223 VMYAGRIVEEGPVEELFEN 241
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1023-1236 |
1.61e-15 |
|
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: 77.02 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIF----DGKIVIDGIDISKLPLHTl 1096
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTT----LRMLAGLlepdAGFATVDGFDVVKEPAEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1097 RSRLSIilqdpilFSGSIRFNldpeckctdDRL--WEALEI---------AQLKNMVKSLPGGLD--AVVTEGGENFSVG 1163
Cdd:cd03266 77 RRRLGF-------VSDSTGLY---------DRLtaRENLEYfaglyglkgDELTARLEELADRLGmeELLDRRVGGFSTG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1786986074 1164 QRQLFCLARAFVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNIL 1236
Cdd:cd03266 141 MRQKVAIARALVHDPPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
400-610 |
1.99e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 79.36 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSfeatRRNRySVAYAAQKPWLL-NATVE 478
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH----ARDR-KVGFVFQHYALFrHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 479 ENITFGS---PFNKQRYKAVTDACSLQpdidLLPFGDQTEIGER-GINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 554
Cdd:PRK10851 93 DNIAFGLtvlPRRERPNAAAIKAKVTQ----LLEMVQLAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 555 IHLSDHLmQEGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 610
Cdd:PRK10851 169 AQVRKEL-RRWLRQLHEELKFTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1023-1221 |
2.17e-15 |
|
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: 76.68 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNLkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSR 1099
Cdd:cd03292 1 IEFINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1100 LSIILQDPILFSG-----SIRFNLdpECKCTDDRLW-----EALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 1169
Cdd:cd03292 80 IGVVFQDFRLLPDrnvyeNVAFAL--EVTGVPPREIrkrvpAALELVGLSHKHRALPAEL-----------SGGEQQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 1170 LARAFVRKSSILIMDEATASIDMATE----NILQK-------VVMTAFADRTVVTIAHRVHTI 1221
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTweimNLLKKinkagttVVVATHAKELVDTTRHRVIAL 209
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1023-1237 |
2.97e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 76.24 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSR 1099
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1100 LSIILQD-PILFSGSIRFNL----------DPECKctdDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1168
Cdd:COG2884 81 IGVVFQDfRLLPDRTVYENValplrvtgksRKEIR---RRVREVLDLVGLSDKAKALPHEL-----------SGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786986074 1169 CLARAFVRKSSILIMDEATASIDMAT-ENILQkvVMTAFADR--TVVtIA-HRVHTILTADL-VIVMKRGNILE 1237
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETsWEIME--LLEEINRRgtTVL-IAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
396-620 |
3.15e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 79.11 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 396 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESE-PSFeatRR--NRYSVAYAAqkpwL 472
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHvPPY---QRpiNMMFQSYAL----F 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 473 LNATVEENITFGSPFNKQRYKAVTDACSlqpdiDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFS 551
Cdd:PRK11607 104 PHMTVEQNIAFGLKQDKLPKAEIASRVN-----EMLGLVHMQEFAKRKPHqLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 552 ALDIHLSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKdiqtkdvELYEH 620
Cdd:PRK11607 179 ALDKKLRDR-MQLEVVDILERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPE-------EIYEH 240
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1023-1191 |
3.16e-15 |
|
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: 75.59 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDGIDISKLPLHtLRS 1098
Cdd:COG4133 3 LEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTL----LRILagllPPSAGEVLWNGEPIRDARED-YRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1099 RLSIILQDPILFSG-SIRFNLD-----PECKCTDDRLWEALEIAqlknmvkslpgGLDAVVTEGGENFSVGQRQLFCLAR 1172
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLRfwaalYGLRADREAIDEALEAV-----------GLAGLADLPVRQLSAGQKRRVALAR 144
|
170
....*....|....*....
gi 1786986074 1173 AFVRKSSILIMDEATASID 1191
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALD 163
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
458-624 |
3.17e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 81.23 E-value: 3.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 458 RNRYSVAyaAQKPWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARA 536
Cdd:PTZ00265 1295 RNLFSIV--SQEPMLFNMSIYENIKFGKEdATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARA 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 537 LYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAM----KDGS-VLREGTLKDIQ 611
Cdd:PTZ00265 1373 LLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSfVQAHGTHEELL 1451
|
170
....*....|...
gi 1786986074 612 TKDVELYEHWKTL 624
Cdd:PTZ00265 1452 SVQDGVYKKYVKL 1464
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
404-601 |
3.25e-15 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 76.05 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 404 DIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEG--KVHWSNVNESEPSfeatrrnRYSVAYAAQKPWLL-NATVEEN 480
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGsiKVNDQSHTGLAPY-------QRPVSMLFQENNLFaHLTVRQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 481 ITFG-SPFNK----QRYKAVTDACSLQPD--IDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSAL 553
Cdd:TIGR01277 91 IGLGlHPGLKlnaeQQEKVVDAAQQVGIAdyLDRLPE-----------QLSGGQRQRVALARCLVRPNPILLLDEPFSAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1786986074 554 DIHLSDHlMQEGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSV 601
Cdd:TIGR01277 160 DPLLREE-MLALVKQLCSERQRTLLMVTHHLSDARAiASQIAVVSQGKI 207
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
384-599 |
3.63e-15 |
|
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: 75.64 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI--LGEMQ----TLEGKvhwsNVNESEPSFEATR 457
Cdd:cd03262 1 IEIKNLHKSFG-DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlLEEPDsgtiIIDGL----KLTDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 458 RNrysVAYAAQKPWLL-NATVEENITFGsP---FNKQRYKAVTDACSLQPDIDLLPFGDQteigeRGINLSGGQRQRICV 533
Cdd:cd03262 76 QK---VGMVFQQFNLFpHLTVLENITLA-PikvKGMSKAEAEERALELLEKVGLADKADA-----YPAQLSGGQQQRVAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 534 ARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDG 599
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPELVGEVLD--VMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDG 211
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
400-582 |
3.64e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 75.60 E-value: 3.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ---TLEGKVhWSNvNESEPSFEATRRNrysVAYAAQKPWLL-NA 475
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEV-LLN-GRRLTALPAEQRR---IGILFQDDLLFpHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 476 TVEENITFGSP--FNK-QRYKAVTDAcsLQpDIDLLPFGDQTeIGErginLSGGQRQRICVARALYQNTNIVFLDDPFSA 552
Cdd:COG4136 92 SVGENLAFALPptIGRaQRRARVEQA--LE-EAGLAGFADRD-PAT----LSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
170 180 190
....*....|....*....|....*....|..
gi 1786986074 553 LDIHLSDHLMQegiLKFLQDDKRTL--VLVTH 582
Cdd:COG4136 164 LDAALRAQFRE---FVFEQIRQRGIpaLLVTH 192
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1037-1236 |
3.88e-15 |
|
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: 75.28 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1037 KPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDIFDGKIVIDGIDISKlplHTLRSRLSIILQDPILFSgsi 1114
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLlnALAGRRTGLGVSGEVLINGRPLDK---RSFRKIIGYVPQDDILHP--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1115 rfnldpeckctDDRLWEALEI-AQLknmvKSLPGgldavvteggenfsvGQRQLFCLARAFVRKSSILIMDEATASIDMA 1193
Cdd:cd03213 96 -----------TLTVRETLMFaAKL----RGLSG---------------GERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1786986074 1194 TENILQKVVMtAFAD--RTVVTIAHRVHTILTA--DLVIVMKRGNIL 1236
Cdd:cd03213 146 SALQVMSLLR-RLADtgRTIICSIHQPSSEIFElfDKLLLLSQGRVI 191
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
384-605 |
4.59e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 75.86 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNRYSV 463
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 464 AYAAQKPWLL-NATVEENITF-----GSPfNKQRYKAVTDACS---LQPDIDLLPfgdqteigergINLSGGQRQRICVA 534
Cdd:COG2884 82 GVVFQDFRLLpDRTVYENVALplrvtGKS-RKEIRRRVREVLDlvgLSDKAKALP-----------HELSGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 535 RALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTHADW-IIAMKDGSVLREG 605
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIME--LLEEINRRGTTVLIATHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
384-610 |
4.79e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 77.04 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnVNESEPSFEATR--RNRY 461
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVL---IKGEPIKYDKKSllEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 462 SVAYAAQKP--WLLNATVEENITFGsPFN-----KQRYKAVTDACSlqpdidllpfgdqtEIGERGI------NLSGGQR 528
Cdd:PRK13639 79 TVGIVFQNPddQLFAPTVEEDVAFG-PLNlglskEEVEKRVKEALK--------------AVGMEGFenkpphHLSGGQK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 529 QRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYL-THADWIIAMKDGSVLREGTL 607
Cdd:PRK13639 144 KRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMK--LLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTP 221
|
...
gi 1786986074 608 KDI 610
Cdd:PRK13639 222 KEV 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
396-612 |
7.49e-15 |
|
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: 75.55 E-value: 7.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 396 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESepSFEATRRNRYSVAYAAQKPWLL-N 474
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDIT--GLPPHEIARLGIGRTFQIPRLFpE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 475 ATVEENITFGSPFNKQRYKAVTDACSLQPDI-----DLLpfgDQTEIGERG----INLSGGQRQRICVARALYQNTNIVF 545
Cdd:cd03219 90 LTVLENVMVAAQARTGSGLLLARARREEREAreraeELL---ERVGLADLAdrpaGELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1786986074 546 LDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDIQT 612
Cdd:cd03219 167 LDEPAAGLNPEETEELAE--LIRELRERGITVLLVEHDMDVVMsLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
388-618 |
7.60e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 77.76 E-value: 7.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 388 NGYFSWGSGLATlSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN--VNESEPSfeatRRNRYSV-- 463
Cdd:PRK11000 8 NVTKAYGDVVIS-KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrMNDVPPA----ERGVGMVfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 464 AYAAQkPWLlnaTVEENITFGSPFNK-------QRYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARA 536
Cdd:PRK11000 83 SYALY-PHL---SVAENMSFGLKLAGakkeeinQRVNQVAEVLQLAHLLDRKP-----------KALSGGQRQRVAIGRT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 537 LYQNTNIVFLDDPFSALDIHLSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLTHADWIIAMKDGSVLREGtlkdiqtKDV 615
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLDAALRVQ-MRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG-------KPL 219
|
...
gi 1786986074 616 ELY 618
Cdd:PRK11000 220 ELY 222
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
396-608 |
7.63e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 75.94 E-value: 7.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 396 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLL--LAILGEMQTLEGKVHWSNVNESEPSFE---ATRRNRYSVAYAAQKP 470
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLrcINLLEQPEAGTIRVGDITIDTARSLSQqkgLIRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 471 WLL-NATVEENITFGSPFNKQ--RYKAVTDACSLQPDIDLLpfGDQTEIGERginLSGGQRQRICVARALYQNTNIVFLD 547
Cdd:PRK11264 95 NLFpHRTVLENIIEGPVIVKGepKEEATARARELLAKVGLA--GKETSYPRR---LSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 548 DPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLK 608
Cdd:PRK11264 170 EPTSALDPELVGEVLN--TIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAK 229
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
398-619 |
1.17e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 75.99 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 398 ATLSNIDIRIPTGQLTMIVGQVGCGKSS---LLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNrysVAYAAQKP--WL 472
Cdd:PRK13640 21 PALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK---VGIVFQNPdnQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 473 LNATVEENITFGSPfNKQ--RYKAVTDACSLQPDIDLLPFGDQTEIgergiNLSGGQRQRICVARALYQNTNIVFLDDPF 550
Cdd:PRK13640 98 VGATVGDDVAFGLE-NRAvpRPEMIKIVRDVLADVGMLDYIDSEPA-----NLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 551 SALDIHLSDHLMQegILKFLQDDKR-TLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYE 619
Cdd:PRK13640 172 SMLDPAGKEQILK--LIRKLKKKNNlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVEMLKE 239
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1023-1249 |
1.25e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 75.92 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNL-KPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIF----DGKIVIDGIDISKLPLHTLR 1097
Cdd:PRK13650 5 IEVKNLTFKYKEDQeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTT----VRLIDGLleaeSGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1098 SRLSIILQDPI-LFSGS-----IRFNLDP---ECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1168
Cdd:PRK13650 81 HKIGMVFQNPDnQFVGAtveddVAFGLENkgiPHEEMKERVNEALELVGMQDFKEREPARL-----------SGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1169 CLARAFVRKSSILIMDEATASID--------MATENILQKVVMTafadrtVVTIAHRVHTILTADLVIVMKRGNILEYDT 1240
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDpegrleliKTIKGIRDDYQMT------VISITHDLDEVALSDRVLVMKNGQVESTST 223
|
....*....
gi 1786986074 1241 PESLLAQEN 1249
Cdd:PRK13650 224 PRELFSRGN 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1023-1247 |
1.49e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.51 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENN----LKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP-LHTLR 1097
Cdd:PRK13633 5 IKCKNVSYKYESNeestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1098 SRLSIILQDP------ILFSGSIRF---NLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1168
Cdd:PRK13633 85 NKAGMVFQNPdnqivaTIVEEDVAFgpeNLGIPPEEIRERVDESLKKVGMYEYRRHAPHLL-----------SGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1169 CLARAFVRKSSILIMDEATASIDmateNILQKVVMTAFADR------TVVTIAHRVHTILTADLVIVMKRGNILEYDTPE 1242
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLD----PSGRREVVNTIKELnkkygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPK 229
|
....*
gi 1786986074 1243 SLLAQ 1247
Cdd:PRK13633 230 EIFKE 234
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
353-600 |
1.57e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 78.31 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 353 TINRkqpgryhLDSYEQSTRRLRPAETEDIAIKVTNGyfswgSGLAT-------------LSNIDIRIPTGQLTMIVGQV 419
Cdd:COG4178 331 TVDR-------LAGFEEALEAADALPEAASRIETSED-----GALALedltlrtpdgrplLEDLSLSLKPGERLLITGPS 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 420 GCGKSSLLLAILGemqtL----EGKVHwsnvnesepsfeatRRNRYSVAYAAQKPWLLNATVEENITFGSP---FNKQRY 492
Cdd:COG4178 399 GSGKSTLLRAIAG----LwpygSGRIA--------------RPAGARVLFLPQRPYLPLGTLREALLYPATaeaFSDAEL 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 493 KAVTDACSLQPDIDLLpfgDQTEIGERGinLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQD 572
Cdd:COG4178 461 REALEAVGLGHLAERL---DEEADWDQV--LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-LREELPG 534
|
250 260
....*....|....*....|....*...
gi 1786986074 573 dkRTLVLVTHKLQYLTHADWIIAMKDGS 600
Cdd:COG4178 535 --TTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1023-1248 |
2.00e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 75.27 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG--IDISKLPLHTLRSRL 1100
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1101 SIILQDP--ILFSGSIR-------FNLDPECKCTDDRLWEALE---IAQLKNmvkslpggldavvtEGGENFSVGQRQLF 1168
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYqdvsfgaVNLKLPEDEVRKRVDNALKrtgIEHLKD--------------KPTHCLSFGQKKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1169 CLARAFVRKSSILIMDEATASID-MATENILQKVVMTAFA-DRTVVTIAHRVHTI-LTADLVIVMKRGNILEYDTPESLL 1245
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDpMGVSEIMKLLVEMQKElGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVF 230
|
...
gi 1786986074 1246 AQE 1248
Cdd:PRK13636 231 AEK 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1023-1251 |
2.17e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 74.79 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1102
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1103 ILQDPI-LFSGSI-----RFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARA 1173
Cdd:PRK13648 88 VFQNPDnQFVGSIvkydvAFGLENHAVPYDEmhrRVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1174 FVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQENGV 1251
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
402-610 |
2.35e-14 |
|
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: 77.42 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 402 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGeMQTLEGKVHWSNVNESEPSFEATRRNRYSVA------YAAQKPWLlna 475
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLSRRALRPLRRRMQvvfqdpFGSLSPRM--- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 476 TVEENITFG--------SPfnKQRYKAVTDAcsLQpDIDLLPfgdqtEIGERGIN-LSGGQRQRICVARALYQNTNIVFL 546
Cdd:COG4172 380 TVGQIIAEGlrvhgpglSA--AERRARVAEA--LE-EVGLDP-----AARHRYPHeFSGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1786986074 547 DDPFSALDIHLsdhlmQEGILKFLQD--DKRTL--VLVTHKLQ---YLTHadWIIAMKDGSVLREGTLKDI 610
Cdd:COG4172 450 DEPTSALDVSV-----QAQILDLLRDlqREHGLayLFISHDLAvvrALAH--RVMVMKDGKVVEQGPTEQV 513
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1023-1248 |
2.90e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 74.84 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSlaffRMV-------DIFDGKIVIDGIDISKLPLHT 1095
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTIS----KLInglllpdDNPNSKITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1096 LRSRLSIILQDPI-LFSGS-----IRFNLDpeckctdDRLWEALEIAQLKNMVKSLPGGLDAVVTEGgENFSVGQRQLFC 1169
Cdd:PRK13640 82 IREKVGIVFQNPDnQFVGAtvgddVAFGLE-------NRAVPRPEMIKIVRDVLADVGMLDYIDSEP-ANLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1170 LARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1247
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
.
gi 1786986074 1248 E 1248
Cdd:PRK13640 234 V 234
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1038-1247 |
3.33e-14 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 74.51 E-value: 3.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1038 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSGSIRFN 1117
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1118 LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE-N 1196
Cdd:cd03291 118 IIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEkE 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1786986074 1197 ILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1247
Cdd:cd03291 198 IFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
384-619 |
3.52e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 74.70 E-value: 3.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSW--GSGLAT--LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRn 459
Cdd:PRK13637 3 IKIENLTHIYmeGTPFEKkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDI- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 460 RYSVAYAAQKP--WLLNATVEENITFGsPFN--------KQRYKAVTDACSLQPDI--DLLPFgdqteigergiNLSGGQ 527
Cdd:PRK13637 82 RKKVGLVFQYPeyQLFEETIEKDIAFG-PINlglseeeiENRVKRAMNIVGLDYEDykDKSPF-----------ELSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 528 RQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDD-KRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREG 605
Cdd:PRK13637 150 KRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNK--IKELHKEyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQG 227
|
250
....*....|....
gi 1786986074 606 TLKDIqTKDVELYE 619
Cdd:PRK13637 228 TPREV-FKEVETLE 240
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1018-1233 |
4.01e-14 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 73.97 E-value: 4.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1018 PQEGEIKIHDLCVRY--ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDGidiskL 1091
Cdd:COG1116 3 AAAPALELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLIagleKPTSGEVLVDG-----K 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1092 PLHTLRSRLSIILQDPILF-----SGSIRFNLD------PECKctdDRLWEALEIAQLKNMVKSLPGGLdavvteggenf 1160
Cdd:COG1116 74 PVTGPGPDRGVVFQEPALLpwltvLDNVALGLElrgvpkAERR---ERARELLELVGLAGFEDAYPHQL----------- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1786986074 1161 SVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVH-TILTADLVIVMKRG 1233
Cdd:COG1116 140 SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTHDVDeAVFLADRVVVLSAR 215
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1040-1245 |
4.74e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.84 E-value: 4.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1040 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS----RLSIILQDpilfsgsir 1115
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQS--------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1116 FNLDPECKCTDDRLWeALEIAQLKNMVKSlPGGLDAVVTEGGENF--------SVGQRQLFCLARAFVRKSSILIMDEAT 1187
Cdd:PRK10070 115 FALMPHMTVLDNTAF-GMELAGINAEERR-EKALDALRQVGLENYahsypdelSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1786986074 1188 ASID--MATENILQKVVMTAFADRTVVTIAHRV-HTILTADLVIVMKRGNILEYDTPESLL 1245
Cdd:PRK10070 193 SALDplIRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
400-610 |
5.27e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.00 E-value: 5.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEAT---RRNRYSVAYAAQKPWLLNAT 476
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEikpVRKKVGVVFQFPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 477 VEENITFGsPFNKQRYKAVTDACSLQpdiDLLPFGDQTEIGERG-INLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 555
Cdd:PRK13643 102 VLKDVAFG-PQNFGIPKEKAEKIAAE---KLEMVGLADEFWEKSpFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1786986074 556 HLSDHLMQegILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDI 610
Cdd:PRK13643 178 KARIEMMQ--LFESIHQSGQTVVLVTHLMDDVAdYADYVYLLEKGHIISCGTPSDV 231
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
380-610 |
5.77e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 73.73 E-value: 5.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 380 EDIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNvNESEPSFEATRRN 459
Cdd:PRK13636 2 EDYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDG-KPIDYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 460 RYSVAYAAQKP--WLLNATVEENITFGsPFNKQrykavtdacslqpdidlLPfgdQTEIGER--------GIN------- 522
Cdd:PRK13636 81 RESVGMVFQDPdnQLFSASVYQDVSFG-AVNLK-----------------LP---EDEVRKRvdnalkrtGIEhlkdkpt 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 523 --LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDG 599
Cdd:PRK13636 140 hcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIM-KLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEG 218
|
250
....*....|.
gi 1786986074 600 SVLREGTLKDI 610
Cdd:PRK13636 219 RVILQGNPKEV 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1023-1243 |
6.62e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 73.54 E-value: 6.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNL---KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIS--KLPLHTLR 1097
Cdd:PRK13637 3 IKIENLTHIYMEGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1098 SRLSIILQDP------------ILFsGSIRFNL-DPECKctdDRLWEALEIAqlknmvkslpgGLDAVVTEGGENF--SV 1162
Cdd:PRK13637 83 KKVGLVFQYPeyqlfeetiekdIAF-GPINLGLsEEEIE---NRVKRAMNIV-----------GLDYEDYKDKSPFelSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1163 GQRQLFCLARAFVRKSSILIMDEATASID-MATENILQKV-VMTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYD 1239
Cdd:PRK13637 148 GQKRRVAIAGVVAMEPKILILDEPTAGLDpKGRDEILNKIkELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQG 227
|
....
gi 1786986074 1240 TPES 1243
Cdd:PRK13637 228 TPRE 231
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
383-623 |
7.17e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 72.95 E-value: 7.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 383 AIKVTNGYFSWGSGlATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI-----LGEMQTLEGKVHWSNVNESEPSFEATR 457
Cdd:PRK14267 4 AIETVNLRVYYGSN-HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 458 -RNRYSVAYAAQKPWLlNATVEENITFGSPFNK---------QRYKAVTDACSLQPDIdllpfgdQTEIGERGINLSGGQ 527
Cdd:PRK14267 83 vRREVGMVFQYPNPFP-HLTIYDNVAIGVKLNGlvkskkeldERVEWALKKAALWDEV-------KDRLNDYPSNLSGGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 528 RQRICVARALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDdkRTLVLVTHK-LQYLTHADWIIAMKDGSVLREG- 605
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANID-PVGTAKIEELLFELKKE--YTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGp 231
|
250
....*....|....*...
