|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-1502 |
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: 1484.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 14 WNQTEPEpaatslLSLCFLRTAGVWVPPMYLWVLGPIYLLFIHHHGRGYLRMSPLFKAKMVLGFALIVLCTSSVAVALWK 93
Cdd:TIGR00957 16 WHTSNPD------FTKCFQNTVLAWVPCFYLWVCFPCYFLYLSRHDRGYIQMTHLNKTKTALGFLLWIVCWADLFYSFWE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 94 IQQGTPEAPEFLIHPTVWLTTMSFAVFLIHTERKKGVQSSGVLFGYWLLCFV---LPATNAAQQASGAGFQSDPVRHLST 170
Cdd:TIGR00957 90 RSHGRAPAPVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALVcalAILRSKILLALKEDAIVDPFRDTTF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 171 YLCLSLVVAQFVLSCLADQPPFFPEDPQQSNPCPETGAAFPSKATFWWVSGLVWRGYRRPLRPKDLWSLGRENSSEELVS 250
Cdd:TIGR00957 170 YIYFALVLSQLVLSCFSDKSPLFSETNHDPNPCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 251 RLEKEWMRNRSAARRHNKAIAF------KRKGGSGMKAPETEPFL--RQEGSQWRP-LLKAIWQVFHSTFLLGTLSLIIS 321
Cdd:TIGR00957 250 VLVENWKKECKKTRKQPVSAVYgkkdpsKPKGSSQLDANEEVEALivKSPHKPRKPsLFKVLYKTFGPYFLMSFCFKAIH 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 322 DVFRFTVPKLLSLFLEFIGDPKPPAWKGYLLAVLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITGLVYRKVLALSSGSR 401
Cdd:TIGR00957 330 DLMMFIGPQILSLLIRFVNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSAR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 402 KASAVGDVVNLVSVDVQRLTESVLYLNGLWLPLVWIVVCFVYLWQLLGPSALTAIAVFLSLLPLNFFISKKRNHHQEEQM 481
Cdd:TIGR00957 410 KSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHM 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 482 RQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLLFSVSLVSFQVSTFLVALVVFAVHTLVAE-N 560
Cdd:TIGR00957 490 KSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDEnN 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 561 AMNAEKAFVTLTVLNILNKAQAFLPFSIHSLVQARVSFDRLVTFLCLEEVDPGVVDSSSSGSAAGkDCITIHSATFAWSQ 640
Cdd:TIGR00957 570 ILDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEG-NSITVHNATFTWAR 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 641 ESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQEAWVQNTSVVENVCFGQELDPP 720
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEK 728
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 721 WLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVIGPGG 800
Cdd:TIGR00957 729 YYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEG 808
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 801 LLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGAL---MCLLDQARQPGDRGE----GETEPGTSTKD 873
Cdd:TIGR00957 809 VLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFaefLRTYAPDEQQGHLEDswtaLVSGEGKEAKL 888
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 874 PRGT-----SAGRrpELRRERSIKSVPEKDRTTSEAQT-EVPLDDPDRAGWP-AGKDSIQYGRVKATVHLAYLRAVGTPL 946
Cdd:TIGR00957 889 IENGmlvtdVVGK--QLQRQLSASSSDSGDQSRHHGSSaELQKAEAKEETWKlMEADKAQTGQVELSVYWDYMKAIGLFI 966
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 947 CLYALFLFLCQQVASFCRGYWLSLWADDPAVGGQQTQAALRGGIFGLLGCLQAIGLFASMAAVLLGGARASRLLFQRLLW 1026
Cdd:TIGR00957 967 TFLSIFLFVCNHVSALASNYWLSLWTDDPMVNGTQNNTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLH 1046
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1027 DVVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLLYAGFQSLYV 1106
Cdd:TIGR00957 1047 NKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYV 1126
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1107 VSSCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANVELLGNGLVFAA 1186
Cdd:TIGR00957 1127 ASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFA 1206
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1187 ATCAVLSKAHLSAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDYAWTPKEAPWRLPTCAAQPPWPQGGQIE 1266
Cdd:TIGR00957 1207 ALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSGWPPRGRVE 1286
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1267 FRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIP 1346
Cdd:TIGR00957 1287 FRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIP 1366
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1347 QDPILFPGSLRMNLDLLQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILD 1426
Cdd:TIGR00957 1367 QDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLD 1446
|
1450 1460 1470 1480 1490 1500 1510
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 1427 EATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFYRLAQESGL 1502
Cdd:TIGR00957 1447 EATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAKDAGL 1522
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
171-1501 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 761.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 171 YLCLSLVVAQFVLSCLA-----------DQPPFFPEDPQQS---------NPCPETGAAFPSKATFWWVSGLVWRGYRRP 230
Cdd:PLN03130 175 YLYISEVAAQVLFGILLlvyfpnldpypGYTPIGSESVDDYeyeelpggeQICPERHANIFSRIFFGWMTPLMQLGYKRP 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 231 LRPKDLWSLGRENSSEELVSRLEKEWMRNRSAARrhnkaiafkrkggsgmkapetepflrqegsQWrpLLKAIWQVFHST 310
Cdd:PLN03130 255 LTEKDVWKLDTWDQTETLYRSFQKCWDEELKKPK------------------------------PW--LLRALNNSLGGR 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 311 FLLGTLSLIISDVFRFTVPKLLSLFLEFI--GDPkppAWKGYLLAVLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITGL 388
Cdd:PLN03130 303 FWLGGFFKIGNDLSQFVGPLLLNLLLESMqnGEP---AWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLVAA 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 389 VYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTESVLYLNGLWLPLVWIVVCFVYLWQLLGPSALTAIAVFLSLLPLNFF 468
Cdd:PLN03130 380 VFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQTF 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 469 ISKKRNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLLFSVSLVSFQVSTFLVAL 548
Cdd:PLN03130 460 IISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNSIPVLVTV 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 549 VVFAVHTLVAENAMNAeKAFVTLTVLNILNKAQAFLPFSIHSLVQARVSFDRLVTFLCLEE--------VDPGVvdssss 620
Cdd:PLN03130 540 VSFGVFTLLGGDLTPA-RAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEErvllpnppLEPGL------ 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 621 gsaagkDCITIHSATFAW-SQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVE-GFVSIEGAVAYVPQ 698
Cdd:PLN03130 613 ------PAISIKNGYFSWdSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTVAYVPQ 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 699 EAWVQNTSVVENVCFGQELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDD 778
Cdd:PLN03130 687 VSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDD 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 779 PLAALDAHVGQHVFNQVIGpgGLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGALMCLLDQARQPG 858
Cdd:PLN03130 767 PLSALDAHVGRQVFDKCIK--DELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAGKME 844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 859 DRGEGETEPGTSTKDPRGTSAGRRPELRRERSIKSVPEKDRTTSEAQTEVplddpdragwpagkdsiQYGRVKATVHLAY 938
Cdd:PLN03130 845 EYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKKKSKEGKSVLIKQEER-----------------ETGVVSWKVLERY 907
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 939 LRAVGTPLCLYALFLF-LCQQVASFCRGYWLSLWADdpAVGGQQTQAALRGGIFGLLGCLQAIGLFASMAAVLLGGARAS 1017
Cdd:PLN03130 908 KNALGGAWVVMILFLCyVLTEVFRVSSSTWLSEWTD--QGTPKTHGPLFYNLIYALLSFGQVLVTLLNSYWLIMSSLYAA 985
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1018 RLLFQRLLWDVVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLL 1097
Cdd:PLN03130 986 KRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVL 1065
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1098 YAGFQSLYVVSSCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANVEL 1177
Cdd:PLN03130 1066 FYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLET 1145
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1178 LGNGLVFAAATCAVLSKAHLS-----AGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDYAWTPKEAPWRLPT 1252
Cdd:PLN03130 1146 LGGLMIWLTASFAVMQNGRAEnqaafASTMGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPSEAPLVIEN 1225
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1253 CAAQPPWPQGGQIEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAH 1332
Cdd:PLN03130 1226 NRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISK 1305
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1333 VGLHTLRSRISIIPQDPILFPGSLRMNLDLLQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCL 1412
Cdd:PLN03130 1306 FGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSL 1385
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1413 ARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKG- 1491
Cdd:PLN03130 1386 ARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGs 1465
|
1370
....*....|
gi 1827346401 1492 LFYRLAQESG 1501
Cdd:PLN03130 1466 AFSKMVQSTG 1475
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
197-1501 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 752.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 197 PQQSNPCPETGAAFPSKATFWWVSGLVWRGYRRPLRPKDLWSLGRENSSEELVSRLEKEWMrnrsaarrhnkaiafkrkg 276
Cdd:PLN03232 221 RGGENICPERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWT------------------- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 277 gsgmkapetepflrQEGSQWRP-LLKAIWQVFHSTFLLGTLSLIISDVFRFTVPKLLSLFLEFI--GDPkppAWKGYLLA 353
Cdd:PLN03232 282 --------------EESRRPKPwLLRALNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMqeGDP---AWVGYVYA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 354 VLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITGLVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTESVLYLNGLWLP 433
Cdd:PLN03232 345 FLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSA 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 434 LVWIVVCFVYLWQLLGPSALTAIAVFLSLLPLNFFISKKRNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDR 513
Cdd:PLN03232 425 PFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESR 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 514 VLGIRGQELGALRTSGLLFSVSlvSFQVSTF--LVALVVFAVHTLVAENAMNAeKAFVTLTVLNILNKAQAFLPFSIHSL 591
Cdd:PLN03232 505 IQGIRNEELSWFRKAQLLSAFN--SFILNSIpvVVTLVSFGVFVLLGGDLTPA-RAFTSLSLFAVLRSPLNMLPNLLSQV 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 592 VQARVSFDRLVTFLCLEE--------VDPGVvdssssgsaagkDCITIHSATFAW-SQESPPCLHRINLTVPQGCLLAVV 662
Cdd:PLN03232 582 VNANVSLQRIEELLLSEErilaqnppLQPGA------------PAISIKNGYFSWdSKTSKPTLSDINLEIPVGSLVAIV 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 663 GPVGAGKSSLLSALLGELSKVE-GFVSIEGAVAYVPQEAWVQNTSVVENVCFGQELDPPWLERVLEACALQPDVDSFPEG 741
Cdd:PLN03232 650 GGTGEGKTSLISAMLGELSHAEtSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGR 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 742 IHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVIGPGglLQGTTRILVTHALHILPQAD 821
Cdd:PLN03232 730 DLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDE--LKGKTRVLVTNQLHFLPLMD 807
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 822 WIIVLANGAIAEMGSYQELLQRKGALMCLLDQArqpgdrGEGETEPGTSTKDPRGTSAGRRPELR-RERSIKSVPEKDRT 900
Cdd:PLN03232 808 RIILVSEGMIKEEGTFAELSKSGSLFKKLMENA------GKMDATQEVNTNDENILKLGPTVTIDvSERNLGSTKQGKRG 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 901 TSeaqteVPLDDPDRagwpagkdsiQYGRVKATVHLAYLRAVGTPLCLYALFL-FLCQQVASFCRGYWLSLWADdpavgg 979
Cdd:PLN03232 882 RS-----VLVKQEER----------ETGIISWNVLMRYNKAVGGLWVVMILLVcYLTTEVLRVSSSTWLSIWTD------ 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 980 QQTQAALRGG----IFGLLGCLQAIGLFASMAAVLLGGARASRLLFQRLLWDVVRSPISFFERTPIGHLLNRFSKETDTV 1055
Cdd:PLN03232 941 QSTPKSYSPGfyivVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDI 1020
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1056 DVDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLLYAGFQSLYVVSSCQLRRLESASYSSVCSHMAETFQGST 1135
Cdd:PLN03232 1021 DRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLS 1100
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1136 VVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANVELLGNGLVFAAATCAVLSKAHLS-----AGLVGFSVSAAL 1210
Cdd:PLN03232 1101 SIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLRNGNAEnqagfASTMGLLLSYTL 1180
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1211 QVTQTLQWVVRNWTDLENSIVSVERMQDYAWTPKEAPWRLPTCAAQPPWPQGGQIEFRDFGLRYRPELPLAVQGVSFKIH 1290
Cdd:PLN03232 1181 NITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVS 1260
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1291 AGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLDLLQEHSDEA 1370
Cdd:PLN03232 1261 PSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDAD 1340
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1371 IWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ 1450
Cdd:PLN03232 1341 LWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKS 1420
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 1451 CTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKG-LFYRLAQESG 1501
Cdd:PLN03232 1421 CTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVHSTG 1472
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
297-1486 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 631.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 297 RPLLKAIWQVFHSTFLLgtlsLIISDVFRFTVPKLLSLFLEFIGDPkPPAW-KGYLLAVLMFLSACLQTLFEQQNMYRLK 375
Cdd:PTZ00243 236 RTLFAALPYYVWWQIPF----KLLSDVCTLTLPVLLKYFVKFLDAD-NATWgRGLGLVLTLFLTQLIQSVCLHRFYYISI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 376 VLQMRLRSAITGLVYRKVLALSSGS--RKASAVGDVVNLVSVDVQRLTESVLYLNGLWLPLVWIVVCFVYLWQLLGPSAL 453
Cdd:PTZ00243 311 RCGLQYRSALNALIFEKCFTISSKSlaQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCAL 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 454 TAIAVFLSLLPLNFFISKKRNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALR---TSGL 530
Cdd:PTZ00243 391 MAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRdvqLARV 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 531 LFSvsLVSFQVSTFLVAlVVFAVHTLVAeNAMNAEKAFVTLTVLNILNKAQAFLPFSIHSLVQARVSFDRLVTFL----- 605
Cdd:PTZ00243 471 ATS--FVNNATPTLMIA-VVFTVYYLLG-HELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLecdna 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 606 -----------------------------------------------------------CLEEVDP--------GVVDSS 618
Cdd:PTZ00243 547 tcstvqdmeeywreqrehstacqlaavlenvdvtafvpvklprapkvktsllsralrmlCCEQCRPtkrhpspsVVVEDT 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 619 SSGSAAGKDCITIHSATFAWSQESPP----------------------CLHRINLTVPQGCLLAVVGPVGAGKSSLLSAL 676
Cdd:PTZ00243 627 DYGSPSSASRHIVEGGTGGGHEATPTsersaktpkmktddffelepkvLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSL 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 677 LGELSKVEGFVSIEGAVAYVPQEAWVQNTSVVENVCFGQELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGG 756
Cdd:PTZ00243 707 LSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGG 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 757 QKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVIgpGGLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGS 836
Cdd:PTZ00243 787 QKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF--LGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGS 864
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 837 YQELLQRKgalMClldqarqpgdrgEGETEPGTSTKDPRGTSAGRR-PELRRERSIKSVPEKDRTTSEAQTEVplDDPDR 915
Cdd:PTZ00243 865 SADFMRTS---LY------------ATLAAELKENKDSKEGDADAEvAEVDAAPGGAVDHEPPVAKQEGNAEG--GDGAA 927
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 916 AGWPAGKDSIQ----YGRVKATVHLAYLRAV-GTPLCLYALFLFLCQQVASFCRGYWLSLWADDPavggqqtqaalrggi 990
Cdd:PTZ00243 928 LDAAAGRLMTReekaSGSVPWSTYVAYLRFCgGLHAAGFVLATFAVTELVTVSSGVWLSMWSTRS--------------- 992
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 991 fglLGCLQAIGLFASMAAVLLGGA--------------RASRLLFQRLLWDVVRSPISFFERTPIGHLLNRFSKETDTVD 1056
Cdd:PTZ00243 993 ---FKLSAATYLYVYLGIVLLGTFsvplrfflsyeamrRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILD 1069
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1057 VDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLLYAGFQSLYVVSSCQLRRLESASYSSVCSHMAETFQGSTV 1136
Cdd:PTZ00243 1070 NTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSAT 1149
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1137 VRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANVELLGNGLVFAAA----TCAVLSKAHLSAGLVGFSVSAALQV 1212
Cdd:PTZ00243 1150 ITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIAligvIGTMLRATSQEIGLVSLSLTMAMQT 1229
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1213 TQTLQWVVRNWTDLENSIVSVERMQDYA-WTPKEAPWRL---------------------------PTCAAqPPWPQGGQ 1264
Cdd:PTZ00243 1230 TATLNWLVRQVATVEADMNSVERLLYYTdEVPHEDMPELdeevdalerrtgmaadvtgtvviepasPTSAA-PHPVQAGS 1308
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISI 1344
Cdd:PTZ00243 1309 LVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSM 1388
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1345 IPQDPILFPGSLRMNLDLLQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILI 1424
Cdd:PTZ00243 1389 IPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFI 1468