gi 1786986074 606 TLKDIQTKDVELYEHWKT 623
Cdd:PRK14267 232 TRKVFENPEHELTEKYVT 249
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1023-1235 |
7.82e-14 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 71.79 E-value: 7.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDI--SKLPLHTLRSRL 1100
Cdd:cd03262 1 IEIKNLHKSFGDF--HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1101 SIILQDpilfsgsirFNLDPECK----CTDDRLW-------EALEIA-------QLKNMVKSLPGGLdavvteggenfSV 1162
Cdd:cd03262 79 GMVFQQ---------FNLFPHLTvlenITLAPIKvkgmskaEAEERAlellekvGLADKADAYPAQL-----------SG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1786986074 1163 GQRQLFCLARAFVRKSSILIMDEATASID--MATEnILQkvVMTAFADR--TVVTIAHRVHTIL-TADLVIVMKRGNI 1235
Cdd:cd03262 139 GQQQRVAIARALAMNPKVMLFDEPTSALDpeLVGE-VLD--VMKDLAEEgmTMVVVTHEMGFAReVADRVIFMDDGRI 213
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1023-1248 |
7.82e-14 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 72.19 E-value: 7.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslaFFRMVDIF---DGKIVIDGIDISKLPLHTlRSR 1099
Cdd:cd03218 1 LRAENLSKRYGK--RKVVNGVSLSVKQGEIVGLLGPNGAGKTTT---FYMIVGLVkpdSGKILLDGQDITKLPMHK-RAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1100 LSIIL--QDPILFSG-SIRFNL--------DPEcKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1168
Cdd:cd03218 75 LGIGYlpQEASIFRKlTVEENIlavleirgLSK-KEREEKLEELLEEFHITHLRKSKASSL-----------SGGERRRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1169 CLARAFVRKSSILIMDEATASID-MATENIlQKVVMTaFADRTV-VTIA-HRVHTIL-TADLVIVMKRGNILEYDTPESL 1244
Cdd:cd03218 143 EIARALATNPKFLLLDEPFAGVDpIAVQDI-QKIIKI-LKDRGIgVLITdHNVRETLsITDRAYIIYEGKVLAEGTPEEI 220
|
....
gi 1786986074 1245 LAQE 1248
Cdd:cd03218 221 AANE 224
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
400-594 |
9.20e-14 |
|
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: 70.26 E-value: 9.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnvnesepsfEATRRNrysVAYAAQKPWLLNATVEE 479
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG-----------MPEGED---LLFLPQRPYLPLGTLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 480 NITFgspfnkqrykavtdacslqpdidllPFGDqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD 559
Cdd:cd03223 83 QLIY-------------------------PWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180 190
....*....|....*....|....*....|....*
gi 1786986074 560 HLMQegilkFLQDDKRTLVLVTHKLQYLTHADWII 594
Cdd:cd03223 129 RLYQ-----LLKELGITVISVGHRPSLWKFHDRVL 158
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
400-606 |
9.29e-14 |
|
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: 71.77 E-value: 9.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnVNESEpsfeaTRRNRY----SVAYAAQK---PWL 472
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAY---INGYS-----IRTDRKaarqSLGYCPQFdalFDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 473 LnaTVEENITF-----GSPFNKQRY--KAVTDACSLQPDIDllpfgdqTEIGergiNLSGGQRQRICVARALYQNTNIVF 545
Cdd:cd03263 90 L--TVREHLRFyarlkGLPKSEIKEevELLLRVLGLTDKAN-------KRAR----TLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1786986074 546 LDDPFSALdihlsDHLMQEGILKFLQDDK--RTLVLVTHKLQ---YLthADWIIAMKDGSVLREGT 606
Cdd:cd03263 157 LDEPTSGL-----DPASRRAIWDLILEVRkgRSIILTTHSMDeaeAL--CDRIAIMSDGKLRCIGS 215
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
400-636 |
1.05e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 73.12 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLL-----LAILGEMQTLEGKVhwsNVNESEPSFEATRRNRYSVAYAAQKP--WL 472
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIqltngLIISETGQTIVGDY---AIPANLKKIKEVKRLRKEIGLVFQFPeyQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 473 LNATVEENITFGsPFN-----KQRYKAVTDACSLQPdidlLPfgdqTEIGERG-INLSGGQRQRICVARALYQNTNIVFL 546
Cdd:PRK13645 104 FQETIEKDIAFG-PVNlgenkQEAYKKVPELLKLVQ----LP----EDYVKRSpFELSGGQKRRVALAGIIAMDGNTLVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 547 DDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGT----------LKDIQTKDV 615
Cdd:PRK13645 175 DEPTGGLDPKGEEDFINL-FERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSpfeifsnqelLTKIEIDPP 253
|
250 260
....*....|....*....|.
gi 1786986074 616 ELYEHWKTLMNRQDQELEKDM 636
Cdd:PRK13645 254 KLYQLMYKLKNKGIDLLNKNI 274
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1021-1256 |
1.31e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 73.95 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1021 GEIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLsLaffRMV----DIFDGKIVIDGIDISKLPlhTL 1096
Cdd:COG3839 2 ASLELENVSKSYGG--VEALKDIDLDIEDGEFLVLLGPSGCGKSTL-L---RMIagleDPTSGEILIGGRDVTDLP--PK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1097 RSRLSIILQDPILF-SGSIRFNL----------DPEckcTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQR 1165
Cdd:COG3839 74 DRNIAMVFQSYALYpHMTVYENIafplklrkvpKAE---IDRRVREAAELLGLEDLLDRKPKQL-----------SGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1166 QLFCLARAFVRKSSILIMDEATASID------MATE--NILQKVVMTafadrTV-VTiaHRVHTILT-ADLVIVMKRGNI 1235
Cdd:COG3839 140 QRVALGRALVREPKVFLLDEPLSNLDaklrveMRAEikRLHRRLGTT-----TIyVT--HDQVEAMTlADRIAVMNDGRI 212
|
250 260
....*....|....*....|..
gi 1786986074 1236 LEYDTPESLLAQENGVF-ASFV 1256
Cdd:COG3839 213 QQVGTPEELYDRPANLFvAGFI 234
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
384-599 |
1.42e-13 |
|
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: 69.01 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGSGLaTLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNEsepsfeatrrnrysV 463
Cdd:cd03221 1 IELENLSKTYGGKL-LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK--------------I 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 464 AYAAQkpwllnatveenitfgspfnkqrykavtdacslqpdidllpfgdqteigerginLSGGQRQRICVARALYQNTNI 543
Cdd:cd03221 66 GYFEQ------------------------------------------------------LSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 544 VFLDDPFSALDIHLSDHLMQegilkFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDG 599
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEE-----ALKEYPGTVILVSHDRYFLDQvATKIIELEDG 143
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1038-1248 |
1.86e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 75.72 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1038 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSGSIRFN 1117
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1118 LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE-N 1196
Cdd:TIGR01271 507 IIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEkE 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 1197 ILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQE 1248
Cdd:TIGR01271 587 IFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
384-611 |
2.14e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 72.43 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGSGLAT----LSNIDIRIPTGQLTMIVGQVGCGKSS-------LLLAILGEM-----------QTLEGKV 441
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTfiehlnaLLLPDTGTIewifkdeknkkKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 442 HWSNVNESEPSFEATR-----RNRYSVAYAAQKPWLLNATVEENITFGsPFN--------KQRYKAVTDACSLqpDIDLL 508
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKkikeiRRRVGVVFQFAEYQLFEQTIEKDIIFG-PVSmgvskeeaKKRAAKYIELVGL--DESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 509 ---PFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQ 585
Cdd:PRK13651 160 qrsPF-----------ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLD 226
|
250 260 270
....*....|....*....|....*....|.
gi 1786986074 586 Y-LTHADWIIAMKDGSVLREG----TLKDIQ 611
Cdd:PRK13651 227 NvLEWTKRTIFFKDGKIIKDGdtydILSDNK 257
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1035-1245 |
2.16e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 71.62 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1035 NLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGI------DISKLPLHTLRSRLSIILQDPI 1108
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1109 LFSG-SIRFNLDPECKCTDDRlwEALEIAQLKNMVKSLPGGLDAV---VTEGGENFSVGQRQLFCLARAFVRKSSILIMD 1184
Cdd:PRK14246 101 PFPHlSIYDNIAYPLKSHGIK--EKREIKKIVEECLRKVGLWKEVydrLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 1185 EATASIDMATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLL 1245
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVArVADYVAFLYNGELVEWGSSNEIF 240
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1023-1256 |
2.32e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 73.21 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDifDGKIVIDGIDISKLPLHtlRSRL 1100
Cdd:COG3842 6 LELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPSGCGKTTLlrMIAGFETPD--SGRILLDGRDVTGLPPE--KRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1101 SIILQDPILF-----SGSIRFNLD------PECKctdDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 1169
Cdd:COG3842 80 GMVFQDYALFphltvAENVAFGLRmrgvpkAEIR---ARVAELLELVGLEGLADRYPHQL-----------SGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1170 LARAFVRKSSILIMDEATASID------MATE--NILQKVVMTAFadrtVVTiaHRVHTILT-ADLVIVMKRGNILEYDT 1240
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDaklreeMREElrRLQRELGITFI----YVT--HDQEEALAlADRIAVMNDGRIEQVGT 219
|
250
....*....|....*..
gi 1786986074 1241 PESLLAQENGVF-ASFV 1256
Cdd:COG3842 220 PEEIYERPATRFvADFI 236
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1023-1236 |
2.62e-13 |
|
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: 70.30 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENnlKPVLKHVKAYIKPGQkVGICGRTGSGKSSL--SLA-FFRMVDifdGKIVIDGIDISKLPlHTLRSR 1099
Cdd:cd03264 1 LQLENLTKRYGK--KRALDGVSLTLGPGM-YGLLGPNGAGKTTLmrILAtLTPPSS---GTIRIDGQDVLKQP-QKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1100 LSIILQDpilFSGSIRFnldpeckctddRLWEALE-IAQLKNMVKS-----LPGGLDAVVTEGGEN-----FSVGQRQLF 1168
Cdd:cd03264 74 IGYLPQE---FGVYPNF-----------TVREFLDyIAWLKGIPSKevkarVDEVLELVNLGDRAKkkigsLSGGMRRRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 1169 CLARAFVRKSSILIMDEATASID----MATENILQKVVmtafADRTVVTIAHRVHTI-LTADLVIVMKRGNIL 1236
Cdd:cd03264 140 GIAQALVGDPSILIVDEPTAGLDpeerIRFRNLLSELG----EDRIVILSTHIVEDVeSLCNQVAVLNKGKLV 208
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1023-1233 |
3.32e-13 |
|
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: 68.61 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL-PLHTLRSRLS 1101
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAsPRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1102 IILQdpilfsgsirfnldpeckctddrlwealeiaqlknmvkslpggldavvteggenFSVGQRQLFCLARAFVRKSSIL 1181
Cdd:cd03216 79 MVYQ------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1786986074 1182 IMDEATASIDMA-TENILQkvVMTAFADR--TVVTIAHRVHTIL-TADLVIVMKRG 1233
Cdd:cd03216 105 ILDEPTAALTPAeVERLFK--VIRRLRAQgvAVIFISHRLDEVFeIADRVTVLRDG 158
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
396-582 |
3.49e-13 |
|
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: 69.83 E-value: 3.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 396 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRrnrySVAYAAQKPWLLNA 475
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIAR----GLLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 476 -TVEENITFGSPFNKQryKAVTDACSlqpDIDLLPFGDqteigeRGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSAL 553
Cdd:cd03231 88 lSVLENLRFWHADHSD--EQVEEALA---RVGLNGFED------RPVAqLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 1786986074 554 DI--------HLSDHLMQEGIlkflqddkrtLVLVTH 582
Cdd:cd03231 157 DKagvarfaeAMAGHCARGGM----------VVLTTH 183
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
384-635 |
4.34e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 72.05 E-value: 4.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFsW--GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNRY 461
Cdd:PRK15079 20 IKDGKQWF-WqpPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 462 SVAYAAQKPWL-LNA--TVEENI-----TFGSPFNKQ----RYKAVTDACSLQPDIdllpfgdqteigergIN-----LS 524
Cdd:PRK15079 99 DIQMIFQDPLAsLNPrmTIGEIIaeplrTYHPKLSRQevkdRVKAMMLKVGLLPNL---------------INrypheFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 525 GGQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMKDG 599
Cdd:PRK15079 164 GGQCQRIGIARALILEPKLIICDEPVSALDVSI-----QAQVVNLLQQLQRemglSLIFIAHDLAVVKHiSDRVLVMYLG 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1786986074 600 SVLREGTlkdiqtkDVELYEH-----WKTLMNR---QDQELEKD 635
Cdd:PRK15079 239 HAVELGT-------YDEVYHNplhpyTKALMSAvpiPDPDLERN 275
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1023-1217 |
4.67e-13 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 68.33 E-value: 4.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIdgidisklplhTLRS 1098
Cdd:cd03223 1 IELENLSLATPDG-RVLLKDLSFEIKPGDRLLITGPSGTGKSSL----FRALaglwPWGSGRIGM-----------PEGE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1099 RLSIILQDPILFSGSIRfnldpeckctddrlwealeiaqlknmvkslpgglDAVVTEGGENFSVGQRQLFCLARAFVRKS 1178
Cdd:cd03223 65 DLLFLPQRPYLPLGTLR----------------------------------EQLIYPWDDVLSGGEQQRLAFARLLLHKP 110
|
170 180 190
....*....|....*....|....*....|....*....
gi 1786986074 1179 SILIMDEATASIDMATENILQKVVMTAFAdrTVVTIAHR 1217
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
960-1237 |
1.44e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 71.66 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 960 GLGLLYaltITNYLNwVVRNLADLEVQMGAVKKV--NSFLTMESE----------NYEGTMDPSQVPEhwPQEGEIKIHD 1027
Cdd:PRK15134 207 NMGLLF---ITHNLS-IVRKLADRVAVMQNGRCVeqNRAATLFSApthpytqkllNSEPSGDPVPLPE--PASPLLDVEQ 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1028 LCVRYE---------NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGidiskLPLHTL-- 1096
Cdd:PRK15134 281 LQVAFPirkgilkrtVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDG-----QPLHNLnr 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1097 ------RSRLSIILQDPilfSGSIRFNLDPEckctdDRLWEALEI-------AQLKNMVKSLPG--GLDAVV-----TEg 1156
Cdd:PRK15134 355 rqllpvRHRIQVVFQDP---NSSLNPRLNVL-----QIIEEGLRVhqptlsaAQREQQVIAVMEevGLDPETrhrypAE- 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1157 genFSVGQRQLFCLARAFVRKSSILIMDEATASID-------MATENILQKVVMTAFadrtvVTIAHRVHTILT-ADLVI 1228
Cdd:PRK15134 426 ---FSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqaqiLALLKSLQQKHQLAY-----LFISHDLHVVRAlCHQVI 497
|
....*....
gi 1786986074 1229 VMKRGNILE 1237
Cdd:PRK15134 498 VLRQGEVVE 506
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
400-610 |
1.70e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.59 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLlAIL--------GEMqTLEGK-VHWSNVNESEpsfeatrrnRYSVAYAAQKP 470
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLM-KILsgvyqpdsGEI-LLDGEpVRFRSPRDAQ---------AAGIAIIHQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 471 WLL-NATVEENITFGSPFNK----------QRYKAVTDacSLQPDIDLlpfgdQTEIGErginLSGGQRQRICVARALYQ 539
Cdd:COG1129 89 NLVpNLSVAENIFLGREPRRgglidwramrRRARELLA--RLGLDIDP-----DTPVGD----LSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 540 NTNIVFLDDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDI 610
Cdd:COG1129 158 DARVLILDEPTASLTEREVERLF--RIIRRLKAQGVAIIYISHRLdEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
400-623 |
1.82e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 68.79 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTL--EGKVHWSNVNESEPSFE---ATRRNRYSVAYAAQKPwLLN 474
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLL-RVFNRLIELypEARVSGEVYLDGQDIFKmdvIELRRRVQMVFQIPNP-IPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 475 ATVEENITFGSPFNK---------QRYKAVTDACSLQPDIdllpfgdQTEIGERGINLSGGQRQRICVARALYQNTNIVF 545
Cdd:PRK14247 97 LSIFENVALGLKLNRlvkskkelqERVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 546 LDDPFSALDIHLSDHLmqEGILKFLQDDKrTLVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKDIQTKDV-ELYEHWKT 623
Cdd:PRK14247 170 ADEPTANLDPENTAKI--ESLFLELKKDM-TIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRhELTEKYVT 246
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
395-615 |
2.02e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.24 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 395 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEG--KVHWSNVNESEPSfEATRRNRYSVayaAQKPWL 472
Cdd:PRK15439 22 SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGtlEIGGNPCARLTPA-KAHQLGIYLV---PQEPLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 473 L-NATVEENITFGSPFNKQRYKAVTD-----ACSLQPDID--LLPFGDQteigerginlsggqrQRICVARALYQNTNIV 544
Cdd:PRK15439 98 FpNLSVKENILFGLPKRQASMQKMKQllaalGCQLDLDSSagSLEVADR---------------QIVEILRGLMRDSRIL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 545 FLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKDV 615
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSR--IRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTDDI 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1023-1258 |
2.51e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.61 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1102
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1103 ILQDP--ILFSGSI-------RFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARA 1173
Cdd:PRK13647 84 VFQDPddQVFSSTVwddvafgPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1174 FVRKSSILIMDEATASIDMATenilQKVVMTAFAD-----RTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPeSLLAQ 1247
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRG----QETLMEILDRlhnqgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDK-SLLTD 227
|
250
....*....|.
gi 1786986074 1248 ENGVFASFVRA 1258
Cdd:PRK13647 228 EDIVEQAGLRL 238
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
387-612 |
2.77e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 68.56 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 387 TNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNRYSVAYA 466
Cdd:PRK10419 15 HGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 467 AQ-KPWLLNA--TVEENItfGSPF----------NKQRYKAVTDACSLQPDI-DLLPfgdqteigergINLSGGQRQRIC 532
Cdd:PRK10419 95 FQdSISAVNPrkTVREII--REPLrhllsldkaeRLARASEMLRAVDLDDSVlDKRP-----------PQLSGGQLQRVC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 533 VARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKRTL----VLVTHKL---QYLTHAdwIIAMKDGSVLREG 605
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVL-----QAGVIRLLKKLQQQFgtacLFITHDLrlvERFCQR--VMVMDNGQIVETQ 234
|
....*..
gi 1786986074 606 TLKDIQT 612
Cdd:PRK10419 235 PVGDKLT 241
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
400-617 |
2.91e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 68.58 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNRYSVAYaaQKP--WLLNATV 477
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVF--QNPdnQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 478 EENITFGsPFNkqrykavtdaCSLQPDidllpfgdqtEIGERGIN-----------------LSGGQRQRICVARALYQN 540
Cdd:PRK13633 104 EEDVAFG-PEN----------LGIPPE----------EIRERVDEslkkvgmyeyrrhaphlLSGGQKQRVAIAGILAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 541 TNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIqTKDVEL 617
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNT-IKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI-FKEVEM 237
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
400-605 |
2.99e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 68.46 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN-----VNESEPSFEATR-------RNRYSVAYAA 467
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlVRDKDGQLKVADknqlrllRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 468 QKPWLlNATVEENI------TFGSPFNKQRYKAVTdacslqpdidllpFGDQTEIGERG-----INLSGGQRQRICVARA 536
Cdd:PRK10619 101 FNLWS-HMTVLENVmeapiqVLGLSKQEARERAVK-------------YLAKVGIDERAqgkypVHLSGGQQQRVSIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 537 LYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREG 605
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDPELVGEVLR--IMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEG 234
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
400-610 |
3.46e-12 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 67.71 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLL--LAILGEMQ----TLEGKvhwsNVNESEPSFEATRRNrysVAYAAQK---- 469
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLrcINLLEEPDsgtiTVDGE----DLTDSKKDINKLRRK---VGMVFQQfnlf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 470 PwllNATVEENITFGsP---FNKQRYKAVTDAcslqpdIDLLpfgDQTEIGERG----INLSGGQRQRICVARALYQNTN 542
Cdd:COG1126 90 P---HLTVLENVTLA-PikvKKMSKAEAEERA------MELL---ERVGLADKAdaypAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1786986074 543 IVFLDDPFSALDIHLSdhlmQE--GILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 610
Cdd:COG1126 157 VMLFDEPTSALDPELV----GEvlDVMRDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
404-584 |
3.53e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 67.68 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 404 DIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ------TLEGKVHwsnvNESEPSfeatrrnRYSVAYAAQKPWLLN-AT 476
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTpasgslTLNGQDH----TTTPPS-------RRPVSMLFQENNLFShLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 477 VEENITFG-------SPFNKQRYKAVTDACSLQPDIDLLPfgdqteiGErginLSGGQRQRICVARALYQNTNIVFLDDP 549
Cdd:PRK10771 88 VAQNIGLGlnpglklNAAQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 1786986074 550 FSALDihlsDHLMQEgILKFLQD--DKR--TLVLVTHKL 584
Cdd:PRK10771 157 FSALD----PALRQE-MLTLVSQvcQERqlTLLMVSHSL 190
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
400-586 |
3.62e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 67.81 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI--LGEMQTLEGKVHWSNVNESEPSFEATRRNRYSVAyaaQKPWLL-NAT 476
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITSGDLIVDGLKVNDPKVDERLIRQEAGMVF---QQFYLFpHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 477 VEENITFGSpfnkQRYKAVTDACSLQPDIDLLpfgDQTEIGERG----INLSGGQRQRICVARALYQNTNIVFLDDPFSA 552
Cdd:PRK09493 94 ALENVMFGP----LRVRGASKEEAEKQARELL---AKVGLAERAhhypSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190
....*....|....*....|....*....|....
gi 1786986074 553 LDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQY 586
Cdd:PRK09493 167 LDPELRHEVLK--VMQDLAEEGMTMVIVTHEIGF 198
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1023-1248 |
4.14e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 67.30 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENnlkpvLK-HVKAYIKPGQKVGICGRTGSGKSSL-SL-AFFRMVDifDGKIVIDGIDisklplHTL--- 1096
Cdd:PRK10771 2 LKLTDITWLYHH-----LPmRFDLTVERGERVAILGPSGAGKSTLlNLiAGFLTPA--SGSLTLNGQD------HTTtpp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1097 -RSRLSIILQDPILFSG-SIRFN----LDPECKCTDDRLWEALEIAQ---LKNMVKSLPGGLdavvteggenfSVGQRQL 1167
Cdd:PRK10771 69 sRRPVSMLFQENNLFSHlTVAQNiglgLNPGLKLNAAQREKLHAIARqmgIEDLLARLPGQL-----------SGGQRQR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1168 FCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRV---HTILTADLVIVmkRGNILeYDTP- 1241
Cdd:PRK10771 138 VALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLedaARIAPRSLVVA--DGRIA-WDGPt 214
|
....*..