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 1425 L-DEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQL 1486
Cdd:PTZ00243 1469 LmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
204-1493 |
1.78e-140 |
|
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: 469.78 E-value: 1.78e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 204 PETGAAFPSKATFWWVSGLVWRGYRRPLRPKDLWSLGRENSSEELVSRLEKEWMRNRSAARRHNKaiafkrkggsgmkap 283
Cdd:TIGR01271 5 PVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAKKNPK--------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 284 etepflrqegsqwrpLLKAIWQVFHSTFLLGTLSLIISDVFRFTVPKLLS-LFLEFIGDPKPPAWKGYLLAVLMFLSACL 362
Cdd:TIGR01271 70 ---------------LLNALRRCFFWRFVFYGILLYFGEATKAVQPLLLGrIIASYDPFNAPEREIAYYLALGLCLLFIV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 363 QTLFEQQNMYRLKVLQMRLRSAITGLVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTESVLYLNGLWLPLVWIVVCFV 442
Cdd:TIGR01271 135 RTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 443 YLWQLLGPSALTAIAVFLSLLPLNFFISKKRNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQEL 522
Cdd:TIGR01271 215 LIWELLEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDEL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 523 GALRTSGLLFSVSLVSFQVSTFLVALVVFAVHTLVaeNAMNAEKAFVTLT---VLNILNKAQafLPFSIHSLVQARVSFD 599
Cdd:TIGR01271 295 KLTRKIAYLRYFYSSAFFFSGFFVVFLSVVPYALI--KGIILRRIFTTISyciVLRMTVTRQ--FPGAIQTWYDSLGAIT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 600 RLVTFLCLEEV---------------------DPGVVDSSSSGSAAGKDCITIH---SATFA-WSQESPPCLHRINLTVP 654
Cdd:TIGR01271 371 KIQDFLCKEEYktleynltttevemvnvtaswDEGIGELFEKIKQNNKARKQPNgddGLFFSnFSLYVTPVLKNISFKLE 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 655 QGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQEAWVQNTSVVENVCFGQELDPPWLERVLEACALQPD 734
Cdd:TIGR01271 451 KGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEED 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 735 VDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVIGPggLLQGTTRILVTHAL 814
Cdd:TIGR01271 531 IALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCK--LMSNKTRILVTSKL 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 815 HILPQADWIIVLANGAIAEMGSYQELLQRKGALMCLL------------------------------------------- 851
Cdd:TIGR01271 609 EHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLlgleafdnfsaerrnsiltetlrrvsidgdstvfsgpetikqs 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 852 -------------------------------------------DQARQPGDRGEG---ETEPGTSTKdPRG--------- 876
Cdd:TIGR01271 689 fkqpppefaekrkqsiilnpiasarkfsfvqmgpqkaqattieDAVREPSERKFSlvpEDEQGEESL-PRGnqyhhglqh 767
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 877 ------------TSAGRRPELRRE-----RSIKSVPEKDRTTSEA-------------QTEVPLDDPDRAGWPAGKDSIQ 926
Cdd:TIGR01271 768 qaqrrqsvlqlmTHSNRGENRREQlqtsfRKKSSITQQNELASELdiysrrlskdsvyEISEEINEEDLKECFADERENV 847
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 927 YgrvKATVHLAYLRAVGTP-----LCLYALFLFLCQQVASFCrGYWLslWADDPAVGGQQTQAALRGG------------ 989
Cdd:TIGR01271 848 F---ETTTWNTYLRYITTNrnlvfVLIFCLVIFLAEVAASLL-GLWL--ITDNPSAPNYVDQQHANASspdvqkpviitp 921
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 990 -----IF----GLLGCLQAIGLFASMAAV--LLggaRASRLLFQRLLWDVVRSPISFFERTPIGHLLNRFSKETDTVDVD 1058
Cdd:TIGR01271 922 tsayyIFyiyvGTADSVLALGFFRGLPLVhtLL---TVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDM 998
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1059 IPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLLYAGFQSLYVVSSCQLRRLESASYSSVCSHMAETFQGSTVVR 1138
Cdd:TIGR01271 999 LPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIR 1078
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1139 AFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANVELLGNgLVFAAATCAVLSKAHLSAGLVGFSVSAALQVTQTLQW 1218
Cdd:TIGR01271 1079 AFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFV-FFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQW 1157
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1219 VVRNWTDLENSIVSVERMQDYAWTPKEAPwrLPTCAAQPP----------------WPQGGQIEFRDFGLRYRPELPLAV 1282
Cdd:TIGR01271 1158 AVNSSIDVDGLMRSVSRVFKFIDLPQEEP--RPSGGGGKYqlstvlvienphaqkcWPSGGQMDVQGLTAKYTEAGRAVL 1235
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1283 QGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQeAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLDL 1362
Cdd:TIGR01271 1236 QDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDP 1314
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1363 LQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQA 1442
Cdd:TIGR01271 1315 YEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRK 1394
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 1443 MLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLF 1493
Cdd:TIGR01271 1395 TLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
947-1240 |
4.43e-125 |
|
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: 391.46 E-value: 4.43e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 947 CLYALFLFLCQQVASFCRGYWLSLWADDPAVGGQQT--QAALRGGIFGLLGCLQAIGLFASMAAVLLGGARASRLLFQRL 1024
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDteQRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1025 LWDVVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLLYAGFQSL 1104
Cdd:cd18603 81 LHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1105 YVVSSCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANVELLGNGLVF 1184
Cdd:cd18603 161 YVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 1185 AAATCAVLSKAHLSAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDYA 1240
Cdd:cd18603 241 FAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
313-601 |
1.82e-117 |
|
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: 370.26 E-value: 1.82e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 313 LGTLSLIISDVFRFTVPKLLSLFLEFIGDPKPPAWKGYLLAVLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITGLVYRK 392
Cdd:cd18595 1 LAALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 393 VLALSSGSRKASAVGDVVNLVSVDVQRLTESVLYLNGLWLPLVWIVVCFVYLWQLLGPSALTAIAVFLSLLPLNFFISKK 472
Cdd:cd18595 81 ALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 473 RNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLLFSVSLVSFQVSTFLVALVVFA 552
Cdd:cd18595 161 IKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1827346401 553 VHTLVAE-NAMNAEKAFVTLTVLNILNKAQAFLPFSIHSLVQARVSFDRL 601
Cdd:cd18595 241 TYVLSDPdNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1263-1483 |
2.06e-112 |
|
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: 353.72 E-value: 2.06e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1263 GQIEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRI 1342
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1343 SIIPQDPILFPGSLRMNLDLLQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQI 1422
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 1423 LILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSP 1483
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
629-829 |
1.11e-106 |
|
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: 337.13 E-value: 1.11e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAW---SQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQEAWVQNT 705
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 706 SVVENVCFGQELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDA 785
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1827346401 786 HVGQHVFNQVIGpGGLLQGTTRILVTHALHILPQADWIIVLANG 829
Cdd:cd03250 161 HVGRHIFENCIL-GLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
936-1498 |
1.18e-98 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 329.43 E-value: 1.18e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 936 LAYLRAVGTPLCLyALFLFLCQQVASFCRGYWLSLWADDPAVGGQQTQAALRGGIFGLLGCLQAIGLFASMAAVLLGGAR 1015
Cdd:COG1132 13 LRYLRPYRGLLIL-ALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1016 ASRLLFQRLLWDVVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLeVSLVVAVAT-PLATVAILPL 1094
Cdd:COG1132 92 VVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLI-GALVVLFVIdWRLALIVLLV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1095 FLLYAGFQSLYVVSSCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAAN 1174
Cdd:COG1132 171 LPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1175 VELLGNGLVFAAATCAVL--SKAHLSAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDYAWTPKEAPwrlPT 1252
Cdd:COG1132 251 MELLGNLGLALVLLVGGLlvLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP---DP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1253 CAAQPPWPQGGQIEFRDFGLRYRPELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAH 1332
Cdd:COG1132 328 PGAVPLPPVRGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRD 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1333 VGLHTLRSRISIIPQDPILFPGSLRMNLDL-LQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQ--- 1408
Cdd:COG1132 407 LTLESLRRQIGVVPQDTFLFSGTIRENIRYgRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQria 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1409 ------LlclarallrKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGS 1482
Cdd:COG1132 487 iarallK---------DPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
570
....*....|....*.
gi 1827346401 1483 PAQLLAQKGLFYRLAQ 1498
Cdd:COG1132 558 HEELLARGGLYARLYR 573
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
313-601 |
2.62e-90 |
|
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: 294.78 E-value: 2.62e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 313 LGTLSLIISDVFRFTVPKLLSLFLEFIGD-PKPPAWKGYLLAVLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITGLVYR 391
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSyPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 392 KVLALSSGSRKASAVGDVVNLVSVDVQRLTESVLYLNGLWLPLVWIVVCFVYLWQLLGPSALTAIAVFLSLLPLNFFISK 471
Cdd:cd18579 81 KALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 472 KRNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLLFSVSLVSFQVSTFLVALVVF 551
Cdd:cd18579 161 LISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1827346401 552 AVHTLVAeNAMNAEKAFVTLTVLNILNKAQAFLPFSIHSLVQARVSFDRL 601
Cdd:cd18579 241 ATYVLLG-NPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
951-1240 |
3.23e-85 |
|
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: 280.54 E-value: 3.23e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 951 LFLFLCQQVASFCRGYWLSLWADDPAVGGQQTQAALRGGIFGLLGCLQAIGLFASMAAVLLGGARASRLLFQRLLWDVVR 1030
Cdd:cd18580 5 LLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1031 SPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLLYAGFQSLYVVSSC 1110
Cdd:cd18580 85 APMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYLRTSR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1111 QLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANVELLGNGLVFAAATCA 1190
Cdd:cd18580 165 QLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALVVALLA 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1191 VLSKAHLSAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDYA 1240
Cdd:cd18580 245 VLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
988-1499 |
3.11e-83 |
|
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: 289.43 E-value: 3.11e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 988 GGIFGLLGCLQAIGLFASMAAVLLGGARASRLLFQRLLWDVVRSPISFFERTPIGHLLNRFSkETDTVDVDIPDKLRSLL 1067
Cdd:COG2274 199 AIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTAL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1068 MYAFGLLeVSLVV--AVATPLATVAILpLFLLYAGfqsLYVVSSCQLRRL---ESASYSSVCSHMAETFQGSTVVRAFRT 1142
Cdd:COG2274 278 LDLLFVL-IFLIVlfFYSPPLALVVLL-LIPLYVL---LGLLFQPRLRRLsreESEASAKRQSLLVETLRGIETIKALGA 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1143 QAPFVAQNNARVDESQRISFPRLVADRWL---AANVELLGNGLVFAAATCAVLSKaHLSAG-LVGFSvSAALQVTQTLQW 1218
Cdd:COG2274 353 ESRFRRRWENLLAKYLNARFKLRRLSNLLstlSGLLQQLATVALLWLGAYLVIDG-QLTLGqLIAFN-ILSGRFLAPVAQ 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1219 VVRNWTDLENSIVSVERMQDYAWTPKEapwRLPTCAAQPPWPQGGQIEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIV 1298
Cdd:COG2274 431 LIGLLQRFQDAKIALERLDDILDLPPE---REEGRSKLSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIV 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1299 GRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLDLLQEH-SDEAIWAALET 1377
Cdd:COG2274 508 GRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDaTDEEIIEAARL 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1378 VQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIA 1457
Cdd:COG2274 588 AGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIA 667
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1827346401 1458 HRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFYRLAQE 1499
Cdd:COG2274 668 HRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1259-1483 |
5.26e-76 |
|
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: 250.79 E-value: 5.26e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1259 WPQGGQIEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTL 1338
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1339 RSRISIIPQDPILFPGSLRMNLDLLQEHSDEAIWAALetvqlkalvaslpgqlqyKCADRGEDLSVGQKQLLCLARALLR 1418
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 1419 KTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSP 1483
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
950-1240 |
1.82e-72 |
|
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: 243.92 E-value: 1.82e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 950 ALFLFLCQQVASFCRGYWLSLWADD-PAVGGQQTQaalrgGIFGLLGCLQAIGLFASMAAVLLGGARASRLLFQRLLWDV 1028
Cdd:cd18606 4 LLLLLILSQFAQVFTNLWLSFWTEDfFGLSQGFYI-----GIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1029 VRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLLYAGFQSLYVVS 1108
Cdd:cd18606 79 LRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1109 SCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANVELLGNGLVFAAAT 1188
Cdd:cd18606 159 SRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLIVAL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 1189 CAVLSKAHLSAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDYA 1240
Cdd:cd18606 239 LCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
950-1239 |
5.58e-70 |
|
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: 236.98 E-value: 5.58e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 950 ALFLFLCQQVASFCRGYWLSLWADDPAVGGQQTQAALR----GGIFGLLGCLQAIGLFASMAAVLLGGARASRLLFQRLL 1025
Cdd:cd18604 4 LLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVSvlyyLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1026 WDVVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLLYAGFQSLY 1105
Cdd:cd18604 84 HSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGRLY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1106 VVSSCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANVELLGnGLVFA 1185
Cdd:cd18604 164 LRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLG-ALFSF 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 1186 AATCAVLSKAHLSAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDY 1239
Cdd:cd18604 243 ATAALLVYGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEY 296
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
297-853 |
1.40e-69 |
|
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: 248.98 E-value: 1.40e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 297 RPLLKAIWQVFHSTFLLGTLSLIISDVFRFTVPK-LLSLFLEFIgdpkppawkgYLLAVLMFLSACLQTLFEQQNMYRLK 375
Cdd:COG2274 152 RRYRRLLLQVLLASLLINLLALATPLFTQVVIDRvLPNQDLSTL----------WVLAIGLLLALLFEGLLRLLRSYLLL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 376 VLQMRLRSAITGLVYRKVLALSSGSRKASAVGDVVNLVSvDVQR----LTESVL--YLNGLWLpLVWIVVCFVYLWQLLG 449
Cdd:COG2274 222 RLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESirefLTGSLLtaLLDLLFV-LIFLIVLFFYSPPLAL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 450 PSALTAIAVFLsllpLNFFISKKRNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQ----ELGAL 525
Cdd:COG2274 300 VVLLLIPLYVL----LGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKylnaRFKLR 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 526 RTSGLLFSVSLVSFQVSTflVALVVFAVHtLVAENAMnaekafvTLTVL---NILnKAQAFLPFS-----IHSLVQARVS 597
Cdd:COG2274 376 RLSNLLSTLSGLLQQLAT--VALLWLGAY-LVIDGQL-------TLGQLiafNIL-SGRFLAPVAqliglLQRFQDAKIA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 598 FDRLVTFLCLE-EVDPGvvdSSSSGSAAGKDCITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSAL 676
Cdd:COG2274 445 LERLDDILDLPpEREEG---RSKLSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 677 LGELSKVEGFVSIEG-------------AVAYVPQEAWVQNTSVVENVCFG-QELDPPWLERVLEACALQPDVDSFPEGI 742
Cdd:COG2274 522 LGLYEPTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGTIRENITLGdPDATDEEIIEAARLAGLHDFIEALPMGY 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 743 HTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVigpGGLLQGTTRILVTHALHILPQADW 822
Cdd:COG2274 602 DTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENL---RRLLKGRTVIIIAHRLSTIRLADR 678
|
570 580 590
....*....|....*....|....*....|.