gi 1786986074 1242 ESLLAQE 1248
Cdd:PRK10771 215 DELLSGK 221
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
396-582 |
5.38e-12 |
|
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: 66.23 E-value: 5.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 396 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRrnrySVAYAAQKPWLLNA 475
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE----NILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 476 -TVEENITFGSPFNKQRYKAVTDACslqpdidllpfgdqTEIGERGIN------LSGGQRQRICVARALYQNTNIVFLDD 548
Cdd:TIGR01189 88 lSALENLHFWAAIHGGAQRTIEDAL--------------AAVGLTGFEdlpaaqLSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1786986074 549 PFSALDI--------HLSDHLMQEGIlkflqddkrtLVLVTH 582
Cdd:TIGR01189 154 PTTALDKagvallagLLRAHLARGGI----------VLLTTH 185
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
400-610 |
5.71e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 69.29 E-value: 5.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRR-NRYSVAYAAQKPWLL-NATV 477
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvRRKKIAMVFQSFALMpHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 478 EENITFGS-----PFNKQRYKAVtDACSlQPDIDLLPFGDQTEigerginLSGGQRQRICVARALYQNTNIVFLDDPFSA 552
Cdd:PRK10070 124 LDNTAFGMelagiNAEERREKAL-DALR-QVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1786986074 553 LDIHLSDHlMQEGILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDI 610
Cdd:PRK10070 195 LDPLIRTE-MQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1023-1248 |
5.95e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 68.57 E-value: 5.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLSlaffRMVDIFD----GKIVIDGIDISKLP---L 1093
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLI----RCINLLErptsGSVLVDGVDLTALSereL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1094 HTLRSRLSIILQDpilfsgsirFNLdpeckctddrLWE---------ALEIA-----QLKNMVKSLpggLDAVVTEGGEN 1159
Cdd:COG1135 78 RAARRKIGMIFQH---------FNL----------LSSrtvaenvalPLEIAgvpkaEIRKRVAEL---LELVGLSDKAD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1160 F-----SVGQRQLFCLARAFVRKSSILIMDEATASIDMA-TENIL---QKVvmtafADR---TVVTIAHRVHTILT-ADL 1226
Cdd:COG1135 136 AypsqlSGGQKQRVGIARALANNPKVLLCDEATSALDPEtTRSILdllKDI-----NRElglTIVLITHEMDVVRRiCDR 210
|
250 260
....*....|....*....|....*....
gi 1786986074 1227 VIVMKRGNILEYDT-------PESLLAQE 1248
Cdd:COG1135 211 VAVLENGRIVEQGPvldvfanPQSELTRR 239
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
383-606 |
6.01e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 66.96 E-value: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 383 AIKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI-LGEMQTlEGKVHWSNVN---ESEPSFEATRR 458
Cdd:PRK11124 2 SIQLNGINCFYGAHQA-LFDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPR-SGTLNIAGNHfdfSKTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 459 NRYSVAYAAQK----PWLlnaTVEENITfGSP-----FNKQryKAVTDACSLQPDIDLLPFGDQTEIgergiNLSGGQRQ 529
Cdd:PRK11124 80 LRRNVGMVFQQynlwPHL---TVQQNLI-EAPcrvlgLSKD--QALARAEKLLERLRLKPYADRFPL-----HLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1786986074 530 RICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGT 606
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQIVS--IIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGD 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1023-1235 |
6.78e-12 |
|
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: 66.12 E-value: 6.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDGIDISKLPlhtLRS 1098
Cdd:cd03301 1 VELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIagleEPTSGRIYIGGRDVTDLP---PKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1099 R-LSIILQDPILFS-----GSIRFNLD----PEcKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1168
Cdd:cd03301 72 RdIAMVFQNYALYPhmtvyDNIAFGLKlrkvPK-DEIDERVREVAELLQIEHLLDRKPKQL-----------SGGQRQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1786986074 1169 CLARAFVRKSSILIMDEATASID------MATE-NILQKVVmtafaDRTVVTIAH-RVHTILTADLVIVMKRGNI 1235
Cdd:cd03301 140 ALGRAIVREPKVFLMDEPLSNLDaklrvqMRAElKRLQQRL-----GTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
386-610 |
7.14e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 68.07 E-value: 7.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 386 VTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLllailGEMQTL-----EGKVHWSNVNESEPSFEATRRNR 460
Cdd:PRK11308 17 VKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTL-----ARLLTMietptGGELYYQGQDLLKADPEAQKLLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 461 YSVAYAAQKPW-LLN------ATVEE----NITFGSPFNKQRYKAVTDACSLQPD-IDLLP--FgdqteigerginlSGG 526
Cdd:PRK11308 92 QKIQIVFQNPYgSLNprkkvgQILEEplliNTSLSAAERREKALAMMAKVGLRPEhYDRYPhmF-------------SGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 527 QRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKRTL----VLVTHKLQYLTH-ADWIIAMKDGSV 601
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALDVSV-----QAQVLNLMMDLQQELglsyVFISHDLSVVEHiADEVMVMYLGRC 233
|
....*....
gi 1786986074 602 LREGTLKDI 610
Cdd:PRK11308 234 VEKGTKEQI 242
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1023-1249 |
8.54e-12 |
|
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: 66.65 E-value: 8.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSL-SLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 1101
Cdd:COG1119 4 LELRNVTVRRGG--KTILDDISWTVKPGEHWAILGPNGAGKSTLlSLITGDLPPTYGNDVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1102 II---LQDPIL------------FSGSI-RF-NLDPECKCTDDRLWEALEIAQLKNM-VKSLpggldavvteggenfSVG 1163
Cdd:COG1119 82 LVspaLQLRFPrdetvldvvlsgFFDSIgLYrEPTDEQRERARELLELLGLAHLADRpFGTL---------------SQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1164 QRQLFCLARAFVRKSSILIMDEATASIDM-ATENILQkvVMTAFA---DRTVVTIAHRVHTILTA-DLVIVMKRGNILEY 1238
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLgARELLLA--LLDKLAaegAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAA 224
|
250
....*....|.
gi 1786986074 1239 DTPESLLAQEN 1249
Cdd:COG1119 225 GPKEEVLTSEN 235
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
400-619 |
1.28e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 66.69 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsNVNESEpsFEATRRN------RYSVAYAAQKP--W 471
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSV---RVDDTL--ITSTSKNkdikqiRKKVGLVFQFPesQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 472 LLNATVEENITFGsPFNKQRYKAVTDACSLQpdiDLLPFGDQTEIGERG-INLSGGQRQRICVARALYQNTNIVFLDDPF 550
Cdd:PRK13649 98 LFEETVLKDVAFG-PQNFGVSQEEAEALARE---KLALVGISESLFEKNpFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 551 SALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDIqTKDVELYE 619
Cdd:PRK13649 174 AGLDPKGRKELMT--LFKKLHQSGMTIVLVTHLMDDVAnYADFVYVLEKGKLVLSGKPKDI-FQDVDFLE 240
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1023-1221 |
1.41e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 66.21 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-----FDGKIVIDGIDI--SKLPLHT 1095
Cdd:PRK14258 8 IKVNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELesevrVEGRVEFFNQNIyeRRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1096 LRSRLSIILQDPILFSGSIRFNLDPECKCT--------DDRLWEALEIAQLKNMVKSlpggldaVVTEGGENFSVGQRQL 1167
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAYGVKIVgwrpkleiDDIVESALKDADLWDEIKH-------KIHKSALDLSGGQQQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1786986074 1168 FCLARAFVRKSSILIMDEATASID----MATENILQKVVMTafADRTVVTIAHRVHTI 1221
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLR--SELTMVIVSHNLHQV 214
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1023-1237 |
1.46e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 64.86 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LAFFRMVDIFDGKIVIDGIDISKLPLHtLRSRL 1100
Cdd:cd03217 1 LEIKDLHVSVGG--KEILKGVNLTIKKGEVHALMGPNGSGKSTLAktIMGHPKYEVTEGEILFKGEDITDLPPE-ERARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1101 SIIL--QDPILFSGsirfnldpeckctddrlwealeiAQLKNMVKSLpggldavvtegGENFSVGQRQLFCLARAFVRKS 1178
Cdd:cd03217 78 GIFLafQYPPEIPG-----------------------VKNADFLRYV-----------NEGFSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 1179 SILIMDEATASIDMATENILQKVVMT-AFADRTVVTIAH--RVHTILTADLVIVMKRGNILE 1237
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVK 185
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
396-615 |
1.51e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 66.35 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 396 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKVHWSNVNESEPSFEATRRnrySVAYAAQK-PWLL 473
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLL-KMLGRHQPpSEGEILLDAQPLESWSSKAFAR---KVAYLPQQlPAAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 474 NATVEENITFG--------SPFNKQRYKAVTDACSLqpdIDLLPFGdqteigERGIN-LSGGQRQRICVARALYQNTNIV 544
Cdd:PRK10575 99 GMTVRELVAIGrypwhgalGRFGAADREKVEEAISL---VGLKPLA------HRLVDsLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 545 FLDDPFSALDI-HLSDHLMQegILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDIQTKDV 615
Cdd:PRK10575 170 LLDEPTSALDIaHQVDVLAL--VHRLSQERGLTVIAVLHDINMAArYCDYLVALRGGEMIAQGTPAELMRGET 240
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1023-1256 |
1.61e-11 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 65.72 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHtlRS 1098
Cdd:cd03300 1 IELENVSKFYGG--FVALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLIAGFEtptsGEILLDGKDITNLPPH--KR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1099 RLSIILQDPILFS-----GSIRFNLD----PEcKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 1169
Cdd:cd03300 73 PVNTVFQNYALFPhltvfENIAFGLRlkklPK-AEIKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1170 LARAFVRKSSILIMDEATASIDMATENILQkVVMTAFADRTVVTIAHRVH----TILTADLVIVMKRGNILEYDTPESLL 1245
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDLKLRKDMQ-LELKRLQKELGITFVFVTHdqeeALTMSDRIAVMNKGKIQQIGTPEEIY 219
|
250
....*....|..
gi 1786986074 1246 AQENGVF-ASFV 1256
Cdd:cd03300 220 EEPANRFvADFI 231
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
392-620 |
1.67e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 67.18 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 392 SWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN--VNESEPsfeatrRNRySVA----- 464
Cdd:PRK11650 12 SYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvVNELEP------ADR-DIAmvfqn 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 465 YAaqkpwlL--NATVEENITFG-------SPFNKQRYKAVTDACSLQPDIDLLPfgdqteigeRgiNLSGGQRQRICVAR 535
Cdd:PRK11650 85 YA------LypHMSVRENMAYGlkirgmpKAEIEERVAEAARILELEPLLDRKP---------R--ELSGGQRQRVAMGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 536 ALYQNTNiVFL-DDPFSALDIHLSDHLMQEgiLKFLQddKR---TLVLVTH-KLQYLTHADWIIAMKDGSVLREGTlkdi 610
Cdd:PRK11650 148 AIVREPA-VFLfDEPLSNLDAKLRVQMRLE--IQRLH--RRlktTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGT---- 218
|
250
....*....|
gi 1786986074 611 qtkDVELYEH 620
Cdd:PRK11650 219 ---PVEVYEK 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
400-607 |
1.68e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 65.61 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKVHWS--NVNESEPSFEATRRNRySVAYAAQKPWLL-NA 475
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLL-HLLGGLDTpTSGDVIFNgqPMSKLSSAAKAELRNQ-KLGFIYQFHHLLpDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 476 TVEENITFgsPF---NKQRYKAVTDACSLqpdidLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 552
Cdd:PRK11629 103 TALENVAM--PLligKKKPAEINSRALEM-----LAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1786986074 553 LDIHLSDHLMQegILKFLQDDKRTLVL-VTHKLQYLTHADWIIAMKDGSVLREGTL 607
Cdd:PRK11629 176 LDARNADSIFQ--LLGELNRLQGTAFLvVTHDLQLAKRMSRQLEMRDGRLTAELSL 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
403-605 |
2.13e-11 |
|
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: 65.08 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 403 IDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNRYSVAYAAQKPWLlnaTVEENIT 482
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVSDSTGLYDRL---TARENLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 483 FGSPFNKQRYKAVTDAcsLQPDIDLLPFGDQTEigERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLM 562
Cdd:cd03266 101 YFAGLYGLKGDELTAR--LEELADRLGMEELLD--RRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1786986074 563 QegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREG 605
Cdd:cd03266 177 E--FIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
402-610 |
2.16e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 67.05 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 402 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEatRRNRYSV--AYAAqkpwLLNATVEE 479
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVfqSYAL----FPHMSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 480 NITFG-------SPFNKQRykaVTDACSLqpdIDLLPFGDqteigeRGIN-LSGGQRQRICVARALYQNTNIVFLDDPFS 551
Cdd:PRK11432 98 NVGYGlkmlgvpKEERKQR---VKEALEL---VDLAGFED------RYVDqISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 552 ALDIHLSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKDI 610
Cdd:PRK11432 166 NLDANLRRS-MREKIRELQQQFNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
401-582 |
2.32e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.44 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 401 SNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNvnesepsfEATRRNRysVAYAAQKPWL--LNA--- 475
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG--------EPIRRQR--DEYHQDLLYLghQPGikt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 476 --TVEENITFgspfnkqrykavtdACSLQPDIDllpfGDQT-----EIGERGI------NLSGGQRQRICVARALYQNTN 542
Cdd:PRK13538 88 elTALENLRF--------------YQRLHGPGD----DEALwealaQVGLAGFedvpvrQLSAGQQRRVALARLWLTRAP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1786986074 543 IVFLDDPFSALDI--------HLSDHLMQEGIlkflqddkrtLVLVTH 582
Cdd:PRK13538 150 LWILDEPFTAIDKqgvarleaLLAQHAEQGGM----------VILTTH 187
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1022-1256 |
2.73e-11 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 65.05 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1022 EIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLhtlRSR-L 1100
Cdd:cd03296 2 SIEVRNVSKRFGD--FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV---QERnV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1101 SIILQDPILF-----SGSIRFNLD-------PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1168
Cdd:cd03296 77 GFVFQHYALFrhmtvFDNVAFGLRvkprserPPEAEIRAKVHELLKLVQLDWLADRYPAQL-----------SGGQRQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1169 CLARAFVRKSSILIMDEATASIDMATENILQKVVmTAFADRTVVTIAHRVH----TILTADLVIVMKRGNILEYDTPESL 1244
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWL-RRLHDELHVTTVFVTHdqeeALEVADRVVVMNKGRIEQVGTPDEV 224
|
250
....*....|...
gi 1786986074 1245 LAQENGVF-ASFV 1256
Cdd:cd03296 225 YDHPASPFvYSFL 237
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1023-1248 |
3.46e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 64.86 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-----FDGKIVIDGIDISKLPLHTL- 1096
Cdd:PRK14267 5 IETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELneearVEGEVRLFGRNIYSPDVDPIe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1097 -RSRLSIILQDPILF---------SGSIRFN-LDPECKCTDDRLWEALEIAQL----KNMVKSLPGgldavvteggeNFS 1161
Cdd:PRK14267 83 vRREVGMVFQYPNPFphltiydnvAIGVKLNgLVKSKKELDERVEWALKKAALwdevKDRLNDYPS-----------NLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1162 VGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR-VHTILTADLVIVMKRGNILE--- 1237
Cdd:PRK14267 152 GGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEvgp 231
|
250
....*....|....*
gi 1786986074 1238 ----YDTPESLLAQE 1248
Cdd:PRK14267 232 trkvFENPEHELTEK 246
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1023-1246 |
3.66e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 65.50 E-value: 3.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 1101
Cdd:PRK13642 5 LEVENLVFKYEKESDvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1102 IILQDPI-LFSGSIrfnldpeckcTDDRLWEALEIAQL--KNMVKSLPGGLDAV-----VTEGGENFSVGQRQLFCLARA 1173
Cdd:PRK13642 85 MVFQNPDnQFVGAT----------VEDDVAFGMENQGIprEEMIKRVDEALLAVnmldfKTREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1786986074 1174 FVRKSSILIMDEATASIDMATENILQKVVMtAFADR---TVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLA 1246
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIH-EIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1049-1237 |
3.87e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.57 E-value: 3.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1049 PGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSRLSIILQDPILfsgsirfNLDPEcKCT 1125
Cdd:PRK10261 349 PGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYA-------SLDPR-QTV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1126 DDRLWEALEIAQL---KNMVKSLPGGLDAV------VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE- 1195
Cdd:PRK10261 421 GDSIMEPLRVHGLlpgKAAAARVAWLLERVgllpehAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRg 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 1196 ---NI---LQKVVMTAFA----DRTVVT-IAHRvhtiltadlVIVMKRGNILE 1237
Cdd:PRK10261 501 qiiNLlldLQRDFGIAYLfishDMAVVErISHR---------VAVMYLGQIVE 544
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1039-1248 |
4.08e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.53 E-value: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1039 VLKHVKAYIKPGQKVGICGRTGSGKSSlslAFFRMVDIF---DGKIVIDGIDISKLPLHTlRSRLSI--ILQDPILFSG- 1112
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTT---TFYMVVGIVprdAGNIIIDDEDISLLPLHA-RARRGIgyLPQEASIFRRl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1113 ----------SIRFNLDPECKctDDRLWEALEIAQLKNMVKSLpggldavvtegGENFSVGQRQLFCLARAFVRKSSILI 1182
Cdd:PRK10895 94 svydnlmavlQIRDDLSAEQR--EDRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1786986074 1183 MDEATASIDMATENILQKVVmTAFADR--TVVTIAHRV-HTILTADLVIVMKRGNILEYDTPESLLAQE 1248
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRII-EHLRDSglGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
378-601 |
5.46e-11 |
|
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: 64.88 E-value: 5.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 378 ETEDIAIKVTNGyfswgsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTlEGKVHWSNVNESEPSFEATR 457
Cdd:cd03289 4 TVKDLTAKYTEG------GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 458 RnrySVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARAL 537
Cdd:cd03289 77 K---AFGVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786986074 538 YQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSV 601
Cdd:cd03289 154 LSKAKILLLDEPSAHLD-PITYQVIRKTLKQAFAD--CTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1023-1249 |
6.23e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 64.82 E-value: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1102
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1103 ILQDP--ILFS---------GSIRFNLDPECkcTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLA 1171
Cdd:PRK13652 83 VFQNPddQIFSptveqdiafGPINLGLDEET--VAHRVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1172 RAFVRKSSILIMDEATASID-MATENILQkvVMTAFADR---TVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLA 1246
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDpQGVKELID--FLNDLPETygmTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFL 227
|
...
gi 1786986074 1247 QEN 1249
Cdd:PRK13652 228 QPD 230
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
382-621 |
6.44e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 64.85 E-value: 6.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 382 IAIKVTNGYFSWGSGLAT--LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS----NVNESEPSFEA 455
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAgyhiTPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 456 TRRnRYSVAYAAQKPWLLNATVEENITFGsPFN------KQRYKAVT--DACSLQPD-IDLLPFgdqteigergiNLSGG 526
Cdd:PRK13641 83 LRK-KVSLVFQFPEAQLFENTVLKDVEFG-PKNfgfsedEAKEKALKwlKKVGLSEDlISKSPF-----------ELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 527 QRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREG 605
Cdd:PRK13641 150 QMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQ--LFKDYQKAGHTVILVTHNMDDVAeYADDVLVLEHGKLIKHA 227
|
250
....*....|....*.
gi 1786986074 606 TLKDIQTKDVELYEHW 621
Cdd:PRK13641 228 SPKEIFSDKEWLKKHY 243
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
384-619 |
7.78e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 64.34 E-value: 7.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWG--SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsNVNESEPSFEATRRNRY 461
Cdd:PRK13642 5 LEVENLVFKYEkeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKV---KIDGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 462 SVAYAAQKP--WLLNATVEENITFGSPFN----KQRYKAVTDACSLqpdIDLLPFgdQTEIGERginLSGGQRQRICVAR 535
Cdd:PRK13642 82 KIGMVFQNPdnQFVGATVEDDVAFGMENQgiprEEMIKRVDEALLA---VNMLDF--KTREPAR---LSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 536 ALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVL-VTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKD 614
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMR--VIHEIKEKYQLTVLsITHDLDEAASSDRILVMKAGEIIKEAAPSELFATS 231
|
....*
gi 1786986074 615 VELYE 619
Cdd:PRK13642 232 EDMVE 236
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
400-582 |
8.63e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.86 E-value: 8.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnvnesepsfeaTRRNRYSVAYAAQKPWLL-NATVE 478
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV--------------SIPKGLRIGYLPQEPPLDdDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 479 ENITFG-SPFNK--QRYKAVTDACSlQPDIDLLPFGD-QTEIGER----------------GI----------NLSGGQR 528
Cdd:COG0488 80 DTVLDGdAELRAleAELEELEAKLA-EPDEDLERLAElQEEFEALggweaearaeeilsglGFpeedldrpvsELSGGWR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 529 QRICVARALYQNTNIVFLDDPFSALDIhlsdhlmqEGIL---KFLQDDKRTLVLVTH 582
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDL--------ESIEwleEFLKNYPGTVLVVSH 207
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
400-600 |
1.14e-10 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 61.96 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAIlgemqtlegkvhwsnvnesepsFEATRRNRYsvayaaqkpwllnatvee 479
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG----------------------LYASGKARL------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 480 nITFGSPFNKQRYKAVTdacSLQPDIDL----LPFGDQTEigergiNLSGGQRQRICVARALYQNT-NIVF-LDDPFSAL 553
Cdd:cd03238 51 -ISFLPKFSRNKLIFID---QLQFLIDVglgyLTLGQKLS------TLSGGELQRVKLASELFSEPpGTLFiLDEPSTGL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1786986074 554 DIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGS 600
Cdd:cd03238 121 HQQDINQLLEV--IKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
395-615 |
1.27e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.58 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 395 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNRYSVAYaaQKPWLLN 474
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGIIY--QELSVID 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 475 A-TVEENITFGS-PFNKQRYKAVTDACSLQ--PDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 550
Cdd:PRK09700 94 ElTVLENLYIGRhLTKKVCGVNIIDWREMRvrAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1786986074 551 SALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKDV 615
Cdd:PRK09700 174 SSLTNKEVDYLFL--IMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDVSNDDI 237
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
747-916 |
1.29e-10 |
|
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: 63.98 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 747 VAGFSILCGAGIFLclvTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLT 826
Cdd:cd18552 45 IIGLFLLRGLASYL---QTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 827 RSTLLCLSAIGMISYA----TPVFLVALLPLGVAFYFIQKYFRVASKDLQE-LDDSTQlpllcHFSETAEGLTTIRAFRH 901
Cdd:cd18552 122 RDPLTVIGLLGVLFYLdwklTLIALVVLPLAALPIRRIGKRLRKISRRSQEsMGDLTS-----VLQETLSGIRVVKAFGA 196
|
170
....*....|....*
gi 1786986074 902 ETRFKQRMLELTDTN 916
Cdd:cd18552 197 EDYEIKRFRKANERL 211
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
397-627 |
1.46e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 64.10 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 397 LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNV-------NESEPSFEATR------RNRYSV 463
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIyigdkknNHELITNPYSKkiknfkELRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 464 AYAAQKP--WLLNATVEENITFGsPFN--------KQRYKAVTDACSLQPD-IDLLPFGdqteigerginLSGGQRQRIC 532
Cdd:PRK13631 119 SMVFQFPeyQLFKDTIEKDIMFG-PVAlgvkkseaKKLAKFYLNKMGLDDSyLERSPFG-----------LSGGQKRRVA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 533 VARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDIQ 611
Cdd:PRK13631 187 IAGILAIQPEILIFDEPTAGLDPKGEHEMMQ--LILDAKANNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
250
....*....|....*.