gi 1827346401 823 IIVLANGAIAEMGSYQELLQRKGALMCLLDQ 853
Cdd:COG2274 679 IIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
297-845 |
4.29e-68 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 241.22 E-value: 4.29e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 297 RPLLKAIWQVFHS---TFLLGTLSLIISDVFRFTVPKLLSLFLEFIGDPKPPAwKGYLLAVLMFLSACLQTLFEQQNMYR 373
Cdd:COG1132 6 RKLLRRLLRYLRPyrgLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLS-ALLLLLLLLLGLALLRALLSYLQRYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 374 LKVLQMRLRSAITGLVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTESVLY-LNGLWLPLVWIVVCFVYL----WQLl 448
Cdd:COG1132 85 LARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHgLPQLVRSVVTLIGALVVLfvidWRL- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 449 gpsALTAIAVFLSLLPLNFFISKKRNHHQEEQMRQkdsRARLTSSI---LRNSKTIKFHGWEGAFLDRVLGI----RGQE 521
Cdd:COG1132 164 ---ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEA---LAELNGRLqesLSGIRVVKAFGREERELERFREAneelRRAN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 522 LGALRTSGLLFSVSLVSFQVSTFLValVVFAVHtLVAENAMNAEK--AFVTLtVLNILNKAQAFLpFSIHSLVQARVSFD 599
Cdd:COG1132 238 LRAARLSALFFPLMELLGNLGLALV--LLVGGL-LVLSGSLTVGDlvAFILY-LLRLFGPLRQLA-NVLNQLQRALASAE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 600 RLVTFLcleEVDPGVVDSS-SSGSAAGKDCITIHSATFAWsQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLG 678
Cdd:COG1132 313 RIFELL---DEPPEIPDPPgAVPLPPVRGEIEFENVSFSY-PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 679 ELSKVEGFVSIEG-------------AVAYVPQEAWVQNTSVVENVCFGQ-ELDPPWLERVLEACALQPDVDSFPEGIHT 744
Cdd:COG1132 389 FYDPTSGRILIDGvdirdltleslrrQIGVVPQDTFLFSGTIRENIRYGRpDATDEEVEEAAKAAQAHEFIEALPDGYDT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 745 SIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVigpGGLLQGTTRILVTHALHILPQADWII 824
Cdd:COG1132 469 VVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL---ERLMKGRTTIVIAHRLSTIRNADRIL 545
|
570 580
....*....|....*....|.
gi 1827346401 825 VLANGAIAEMGSYQELLQRKG 845
Cdd:COG1132 546 VLDDGRIVEQGTHEELLARGG 566
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
312-601 |
1.39e-65 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350040 [Multi-domain] Cd Length: 309 Bit Score: 225.07 E-value: 1.39e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 312 LLGTLSLIISdVFRFTVPKLLSLFLEFIGDPKPPA-WKGYLLAVLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITGLVY 390
Cdd:cd18596 1 LQALLAVLSS-VLSFAPPFFLNRLLRYLEDPGEDAtVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 391 RKVL-------------------ALSSGSRKASAVGDVVNLVSVDVQRLTESVLYLNGLWLPLVWIVVCFVYLWQLLGPS 451
Cdd:cd18596 80 EKALrrrdksgssksseskkkdkEEDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 452 ALTAIAVFLSLLPLNFFISKKRNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLL 531
Cdd:cd18596 160 ALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 532 FSVSLVSFQVSTFLVALVVFAVHTLVAENAMNAEKAFVTLTVLNILNKAQAFLPFSIHSLVQARVSFDRL 601
Cdd:cd18596 240 DLLLSLLWFLIPILVTVVTFATYTLVMGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1262-1493 |
9.78e-63 |
|
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: 214.77 E-value: 9.78e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1262 GGQIEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSR 1341
Cdd:cd03288 17 GGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1342 ISIIPQDPILFPGSLRMNLDLLQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQ 1421
Cdd:cd03288 97 LSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 1422 ILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQK-GLF 1493
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVF 249
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1263-1491 |
3.83e-61 |
|
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: 209.00 E-value: 3.83e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1263 GQIEFRDFGLRYRPELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRI 1342
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1343 SIIPQDPILFPGSLRMNLDL-LQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQ 1421
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLgRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1422 ILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKG 1491
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1020-1498 |
4.24e-61 |
|
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: 220.41 E-value: 4.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1020 LFQRLLwdvvRSPISFFERTPIGHLLNRFSKETDTVDvDIPdkLR-------SLLMYAFGLLEVSL------VVAVATPL 1086
Cdd:COG4987 94 LYRRLE----PLAPAGLARLRSGDLLNRLVADVDALD-NLY--LRvllpllvALLVILAAVAFLAFfspalaLVLALGLL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1087 ATVAILPLFLLYAGFQSlyvvsSCQLRRLESASYSSVcshmAETFQGSTVVRAFRTQAPFVAqnnaRVDESQRisfpRLV 1166
Cdd:COG4987 167 LAGLLLPLLAARLGRRA-----GRRLAAARAALRARL----TDLLQGAAELAAYGALDRALA----RLDAAEA----RLA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1167 ADRWLAANVELLGNG---LVFAAATCAVL-------SKAHLSAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERM 1236
Cdd:COG4987 230 AAQRRLARLSALAQAllqLAAGLAVVAVLwlaaplvAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1237 QdyAWTPKEAPWRLPtcAAQPPWPQGGQIEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQ 1316
Cdd:COG4987 310 N--ELLDAPPAVTEP--AEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1317 EAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLdLL--QEHSDEAIWAALETVQLKALVASLPGQLQYK 1394
Cdd:COG4987 386 DPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENL-RLarPDATDEELWAALERVGLGDWLAALPDGLDTW 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1395 CADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDK 1474
Cdd:COG4987 465 LGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLED 544
|
490 500
....*....|....*....|....