gi 1786986074 612 TkDVELYEHWKTLMNR 627
Cdd:PRK13631 265 T-DQHIINSTSIQVPR 279
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
396-633 |
1.50e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 65.21 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 396 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG--EMQTLEGKV--HWSNVNESE----PSFEAT----------- 456
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyHVALCEKCGyverPSKVGEpcpvcggtlep 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 457 -------------RRNRYSVAYAAQKPWLL--NATVEENITfgSPFNKQRYKAVTdacSLQPDIDLLpfgDQTEIGER-- 519
Cdd:TIGR03269 92 eevdfwnlsdklrRRIRKRIAIMLQRTFALygDDTVLDNVL--EALEEIGYEGKE---AVGRAVDLI---EMVQLSHRit 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 520 --GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDhLMQEGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAM 596
Cdd:TIGR03269 164 hiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEEAVKASGISMVLTSHWPEVIEDlSDKAIWL 242
|
250 260 270
....*....|....*....|....*....|....*..
gi 1786986074 597 KDGSVLREGTLKDIQTKDVELYEhwktlMNRQDQELE 633
Cdd:TIGR03269 243 ENGEIKEEGTPDEVVAVFMEGVS-----EVEKECEVE 274
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1035-1244 |
2.02e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.96 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1035 NLKPVlKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL---PLHTLRSRLSIILQDPiLFS 1111
Cdd:PRK15079 33 TLKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMkddEWRAVRSDIQMIFQDP-LAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1112 GSIRFNLdpeckctDDRLWEALEI-------AQLKNMVKSL---PGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSIL 1181
Cdd:PRK15079 111 LNPRMTI-------GEIIAEPLRTyhpklsrQEVKDRVKAMmlkVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1182 IMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHR---VHTIltADLVIVMKRGNILEYDTPESL 1244
Cdd:PRK15079 184 ICDEPVSALDVSIQaqvvNLLQQ--LQREMGLSLIFIAHDlavVKHI--SDRVLVMYLGHAVELGTYDEV 249
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1027-1246 |
2.14e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.10 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1027 DLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG--IDISKLPLHTLRSRLSIIL 1104
Cdd:PRK13638 6 DLWFRYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1105 QDP---ILFS---GSIRFNLD----PECKCTDdRLWEALEIAQLKNMVKslpggldavvtEGGENFSVGQRQLFCLARAF 1174
Cdd:PRK13638 84 QDPeqqIFYTdidSDIAFSLRnlgvPEAEITR-RVDEALTLVDAQHFRH-----------QPIQCLSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 1175 VRKSSILIMDEATASIDMATEN----ILQKVVMTAfadRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLA 1246
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTqmiaIIRRIVAQG---NHVIISSHDIDLIYeISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
384-605 |
2.66e-10 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 61.44 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGSGLAtLSNIDIRIPTGqLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEAtrrnRYSV 463
Cdd:cd03264 1 LQLENLTKRYGKKRA-LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKL----RRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 464 AYAAQKP-WLLNATVEENITF-----GSPfNKQRYKAVTDACSLqpdIDLLPFGDQtEIGErginLSGGQRQRICVARAL 537
Cdd:cd03264 75 GYLPQEFgVYPNFTVREFLDYiawlkGIP-SKEVKARVDEVLEL---VNLGDRAKK-KIGS----LSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 538 YQNTNIVFLDDPFSALD----IHLSDHLMQEGilkflqdDKRTLVLVTHKLQ-YLTHADWIIAMKDGSVLREG 605
Cdd:cd03264 146 VGDPSILIVDEPTAGLDpeerIRFRNLLSELG-------EDRIVILSTHIVEdVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1055-1241 |
2.95e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 63.33 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1055 ICGRTGSGKSSLSLAF----------FRMVDIFDG-KIVIDGIDISKLP-----LHTLRSRLSIILQDP--ILFSGSIRf 1116
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFnglikskygtIQVGDIYIGdKKNNHELITNPYSkkiknFKELRRRVSMVFQFPeyQLFKDTIE- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1117 nldpeckctDDRLWEALEIAQLKNMVKSLPG------GLDAVVTEGGE-NFSVGQRQLFCLARAFVRKSSILIMDEATAS 1189
Cdd:PRK13631 136 ---------KDIMFGPVALGVKKSEAKKLAKfylnkmGLDDSYLERSPfGLSGGQKRRVAIAGILAIQPEILIFDEPTAG 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1786986074 1190 IDMATENILQKVVMTAFAD-RTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTP 1241
Cdd:PRK13631 207 LDPKGEHEMMQLILDAKANnKTVFVITHTMEHVLeVADEVIVMDKGKILKTGTP 260
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
381-601 |
2.99e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 64.32 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 381 DIAIKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW-SNVNesepsfeatrrn 459
Cdd:COG0488 313 KKVLELEGLSKSYG-DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETVK------------ 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 460 rysVAYAAQKPWLL--NATVEENITFGSPFNKQRYkaVTDACSlqpdiDLLpF-GDQ--TEIGergiNLSGGQRQRICVA 534
Cdd:COG0488 380 ---IGYFDQHQEELdpDKTVLDELRDGAPGGTEQE--VRGYLG-----RFL-FsGDDafKPVG----VLSGGEKARLALA 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1786986074 535 RALYQNTNIVFLDDPFSALDIHlsdhlMQEGILKFLQDDKRTLVLVTHKLQYL-THADWIIAMKDGSV 601
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIE-----TLEALEEALDDFPGTVLLVSHDRYFLdRVATRILEFEDGGV 507
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
523-610 |
3.48e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 62.16 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 523 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD---HLMQEgilkfLQDDKR-TLVLVTHKLQYLTH-ADWIIAMK 597
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSqiiNLMLE-----LQEKLGiSYIYVSQHLGIVKHiSDKVLVMH 224
|
90
....*....|...
gi 1786986074 598 DGSVLREGTLKDI 610
Cdd:COG4167 225 QGEVVEYGKTAEV 237
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
776-904 |
4.15e-10 |
|
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: 62.53 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 776 AKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATP-VFLVALL--- 851
Cdd:cd18573 73 VARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPkLTLVMLLvvp 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1786986074 852 PLGVAFYFIQKYFRVASKDLQE-LDDSTQLpllchfsetAE----GLTTIRAFRHETR 904
Cdd:cd18573 153 PIAVGAVFYGRYVRKLSKQVQDaLADATKV---------AEerlsNIRTVRAFAAERK 201
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1040-1246 |
4.52e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 61.73 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1040 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPI----------- 1108
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPStslnprqrisq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1109 LFSGSIRFNLDPECKCTDDRLWEAL-EIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEAT 1187
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREKQIIETLrQVGLLPDHASYYPHML-----------APGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 1188 ASIDMATENILQKVVMTAFADRTVVTIAHRVHTILT---ADLVIVMKRGNILEYDTPESLLA 1246
Cdd:PRK15112 178 ASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMkhiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1023-1248 |
5.52e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 62.94 E-value: 5.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1102
Cdd:PRK09536 4 IDVSDLSVEFGD--TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1103 ILQDPilfsgSIRFNLDPE----------------CKCTDDRLWE-ALEiaqlknmvkslPGGLDAVVTEGGENFSVGQR 1165
Cdd:PRK09536 82 VPQDT-----SLSFEFDVRqvvemgrtphrsrfdtWTETDRAAVErAME-----------RTGVAQFADRPVTSLSGGER 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1166 QLFCLARAFVRKSSILIMDEATASIDMATE-NILQKVVMTAFADRTVVTIAHRVHtiLTA---DLVIVMKRGNILEYDTP 1241
Cdd:PRK09536 146 QRVLLARALAQATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLD--LAArycDELVLLADGRVRAAGPP 223
|
....*..
gi 1786986074 1242 ESLLAQE 1248
Cdd:PRK09536 224 ADVLTAD 230
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1024-1194 |
6.84e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 60.19 E-value: 6.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1024 KIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLsLAF--------FRmvdiFDGKIVIDGIDISKLPlhT 1095
Cdd:COG4136 3 SLENLTITLGG--RPLLAPLSLTVAPGEILTLMGPSGSGKSTL-LAAiagtlspaFS----ASGEVLLNGRRLTALP--A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1096 LRSRLSIILQDPILFS-----GSIRFNLDPECKCTD--DRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1168
Cdd:COG4136 74 EQRRIGILFQDDLLFPhlsvgENLAFALPPTIGRAQrrARVEQALEEAGLAGFADRDPATL-----------SGGQRARV 142
|
170 180
....*....|....*....|....*.
gi 1786986074 1169 CLARAFVRKSSILIMDEATASIDMAT 1194
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAAL 168
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
989-1251 |
7.16e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.07 E-value: 7.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 989 AVKKVNSFltmESENYEGTMDPSQVPEHWPQegeIKIHDLCVRYENN---LKPVlkhvKAYIKPGQKVGICGRTGSGKSS 1065
Cdd:PRK10522 295 AFNKLNKL---ALAPYKAEFPRPQAFPDWQT---LELRNVTFAYQDNgfsVGPI----NLTIKRGELLFLIGGNGSGKST 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1066 LSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSirfnLDPECKCTDDRLWEA-LEIAQLKNMVKs 1144
Cdd:PRK10522 365 LAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALVEKwLERLKMAHKLE- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1145 lpggldavvTEGGE----NFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRV 1218
Cdd:PRK10522 440 ---------LEDGRisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHDD 510
|
250 260 270
....*....|....*....|....*....|...
gi 1786986074 1219 HTILTADLVIVMKRGNILEYDTPESLLAQENGV 1251
Cdd:PRK10522 511 HYFIHADRLLEMRNGQLSELTGEERDAASRDAV 543
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
399-610 |
7.74e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 61.18 E-value: 7.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 399 TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsNVNESEPSFEATRRNRYSVAYAAQKP--WLLNAT 476
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI---TVGGMVLSEETVWDVRRQVGMVFQNPdnQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 477 VEENITFGSPFN----KQRYKAVTDACSLqpdIDLLPFGDQTEIgergiNLSGGQRQRICVARALYQNTNIVFLDDPFSA 552
Cdd:PRK13635 99 VQDDVAFGLENIgvprEEMVERVDQALRQ---VGMEDFLNREPH-----RLSGGQKQRVAIAGVLALQPDIIILDEATSM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1786986074 553 LDIHLSDHLMqeGILKFLQDDKRTLVL-VTHKLQYLTHADWIIAMKDGSVLREGTLKDI 610
Cdd:PRK13635 171 LDPRGRREVL--ETVRQLKEQKGITVLsITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
397-599 |
1.13e-09 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 60.14 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 397 LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW-----SNVNESEpsfEATRRNRySVAYAAQKPW 471
Cdd:COG4181 25 LTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLagqdlFALDEDA---RARLRAR-HVGFVFQSFQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 472 LLNA-TVEENIT-----FGSPFNKQRYKAVTDACSLQPDIDLLPFGdqteigerginLSGGQRQRICVARALYQNTNIVF 545
Cdd:COG4181 101 LLPTlTALENVMlplelAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILF 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1786986074 546 LDDPFSALDIHLSDHLMQegiLKF-LQDDKR-TLVLVTHKLQYLTHADWIIAMKDG 599
Cdd:COG4181 170 ADEPTGNLDAATGEQIID---LLFeLNRERGtTLVLVTHDPALAARCDRVLRLRAG 222
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1022-1216 |
1.14e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 60.57 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1022 EIKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIF-----DGKIVIDGIDI--SKLPLH 1094
Cdd:PRK14243 10 VLRTENLNVYYGSFL--AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIpgfrvEGKVTFHGKNLyaPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1095 TLRSRLSIILQDPILFSGSIRFNLDPECKCT------DDRLWEALEIAQLKNMVKSlpggldaVVTEGGENFSVGQRQLF 1168
Cdd:PRK14243 88 EVRRRIGMVFQKPNPFPKSIYDNIAYGARINgykgdmDELVERSLRQAALWDEVKD-------KLKQSGLSLSGGQQQRL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1786986074 1169 CLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAH 1216
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTH 208
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1037-1256 |
1.22e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 61.78 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1037 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHtlRSRLSIILQDPILF-- 1110
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTL----LRMLAGFEqptaGQIMLDGVDLSHVPPY--QRPINMMFQSYALFph 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1111 ---SGSIRFNLD----PECKCTDdRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIM 1183
Cdd:PRK11607 106 mtvEQNIAFGLKqdklPKAEIAS-RVNEMLGLVHMQEFAKRKPHQL-----------SGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1184 DEATASID------MATE--NILQKVVMTAfadrtvVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQENGVF-A 1253
Cdd:PRK11607 174 DEPMGALDkklrdrMQLEvvDILERVGVTC------VMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIYEHPTTRYsA 247
|
...
gi 1786986074 1254 SFV 1256
Cdd:PRK11607 248 EFI 250
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
700-916 |
1.23e-09 |
|
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: 61.03 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 700 GGFFLLILMIFSKLLKHSVIVAIDYWLATWtseysinntgkadqtyYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNL 779
Cdd:cd07346 11 ATALGLALPLLTKLLIDDVIPAGDLSLLLW----------------IALLLLLLALLRALLSYLRRYLAARLGQRVVFDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 780 HHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIG-MISYATPVFLVALLPL---GV 855
Cdd:cd07346 75 RRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALViLFYLNWKLTLVALLLLplyVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 856 AFYFIQKYFRVASKDLQE-LDDSTQlpllcHFSETAEGLTTIRAFRHETRFKQRMLELTDTN 916
Cdd:cd07346 155 ILRYFRRRIRKASREVREsLAELSA-----FLQESLSGIRVVKAFAAEEREIERFREANRDL 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
966-1247 |
1.44e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 62.13 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 966 ALTITNYLNWVVRNLADLEVQM--GAVKKVNSFLTMESENYEGTMDPSQVPEHWPQEGEIKIHDLCVRYENNLKPVLKHV 1043
Cdd:TIGR03269 221 SMVLTSHWPEVIEDLSDKAIWLenGEIKEEGTPDEVVAVFMEGVSEVEKECEVEVGEPIIKVRNVSKRYISVDRGVVKAV 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1044 KAY---IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVI----DGIDISKlPLHTLRSR----LSIILQDPILFSG 1112
Cdd:TIGR03269 301 DNVsleVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTK-PGPDGRGRakryIGILHQEYDLYPH 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1113 SIRFnldpeckctdDRLWEAL------EIAQLKNMVKSLPGGLD-----AVVTEGGENFSVGQRQLFCLARAFVRKSSIL 1181
Cdd:TIGR03269 380 RTVL----------DNLTEAIglelpdELARMKAVITLKMVGFDeekaeEILDKYPDELSEGERHRVALAQVLIKEPRIV 449
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1786986074 1182 IMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLAQ 1247
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFVLdVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
400-610 |
1.48e-09 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 60.84 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG---EMQTLEGKVHWSNVN---ESEPSFEATRRNRYSV----AYAAqk 469
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDllkLSEKELRKIRGREIQMifqdPMTS-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 470 pwlLN------ATVEENITFGSPFNK-QRYKAVtdacslqpdIDLLpfgdqteigER-GIN------------LSGGQRQ 529
Cdd:COG0444 99 ---LNpvmtvgDQIAEPLRIHGGLSKaEARERA---------IELL---------ERvGLPdperrldrypheLSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 530 RICVARALYQNTNIVFLDDPFSALDIhlsdhLMQEGILKFLQDDKR----TLVLVTHKL---QYLthADWIIAMKDGSVL 602
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDV-----TIQAQILNLLKDLQRelglAILFITHDLgvvAEI--ADRVAVMYAGRIV 230
|
....*...
gi 1786986074 603 REGTLKDI 610
Cdd:COG0444 231 EEGPVEEL 238
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
702-914 |
1.50e-09 |
|
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: 60.88 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 702 FFLLILMIFSKLLkhsvIVAIDYWLATWTSEYSINNTGKADQTY-YVAGFSILCGAGIFLCLVTSLTVEWMGLTAA---- 776
Cdd:cd18547 2 ILVIILAIISTLL----SVLGPYLLGKAIDLIIEGLGGGGGVDFsGLLRILLLLLGLYLLSALFSYLQNRLMARVSqrtv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 777 KNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIG-MISYATPVFLVALLPLGV 855
Cdd:cd18547 78 YDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLImMLYISPLLTLIVLVTVPL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1786986074 856 AFYFI-------QKYFRVASKDLQELDDSTQlpllchfsETAEGLTTIRAFRHETRFKQRMLELTD 914
Cdd:cd18547 158 SLLVTkfiakrsQKYFRKQQKALGELNGYIE--------EMISGQKVVKAFNREEEAIEEFDEINE 215
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1023-1216 |
1.57e-09 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 57.46 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmvdifdgkividgidisklplhtlrsrLSI 1102
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTL---------------------------------LKL 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1103 ILQDPILFSGSIRFNldpeckctddrlwEALEIAQLknmvkslpggldavvteggENFSVGQRQLFCLARAFVRKSSILI 1182
Cdd:cd03221 46 IAGELEPDEGIVTWG-------------STVKIGYF-------------------EQLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....*...
gi 1786986074 1183 MDEATASIDMAT----ENILQKvvmtaFaDRTVVTIAH 1216
Cdd:cd03221 94 LDEPTNHLDLESiealEEALKE-----Y-PGTVILVSH 125
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1040-1251 |
1.77e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.56 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1040 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP----LHTLRSRLSIILQDP-------- 1107
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRPVRKRIGMVFQFPesqlfedt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1108 ----ILFsGSIRFNLDPEcKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIM 1183
Cdd:PRK13646 103 vereIIF-GPKNFKMNLD-EVKNYAHRLLMDLGFSRDVMSQSPFQM-----------SGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1786986074 1184 DEATASIDMATenilQKVVMTAFA------DRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQENGV 1251
Cdd:PRK13646 170 DEPTAGLDPQS----KRQVMRLLKslqtdeNKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKDKKKL 240
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
402-610 |
1.85e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 61.04 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 402 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN--VNESEP--SFEATRRNrysVAYAAQKPWLL-NAT 476
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvLFDAEKgiCLPPEKRR---IGYVFQDARLFpHYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 477 VEENITFG-SPFNKQRYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 555
Cdd:PRK11144 93 VRGNLRYGmAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 556 HLSDHLMQegILKFLQDDKRTLVL-VTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 610
Cdd:PRK11144 162 PRKRELLP--YLERLAREINIPILyVSHSLDEILRlADRVVVLEQGKVKAFGPLEEV 216
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1022-1248 |
1.87e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.03 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1022 EIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 1101
Cdd:PRK11231 2 TLRTENLTVGYGT--KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1102 IILQDPILFSG-SIR----------FNLDPECKCTDDRLWE-ALEIAQLKNMVkslpgglDAVVTEggenFSVGQRQLFC 1169
Cdd:PRK11231 80 LLPQHHLTPEGiTVRelvaygrspwLSLWGRLSAEDNARVNqAMEQTRINHLA-------DRRLTD----LSGGQRQRAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1170 LARAFVRKSSILIMDEATASIDMATENILQKVV-MTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQ 1247
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMrELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMTP 228
|
.
gi 1786986074 1248 E 1248
Cdd:PRK11231 229 G 229
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
400-610 |
2.16e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 60.48 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLL--LAILgEMQTlEGKVHWSNVNESEPSFEATRRNRYSVAYAAQKPWLLNA-T 476
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIrcINLL-ERPT-SGSVLVDGVDLTALSERELRAARRKIGMIFQHFNLLSSrT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 477 VEENITF-----GSPfNKQRYKAVTDacslqpdidLLPFgdqTEIGERG----INLSGGQRQRICVARALYQNTNIVFLD 547
Cdd:COG1135 99 VAENVALpleiaGVP-KAEIRKRVAE---------LLEL---VGLSDKAdaypSQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 548 DPFSALDIHLSDhlmqeGILKFLQDDKR----TLVLVTH------KLqylthADWIIAMKDGSVLREGTLKDI 610
Cdd:COG1135 166 EATSALDPETTR-----SILDLLKDINRelglTIVLITHemdvvrRI-----CDRVAVLENGRIVEQGPVLDV 228
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1038-1245 |
2.33e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 59.34 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1038 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDI--SKLPLHTLRSRLSIILQdpilfsgsiR 1115
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEAGMVFQ---------Q 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1116 FNLDPECKCTDDRLWEALEI-----AQLKNMVKSLPG--GLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA 1188
Cdd:PRK09493 86 FYLFPHLTALENVMFGPLRVrgaskEEAEKQARELLAkvGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 1189 SIDmatENILQKV--VMTAFADR----TVVT----IAHRVHTILtadlvIVMKRGNILEYDTPESLL 1245
Cdd:PRK09493 166 ALD---PELRHEVlkVMQDLAEEgmtmVIVTheigFAEKVASRL-----IFIDKGRIAEDGDPQVLI 224
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
400-620 |
2.36e-09 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 59.33 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEM-----QTLE------GKVHWSNVnesepsfeatrRNRYSVAYAA- 467
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpptygNDVRlfgerrGGEDVWEL-----------RKRIGLVSPAl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 468 QKPWLLNATVEENIT---FGSPFnkqRYKAVTDAcslqpDI----DLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQ 539
Cdd:COG1119 88 QLRFPRDETVLDVVLsgfFDSIG---LYREPTDE-----QRerarELLELLGLAHLADRPFGtLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 540 NTNIVFLDDPFSALDIHlsdhlMQEGILKFL----QDDKRTLVLVTHKLQYL----THAdwiIAMKDGSVLREGTLKDIQ 611
Cdd:COG1119 160 DPELLILDEPTAGLDLG-----ARELLLALLdklaAEGAPTLVLVTHHVEEIppgiTHV---LLLKDGRVVAAGPKEEVL 231
|
250
....*....|.
gi 1786986074 612 TKDV--ELYEH 620
Cdd:COG1119 232 TSENlsEAFGL 242
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
397-604 |
2.55e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.02 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 397 LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW-----SNVNESEpsfEATRRNRySVAYAAQKPW 471
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvgqplHQMDEEA---RAKLRAK-HVGFVFQSFM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 472 L---LNATveENITFGSPFnkqryKAVTDACSLQPDIDLLpfgDQTEIGER----GINLSGGQRQRICVARALYQNTNIV 544
Cdd:PRK10584 99 LiptLNAL--ENVELPALL-----RGESSRQSRNGAKALL---EQLGLGKRldhlPAQLSGGEQQRVALARAFNGRPDVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 545 FLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSvLRE 604
Cdd:PRK10584 169 FADEPTGNLDRQTGDKIA-DLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQ-LQE 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1038-1235 |
2.63e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.22 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1038 PVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LAFFRMVDIfdGKIVIDGIDISKL-PLHTLRSRLSIILQDPILFSG-- 1112
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMkiIAGIVPPDS--GTLEIGGNPCARLtPAKAHQLGIYLVPQEPLLFPNls 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1113 ---SIRFNLdPEckctddrlwEALEIAQLKNMVKSLPGGLDAVVTEGgeNFSVGQRQLFCLARAFVRKSSILIMDEATAS 1189
Cdd:PRK15439 103 vkeNILFGL-PK---------RQASMQKMKQLLAALGCQLDLDSSAG--SLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1786986074 1190 IDMA-TENILQKVVMTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNI 1235
Cdd:PRK15439 171 LTPAeTERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTI 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
400-620 |
2.73e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 58.31 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEmqtlegkvhwsnvnesePSFEATRRnrySVAYAAQKpwLLNATVEE 479
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-----------------PKYEVTEG---EILFKGED--ITDLPPEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 480 N------ITFGSPFnkqRYKAVTDAcslqpdiDLLpfgdqteigeRGIN--LSGGQRQRICVARALYQNTNIVFLDDPFS 551
Cdd:cd03217 74 RarlgifLAFQYPP---EIPGVKNA-------DFL----------RYVNegFSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 552 ALDIhlsDHL-MQEGILKFLQDDKRTLVLVTHKLQYLTH--ADWIIAMKDGSVLREGtlkdiqtkDVELYEH 620
Cdd:cd03217 134 GLDI---DALrLVAEVINKLREEGKSVLIITHYQRLLDYikPDRVHVLYDGRIVKSG--------DKELALE 194
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
351-582 |
3.31e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 60.23 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 351 PKTINRKQPGRYHLDSYEQSTRRlrPAETEDIAIKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI 430
Cdd:PRK13536 11 PRRLELSPIERKHQGISEAKASI--PGSMSTVAIDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 431 LGEMQTLEGKVhwSNVNESEPSfeATRRNRYSVAYAAQKPWL-LNATVEEN-ITFGSPF--NKQRYKAVTDAcslqpdid 506
Cdd:PRK13536 88 LGMTSPDAGKI--TVLGVPVPA--RARLARARIGVVPQFDNLdLEFTVRENlLVFGRYFgmSTREIEAVIPS-------- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 507 LLPFGD-QTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDDKrTLVLVTH 582
Cdd:PRK13536 156 LLEFARlESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARHLIWERLRSLLARGK-TILLTTH 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1039-1251 |
4.68e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 58.94 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1039 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG--IDISKLPLHTLRSRLSIILQDP--ILFSGSI 1114
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTVGIVFQNPddQLFAPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1115 R-------FNLdpeckctddrlweALEIAQLKNMVKSlpgGLDAVVTEGGEN-----FSVGQRQLFCLARAFVRKSSILI 1182
Cdd:PRK13639 97 EedvafgpLNL-------------GLSKEEVEKRVKE---ALKAVGMEGFENkpphhLSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1786986074 1183 MDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTI-LTADLVIVMKRGNILEYDTPESLLAQENGV 1251
Cdd:PRK13639 161 LDEPTSGLDpMGASQIMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDIETI 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
395-616 |
5.02e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.33 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 395 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG--EMQTLEGKVHWS-------NVNESEpsfeatrrnRYSVAY 465
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyPHGTYEGEIIFEgeelqasNIRDTE---------RAGIAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 466 AAQKPWLL-NATVEENITFGS---PFNKQRYKAVTDACS-----LQPDIDllpfgdqteIGERGINLSGGQRQRICVARA 536
Cdd:PRK13549 87 IHQELALVkELSVLENIFLGNeitPGGIMDYDAMYLRAQkllaqLKLDIN---------PATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 537 LYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLqylthaDWIIAMKDG-SVLREGtlKDIQTKDV 615
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLD--IIRDLKAHGIACIYISHKL------NEVKAISDTiCVIRDG--RHIGTRPA 227
|
.
gi 1786986074 616 E 616
Cdd:PRK13549 228 A 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
399-601 |
5.49e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 58.97 E-value: 5.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 399 TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnVNESEPSFEATRRNRYSVAYAAQKP--WLLNAT 476
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQII---IDGDLLTEENVWDIRHKIGMVFQNPdnQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 477 VEENITFGSPfNK-----QRYKAVTDACSLqpdIDLLPFGDQTEIgergiNLSGGQRQRICVARALYQNTNIVFLDDPFS 551
Cdd:PRK13650 99 VEDDVAFGLE-NKgipheEMKERVNEALEL---VGMQDFKEREPA-----RLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1786986074 552 ALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSV 601
Cdd:PRK13650 170 MLDPEGRLELIKT-IKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
398-612 |
5.62e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.52 E-value: 5.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 398 ATLSNIDIRIPTGQLTMIVGQVGCGKSSLL------LAILGEMQTLEGKVHWsnVNESEPSFEATRRnRYSVAYAAQKP- 470
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLkvlnrlIEIYDSKIKVDGKVLY--FGKDIFQIDAIKL-RKEVGMVFQQPn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 471 WLLNATVEENITFgsPF------NKQRYKAVTDACslqpdidLLPFGDQTEIGER----GINLSGGQRQRICVARALYQN 540
Cdd:PRK14246 101 PFPHLSIYDNIAY--PLkshgikEKREIKKIVEEC-------LRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1786986074 541 TNIVFLDDPFSALDIhlsdhLMQEGILKFLQDDKR--TLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQT 612
Cdd:PRK14246 172 PKVLLMDEPTSMIDI-----VNSQAIEKLITELKNeiAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFT 241
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1023-1242 |
6.54e-09 |
|
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: 57.83 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYeNNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIF----DGKIVIDGIDISKLPLHtLRS 1098
Cdd:cd03219 1 LEVRGLTKRF-GGLV-ALDDVSFSVRPGEIHGLIGPNGAGKTTL----FNLISGFlrptSGSVLFDGEDITGLPPH-EIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1099 RLSII--LQDPILFSG-SIRFNLD-----------------PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvtegge 1158
Cdd:cd03219 74 RLGIGrtFQIPRLFPElTVLENVMvaaqartgsglllararREEREARERAEELLERVGLADLADRPAGEL--------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1159 nfSVGQRQLFCLARAFVRKSSILIMDEATASIDMA-TENILQKVVMTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNIL 1236
Cdd:cd03219 145 --SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEeTEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVI 222
|
....*.
gi 1786986074 1237 EYDTPE 1242
Cdd:cd03219 223 AEGTPD 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
396-605 |
6.75e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.92 E-value: 6.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 396 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnVNESEPSFEATRRNRYS-VAYAAQKPWLL- 473
Cdd:PRK11288 16 GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIL---IDGQEMRFASTTAALAAgVAIIYQELHLVp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 474 NATVEENITFGS-P-----FNKQRYKAVTDACSLQPDIDLLPfgdQTEIGErginLSGGQRQRICVARALYQNTNIVFLD 547
Cdd:PRK11288 93 EMTVAENLYLGQlPhkggiVNRRLLNYEAREQLEHLGVDIDP---DTPLKY----LSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1786986074 548 DPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLqylthaDWIIAMKDG-SVLREG 605
Cdd:PRK11288 166 EPTSSLSAREIEQLFR--VIRELRAEGRVILYVSHRM------EEIFALCDAiTVFKDG 216
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
396-616 |
7.94e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 59.84 E-value: 7.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 396 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG--EMQTLEGKVHWSNVNESEPSFEATRRNRYSVAYaaQKPWLL 473
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSPLKASNIRDTERAGIVIIH--QELTLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 474 -NATVEENITFGS----PFNKQRYKAVTDAC-SLQPDIDLLPFGDQTEIGERGinlsGGQRQRICVARALYQNTNIVFLD 547
Cdd:TIGR02633 91 pELSVAENIFLGNeitlPGGRMAYNAMYLRAkNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 548 DPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLqylthaDWIIAMKDG-SVLREGtlKDIQTKDVE 616
Cdd:TIGR02633 167 EPSSSLTEKETEILLD--IIRDLKAHGVACVYISHKL------NEVKAVCDTiCVIRDG--QHVATKDMS 226
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
395-554 |
8.29e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 56.89 E-value: 8.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 395 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI---LGEMQTLEGKVHWSNVnesePSFEATRRNRYSVAYAAQK-- 469
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGI----PYKEFAEKYPGEIIYVSEEdv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 470 --PWLlnaTVEENITFgspfnkqrykavtdACSLQpdidllpfGDQTEigeRGInlSGGQRQRICVARALYQNTNIVFLD 547
Cdd:cd03233 94 hfPTL---TVRETLDF--------------ALRCK--------GNEFV---RGI--SGGERKRVSIAEALVSRASVLCWD 143
|
....*..
gi 1786986074 548 DPFSALD 554
Cdd:cd03233 144 NSTRGLD 150
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1023-1194 |
8.40e-09 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 57.44 E-value: 8.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDIFD-GKIVIDGIDISKL---PLHTL 1096
Cdd:COG4181 9 IELRGLTKTVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTL-LGLLAGLDRPTsGTVRLAGQDLFALdedARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1097 RSR-LSIILQD---------------PILFSGsirfnlDPECKctdDRLWEALEIAQLKNMVKSLPGGLdavvtEGGEnf 1160
Cdd:COG4181 88 RARhVGFVFQSfqllptltalenvmlPLELAG------RRDAR---ARARALLERVGLGHRLDHYPAQL-----SGGE-- 151
|
170 180 190
....*....|....*....|....*....|....
gi 1786986074 1161 svgqRQLFCLARAFVRKSSILIMDEATASIDMAT 1194
Cdd:COG4181 152 ----QQRVALARAFATEPAILFADEPTGNLDAAT 181
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
415-658 |
8.51e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.56 E-value: 8.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 415 IVGQVGCGKSSLLLAILGEMQTLEGkvhwsnvnesepsfEATRRNRYSVAYAAQKPWL-LNATVEENITFGSPFNKQ--- 490
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNG--------------EARPQPGIKVGYLPQEPQLdPTKTVRENVEEGVAEIKDald 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 491 RYKAVTDACS---------------LQPDIDL------------------LPFGDQtEIGergiNLSGGQRQRICVARAL 537
Cdd:TIGR03719 102 RFNEISAKYAepdadfdklaaeqaeLQEIIDAadawdldsqleiamdalrCPPWDA-DVT----KLSGGERRRVALCRLL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 538 YQNTNIVFLDDPfsaldihlSDHLMQEGIL---KFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDG-SVLREGTlkdiqt 612
Cdd:TIGR03719 177 LSKPDMLLLDEP--------TNHLDAESVAwleRHLQEYPGTVVAVTHDRYFLDNvAGWILELDRGrGIPWEGN------ 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1786986074 613 kdvelYEHW---KTlmNRQDQElEKDMEADQTTLERKT--LRRAMYSREAK 658
Cdd:TIGR03719 243 -----YSSWleqKQ--KRLEQE-EKEESARQKTLKRELewVRQSPKGRQAK 285
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
383-605 |
1.17e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 57.80 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 383 AIKVTNGYfswgSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNV---NESEPSFEATRRN 459
Cdd:PRK14271 24 AVNLTLGF----AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVllgGRSIFNYRDVLEF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 460 RYSVAYAAQKPWLLNATVEENITFGSPFNK----QRYKAVTDACSLQPDI-DLLpfgdQTEIGERGINLSGGQRQRICVA 534
Cdd:PRK14271 100 RRRVGMLFQRPNPFPMSIMDNVLAGVRAHKlvprKEFRGVAQARLTEVGLwDAV----KDRLSDSPFRLSGGQQQLLCLA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786986074 535 RALYQNTNIVFLDDPFSALDIHLSdhlmqEGILKFLQD--DKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREG 605
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTT-----EKIEEFIRSlaDRLTVIIVTHNLaQAARISDRAALFFDGRLVEEG 244
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
378-614 |
1.64e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 57.51 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 378 ETEDIAikvtngyFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnVNESEP-SFEAT 456
Cdd:PRK13652 5 ETRDLC-------YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSV----LIRGEPiTKENI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 457 RRNRYSVAYAAQKP--WLLNATVEENITFGsPFN--------KQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGG 526
Cdd:PRK13652 74 REVRKFVGLVFQNPddQIFSPTVEQDIAFG-PINlgldeetvAHRVSSALHMLGLEELRDRVPH-----------HLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 527 QRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLmqegiLKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMKDGSV 601
Cdd:PRK13652 142 EKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKEL-----IDFLNDLPEtygmTVIFSTHQLDLVPEmADYIYVMDKGRI 216
|
250
....*....|...
gi 1786986074 602 LREGTLKDIQTKD 614
Cdd:PRK13652 217 VAYGTVEEIFLQP 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1047-1255 |
1.74e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 57.81 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1047 IKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDGIDISKlplHTLRSR-LSIILQDPILFSG-SIRFNL-- 1118
Cdd:PRK11432 29 IKQGTMVTLLGPSGCGKTTV----LRLVagleKPTEGQIFIDGEDVTH---RSIQQRdICMVFQSYALFPHmSLGENVgy 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1119 --------DPECKctdDRLWEALEIAQLKnmvkslpGGLDAVVteggENFSVGQRQLFCLARAFVRKSSILIMDEATASI 1190
Cdd:PRK11432 102 glkmlgvpKEERK---QRVKEALELVDLA-------GFEDRYV----DQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1786986074 1191 D------MaTENI--LQKVVmtafaDRTVVTIAH-RVHTILTADLVIVMKRGNILEYDTPESLLAQENGVF-ASF 1255
Cdd:PRK11432 168 DanlrrsM-REKIreLQQQF-----NITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFmASF 236
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
400-610 |
1.89e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 57.89 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI-LGEMQTlEGKVHWSNVNESEPSFEATRRNRYSVAYAAQKPWLLNA-TV 477
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCInLLERPT-SGRVLVDGQDLTALSEKELRKARRQIGMIFQHFNLLSSrTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 478 EENITF-----GSPfNKQRYKAVTDacslqpdidLLPFGDQTEIGER-GINLSGGQRQRICVARALYQNTNIVFLDDPFS 551
Cdd:PRK11153 100 FDNVALplelaGTP-KAEIKARVTE---------LLELVGLSDKADRyPAQLSGGQKQRVAIARALASNPKVLLCDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786986074 552 ALDIHLSDhlmqeGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 610
Cdd:PRK11153 170 ALDPATTR-----SILELLKDINRelglTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSEV 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
400-604 |
1.93e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 57.02 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNES-EPSFeatRRNRYsVAYAAQKPwLL----N 474
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTkLPEY---KRAKY-IGRVFQDP-MMgtapS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 475 ATVEENI----------TFGSPFNKQRYKAVTDACSlqpDIDL-----LpfgdQTEIGergiNLSGGQRQRICVARALYQ 539
Cdd:COG1101 97 MTIEENLalayrrgkrrGLRRGLTKKRRELFRELLA---TLGLglenrL----DTKVG----LLSGGQRQALSLLMATLT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1786986074 540 NTNIVFLDDPFSALDIHLSDHLMQegiL--KFLQDDKRTLVLVTHKLQY-LTHADWIIAMKDGSVLRE 604
Cdd:COG1101 166 KPKLLLLDEHTAALDPKTAALVLE---LteKIVEENNLTTLMVTHNMEQaLDYGNRLIMMHEGRIILD 230
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1023-1249 |
2.04e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 56.70 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1102
Cdd:PRK13548 3 LEARNLSVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1103 ILQDPIL-FSGS----IRFNLDP--ECKCTDDRLWEA----LEIAQLKNmvKSLPggldavVTEGGENfsvgQR-QlfcL 1170
Cdd:PRK13548 81 LPQHSSLsFPFTveevVAMGRAPhgLSRAEDDALVAAalaqVDLAHLAG--RDYP------QLSGGEQ----QRvQ---L 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1171 ARAFVR------KSSILIMDEATASIDMATenilQKVVMTA---FADR---TVVTIAHRVH-TILTADLVIVMKRGNILE 1237
Cdd:PRK13548 146 ARVLAQlwepdgPPRWLLLDEPTSALDLAH----QHHVLRLarqLAHErglAVIVVLHDLNlAARYADRIVLLHQGRLVA 221
|
250
....*....|..
gi 1786986074 1238 YDTPESLLAQEN 1249
Cdd:PRK13548 222 DGTPAEVLTPET 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
372-610 |
2.10e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 58.28 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 372 RRLRPAETEDIAIKVTN---GYFSWGSGLA-TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH----- 442
Cdd:TIGR03269 268 EKECEVEVGEPIIKVRNvskRYISVDRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgd 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 443 -WsnVNESEPSFEATRRNRYSVAYAAQKPWLL-NATVEENIT----FGSPFNKQRYKAVtdacslqpdIDLLPFGDQTEI 516
Cdd:TIGR03269 348 eW--VDMTKPGPDGRGRAKRYIGILHQEYDLYpHRTVLDNLTeaigLELPDELARMKAV---------ITLKMVGFDEEK 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 517 GERGIN-----LSGGQRQRICVARALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQY-LTHA 590
Cdd:TIGR03269 417 AEEILDkypdeLSEGERHRVALAQVLIKEPRIVILDEPTGTMD-PITKVDVTHSILKAREEMEQTFIIVSHDMDFvLDVC 495
|
250 260
....*....|....*....|
gi 1786986074 591 DWIIAMKDGSVLREGTLKDI 610
Cdd:TIGR03269 496 DRAALMRDGKIVKIGDPEEI 515
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1023-1239 |
2.12e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 56.71 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYenNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-----FDGKIVIDGIDISKLPLHT-- 1095
Cdd:PRK14239 6 LQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIYSPRTDTvd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1096 LRSRLSIILQDPILFSGSI--------RFNLDPECKCTDDRLWEALEIAQLKNMVKSlpggldaVVTEGGENFSVGQRQL 1167
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIyenvvyglRLKGIKDKQVLDEAVEKSLKGASIWDEVKD-------RLHDSALGLSGGQQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 1168 FCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTI-LTADLVIVMKRGNILEYD 1239
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYN 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
400-610 |
2.87e-08 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 56.01 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESepSFEATRRNRYSVAYAAQKPWLL-NATVE 478
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT--KLPMHKRARLGIGYLPQEASIFrKLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 479 ENI-----TFGSPFNKQRYKAVtdacSLQPDIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 553
Cdd:cd03218 94 ENIlavleIRGLSKKEREEKLE----ELLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 554 D-IHLSDhlMQEgILKFLQdDKRTLVLVT----HKLQYLTHADWIIamKDGSVLREGTLKDI 610
Cdd:cd03218 165 DpIAVQD--IQK-IIKILK-DRGIGVLITdhnvRETLSITDRAYII--YEGKVLAEGTPEEI 220
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1050-1247 |
3.26e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 57.04 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1050 GQKVGICGRTGSGKSSLSLAFFRMV---DIFDGKIVIDGIDISKLP---LHTLRS-RLSIILQDPILfsgsirfNLDPEC 1122
Cdd:PRK09473 42 GETLGIVGESGSGKSQTAFALMGLLaanGRIGGSATFNGREILNLPekeLNKLRAeQISMIFQDPMT-------SLNPYM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1123 KCTDdrlwEALEIAQL-KNMVKSLP-----GGLDAV--------VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA 1188
Cdd:PRK09473 115 RVGE----QLMEVLMLhKGMSKAEAfeesvRMLDAVkmpearkrMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 1189 SID-------MATENILQKVVMTAfadrtVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLAQ 1247
Cdd:PRK09473 191 ALDvtvqaqiMTLLNELKREFNTA-----IIMITHDLGVVAgICDKVLVMYAGRTMEYGNARDVFYQ 252
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
406-593 |
4.19e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 55.84 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 406 RIPT---GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV----HWSNV------NESEPSFEATRRNRYSVA----YAAQ 468
Cdd:cd03236 19 RLPVpreGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppDWDEIldefrgSELQNYFTKLLEGDVKVIvkpqYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 469 KPWLLNATVEENITFGSPFNKQRYkaVTDACSLQPdidllpfgdqteIGERGI-NLSGGQRQRICVARALYQNTNIVFLD 547
Cdd:cd03236 99 IPKAVKGKVGELLKKKDERGKLDE--LVDQLELRH------------VLDRNIdQLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1786986074 548 DPFSALDIHlsDHLMQEGILKFLQDDKRTLVLVTHKLQYLTH-ADWI 593
Cdd:cd03236 165 EPSSYLDIK--QRLNAARLIRELAEDDNYVLVVEHDLAVLDYlSDYI 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1023-1246 |
4.59e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 57.12 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDIFD---GKIV----------------- 1082
Cdd:TIGR03269 1 IEVKNLTKKFDG--KEVLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDQYEptsGRIIyhvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1083 ----------------IDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFnLDPECKCTDDRLWEALE----IAQLKNMV 1142
Cdd:TIGR03269 78 vgepcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTV-LDNVLEALEEIGYEGKEavgrAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1143 KslpggLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHT 1220
Cdd:TIGR03269 157 Q-----LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEV 231
|
250 260
....*....|....*....|....*..
gi 1786986074 1221 IL-TADLVIVMKRGNILEYDTPESLLA 1246
Cdd:TIGR03269 232 IEdLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1038-1242 |
4.64e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 57.34 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1038 PVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LA-FFRMvDifDGKIVIDGIDISKL-PLHTLRSRLSIILQDPILFSG- 1112
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMkiLSgVYQP-D--SGEILLDGEPVRFRsPRDAQAAGIAIIHQELNLVPNl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1113 SIRFNL------------DpeckctddrlWEALeIAQLKNMVKSLpgGLD----AVVteggENFSVGQRQLFCLARAFVR 1176
Cdd:COG1129 95 SVAENIflgreprrggliD----------WRAM-RRRARELLARL--GLDidpdTPV----GDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1786986074 1177 KSSILIMDEATASIDMA-TENILQkvVMTAFADR--TVVTIAHRVHTILT-ADLVIVMKRG-NILEYDTPE 1242
Cdd:COG1129 158 DARVLILDEPTASLTEReVERLFR--IIRRLKAQgvAIIYISHRLDEVFEiADRVTVLRDGrLVGTGPVAE 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1039-1242 |
5.12e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 56.63 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1039 VLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLplHTLRSRLSIILQDPILF---- 1110
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTL----LRIIAGLEhqtsGHIRFHGTDVSRL--HARDRKVGFVFQHYALFrhmt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1111 -SGSIRFNLD-------PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILI 1182
Cdd:PRK10851 91 vFDNIAFGLTvlprrerPNAAAIKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 1183 MDEATASIDMATENILQKVVMTAFADR--TVVTIAH-RVHTILTADLVIVMKRGNILEYDTPE 1242
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1027-1239 |
5.28e-08 |
|
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: 54.99 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1027 DLCVRYENNLKPVlkHVK-AYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDG---IDISK---LPLHt 1095
Cdd:cd03297 1 MLCVDIEKRLPDF--TLKiDFDLNEEVTGIFGASGAGKSTL----LRCIagleKPDGGTIVLNGtvlFDSRKkinLPPQ- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1096 lRSRLSIILQDPILFSG-SIRFNLD---PECKCTDDRLW--EALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 1169
Cdd:cd03297 74 -QRKIGLVFQQYALFPHlNVRENLAfglKRKRNREDRISvdELLDLLGLDHLLNRYPAQL-----------SGGEKQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 1170 LARAFVRKSSILIMDEATASIDMATENILQKVV--MTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYD 1239
Cdd:cd03297 142 LARALAAQPELLLLDEPFSALDRALRLQLLPELkqIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
400-606 |
6.23e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 55.31 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAIL---------------GEMQTLEGKVHWS---NVNESEP-----SFEAT 456
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLypalarrlhlkkeqpGNHDRIEGLEHIDkviVIDQSPIgrtprSNPAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 457 -------------------RRNR--YSVAYAAQK-PWLLNATVEENITFGSPFNKQRYKAVTdacsLQpDIDLlpfgDQT 514
Cdd:cd03271 91 ytgvfdeirelfcevckgkRYNRetLEVRYKGKSiADVLDMTVEEALEFFENIPKIARKLQT----LC-DVGL----GYI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 515 EIGERGINLSGGQRQRICVARALYQNTN---IVFLDDPFSALdiHLSD--HLMQegILKFLQDDKRTLVLVTHKLQYLTH 589
Cdd:cd03271 162 KLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGL--HFHDvkKLLE--VLQRLVDKGNTVVVIEHNLDVIKC 237
|
250 260
....*....|....*....|...