gi 1827346401 1475 GQVAESGSPAQLLAQKGLFYRLAQ 1498
Cdd:COG4987 545 GRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1228-1491 |
8.93e-61 |
|
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: 219.24 E-value: 8.93e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1228 NSIVSVERMQDYAWTPKEAPwrlPTCAAQPPWPQGGQIEFRDFGLRYrPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSS 1307
Cdd:COG4988 303 NGIAAAEKIFALLDAPEPAA---PAGTAPLPAAGPPSIELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKST 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1308 LASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLDLLQEH-SDEAIWAALETVQLKALVAS 1386
Cdd:COG4988 379 LLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDaSDEELEAALEAAGLDEFVAA 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1387 LPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDC 1466
Cdd:COG4988 459 LPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQA 538
|
250 260
....*....|....*....|....*
gi 1827346401 1467 ARVLVMDKGQVAESGSPAQLLAQKG 1491
Cdd:COG4988 539 DRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
374-846 |
8.45e-59 |
|
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: 213.47 E-value: 8.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 374 LKVLQmRLRSAitglVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLteSVLYLNGLwLPLVW----IVVCFVYLWQLLG 449
Cdd:COG4987 84 LRLLA-DLRVR----LYRRLEPLAPAGLARLRSGDLLNRLVADVDAL--DNLYLRVL-LPLLVallvILAAVAFLAFFSP 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 450 PSALTAIAVFLS---LLPLNFFISKKRNHHQEEQMRQkDSRARLTSsILRNSKTIKFHGWEGAFLDRVLGIRGQELGALR 526
Cdd:COG4987 156 ALALVLALGLLLaglLLPLLAARLGRRAGRRLAAARA-ALRARLTD-LLQGAAELAAYGALDRALARLDAAEARLAAAQR 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 527 TSGLL--FSVSLVSFQVSTFLVALVVFAVHtLVAENAMNAekAFVTLTVLNILNKAQAFLPFS--IHSLVQARVSFDRLV 602
Cdd:COG4987 234 RLARLsaLAQALLQLAAGLAVVAVLWLAAP-LVAAGALSG--PLLALLVLAALALFEALAPLPaaAQHLGRVRAAARRLN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 603 TflcLEEVDPGVVDSSSSGSAAGKDCITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSK 682
Cdd:COG4987 311 E---LLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 683 VEGFVSIEG-------------AVAYVPQEAWVQNTSVVENVCFG-QELDPPWLERVLEACALQPDVDSFPEGIHTSIGE 748
Cdd:COG4987 388 QSGSITLGGvdlrdldeddlrrRIAVVPQRPHLFDTTLRENLRLArPDATDEELWAALERVGLGDWLAALPDGLDTWLGE 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 749 QGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVIgpgGLLQGTTRILVTHALHILPQADWIIVLAN 828
Cdd:COG4987 468 GGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLL---EALAGRTVLLITHRLAGLERMDRILVLED 544
|
490
....*....|....*...
gi 1827346401 829 GAIAEMGSYQELLQRKGA 846
Cdd:COG4987 545 GRIVEQGTHEELLAQNGR 562
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
312-601 |
2.84e-57 |
|
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: 200.09 E-value: 2.84e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 312 LLGTLSLIiSDVFRFTVPKLLSLFLEFIGDPKPPAWKGYLLAVLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITGLVYR 391
Cdd:cd18598 1 PLGLLKLL-ADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 392 KVLALSSGSRKASAVGDVVNLVSVDVQRLTESVLYLNGLW-LPLVwIVVCFVYLWQLLGPSALTAIAVFLSLLPLNFFIS 470
Cdd:cd18598 80 KALRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWsLPLQ-IIVALYLLYQQVGVAFLAGLVFALVLIPINKWIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 471 KKRNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLLFSVsLVSFQVST-FLVALV 549
Cdd:cd18598 159 KRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDAL-CVYFWATTpVLISIL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 550 VFAVHTLVAeNAMNAEKAFVTLTVLNIL----NkaqAFlPFSIHSLVQARVSFDRL 601
Cdd:cd18598 238 TFATYVLMG-NTLTAAKVFTSLALFNMLigplN---AF-PWVLNGLVEAWVSLKRL 288
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
993-1496 |
1.12e-56 |
|
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: 207.65 E-value: 1.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 993 LLGCLQAIGLFAS---MAAVLLGGARASRL-LFQRLLwdvvRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLL- 1067
Cdd:TIGR02203 62 GLAVLRGICSFVStylLSWVSNKVVRDIRVrMFEKLL----GLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVr 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1068 --MYAFGLLEVSLVVAVATPLATVAILPLfllyagfqsLYVVSSCQLRRLESASYSSVCSH------MAETFQGSTVVRA 1139
Cdd:TIGR02203 138 etLTVIGLFIVLLYYSWQLTLIVVVMLPV---------LSILMRRVSKRLRRISKEIQNSMgqvttvAEETLQGYRVVKL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1140 FRTQAP----FVAQNNARVDESQRISfprlVADRWLAANVELLGNgLVFAAATCAVLSKA---HLSAG-LVGFsVSAALQ 1211
Cdd:TIGR02203 209 FGGQAYetrrFDAVSNRNRRLAMKMT----SAGSISSPITQLIAS-LALAVVLFIALFQAqagSLTAGdFTAF-ITAMIA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1212 VTQTLQWVVRNWTDLENSIVSVERMQDYAWTPKEapwrlPTCAAQPPWPQGGQIEFRDFGLRYRPELPLAVQGVSFKIHA 1291
Cdd:TIGR02203 283 LIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPE-----KDTGTRAIERARGDVEFRNVTFRYPGRDRPALDSISLVIEP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1292 GEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLDL--LQEHSDE 1369
Cdd:TIGR02203 358 GETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYgrTEQADRA 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1370 AIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFA 1449
Cdd:TIGR02203 438 EIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ 517
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1827346401 1450 QCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFYRL 1496
Cdd:TIGR02203 518 GRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQL 564
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
313-601 |
1.99e-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: 198.06 E-value: 1.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 313 LGTLSLIISDVFRFTVPKLLSLFLEFI-----GDPKPPAWKGYLLAVLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITG 387
Cdd:cd18597 1 LAGLLKLLADVLQVLSPLLLKYLINFVedaylGGPPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 388 LVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTESVLYLNGLWLPLVWIVVCFVYLWQLLGPSALTAIAVFLSLLPLNF 467
Cdd:cd18597 81 AIYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 468 FISKKRNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLLFSVSLVSFQVSTFLVA 547
Cdd:cd18597 161 FLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLAS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 548 LVVFAVHTLVaENAMNAEKAFVTLTVLNILNKAQAFLPFSIHSLVQARVSFDRL 601
Cdd:cd18597 241 MLSFITYYAT-GHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
950-1240 |
1.07e-55 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 196.29 E-value: 1.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 950 ALFLFLCQQVASFCRGYWLSLWA----DDPAVGGQQTQAALRG-------GIFGLLGCLQAIGLFASMAAVLLGGARASR 1018
Cdd:cd18602 4 VLALALLKQGLRVATDFWLADWTeanhDVASVVFNITSSSLEDdevsyyiSVYAGLSLGAVILSLVTNLAGELAGLRAAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1019 LLFQRLLWDVVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLLY 1098
Cdd:cd18602 84 RLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIVY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1099 AGFQSLYVVSSCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQrISFPRL-VADRWLAANVEL 1177