gi 1786986074 590 ADWIIAM------KDGSVLREGT 606
Cdd:cd03271 238 ADWIIDLgpeggdGGGQVVASGT 260
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1023-1248 |
6.63e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.03 E-value: 6.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LAFFRMVDIFDGKIVIDGIDISKLPlHTLRSRL 1100
Cdd:CHL00131 8 LEIKNLHASVNEN--EILKGLNLSINKGEIHAIMGPNGSGKSTLSkvIAGHPAYKILEGDILFKGESILDLE-PEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1101 SIIL--QDPILFSGS-----IRFNLDPECKCTDDRLWEALE----IAQLKNMVKSLPGGLDAVVTEGgenFSVGQRQLFC 1169
Cdd:CHL00131 85 GIFLafQYPIEIPGVsnadfLRLAYNSKRKFQGLPELDPLEfleiINEKLKLVGMDPSFLSRNVNEG---FSGGEKKRNE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1170 LARAFVRKSSILIMDEATASIDM-ATENILQKVVMTAFADRTVVTIAH--RVHTILTADLVIVMKRGNILEydTPESLLA 1246
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIdALKIIAEGINKLMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIK--TGDAELA 239
|
..
gi 1786986074 1247 QE 1248
Cdd:CHL00131 240 KE 241
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
400-605 |
7.18e-08 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 54.21 E-value: 7.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNvnesEPSFEATRRNrysVAYAAQKPWL-LNATVE 478
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG----KPLDIAARNR---IGYLPEERGLyPKMKVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 479 EN-ITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 557
Cdd:cd03269 89 DQlVYLAQLKGLKKEEARRRIDEWLERLELSEYANK-----RVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1786986074 558 SDHLMQEgiLKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREG 605
Cdd:cd03269 164 VELLKDV--IRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1030-1228 |
7.59e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.72 E-value: 7.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1030 VRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPIL 1109
Cdd:PRK10247 13 VGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1110 FSGSIRFNLD-PeckctddrlWEALEIA-QLKNMVKSLP--GGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDE 1185
Cdd:PRK10247 93 FGDTVYDNLIfP---------WQIRNQQpDPAIFLDDLErfALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1786986074 1186 ATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILTADLVI 1228
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVI 208
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
779-993 |
7.62e-08 |
|
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: 55.26 E-value: 7.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 779 LHHNLLNKiilgPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGM---ISYA-TPVFLVALLPLG 854
Cdd:cd18557 75 LFSSLLRQ----EIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIIlfiLSWKlTLVLLLVIPLLL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 855 VAFYFIQKYFRVASKDLQE-LDDSTQlpllcHFSETAEGLTTIRAF----RHETRFKQRMLELTDTNN---IAYLFLSAA 926
Cdd:cd18557 151 IASKIYGRYIRKLSKEVQDaLAKAGQ-----VAEESLSNIRTVRSFsaeeKEIRRYSEALDRSYRLARkkaLANALFQGI 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 927 NRWLEvrtdYLGACIVLtasiasisgSSNSGLVGLG----------LLYALTITNYLNWVVRNLADLEVQMGAVKKV 993
Cdd:cd18557 226 TSLLI----YLSLLLVL---------WYGGYLVLSGqltvgeltsfILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
79-317 |
8.30e-08 |
|
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: 55.25 E-value: 8.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 79 TFLQASYYVTIETGI--NLRGALlamiYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFLF-LCPNLWAMPVQIIM 155
Cdd:cd07346 56 SYLRRYLAARLGQRVvfDLRRDL----FRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSsGLLQLLSDVLTLIG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 156 GVILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWE----HIFCKSVE 231
Cdd:cd07346 130 ALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEereiERFREANR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 232 ETRMKELSSLKTFALYTSLSIFMNAAIPIAAVL--ATFVthayaSGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVK 309
Cdd:cd07346 210 DLRDANLRAARLSALFSPLIGLLTALGTALVLLygGYLV-----LQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQ 284
|
....*...
gi 1786986074 310 AIISVQKL 317
Cdd:cd07346 285 ALASLERI 292
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
384-606 |
8.93e-08 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 54.30 E-value: 8.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 384 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnvnesepSFEATRRN---R 460
Cdd:cd03265 1 IEVENLVKKYGDFEA-VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVA-------GHDVVREPrevR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 461 YSVAYAAQKPWLLNA-TVEENI-TFGSPFNKQRYKAVTDACSLQPDIDLLPFGDqteigERGINLSGGQRQRICVARALY 538
Cdd:cd03265 73 RRIGIVFQDLSVDDElTGWENLyIHARLYGVPGAERRERIDELLDFVGLLEAAD-----RLVKTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 539 QNTNIVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHklqYLTHA----DWIIAMKDGSVLREGT 606
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVW-EYIEKLKEEFGMTILLTTH---YMEEAeqlcDRVAIIDHGRIIAEGT 215
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
395-583 |
1.72e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 55.53 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 395 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGkvhwsnvnesePSFEATRRNRysVAYAAQKPWLLN 474
Cdd:TIGR00954 463 NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLF-RILGELWPVYG-----------GRLTKPAKGK--LFYVPQRPYMTL 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 475 ATVEENITFGSPFNKQRYKAVTDAcSLQPDIDLLpfgDQTEIGERGIN----------LSGGQRQRICVARALYQNTNIV 544
Cdd:TIGR00954 529 GTLRDQIIYPDSSEDMKRRGLSDK-DLEQILDNV---QLTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFA 604
|
170 180 190
....*....|....*....|....*....|....*....
gi 1786986074 545 FLDDPFSALDIHLSDHLMQegilkFLQDDKRTLVLVTHK 583
Cdd:TIGR00954 605 ILDECTSAVSVDVEGYMYR-----LCREFGITLFSVSHR 638
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
396-599 |
1.73e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 53.34 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 396 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNRYSVAYAAQKPWLL-N 474
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLmD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 475 ATVEENITF-----GSPFN--KQRYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQNTNIVFLD 547
Cdd:PRK10908 94 RTVYDNVAIpliiaGASGDdiRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLLAD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1786986074 548 DPFSALDIHLSdhlmqEGILKFLQDDKR---TLVLVTHKLQYLTHADW-IIAMKDG 599
Cdd:PRK10908 163 EPTGNLDDALS-----EGILRLFEEFNRvgvTVLMATHDIGLISRRSYrMLTLSDG 213
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1040-1223 |
1.94e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 53.34 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1040 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL---PLHTLRSRLSIILQD---------- 1106
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrEVPFLRRQIGMIFQDhhllmdrtvy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1107 -----PILFSGSirfnldpeckCTDD---RLWEALEIAQLKNMVKSLPggldaVVTEGGENFSVGqrqlfcLARAFVRKS 1178
Cdd:PRK10908 98 dnvaiPLIIAGA----------SGDDirrRVSAALDKVGLLDKAKNFP-----IQLSGGEQQRVG------IARAVVNKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 1179 SILIMDEATASIDMA-TENILQ------KVVMTAF-ADRTVVTIAHRVHTILT 1223
Cdd:PRK10908 157 AVLLADEPTGNLDDAlSEGILRlfeefnRVGVTVLmATHDIGLISRRSYRMLT 209
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
745-993 |
2.20e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 54.09 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 745 YYVAGFSILCG------AGIFLcLVTSLTVEWMGLTaaknLHHNLLNKiilgPIRFFDTTPLGLILNRFSADTNIIDQHI 818
Cdd:cd18572 40 LLLLLLSVLSGlfsglrGGCFS-YAGTRLVRRLRRD----LFRSLLRQ----DIAFFDATKTGELTSRLTSDCQKVSDPL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 819 PPTLESLTRSTLLCLSAIGMISYATP----VFLVALLPLGVAFYFIQKYFRVASKDLQElddstqlpLLCHFSETAE--- 891
Cdd:cd18572 111 STNLNVFLRNLVQLVGGLAFMFSLSWrltlLAFITVPVIALITKVYGRYYRKLSKEIQD--------ALAEANQVAEeal 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 892 -GLTTIRAFRHET----RFKQRMLELTDTN---NIAYLFLSAANRWLevrtDYLGACIVLtasiasisgssnsgLVGLGL 963
Cdd:cd18572 183 sNIRTVRSFATEErearRYERALDKALKLSvrqALAYAGYVAVNTLL----QNGTQVLVL--------------FYGGHL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1786986074 964 ---------------LYALTITNYLNWVVRNLADLEVQMGAVKKV 993
Cdd:cd18572 245 vlsgrmsagqlvtfmLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1025-1244 |
2.48e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.25 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1025 IHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKI-------------VIDGIDIS 1089
Cdd:PRK10261 15 VENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1090 KLPLHTLR-SRLSIILQDPIL-----------FSGSIRFNLD---PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvt 1154
Cdd:PRK10261 95 AAQMRHVRgADMAMIFQEPMTslnpvftvgeqIAESIRLHQGasrEEAMVEAKRMLDQVRIPEAQTILSRYPHQL----- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1155 eggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE-NILQKV-VMTAFADRTVVTIAHRVHTIL-TADLVIVMK 1231
Cdd:PRK10261 170 ------SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQaQILQLIkVLQKEMSMGVIFITHDMGVVAeIADRVLVMY 243
|
250
....*....|...
gi 1786986074 1232 RGNILEYDTPESL 1244
Cdd:PRK10261 244 QGEAVETGSVEQI 256
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1025-1216 |
2.63e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 54.69 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1025 IHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVID-GIDISKLPlhtlrsr 1099
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTL----LKILagelEPDSGEVSIPkGLRIGYLP------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1100 lsiilQDPILFSG-SIRFNL----------------------DPECKCTD-DRLWEALEIA---QLKNMVKSLPGGL--- 1149
Cdd:COG0488 68 -----QEPPLDDDlTVLDTVldgdaelraleaeleeleaklaEPDEDLERlAELQEEFEALggwEAEARAEEILSGLgfp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1150 ----DAVVTEggenFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT----ENILQK----VVMT----AFADRTVVT 1213
Cdd:COG0488 143 eedlDRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFLKNypgtVLVVshdrYFLDRVATR 218
|
...
gi 1786986074 1214 IAH 1216
Cdd:COG0488 219 ILE 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
402-582 |
2.65e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 54.04 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 402 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNvnesEPSFEATRRNRYSVAYAAQKPWL-LNATVEEN 480
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG----EPVPSRARHARQRVGVVPQFDNLdPDFTVREN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 481 I-TFGspfnkqRYKAVTDACSLQPDIDLLPFGD-----QTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALD 554
Cdd:PRK13537 101 LlVFG------RYFGLSAAAARALVPPLLEFAKlenkaDAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
170 180
....*....|....*....|....*...
gi 1786986074 555 IHlSDHLMQEGiLKFLQDDKRTLVLVTH 582
Cdd:PRK13537 171 PQ-ARHLMWER-LRSLLARGKTILLTTH 196
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1023-1107 |
2.86e-07 |
|
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: 54.69 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRY--ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVD----IFDGKIVIDGIDISKLPLHTL 1096
Cdd:COG4172 7 LSVEDLSVAFgqGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdpaaHPSGSILFDGQDLLGLSEREL 86
|
90
....*....|....*
gi 1786986074 1097 R----SRLSIILQDP 1107
Cdd:COG4172 87 RrirgNRIAMIFQEP 101
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
395-601 |
3.22e-07 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 51.66 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 395 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnVNESEPSFEATR-RNRYSVAYAA----QK 469
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEIT---LDGKPVTRRSPRdAIRAGIAYVPedrkRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 470 PWLLNATVEENITFGSPfnkqrykavtdacslqpdidllpfgdqteigerginLSGGQRQRICVARALYQNTNIVFLDDP 549
Cdd:cd03215 88 GLVLDLSVAENIALSSL------------------------------------LSGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 550 FSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSV 601
Cdd:cd03215 132 TRGVDVGAKAEIYR--LIRELADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
400-606 |
3.44e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.96 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEpsFEATRRNRYSVAYAAQKPWLLN-ATVE 478
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITD--WQTAKIMREAVAIVPEGRRVFSrMTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 479 ENITFGSPF-NKQRYKAvtdacSLQPDIDLLPFGDQTEIgERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD--- 554
Cdd:PRK11614 99 ENLAMGGFFaERDQFQE-----RIKWVYELFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLApii 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1786986074 555 -IHLSDHLMQegilkfLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGT 606
Cdd:PRK11614 173 iQQIFDTIEQ------LREQGMTIFLVEQNAnQALKLADRGYVLENGHVVLEDT 220
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
415-584 |
3.46e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 53.58 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 415 IVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNRYSVAYAAQKPWL-LNA--TVEENItfGSPFN--- 488
Cdd:COG4608 49 LVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQDPYAsLNPrmTVGDII--AEPLRihg 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 489 -------KQRYKAVTDACSLQPD-IDLLPFgdqteigErginLSGGQRQRICVARALYQNTNIVFLDDPFSALDihLSdh 560
Cdd:COG4608 127 laskaerRERVAELLELVGLRPEhADRYPH-------E----FSGGQRQRIGIARALALNPKLIVCDEPVSALD--VS-- 191
|
170 180
....*....|....*....|....*...
gi 1786986074 561 lMQEGILKFLQDDKR----TLVLVTHKL 584
Cdd:COG4608 192 -IQAQVLNLLEDLQDelglTYLFISHDL 218
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
400-605 |
3.56e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 53.09 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN--VNESEPSFEATRRNrysVAYAAQKP--WLLNA 475
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQ---VATVFQDPeqQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 476 TVEENITFgspfnKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALD 554
Cdd:PRK13638 94 DIDSDIAF-----SLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 555 IHLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREG 605
Cdd:PRK13638 169 PAGRTQMI--AIIRRIVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHG 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1039-1246 |
4.61e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 52.44 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1039 VLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVD---IFDGKIVIDG---IDISKLPLHTLRSRLSIILQDpilf 1110
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLlrCINLLEQPEagtIRVGDITIDTarsLSQQKGLIRQLRQHVGFVFQN---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1111 sgsirFNLDPEckctddrlWEALE-IAQLKNMVKSLPGG---------LDAVVTEGGEN-----FSVGQRQLFCLARAFV 1175
Cdd:PRK11264 94 -----FNLFPH--------RTVLEnIIEGPVIVKGEPKEeatararelLAKVGLAGKETsyprrLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786986074 1176 RKSSILIMDEATASID--MATEnILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLA 1246
Cdd:PRK11264 161 MRPEVILFDEPTSALDpeLVGE-VLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKALFA 233
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1037-1246 |
5.34e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.79 E-value: 5.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1037 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-----FDGKIVIDGIDI-SKLPLHTLRSRLSIILQDPILF 1110
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1111 SGSIRFNLDPECKCtdDRLWEALEIAQLKNMVKSLPGGLDAV---VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEAT 1187
Cdd:PRK14271 114 PMSIMDNVLAGVRA--HKLVPRKEFRGVAQARLTEVGLWDAVkdrLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1786986074 1188 ASIDMATENILQKVVMTaFADR-TVVTIAHRV-HTILTADLVIVMKRGNILEYDTPESLLA 1246
Cdd:PRK14271 192 SALDPTTTEKIEEFIRS-LADRlTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
359-555 |
5.39e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.09 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 359 PGRYHLDSYEQSTRRLRPAETEDIA-----IKVTN--GYFSWGSGL--------ATLSNIDIRIPTGQLTMIVGQVGCGK 423
Cdd:PRK10261 284 PRRFPLISLEHPAKQEPPIEQDTVVdgepiLQVRNlvTRFPLRSGLlnrvtrevHAVEKVSFDLWPGETLSLVGESGSGK 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 424 SSLLLAILGEMQTLEGKVHWSNV---NESEPSFEATRRNrysVAYAAQKPWllnATVEENITFG-SPFNKQRYKAVTDAC 499
Cdd:PRK10261 364 STTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRD---IQFIFQDPY---ASLDPRQTVGdSIMEPLRVHGLLPGK 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1786986074 500 SLQPDIDLL--PFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDI 555
Cdd:PRK10261 438 AAAARVAWLleRVGLLPEHAWRYPHeFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
400-585 |
6.19e-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: 51.95 E-value: 6.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsNVNESEPSfeaTRRNRY----SVAYAaQKPWL--- 472
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV---RVAGLVPW---KRRKKFlrriGVVFG-QKTQLwwd 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 473 --------LNATVeenitFGSPfnKQRYKAVTDACSlqpdiDLLPFGDQTEIGERgiNLSGGQRQRICVARALYQNTNIV 544
Cdd:cd03267 110 lpvidsfyLLAAI-----YDLP--PARFKKRLDELS-----ELLDLEELLDTPVR--QLSLGQRMRAEIAAALLHEPEIL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1786986074 545 FLDDPFSALDIHlsdhlMQEGILKFLQDDKR----TLVLVTHKLQ 585
Cdd:cd03267 176 FLDEPTIGLDVV-----AQENIRNFLKEYNRergtTVLLTSHYMK 215
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
523-610 |
9.21e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.44 E-value: 9.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 523 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSV 601
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQII-ELLLELQQKENMALVLITHDLALVAEaAHKIIVMYAGQV 232
|
....*....
gi 1786986074 602 LREGTLKDI 610
Cdd:PRK11022 233 VETGKAHDI 241
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
400-659 |
1.03e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ----TLEGKVHWSNVnesePSFEATRRNRYSVAYAAQK----PW 471
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGI----TPEEIKKHYRGDVVYNAETdvhfPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 472 LlnaTVEENITFG----SPFNkqRYKAVT--DACSLQPDIDLLPFG----DQTEIGE---RGInlSGGQRQRICVARALY 538
Cdd:TIGR00956 153 L---TVGETLDFAarckTPQN--RPDGVSreEYAKHIADVYMATYGlshtRNTKVGNdfvRGV--SGGERKRVSIAEASL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 539 QNTNIVFLDDPFSALD--------------IHLSDHLMQEGILKFLQD-----DKRTLV---------LVTHKLQYL--- 587
Cdd:TIGR00956 226 GGAKIQCWDNATRGLDsatalefiralktsANILDTTPLVAIYQCSQDayelfDKVIVLyegyqiyfgPADKAKQYFekm 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 588 --------THADWIIAMKDGS--VLREGTLKDIQTKDVELYEHWKTLMNRqdQELEKDMEA----DQTTLERKTLRRAMY 653
Cdd:TIGR00956 306 gfkcpdrqTTADFLTSLTSPAerQIKPGYEKKVPRTPQEFETYWRNSPEY--AQLMKEIDEyldrCSESDTKEAYRESHV 383
|
....*.
gi 1786986074 654 SREAKA 659
Cdd:TIGR00956 384 AKQSKR 389
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1037-1256 |
1.86e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 51.87 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1037 KPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDifDGKIVIDGIDISKLP-----LHTlrsrlsiILQDPIL 1109
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVlrLIAGFETPD--SGRIMLDGQDITHVPaenrhVNT-------VFQSYAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1110 FSG-SIRFNLDPECKC-------TDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSIL 1181
Cdd:PRK09452 98 FPHmTVFENVAFGLRMqktpaaeITPRVMEALRMVQLEEFAQRKPHQL-----------SGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1182 IMDEATASID------MATE-NILQKVVMTAFadrtvVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQENGVF- 1252
Cdd:PRK09452 167 LLDESLSALDyklrkqMQNElKALQRKLGITF-----VFVTHDQEEALTmSDRIVVMRDGRIEQDGTPREIYEEPKNLFv 241
|
....
gi 1786986074 1253 ASFV 1256
Cdd:PRK09452 242 ARFI 245
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1023-1238 |
1.86e-06 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 49.97 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV-DIF---DGKIVIDGIDISKLPLHT--- 1095
Cdd:cd03269 1 LEVENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTT----IRMIlGIIlpdSGEVLFDGKPLDIAARNRigy 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1096 ------LRSRLSIilQDPILFSGSIRfNLDP-ECKCTDDRLWEALEIAQLKNmvKSLpggldavvteggENFSVGQRQLF 1168
Cdd:cd03269 75 lpeergLYPKMKV--IDQLVYLAQLK-GLKKeEARRRIDEWLERLELSEYAN--KRV------------EELSKGNQQKV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 1169 CLARAFVRKSSILIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVHTI-LTADLVIVMKRGNILEY 1238
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLY 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
524-605 |
1.90e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.01 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 524 SGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKR-TLVLVTHKLQY---LTHAdwIIAMKDG 599
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILA--LLKSLQQKHQlAYLFISHDLHVvraLCHQ--VIVLRQG 502
|
....*.
gi 1786986074 600 SVLREG 605
Cdd:PRK15134 503 EVVEQG 508
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
400-596 |
2.04e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 50.33 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEmqtlegkvhwsnvnesepsfEATRRNRYSV-AYAAQ------KPWL 472
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYA--------------------EGQRRYVESLsAYARQflgqmdKPDV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 473 LNAT-------VEENITFGSPfnKQRYKAVTDACS----------LQPDIDLLpfgdqTEIG------ERGIN-LSGGQR 528
Cdd:cd03270 71 DSIEglspaiaIDQKTTSRNP--RSTVGTVTEIYDylrllfarvgIRERLGFL-----VDVGlgyltlSRSAPtLSGGEA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 529 QRICVARALYQN-TNIVF-LDDPFSALdiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAM 596
Cdd:cd03270 144 QRIRLATQIGSGlTGVLYvLDEPSIGL--HPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
409-582 |
2.11e-06 |
|
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: 48.91 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 409 TGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNRYsvayaaqkpwllnatveenitfgspfn 488
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 489 kqrykavtdacslqpdidllpfgdqteIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEG--- 565
Cdd:smart00382 54 ---------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelr 106
|
170
....*....|....*...