Cdd:cd18602 164 YFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNN-TAFLFLnTANRWLGIRLDY 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 1178 LGNGLVFAAATCAVLSKAH--LSAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDYA 1240
Cdd:cd18602 243 LGAVIVFLAALSSLTAALAgyISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
289-845 |
2.11e-55 |
|
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: 203.45 E-value: 2.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 289 LRQEGSQWRPL-LKAIWQVFHSTFLLG---TLSLIISDVFRFTVPkLLSLFLEFIgdpkppawkgyLLAVLMFLSACLqT 364
Cdd:COG4988 9 KRLARGARRWLaLAVLLGLLSGLLIIAqawLLASLLAGLIIGGAP-LSALLPLLG-----------LLLAVLLLRALL-A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 365 LFEQQNMYRLkvlQMRLRSAITGLVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTEsvlYLnGLWLP--LVWIVVC-- 440
Cdd:COG4988 76 WLRERAAFRA---AARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDG---YF-ARYLPqlFLAALVPll 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 441 -FVYLWQLLGPSALTaIAVFLSLLPLnFFI-----SKKRNHHQEEQMrqkdsrARLTSSilrnsktikfhgwegaFLDRV 514
Cdd:COG4988 149 iLVAVFPLDWLSGLI-LLVTAPLIPL-FMIlvgkgAAKASRRQWRAL------ARLSGH----------------FLDRL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 515 --------LGIRGQELGALRTSGLLFSVS----L-VSFQVSTFL-------VALV-VFAVHTLVAENaMNAEKAFVTLtv 573
Cdd:COG4988 205 rglttlklFGRAKAEAERIAEASEDFRKRtmkvLrVAFLSSAVLeffaslsIALVaVYIGFRLLGGS-LTLFAALFVL-- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 574 lnILnKAQAFLPF-----SIHSLVQARVSFDRLVTFLclEEVDPGVVDSSSSGSAAGKDCITIHSATFAWSQEsPPCLHR 648
Cdd:COG4988 282 --LL-APEFFLPLrdlgsFYHARANGIAAAEKIFALL--DAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGG-RPALDG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-------------VAYVPQEAWVQNTSVVENVCFGQ 715
Cdd:COG4988 356 LSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpaswrrqIAWVPQNPYLFAGTIRENLRLGR 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 716 -ELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFnQ 794
Cdd:COG4988 436 pDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEIL-Q 514
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 795 VIGPggLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKG 845
Cdd:COG4988 515 ALRR--LAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1265-1496 |
6.21e-55 |
|
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: 191.29 E-value: 6.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISI 1344
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1345 IPQDPILFPGSLRMNLDL-LQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQIL 1423
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYgRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 1424 ILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFYRL 1496
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1265-1499 |
7.79e-55 |
|
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: 191.29 E-value: 7.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELPLaVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISI 1344
Cdd:cd03253 1 IEFENVTFAYDPGRPV-LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1345 IPQDPILFPGSLRMNLDLLQEH-SDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQIL 1423
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 1424 ILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFYRLAQE 1499
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKA 235
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
318-601 |
1.40e-54 |
|
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: 192.46 E-value: 1.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 318 LIISDVFRFTVPKLLSLFLE-FIGDPKPPAWKGYLLAVLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITGLVYRKVLAL 396
Cdd:cd18594 6 LFLEESLKIVQPLLLGRLVAyFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTLKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 397 SSGSRKASAVGDVVNLVSVDVQRLTESVLYLNGLWLPLVWIVVCFVYLWQLLGPSALTAIAVFLSLLPLNFFISKKRNHH 476
Cdd:cd18594 86 SSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 477 QEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLLFSVSLVSFQVSTFLVALVVFAVHTL 556
Cdd:cd18594 166 RRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVL 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1827346401 557 VAeNAMNAEKAFVTLTVLNILNKAQA-FLPFSIHSLVQARVSFDRL 601
Cdd:cd18594 246 TG-NTLTARKVFTVISLLNALRMTITrFFPESIQTLSESRVSLKRI 290
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
951-1239 |
1.07e-52 |
|
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: 187.35 E-value: 1.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 951 LFLFLCQ--QVASFcrgYWLSLWaddpaVGGQQTQAALRGGIFGL--LGCLQAIGLFASMAAVL------LGGARASRLL 1020
Cdd:cd18605 6 LSLILMQasRNLID---FWLSYW-----VSHSNNSFFNFINDSFNffLTVYGFLAGLNSLFTLLraflfaYGGLRAARRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1021 FQRLLWDVVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLLYAG 1100
Cdd:cd18605 78 HNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1101 FQSLYVVSSCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANVELLGN 1180
Cdd:cd18605 158 IQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 1181 GLVFAAATCAVLS---KAHLSAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDY 1239
Cdd:cd18605 238 LIVTFVALTAVVQhffGLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQY 299
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
629-830 |
2.60e-52 |
|
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: 183.30 E-value: 2.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSQESPpCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFV-----------------SIEG 691
Cdd:cd03290 1 VQVTNGYFSWGSGLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 692 AVAYVPQEAWVQNTSVVENVCFGQELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKA 771
Cdd:cd03290 80 SVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 772 AVYLLDDPLAALDAHVGQHVFNQviGPGGLLQGTTR--ILVTHALHILPQADWIIVLANGA 830
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQE--GILKFLQDDKRtlVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1265-1476 |
8.27e-52 |
|
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: 179.89 E-value: 8.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISI 1344
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1345 IPQDPILFPGSLRMNLdllqehsdeaiwaaletvqlkalvaslpgqlqykcadrgedLSVGQKQLLCLARALLRKTQILI 1424
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 1425 LDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQ 1476
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1265-1498 |
4.55e-51 |
|
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: 180.43 E-value: 4.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRY--RPELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRI 1342
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1343 SIIPQDPILFPGSLRMNLDL-LQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQ 1421
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIRYgKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1422 ILILDEATAAVDPGTELQMQ-----AMLGSwfaqcTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFYRL 1496
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQealdrAMKGR-----TTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKL 234
|
..