gi 1786986074 566 -ILKFLQDDKRTLVLVTH 582
Cdd:smart00382 107 lLLLLKSEKNLTVILTTN 124
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
522-605 |
2.51e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.57 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 522 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQ-YLTHADWIiamkdgS 600
Cdd:COG3845 141 DLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFE--ILRRLAAEGKSIIFITHKLReVMAIADRV------T 212
|
....*
gi 1786986074 601 VLREG 605
Cdd:COG3845 213 VLRRG 217
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1030-1239 |
2.53e-06 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 50.02 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1030 VRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmVDIFDGKIVIDGIDISKLPL------HTLRSRLSII 1103
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTT-------LKILSGLLQPTSGEVRVAGLvpwkrrKKFLRRIGVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1104 L------------QDPILFSGSIrFNLDP-ECKCTDDRLWEALEIAQLknmvkslpggLDAVVteggENFSVGQRQLFCL 1170
Cdd:cd03267 100 FgqktqlwwdlpvIDSFYLLAAI-YDLPPaRFKKRLDELSELLDLEEL----------LDTPV----RQLSLGQRMRAEI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 1171 ARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILT-ADLVIVMKRGNILeYD 1239
Cdd:cd03267 165 AAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLL-YD 235
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1049-1247 |
2.63e-06 |
|
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: 51.25 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1049 PGQKV-GICGRTGSGKSSLslafFRMV------DifDGKIVIDG---IDISK---LPLHtlRSRLSIILQDPILFSG-SI 1114
Cdd:COG4148 23 PGRGVtALFGPSGSGKTTL----LRAIaglerpD--SGRIRLGGevlQDSARgifLPPH--RRRIGYVFQEARLFPHlSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1115 RFNLD--------PECKCTDDRLWEALEIAQLknmVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEA 1186
Cdd:COG4148 95 RGNLLygrkraprAERRISFDEVVELLGIGHL---LDRRPATL-----------SGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1786986074 1187 TASIDMATEN----ILQKVvmtafADRT---VVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQ 1247
Cdd:COG4148 161 LAALDLARKAeilpYLERL-----RDELdipILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
397-610 |
2.69e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.78 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 397 LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN----------VNESEPSFEATRRNRYS-VAY 465
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRHVRGAdMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 466 AAQKPWL-LNA--TVEENITFGSPFNK--QRYKAVTDACSLqpdIDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQ 539
Cdd:PRK10261 109 IFQEPMTsLNPvfTVGEQIAESIRLHQgaSREEAMVEAKRM---LDQVRIPEAQTILSRYPHqLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 540 NTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRT-LVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 610
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQ--LIKVLQKEMSMgVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQI 256
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
400-610 |
3.44e-06 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 51.22 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG----EMQTLEGKVHWSNVN---ESEPSFEATRRNRysVAYAAQKPWL 472
Cdd:COG4172 26 VKGVSFDIAAGETLALVGESGSGKSVTALSILRllpdPAAHPSGSILFDGQDllgLSERELRRIRGNR--IAMIFQEPMT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 473 -LNA--TVEENItfGSPFnkQRYKAVTDACSLQPDIDLLpfgDQTEI--GERGIN-----LSGGQRQRICVARALYQNTN 542
Cdd:COG4172 104 sLNPlhTIGKQI--AEVL--RLHRGLSGAAARARALELL---ERVGIpdPERRLDayphqLSGGQRQRVMIAMALANEPD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 543 IVFLDDPFSALDIHLsdhlmQEGILKFLQDDKRT----LVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 610
Cdd:COG4172 177 LLIADEPTTALDVTV-----QAQILDLLKDLQRElgmaLLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAEL 244
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
400-609 |
3.95e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.03 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ--TLEGKVHwsnVNESEPSFEATRRnrysVAYAAQKPWLL-NAT 476
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnNFTGTIL---ANNRKPTKQILKR----TGFVTQDDILYpHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 477 VEENITFGS----PFNKQRYKAVTDACSLQPDIDLLPFGDqTEIGE---RGInlSGGQRQRICVARALYQNTNIVFLDDP 549
Cdd:PLN03211 157 VRETLVFCSllrlPKSLTKQEKILVAESVISELGLTKCEN-TIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 550 FSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTHA--DWIIAMKDGSVLREGTLKD 609
Cdd:PLN03211 234 TSGLDATAAYRLVL--TLGSLAQKGKTIVTSMHQPSSRVYQmfDSVLVLSEGRCLFFGKGSD 293
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1033-1241 |
5.02e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.00 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1033 ENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmVDIFDGKIV---IDG-IDISKLP-LHTLRSRLS------ 1101
Cdd:PLN03140 890 EDRLQ-LLREVTGAFRPGVLTALMGVSGAGKTTL-------MDVLAGRKTggyIEGdIRISGFPkKQETFARISgyceqn 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1102 ------IILQDPILFSGSIRfnLDPECKCTD-----DRLWEALEIAQLKNMVKSLPGgldavVTeggeNFSVGQRQLFCL 1170
Cdd:PLN03140 962 dihspqVTVRESLIYSAFLR--LPKEVSKEEkmmfvDEVMELVELDNLKDAIVGLPG-----VT----GLSTEQRKRLTI 1030
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786986074 1171 ARAFVRKSSILIMDEATASIDMATENILQKVVM-TAFADRTVVTIAHRVHT-ILTA-DLVIVMKRGNILEYDTP 1241
Cdd:PLN03140 1031 AVELVANPSIIFMDEPTSGLDARAAAIVMRTVRnTVDTGRTVVCTIHQPSIdIFEAfDELLLMKRGGQVIYSGP 1104
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1047-1202 |
6.21e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 50.21 E-value: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1047 IKPGQKVGICGRTGSGKSSLS--LAFFRMVDIFDGKIVIDGIDISKLPLH-TLRSRLSIILQDPILFSG-SIRFN--LDP 1120
Cdd:TIGR02633 24 VRPGECVGLCGENGAGKSTLMkiLSGVYPHGTWDGEIYWSGSPLKASNIRdTERAGIVIIHQELTLVPElSVAENifLGN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1121 ECKCTDDRLWEALEIAQLKNMVKSLPggLDAV-VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQ 1199
Cdd:TIGR02633 104 EITLPGGRMAYNAMYLRAKNLLRELQ--LDADnVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILL 181
|
...
gi 1786986074 1200 KVV 1202
Cdd:TIGR02633 182 DII 184
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
722-933 |
9.00e-06 |
|
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: 49.02 E-value: 9.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 722 IDYWLATwtseysiNNTGKADQTyyvagFSILCGAGIFLCLVTSL---TVEWMGLTAAKNLHHNLLNKIILGPIRFFDTT 798
Cdd:cd18575 23 IDQGFAA-------GNTALLNRA-----FLLLLAVALVLALASALrfyLVSWLGERVVADLRKAVFAHLLRLSPSFFETT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 799 PLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATP---VFLVALLPLGVA-FYFIQKYFRVASKDLQE- 873
Cdd:cd18575 91 RTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPkltLLVLLVIPLVVLpIILFGRRVRRLSRASQDr 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 874 LDDSTQlpllcHFSETAEGLTTIRAFRHETRFKQRMLELTDTNniaylfLSAANRWLEVR 933
Cdd:cd18575 171 LADLSA-----FAEETLSAIKTVQAFTREDAERQRFATAVEAA------FAAALRRIRAR 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
457-610 |
1.33e-05 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 48.10 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 457 RRNRYSVAYAAQKP---WLLnaTVEENI-----TFGSPFNKQRYKAVtdacSLQPDIDLLPFGDQteigeRGINLSGGQR 528
Cdd:COG1137 74 KRARLGIGYLPQEAsifRKL--TVEDNIlavleLRKLSKKEREERLE----ELLEEFGITHLRKS-----KAYSLSGGER 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 529 QRICVARALYQNTNIVFLDDPFSALD-IHLSDhlMQEgILKFLQDdkRTL-VLVT-HK----LQ-----YLthadwiiaM 596
Cdd:COG1137 143 RRVEIARALATNPKFILLDEPFAGVDpIAVAD--IQK-IIRHLKE--RGIgVLITdHNvretLGicdraYI--------I 209
|
170
....*....|....
gi 1786986074 597 KDGSVLREGTLKDI 610
Cdd:COG1137 210 SEGKVLAEGTPEEI 223
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
511-658 |
1.82e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.01 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 511 GDQ-TEIGERginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQ-----EGILKFLQDDKRTLVLVTHKL 584
Cdd:PRK10636 421 GDKvTEETRR---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEalidfEGALVVVSHDRHLLRSTTDDL 497
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786986074 585 qYLTHadwiiamkDGSVlregtlkDIQTKDVELYEHWktLMNRQDQELEKDMEADQTTLERKTLRRAMYSREAK 658
Cdd:PRK10636 498 -YLVH--------DGKV-------EPFDGDLEDYQQW--LSDVQKQENQTDEAPKENNANSAQARKDQKRREAE 553
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
415-593 |
2.01e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.96 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 415 IVGQVGCGKSSLLLAILGEMQTLEGkvhwsnvnesepsfEATRRNRYSVAYAAQKPWL-LNATVEENIT--FGSPFNKQ- 490
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEG--------------EARPAPGIKVGYLPQEPQLdPEKTVRENVEegVAEVKAALd 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 491 RYKAVTDACS---------------LQPDIDL------------------LPFGDqTEIGergiNLSGGQRQRICVARAL 537
Cdd:PRK11819 104 RFNEIYAAYAepdadfdalaaeqgeLQEIIDAadawdldsqleiamdalrCPPWD-AKVT----KLSGGERRRVALCRLL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 538 YQNTNIVFLDDPfsaldihlSDHLMQEGIL---KFLQDDKRTLVLVTHKLQYLTH-ADWI 593
Cdd:PRK11819 179 LEKPDMLLLDEP--------TNHLDAESVAwleQFLHDYPGTVVAVTHDRYFLDNvAGWI 230
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
518-610 |
2.06e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.86 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 518 ERGIN-LSGGQRQRICVARAL-YQNTNIVF-LDDPfsALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWII 594
Cdd:TIGR00630 483 SRAAGtLSGGEAQRIRLATQIgSGLTGVLYvLDEP--SIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVI 560
|
90 100
....*....|....*....|..
gi 1786986074 595 AM------KDGSVLREGTLKDI 610
Cdd:TIGR00630 561 DIgpgageHGGEVVASGTPEEI 582
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1021-1236 |
2.25e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 48.72 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1021 GEIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDIFDGKIVIDGIDISKlplHTLRs 1098
Cdd:PLN03211 67 HKPKISDETRQIQE--RTILNGVTGMASPGEILAVLGPSGSGKSTLlnALAGRIQGNNFTGTILANNRKPTK---QILK- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1099 RLSIILQDPILFSG-SIRFNLdpeCKCTDDRLWEALEiAQLKNMVKslpgglDAVVTEGG----EN----------FSVG 1163
Cdd:PLN03211 141 RTGFVTQDDILYPHlTVRETL---VFCSLLRLPKSLT-KQEKILVA------ESVISELGltkcENtiignsfirgISGG 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1786986074 1164 QRQLFCLARAFVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAH----RVHTILtaDLVIVMKRGNIL 1236
Cdd:PLN03211 211 ERKRVSIAHEMLINPSLLILDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHqpssRVYQMF--DSVLVLSEGRCL 286
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
521-594 |
2.25e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.41 E-value: 2.25e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1786986074 521 INLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQeGILKFLQDDKRTLVLVTHKLQYLTH-ADWII 594
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAAR-AIRRLSEEGKKTALVVEHDLAVLDYlSDRIH 143
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
392-605 |
2.31e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 47.61 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 392 SWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNvNESEPSF-----EATRRN--RYSVA 464
Cdd:PRK11701 15 LYGPRKG-CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRM-RDGQLRDlyalsEAERRRllRTEWG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 465 YAAQKPWL-LNATVEENITFGSP--------FNKQRYKAVT--DACSLQPD-IDLLP--FgdqteigerginlSGGQRQR 530
Cdd:PRK11701 93 FVHQHPRDgLRMQVSAGGNIGERlmavgarhYGDIRATAGDwlERVEIDAArIDDLPttF-------------SGGMQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 531 ICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLqddkRTLV--------LVTHKL---QYLTHAdwIIAMKDG 599
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVSV-----QARLLDLL----RGLVrelglavvIVTHDLavaRLLAHR--LLVMKQG 228
|
....*.
gi 1786986074 600 SVLREG 605
Cdd:PRK11701 229 RVVESG 234
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
701-921 |
2.60e-05 |
|
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: 47.77 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 701 GFFLLILMIFSKLLKHSVI-VAIDywlatwtsEYSINNTGKADQTYYVAGFSILCGAGIFLCL-VTSLTVEWMGLTAAKN 778
Cdd:cd18544 4 ALLLLLLATALELLGPLLIkRAID--------DYIVPGQGDLQGLLLLALLYLGLLLLSFLLQyLQTYLLQKLGQRIIYD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 779 LHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISY----ATPVFLVALLPLG 854
Cdd:cd18544 76 LRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLlnwrLALISLLVLPLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1786986074 855 VAFYFIQKYFRVASKDLQEL--DDSTQLpllchfSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYL 921
Cdd:cd18544 156 LATYLFRKKSRKAYREVREKlsRLNAFL------QESISGMSVIQLFNREKREFEEFDEINQEYRKANL 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
395-584 |
2.73e-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: 48.86 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 395 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNvNESEPSFEATRRnrySVAYAAQKPWLLN 474
Cdd:TIGR01257 941 SGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG-KDIETNLDAVRQ---SLGMCPQHNILFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 475 -ATVEENITFGSPFNKQRYkavtDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 553
Cdd:TIGR01257 1017 hLTVAEHILFYAQLKGRSW----EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190
....*....|....*....|....*....|.
gi 1786986074 554 DIHlSDHLMQEGILKFlqDDKRTLVLVTHKL 584
Cdd:TIGR01257 1093 DPY-SRRSIWDLLLKY--RSGRTIIMSTHHM 1120
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
999-1217 |
2.89e-05 |
|
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: 48.59 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 999 MESENYEGTMDP--------SQVPEHWPQEGEIKIHDLCVRYEN------NLKPVLKHVKAYIKPGQKVGICGRTGSGKS 1064
Cdd:TIGR00954 413 VKSGNFKRPRVEeiesgregGRNSNLVPGRGIVEYQDNGIKFENiplvtpNGDVLIESLSFEVPSGNNLLICGPNGCGKS 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1065 SLslafFRMVD----IFDGKIVIDG----IDISKLPLHTLRSrlsiiLQDPILFSGSIrfnLDPECK-CTDDRLWEALEI 1135
Cdd:TIGR00954 493 SL----FRILGelwpVYGGRLTKPAkgklFYVPQRPYMTLGT-----LRDQIIYPDSS---EDMKRRgLSDKDLEQILDN 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1136 AQLKNMVKSlPGGLDAVvTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA--SIDM--ATENILQKVVMTAFadrtv 1211
Cdd:TIGR00954 561 VQLTHILER-EGGWSAV-QDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSavSVDVegYMYRLCREFGITLF----- 633
|
....*.
gi 1786986074 1212 vTIAHR 1217
Cdd:TIGR00954 634 -SVSHR 638
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1047-1242 |
3.15e-05 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 46.96 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1047 IKPGQKVGICGRTGSGKSSLslafFRMV------DifDGKIVIDGIDISKLPLHtLRSRLSII--LQDPILFSG------ 1112
Cdd:COG0411 27 VERGEIVGLIGPNGAGKTTL----FNLItgfyrpT--SGRILFDGRDITGLPPH-RIARLGIArtFQNPRLFPEltvlen 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1113 --------------SIRFNLDP---ECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFV 1175
Cdd:COG0411 100 vlvaaharlgrgllAALLRLPRarrEEREARERAEELLERVGLADRADEPAGNL-----------SYGQQRRLEIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1176 RKSSILIMDEATASIDMA-TENILQKVV-MTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPE 1242
Cdd:COG0411 169 TEPKLLLLDEPAAGLNPEeTEELAELIRrLRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPA 238
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
396-610 |
3.56e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.80 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 396 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRRNRYSVAYAaQKPWLLNA 475
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQ-ELNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 476 TVEENITFG-----SPF--NKQRYKAvTDACSLQPDIDLLPfgdqteiGERGINLSGGQRQRICVARALYQNTNIVFLDD 548
Cdd:PRK10982 89 SVMDNMWLGryptkGMFvdQDKMYRD-TKAIFDELDIDIDP-------RAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 549 PFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 610
Cdd:PRK10982 161 PTSSLTEKEVNHLFT--IIRKLKERGCGIVYISHKMEEIFQlCDEITILRDGQWIATQPLAGL 221
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
410-615 |
4.60e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 46.46 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 410 GQLTMIVGQVGCGKSSLLLAILGeMQTLEGKVHWSNVNESEPSFEATRRNRysvAYAAQK-PWLLNATVEENITFGSPFN 488
Cdd:PRK03695 22 GEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAWSAAELARHR---AYLSQQqTPPFAMPVFQYLTLHQPDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 489 KQRY---KAVTDACSLQPDIDLLPfgdqteigeRGIN-LSGGQRQRICVARALYQ-------NTNIVFLDDPFSALDI-- 555
Cdd:PRK03695 98 TRTEavaSALNEVAEALGLDDKLG---------RSVNqLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVaq 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1786986074 556 -----HLSDHLMQEGIlkflqddkrTLVLVTHKLQY-LTHADWIIAMKDGSVLREGTLKDIQTKDV 615
Cdd:PRK03695 169 qaaldRLLSELCQQGI---------AVVMSSHDLNHtLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1028-1193 |
5.19e-05 |
|
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: 45.81 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1028 LCVRYEnnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDP 1107
Cdd:TIGR01189 7 ACSRGE---RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1108 ILFSGSIRFNLD---PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMD 1184
Cdd:TIGR01189 84 LKPELSALENLHfwaAIHGGAQRTIEDALAAVGLTGFEDLPAAQL-----------SAGQQRRLALARLWLSRRPLWILD 152
|
....*....
gi 1786986074 1185 EATASIDMA 1193
Cdd:TIGR01189 153 EPTTALDKA 161
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
770-912 |
7.13e-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: 350020 [Multi-domain] Cd Length: 289 Bit Score: 46.32 E-value: 7.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 770 WMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATP---VF 846
Cdd:cd18576 62 RVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWkltLL 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 847 LVALLP-LGVAFYFIQKYFRVASKDLQ-ELDDSTQlpllcHFSETAEGLTTIRAFRHE----TRFKQRMLEL 912
Cdd:cd18576 142 MLATVPvVVLVAVLFGRRIRKLSKKVQdELAEANT-----IVEETLQGIRVVKAFTREdyeiERYRKALERV 208
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1023-1239 |
7.78e-05 |
|
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: 45.60 E-value: 7.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNLKP--------------------VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIV 1082
Cdd:cd03220 1 IELENVSKSYPTYKGGssslkklgilgrkgevgefwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1083 IDGIDISKLPLHT-LRSRLSIIlqDPILFSGSIrFNLDPecKCTDDRLWEALEIAQLKNMvkslpggLDAVVteggENFS 1161
Cdd:cd03220 81 VRGRVSSLLGLGGgFNPELTGR--ENIYLNGRL-LGLSR--KEIDEKIDEIIEFSELGDF-------IDLPV----KTYS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1162 VGQ--RQLFCLARAFvrKSSILIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTIL-TADLVIVMKRGNILE 1237
Cdd:cd03220 145 SGMkaRLAFAIATAL--EPDILLIDEVLAVGDAAFQEKCQRRLRELLKQgKTVILVSHDPSSIKrLCDRALVLEKGKIRF 222
|
..
gi 1786986074 1238 YD 1239
Cdd:cd03220 223 DG 224
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
400-582 |
9.37e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 46.58 E-value: 9.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKVHWSNVNESEPsFEATRRNRYSvAYAAQKPWLLNA-TVE 478
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLM-NALAFRSPKGVKGSGSVLLNGMP-IDAKEMRAIS-AYVQQDDLFIPTlTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 479 ENITFGSPF----------NKQRYKAVTDACSLQPDIDllpfgdqTEIGERGI--NLSGGQRQRICVARALYQNTNIVFL 546
Cdd:TIGR00955 118 EHLMFQAHLrmprrvtkkeKRERVDEVLQALGLRKCAN-------TRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190
....*....|....*....|....*....|....*.
gi 1786986074 547 DDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTH 582
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQ--VLKGLAQKGKTIICTIH 224
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1047-1237 |
9.46e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.89 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1047 IKPGQKVGICGRTGSGKSSLSLAFFRMVDiFDGKIV-----IDGIDISKLPLHTLR----SRLSIILQDPILfsgsirfN 1117
Cdd:PRK11022 30 VKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMaekleFNGQDLQRISEKERRnlvgAEVAMIFQDPMT-------S 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1118 LDPeCKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEG-----------GENFSVGQRQLFCLARAFVRKSSILIMDEA 1186
Cdd:PRK11022 102 LNP-CYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGipdpasrldvyPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1187 TASIDMATE--------NILQKVVMtafadrTVVTIAHRVHTIL-TADLVIVMKRGNILE 1237
Cdd:PRK11022 181 TTALDVTIQaqiielllELQQKENM------ALVLITHDLALVAeAAHKIIVMYAGQVVE 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1047-1248 |
9.53e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 46.36 E-value: 9.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1047 IKPGQKVGICGRTGSGKSSLSLAFFRMVD-IFDGKIVIDG--IDIsKLPLHTLRSRLSIILQD-------PIL------- 1109
Cdd:TIGR02633 283 LRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGkpVDI-RNPAQAIRAGIAMVPEDrkrhgivPILgvgknit 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1110 ------FSGSIRFNLDPECKCTDdrlwEALEIAQLKNMVKSLP-GGLdavvteggenfSVGQRQLFCLARAFVRKSSILI 1182
Cdd:TIGR02633 362 lsvlksFCFKMRIDAAAELQIIG----SAIQRLKVKTASPFLPiGRL-----------SGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1786986074 1183 MDEATASIDM-ATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNiLEYDTPESLLAQE 1248
Cdd:TIGR02633 427 LDEPTRGVDVgAKYEIYKLINQLAQEGVAIIVVSSELAEVLgLSDRVLVIGEGK-LKGDFVNHALTQE 493
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
415-586 |
1.01e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 415 IVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNEsepsfeatrrnrysVAYAAQKPWLLNA--TVEENITFGspfnKQ-- 490
Cdd:PRK11147 350 LIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLE--------------VAYFDQHRAELDPekTVMDNLAEG----KQev 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 491 ----RYKAVTDacSLQpdiDLL--PFGDQTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDhLMQE 564
Cdd:PRK11147 412 mvngRPRHVLG--YLQ---DFLfhPKRAMTPVKA----LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLE-LLEE 481
|
170 180
....*....|....*....|..
gi 1786986074 565 gilkFLQDDKRTLVLVTHKLQY 586
Cdd:PRK11147 482 ----LLDSYQGTVLLVSHDRQF 499
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1037-1191 |
1.04e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 45.98 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1037 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKlPLHTLRSRLSIILQdpilFSgsirf 1116
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQ----FD----- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1117 NLDPECKCTDD------------RLWEA-----LEIAQLKNMVkslpgglDAVVTEggenFSVGQRQLFCLARAFVRKSS 1179
Cdd:PRK13536 124 NLDLEFTVRENllvfgryfgmstREIEAvipslLEFARLESKA-------DARVSD----LSGGMKRRLTLARALINDPQ 192
|
170
....*....|..
gi 1786986074 1180 ILIMDEATASID 1191
Cdd:PRK13536 193 LLILDEPTTGLD 204
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
400-606 |
1.04e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.93 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAIL---------------GEMQTLEGKVHWS---NVNESEP-----SFEAT 456
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINDTLypalanrlngaktvpGRYTSIEGLEHLDkviHIDQSPIgrtprSNPAT 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 457 rrnrYSVAYA------AQKP-----------------------------------WLLNATVEENITFGSPFNKQ----R 491
Cdd:TIGR00630 704 ----YTGVFDeirelfAETPeakvrgytpgrfsfnvkggrceacqgdgvikiemhFLPDVYVPCEVCKGKRYNREtlevK 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 492 YKAVTDACSLQ-------------PDID-----LLPFGDQ-TEIGERGINLSGGQRQRICVARALYQNTN---IVFLDDP 549
Cdd:TIGR00630 780 YKGKNIADVLDmtveeayeffeavPSISrklqtLCDVGLGyIRLGQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEP 859
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1786986074 550 FSALdiHLSD--HLMQegILKFLQDDKRTLVLVTHKLQYLTHADWII------AMKDGSVLREGT 606
Cdd:TIGR00630 860 TTGL--HFDDikKLLE--VLQRLVDKGNTVVVIEHNLDVIKTADYIIdlgpegGDGGGTVVASGT 920
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1049-1228 |
1.34e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.52 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1049 PGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIdgIDISKLPLHTLRSRLSIILQDPILFSGSIRfnldpeckctddr 1128
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--IDGEDILEEVLDQLLLIIVGGKKASGSGEL------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1129 lwealeiaqlknmvkslpggldavvteggenfsvGQRQLFclARAFVRKSSILIMDEATASIDMATENILQKVVMTAF-- 1206
Cdd:smart00382 66 ----------------------------------RLRLAL--ALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLll 109
|
170 180
....*....|....*....|....*..
gi 1786986074 1207 -----ADRTVVTIAHRVHTILTADLVI 1228
Cdd:smart00382 110 llkseKNLTVILTTNDEKDLGPALLRR 136
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
520-622 |
1.43e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 44.88 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 520 GINLSGGQRQRICVARALYQNTNIVFLDDPFSALD-IHLSDhlmQEGILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMK 597
Cdd:PRK10895 135 GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDpISVID---IKRIIEHLRDSGLGVLITDHNVrETLAVCERAYIVS 211
|
90 100
....*....|....*....|....*....
gi 1786986074 598 DGSVLREGT----LKDIQTKDVELYEHWK 622
Cdd:PRK10895 212 QGHLIAHGTpteiLQDEHVKRVYLGEDFR 240
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
779-908 |
1.46e-04 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 45.32 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 779 LHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIG---MISYA-TPVFLVALLPLG 854
Cdd:cd18780 77 LRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVfmfTTSWKlTLVMLSVVPPLS 156
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1786986074 855 VAFYFIQKYFRVASKDLQ-ELDDStqlpllchfSETAE----GLTTIRAFRHETRFKQR 908
Cdd:cd18780 157 IGAVIYGKYVRKLSKKFQdALAAA---------STVAEesisNIRTVRSFAKETKEVSR 206
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
771-914 |
1.46e-04 |
|
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: 45.12 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 771 MGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADT----NIIDQHIPptlESLTRSTLLCLSAIGMISYATPVF 846
Cdd:cd18551 63 TGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTtllrELITSGLP---QLVTGVLTVVGAVVLMFLLDWVLT 139
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786986074 847 LVALLPLGVAF---YFIQKYFRVASKDLQE-LDDSTQlpllcHFSETAEGLTTIRAFRHETRFKQRMLELTD 914
Cdd:cd18551 140 LVTLAVVPLAFliiLPLGRRIRKASKRAQDaLGELSA-----ALERALSAIRTVKASNAEERETKRGGEAAE 206
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
412-594 |
1.51e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.52 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 412 LTMIVGQVGCGKSSLLLAIL----GEM-QTLEGKVHwsnvnesEPSFEATRRNRYSVayaaqkpwllnaTVEENITFGSP 486
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALKyaltGELpPNSKGGAH-------DPKLIREGEVRAQV------------KLAFENANGKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 487 FNKQRYKAVTDACSL--QPDID-LLPFgdqteigERGiNLSGGQRQ------RICVARALYQNTNIVFLDDPFSALDihl 557
Cdd:cd03240 85 YTITRSLAILENVIFchQGESNwPLLD-------MRG-RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD--- 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1786986074 558 SDHLMQ--EGILKFLQDDK-RTLVLVTHKLQYLTHADWII 594
Cdd:cd03240 154 EENIEEslAEIIEERKSQKnFQLIVITHDEELVDAADHIY 193
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1023-1239 |
1.52e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 45.83 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRM----VDIFDGKIVI-DGIDISKLPlhtlr 1097
Cdd:COG0488 316 LELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTL----LKLlageLEPDSGTVKLgETVKIGYFD----- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1098 srlsiilQDpilfsgsiRFNLDPeckctDDRLWEAL-------EIAQLKNMVKSL--PGglDAVVTEGGeNFSVGQRQLF 1168
Cdd:COG0488 385 -------QH--------QEELDP-----DKTVLDELrdgapggTEQEVRGYLGRFlfSG--DDAFKPVG-VLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 1169 CLARAFVRKSSILIMDEATASIDMATENILQKVVMTaFaDRTVVTIAH------RVhtiltADLVIVMKRGNILEYD 1239
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD-F-PGTVLLVSHdryfldRV-----ATRILEFEDGGVREYP 511
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
523-599 |
1.54e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.85 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 523 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMK 597
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSV-----QAQILQLLRELQQelnmGLLFITHNLSIVRKlADRVAVMQ 231
|
..
gi 1786986074 598 DG 599
Cdd:PRK15134 232 NG 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1149-1233 |
2.22e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.40 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1149 LDAVVteggENFSVGQRQLFCLARAFVRKSSILIMDEATASI-DMATENILQkvVMTAFAD--RTVVTIAHRVHTILT-A 1224
Cdd:COG3845 135 PDAKV----EDLSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADELFE--ILRRLAAegKSIIFITHKLREVMAiA 208
|
....*....
gi 1786986074 1225 DLVIVMKRG 1233
Cdd:COG3845 209 DRVTVLRRG 217
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
400-605 |
2.36e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 44.18 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGK----VHWSNVNESEPSFEATRRNRySVAYAAQkpwLLNA 475
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAgcvdVPDNQFGREASLIDAIGRKG-DFKDAVE---LLNA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 476 T-VEENITFGSPFNkqrykavtdacslqpdidllpfgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALD 554
Cdd:COG2401 122 VgLSDAVLWLRRFK---------------------------------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1786986074 555 IHLSdHLMQEGILKFLQDDKRTLVLVTHklqyltHADWIIAMKDGSVLREG 605
Cdd:COG2401 169 RQTA-KRVARNLQKLARRAGITLVVATH------HYDVIDDLQPDLLIFVG 212
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
400-583 |
3.83e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.10 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQT--LEGKVHWSNVNESEPSFEAtrrnrySVAYAAQKPW-LLNAT 476
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgvITGGDRLVNGRPLDSSFQR------SIGYVQQQDLhLPTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 477 VEENITFgSPFNKQRyKAVTDACS---LQPDIDLLPFGDQTE--IGERGINLSGGQRQRICVARALYQNTN-IVFLDDPF 550
Cdd:TIGR00956 853 VRESLRF-SAYLRQP-KSVSKSEKmeyVEEVIKLLEMESYADavVGVPGEGLNVEQRKRLTIGVELVAKPKlLLFLDEPT 930
|
170 180 190
....*....|....*....|....*....|...
gi 1786986074 551 SALDIHLSDHLMQegILKFLQDDKRTLVLVTHK 583
Cdd:TIGR00956 931 SGLDSQTAWSICK--LMRKLADHGQAILCTIHQ 961
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1028-1241 |
4.51e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 45.00 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1028 LCVR-----YENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIsKLPLHTLRSRLSI 1102
Cdd:TIGR01257 929 VCVKnlvkiFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGM 1007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1103 ILQDPILF-----SGSIRFNLDpeckcTDDRLWEALEIaQLKNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFVRK 1177
Cdd:TIGR01257 1008 CPQHNILFhhltvAEHILFYAQ-----LKGRSWEEAQL-EMEAMLEDT--GLHHKRNEEAQDLSGGMQRKLSVAIAFVGD 1079
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1786986074 1178 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRV-HTILTADLVIVMKRGNILEYDTP 1241
Cdd:TIGR01257 1080 AKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMdEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
410-582 |
5.80e-04 |
|
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: 43.17 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 410 GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVnesepsfeatrrnrySVAYaaqKPWLLNA----TVEENItfgs 485
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD---------------TVSY---KPQYIKAdyegTVRDLL---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 486 pfnkqrYKAVTDACS---LQPDIdLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlsDHLM 562
Cdd:cd03237 83 ------SSITKDFYThpyFKTEI-AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE--QRLM 153
|
170 180
....*....|....*....|.
gi 1786986074 563 QEGILK-FLQDDKRTLVLVTH 582
Cdd:cd03237 154 ASKVIRrFAENNEKTAFVVEH 174
|
|
| PduV-EutP |
pfam10662 |
Ethanolamine utilization - propanediol utilization; Members of this family function in ... |
413-528 |
5.81e-04 |
|
Ethanolamine utilization - propanediol utilization; Members of this family function in ethanolamine and propanediol degradation pathways. PduV may be involved in the association of the bacterial microcompartments (BMCs) to filaments.
Pssm-ID: 402341 [Multi-domain] Cd Length: 137 Bit Score: 41.50 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 413 TMIVGQVGCGKSSLLLAILGE------MQTLEgkvhWSNVNESEPSFEATRRNRYSV----AYAAQKPWLL-NATVEENI 481
Cdd:pfam10662 4 IMLIGPTGCGKTTLCQALSGEelkykkTQAIE----FYDNAIDTPGEYLENRRYYSAlivtSADADVIALVqDATEPEST 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1786986074 482 ---TFGSPFNKQRYKAVTdacslqpDIDLLPFGDQTEIGERGINLSGGQR 528
Cdd:pfam10662 80 fppGFASMFNKPVIGIIT-------KIDLAKDEANIEIAEEWLSLAGAQK 122
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
791-926 |
6.03e-04 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 43.17 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 791 PIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIG-MISYATPVFLVALLPL---GVAFYFIQKYFRV 866
Cdd:cd18541 87 SPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVmMFTISPKLTLIALLPLpllALLVYRLGKKIHK 166
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786986074 867 ASKDLQE----LDDSTQlpllchfsETAEGLTTIRAFRHETRFKQRMLELTDTN---NIAYLFLSAA 926
Cdd:cd18541 167 RFRKVQEafsdLSDRVQ--------ESFSGIRVIKAFVQEEAEIERFDKLNEEYvekNLRLARVDAL 225
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
736-928 |
6.14e-04 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 43.18 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 736 NNTGKADQTYYVAGFSILCGAGIFLCL------VTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSA 809
Cdd:cd18554 32 GSSLTLDEKVYKLFTIIGIMFFIFLILrppveyYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVIN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 810 DTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVA---LLPL-GVAFYFIQKYFRVASKDL-QELDDstqlpLLC 884
Cdd:cd18554 112 DVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVslvIFPFyILAVKYFFGRLRKLTKERsQALAE-----VQG 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1786986074 885 HFSETAEGLTTIRAFRHETRFKQrmlELTDTNNiayLFLSAANR 928
Cdd:cd18554 187 FLHERIQGMSVIKSFALEKHEQK---QFDKRNG---HFLTRALK 224
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1049-1192 |
6.48e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 43.32 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1049 PGQKV-GICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG---IDISK---LPLHtlRSRLSIILQDPILFSG-SIRFNLDP 1120
Cdd:PRK11144 22 PAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgicLPPE--KRRIGYVFQDARLFPHyKVRGNLRY 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1786986074 1121 ECKCTD----DRLWEALEIAQLknmVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDM 1192
Cdd:PRK11144 100 GMAKSMvaqfDKIVALLGIEPL---LDRYPGSL-----------SGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
406-555 |
6.69e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.03 E-value: 6.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 406 RIPT---GQLTMIVGQVGCGKSSLLLAILGEMQ----TLEGKVHWSNV------NESEPSFEATRRNRYSVA----YAAQ 468
Cdd:PRK13409 92 GLPIpkeGKVTGILGPNGIGKTTAVKILSGELIpnlgDYEEEPSWDEVlkrfrgTELQNYFKKLYNGEIKVVhkpqYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 469 KPWLLNATVEENItfgspfnkqryKAVTDACSLQPDIDLLpfgDQTEIGERGI-NLSGGQRQRICVARALYQNTNIVFLD 547
Cdd:PRK13409 172 IPKVFKGKVRELL-----------KKVDERGKLDEVVERL---GLENILDRDIsELSGGELQRVAIAAALLRDADFYFFD 237
|
....*...
gi 1786986074 548 DPFSALDI 555
Cdd:PRK13409 238 EPTSYLDI 245
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1023-1191 |
7.45e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 43.26 E-value: 7.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1023 IKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTlRSRLSI 1102
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1103 ILQdpilFSgsirfNLDPECKCTDDRL----WEALEIAQLKNMVKSL------PGGLDAVVTEggenFSVGQRQLFCLAR 1172
Cdd:PRK13537 85 VPQ----FD-----NLDPDFTVRENLLvfgrYFGLSAAAARALVPPLlefaklENKADAKVGE----LSGGMKRRLTLAR 151
|
170
....*....|....*....
gi 1786986074 1173 AFVRKSSILIMDEATASID 1191
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLD 170
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
524-610 |
9.55e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 42.79 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 524 SGGQRQRICVARALYQNTNIVFLDDPFSALDIhlsdhLMQEGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMKD 598
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDV-----TVQAQIMTLLNELKRefntAIIMITHDLGVVAGiCDKVLVMYA 237
|
90
....*....|..
gi 1786986074 599 GSVLREGTLKDI 610
Cdd:PRK09473 238 GRTMEYGNARDV 249
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
400-554 |
1.25e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.40 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEpsfeatrrnrysvayaAQKPWL------- 472
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN----------------IAKPYCtyighnl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 473 ---LNATVEENITFGSPFnkqrYKAVTdacSLQPDIDLLPFGDQteIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 549
Cdd:PRK13541 80 glkLEMTVFENLKFWSEI----YNSAE---TLYAAIHYFKLHDL--LDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEV 150
|
....*
gi 1786986074 550 FSALD 554
Cdd:PRK13541 151 ETNLS 155
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
400-569 |
1.50e-03 |
|
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: 42.61 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 400 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGK------VHWSNVNESEPSFEAtrrnrysvayaaqkpwll 473
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTieigetVKLAYVDQSRDALDP------------------ 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 474 NATVEENITFGSpfnkqrykavtdacslqpdidllpfgDQTEIGERGIN---------------------LSGGQRQRIC 532
Cdd:TIGR03719 400 NKTVWEEISGGL--------------------------DIIKLGKREIPsrayvgrfnfkgsdqqkkvgqLSGGERNRVH 453
|
170 180 190
....*....|....*....|....*....|....*..
gi 1786986074 533 VARALYQNTNIVFLDDPFSALDIHLSDHLmQEGILKF 569
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDVETLRAL-EEALLNF 489
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
523-610 |
1.79e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 41.70 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 523 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD---HLMQEgilkfLQDDKR-TLVLVTHKLQYLTH-ADWIIAMK 597
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSqliNLMLE-----LQEKQGiSYIYVTQHLGMMKHiSDQVLVMH 224
|
90
....*....|...
gi 1786986074 598 DGSVLREGTLKDI 610
Cdd:PRK15112 225 QGEVVERGSTADV 237
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1050-1207 |
2.13e-03 |
|
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: 40.94 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1050 GQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECK-CTDDR 1128
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHAdHSDEQ 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1786986074 1129 LWEALEIAQLkNMVKSLPGGldavvteggeNFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILqkvvMTAFA 1207
Cdd:cd03231 106 VEEALARVGL-NGFEDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF----AEAMA 169
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
406-584 |
2.14e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 42.08 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 406 RIPT---GQLTMIVGQVGCGKSSLLlAIL-GEMQ----TLEGKVHWSNV------NESEPSFEATRRNRYSVAYAAQK-- 469
Cdd:COG1245 92 GLPVpkkGKVTGILGPNGIGKSTAL-KILsGELKpnlgDYDEEPSWDEVlkrfrgTELQDYFKKLANGEIKVAHKPQYvd 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 470 --PWLLNATVEENItfgspfnkqryKAVTDACSLQPDIDLLpfgDQTEIGERGI-NLSGGQRQRICVARALYQNTNIVFL 546
Cdd:COG1245 171 liPKVFKGTVRELL-----------EKVDERGKLDELAEKL---GLENILDRDIsELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|....*...
gi 1786986074 547 DDPFSALDIhlSDHLMQEGILKFLQDDKRTLVLVTHKL 584
Cdd:COG1245 237 DEPSSYLDI--YQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
782-944 |
2.15e-03 |
|
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: 41.53 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 782 NLLNK-IILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTllcLSAIGMI------SYATPVFLVALLPL- 853
Cdd:cd18784 73 NLLFRsIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSL---VKAIGVIvfmfklSWQLSLVTLIGLPLi 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 854 -GVAFYFiQKYFRVASKDLQeldDStqlplLCHFSETAE----GLTTIRAFRHET----RFK---QRMLELTDTNNIAYL 921
Cdd:cd18784 150 aIVSKVY-GDYYKKLSKAVQ---DS-----LAKANEVAEetisSIRTVRSFANEDgeanRYSeklKDTYKLKIKEALAYG 220
|
170 180
....*....|....*....|....*..
gi 1786986074 922 FLSAANRWLE----VRTDYLGACIVLT 944
Cdd:cd18784 221 GYVWSNELTElaltVSTLYYGGHLVIT 247
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
524-587 |
2.21e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 2.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786986074 524 SGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLmQEGILKFlqddKRTLVLVTHKLQYL 587
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWL-ETYLLKW----PKTFIVVSHAREFL 404
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
410-619 |
2.88e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.14 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 410 GQLTMIVGQVGCGKSSLLLAILGEMQT--LEGKVHWSNVNESEPSFeaTRRNRYSVAYAAQKPwllNATVEENITFgSPF 487
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFPKKQETF--ARISGYCEQNDIHSP---QVTVRESLIY-SAF 979
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 488 -------NKQRYKAVTDACSLQPDIDLLpfgDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD 559
Cdd:PLN03140 980 lrlpkevSKEEKMMFVDEVMELVELDNL---KDAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAA 1056
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 560 HLMQEgiLKFLQDDKRTLVLVTHK--LQYLTHADWIIAMK-DGSVLREGTLKDIQTKDVELYE 619
Cdd:PLN03140 1057 IVMRT--VRNTVDTGRTVVCTIHQpsIDIFEAFDELLLMKrGGQVIYSGPLGRNSHKIIEYFE 1117
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
518-651 |
3.05e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 518 ERGIN-LSGGQRQRICVARAL-YQNTNIVF-LDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTHADWII 594
Cdd:PRK00635 471 ERALAtLSGGEQERTALAKHLgAELIGITYiLDEPSIGLHPQDTHKLIN--VIKKLRDQGNTVLLVEHDEQMISLADRII 548
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786986074 595 ------AMKDGSVLREGTLKDIQTKDVELYEHWKtlmnRQDQELEKDmEADQTTLERKTLRRA 651
Cdd:PRK00635 549 digpgaGIFGGEVLFNGSPREFLAKSDSLTAKYL----RQELTIPIP-EKRTNSLGTLTLSKA 606
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1047-1235 |
4.56e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.05 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1047 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG--IDISKlPLHTLRSrlSIIL------QDPILFSGSIRFNL 1118
Cdd:PRK11288 276 VRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRS-PRDAIRA--GIMLcpedrkAEGIIPVHSVADNI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1119 DPECK-------CTDDRLWEA----LEIAQLKnmVKSlPGGLDAVVteggeNFSVGQRQLFCLARAFVRKSSILIMDEAT 1187
Cdd:PRK11288 353 NISARrhhlragCLINNRWEAenadRFIRSLN--IKT-PSREQLIM-----NLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1188 ASIDM-ATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNI 1235
Cdd:PRK11288 425 RGIDVgAKHEIYNVIYELAAQGVAVLFVSSDLPEVLgVADRIVVMREGRI 474
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
784-908 |
4.70e-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: 40.51 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 784 LNKIILGPIRFFDTTPLGLILNRFSaDTNIIDQHIPPTLESLTRSTLLCL-SAIGMISYATPVFLVALLPL---GVAFYF 859
Cdd:cd18570 82 FKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIiSGIILFFYNWKLFLITLLIIplyILIILL 160
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1786986074 860 IQKYFRVASKDLQELDDSTQlpllCHFSETAEGLTTIRAFRHETRFKQR 908
Cdd:cd18570 161 FNKPFKKKNREVMESNAELN----SYLIESLKGIETIKSLNAEEQFLKK 205
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
516-627 |
5.99e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 516 IGERGINLSGGQRQRICVARALY---QNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLTHADW 592
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQ--LRTLVSLGHSVIYIDHDPALLKQADY 1770
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1786986074 593 IIAM------KDGSVLREGTLKDIQ-TKDVELyehwKTLMNR 627
Cdd:PRK00635 1771 LIEMgpgsgkTGGKILFSGPPKDISaSKDSLL----KTYMCN 1808
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1055-1216 |
6.43e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.51 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1055 ICGRTGSGKSSLslaffrmvdifdgkivIDGIDISKLPLHTLRSRLSIILQDPIlFSGSIRFNLDPECKCTDDRLWEAL- 1133
Cdd:cd03240 27 IVGQNGAGKTTI----------------IEALKYALTGELPPNSKGGAHDPKLI-REGEVRAQVKLAFENANGKKYTITr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 1134 EIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFC------LARAFVRKSSILIMDEATASIDmaTENILQKVV----- 1202
Cdd:cd03240 90 SLAILENVIFCHQGESNWPLLDMRGRCSGGEKVLASliirlaLAETFGSNCGILALDEPTTNLD--EENIEESLAeiiee 167
|
170
....*....|....
gi 1786986074 1203 MTAFADRTVVTIAH 1216
Cdd:cd03240 168 RKSQKNFQLIVITH 181
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
523-597 |
6.65e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.88 E-value: 6.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1786986074 523 LSGGQRQRICVARAL----YQNTNIVFLDDPFSALDIHLSDHLMqEGILKFLqDDKRTLVLVTHKLQYLTHADWIIAMK 597
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALA-EAILEHL-VKGAQVIVITHLPELAELADKLIHIK 154
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
754-920 |
7.18e-03 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 40.01 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 754 CGAGIFLCLVTSLTvewmgltaaKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCL 833
Cdd:cd18590 55 LRGGLFMCTLSRLN---------LRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 834 SAIG-MISYATPVFLVALL--PLGVAfyfIQK----YFRVASKDLQE-LDDSTQLPllchfSETAEGLTTIRAFRHET-- 903
Cdd:cd18590 126 GMLGfMLSLSWQLTLLTLIemPLTAI---AQKvyntYHQKLSQAVQDsIAKAGELA-----REAVSSIRTVRSFKAEEee 197
|
170 180
....*....|....*....|..
gi 1786986074 904 --RFKQ---RMLELTDTNNIAY 920
Cdd:cd18590 198 acRYSEaleRTYNLKDRRDTVR 219
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
748-913 |
9.41e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 39.75 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 748 AGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSAdTNIIDQHIPPTL-ESLT 826
Cdd:cd18567 46 IGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSRFGS-LDEIQQTLTTGFvEALL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786986074 827 RSTLLCLSAIGMISYATPVFLVALlpLGVAFYFI-----QKYFRVASKDLQELD---DStqlpllcHFSETAEGLTTIRA 898
Cdd:cd18567 125 DGLMAILTLVMMFLYSPKLALIVL--AAVALYALlrlalYPPLRRATEEQIVASakeQS-------HFLETIRGIQTIKL 195
|
170
....*....|....*
gi 1786986074 899 FRHETRFKQRMLELT 913
Cdd:cd18567 196 FGREAEREARWLNLL 210
|
|
| |