gi 1827346401 1497 AQ 1498
Cdd:cd03249 235 VK 236
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1015-1498 |
1.47e-50 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 189.93 E-value: 1.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1015 RASRLLFQRLLWDV----VRSPISFFERTPIGHLLNRFSKETDT-----VDVdIPDKLRSL-LMYAFGLLEVSLVVAVAt 1084
Cdd:PRK10790 91 RAAVGVVQQLRTDVmdaaLRQPLSAFDTQPVGQLISRVTNDTEVirdlyVTV-VATVLRSAaLIGAMLVAMFSLDWRMA- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1085 pLATVAILPLFLLYAGFQSLYvvSSCQLRRLESasY-SSVCSHMAETFQGSTVVRAFRTQAPFvaqnNARVDESQRISF- 1162
Cdd:PRK10790 169 -LVAIMIFPAVLVVMVIYQRY--STPIVRRVRA--YlADINDGFNEVINGMSVIQQFRQQARF----GERMGEASRSHYm 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1163 PRLVA---DRWLAAnvELLGngLVFAAATCAVLSkahlsagLVGFSVSAALQV-------------TQTLQWVVRNWTDL 1226
Cdd:PRK10790 240 ARMQTlrlDGFLLR--PLLS--LFSALILCGLLM-------LFGFSASGTIEVgvlyafisylgrlNEPLIELTTQQSML 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1227 ENSIVSVER--------MQDYAwtPKEAPWrlptcaaqppwpQGGQIEFRDFGLRYRPELPLaVQGVSFKIHAGEKVGIV 1298
Cdd:PRK10790 309 QQAVVAGERvfelmdgpRQQYG--NDDRPL------------QSGRIDIDNVSFAYRDDNLV-LQNINLSVPSRGFVALV 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1299 GRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLDLLQEHSDEAIWAALETV 1378
Cdd:PRK10790 374 GHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETV 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1379 QLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAH 1458
Cdd:PRK10790 454 QLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAH 533
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1827346401 1459 RLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFYRLAQ 1498
Cdd:PRK10790 534 RLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQ 573
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
313-601 |
3.69e-50 |
|
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: 180.51 E-value: 3.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 313 LGTLSLIISDVFRFTVPKLLSLFLEFIGD-------------PKPPAWK-----GYLLAVLMFLSACLQTLFEQQNMYRL 374
Cdd:cd18591 1 LGGILKLLGDLLGFVGPLCISGIVDYVEEntysssnstdklsVSYVTVEeffsnGYVLAVILFLALLLQATFSQASYHIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 375 KVLQMRLRSAITGLVYRKVLALSSGSRKASAV--GDVVNLVSVDVQRLTESVLYLNGLW-LPLVwIVVCFVYLWQLLGPS 451
Cdd:cd18591 81 IREGIRLKTALQAMIYEKALRLSSWNLSSGSMtiGQITNHMSEDANNIMFFFWLIHYLWaIPLK-IIVGLILLYLKLGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 452 ALTAIAVFLSLLPLNFFISKKRNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLL 531
Cdd:cd18591 160 ALIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVY 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 532 FSVSLVSFQVSTFLVALVVFAVHTLVAENAMNAEKAFVTLTVLNILNKAQAFLPFSIHSLVQARVSFDRL 601
Cdd:cd18591 240 WSLMTFLTQASPILVTLVTFGLYPYLEGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
316-601 |
4.48e-50 |
|
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: 179.29 E-value: 4.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 316 LSLIISDVFRFTVPK-LLSLFLEFIGDPKPPAWKGYLLAVLMFLSACLQTLFEQQN---MYRLKVlqmRLRSAITGLVYR 391
Cdd:cd18592 4 LLLLISLIFGFIGPTiLIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTwaiSYRTGI---RLRGAVLGLLYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 392 KVLALSSGSRKAsaVGDVVNLVSVDVQRLTESVLYLNGLWLPLVWIVVCFVYLWQLLGPSALTAIAVFLSLLPLNFFISK 471
Cdd:cd18592 81 KILRLRSLGDKS--VGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 472 KRNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLLFSVSLVSFQVSTFLVALVVF 551
Cdd:cd18592 159 LTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTF 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1827346401 552 AVHTLvAENAMNAEKAFVTLTVLNILNKAQAFLPFSIHSLVQARVSFDRL 601
Cdd:cd18592 239 LAHVA-LGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1255-1496 |
1.07e-49 |
|
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: 187.33 E-value: 1.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1255 AQPPWPQGGQIEFRDFGLRYRPELPLaVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG 1334
Cdd:COG5265 348 APPLVVGGGEVRFENVSFGYDPERPI-LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1335 LHTLRSRISIIPQDPILFPGSLRMNLDLLQEH-SDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLA 1413
Cdd:COG5265 427 QASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIA 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1414 RALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLF 1493
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLY 586
|
...
gi 1827346401 1494 YRL 1496
Cdd:COG5265 587 AQM 589
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1263-1477 |
2.83e-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: 174.70 E-value: 2.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1263 GQIEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRI 1342
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1343 SIIPQDPILFPGSLRMNLDL-LQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQ 1421
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLgAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 1422 ILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQV 1477
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
943-1240 |
5.55e-49 |
|
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: 177.37 E-value: 5.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 943 GTPLCLYALFLFLCQQVASFCRGYWLSLWADDP---AVGGQQTQAALR----------------GGIFGLLGCLQAIGLF 1003
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGsgnTTNNVDNSTVDSgnisdnpdlnfyqlvyGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1004 ASMAAVLlggaRASRLLFQRLLWDVVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVA 1083
Cdd:cd18599 81 VFVKVTL----RASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1084 TPLATVAILPLFLLYAGFQSLYVVSSCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFP 1163
Cdd:cd18599 157 FPWFLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827346401 1164 RLVADRWLAANVELLGNGLVFAAATCAVLSKAHLSAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDYA 1240
Cdd:cd18599 237 FNCAMRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1263-1493 |
2.78e-48 |
|
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: 173.89 E-value: 2.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1263 GQIEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAaEGGIWIDGVPIAHVGLHTLRSRI 1342
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1343 SIIPQDPILFPGSLRMNLDLLQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQI 1422
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 1423 LILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLF 1493
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
948-1239 |
8.69e-48 |
|
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: 173.17 E-value: 8.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 948 LYALFLFLCQQVASFCRGYWLSLWADDPaVGGQQTQAALRGGIFGLLGCLQAIGLFASMAAVLLGGARASRLLFQRLLWD 1027
Cdd:cd18559 2 FLLIKLVLCNHVFSGPSNLWLLLWFDDP-VNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1028 VVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPLAtVAILPLFLLYAGFQSLYVV 1107
Cdd:cd18559 81 ALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMA-AVGIPLGLLYVPVNRVYAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1108 SSCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDEsQRISFPRLVADRWLAANVELLGNGLVFAAA 1187
Cdd:cd18559 160 SSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDN-ELAYLPSIVYLRALAVRLWCVGPCIVLFAS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 1188 TCAVLSKAHLsAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDY 1239
Cdd:cd18559 239 FFAYVSRHSL-AGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLER 289
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
976-1496 |
1.14e-47 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 183.38 E-value: 1.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 976 AVGGQQTQAALRGGIFgLLGCLQaigLFASMAAVLLGG------ARASRLLFQRLLWDVVRSPISFFERTPIGHLLNRFS 1049
Cdd:TIGR00958 190 TLGGDKGPPALASAIF-FMCLLS---IASSVSAGLRGGsfnytmARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLS 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1050 KETDTVDVDIPDK----LRSLLMyAFGLLEVSLVVAVATPLATVAILPL-FLLYAGFQSLYVVSSCQLRrlESASYSSvc 1124
Cdd:TIGR00958 266 SDTQTMSRSLSLNvnvlLRNLVM-LLGLLGFMLWLSPRLTMVTLINLPLvFLAEKVFGKRYQLLSEELQ--EAVAKAN-- 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1125 sHMAETfqgstVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANV------ELLGNGLVFAAATCA---VLSKA 1195
Cdd:TIGR00958 341 -QVAEE-----ALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAgylwttSVLGMLIQVLVLYYGgqlVLTGK 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1196 HLSAGLVGFsVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDYAwtpkEAPWRLPTCAAQPPWPQGGQIEFRDFGLRY- 1274
Cdd:TIGR00958 415 VSSGNLVSF-LLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYL----DRKPNIPLTGTLAPLNLEGLIEFQDVSFSYp 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1275 -RPELPLaVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFP 1353
Cdd:TIGR00958 490 nRPDVPV-LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFS 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1354 GSLRMNLDL-LQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAV 1432
Cdd:TIGR00958 569 GSVRENIAYgLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 1433 DpgteLQMQAMLGSW--FAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFYRL 1496
Cdd:TIGR00958 649 D----AECEQLLQESrsRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
326-601 |
1.72e-47 |
|
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: 172.01 E-value: 1.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 326 FTVPKLLSLFLEFIGDPKPPAWKGYLLAVLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITGLVYRKVLALSSGSRKASA 405
Cdd:cd18559 14 FSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 406 VGDVVNLVSVDVQRLTESVLYLNGLWLPLVWIVVCFVYLWQLLGPSALTAIAVFLSLLPLNFFISKKRNHHQEEQMRQKD 485
Cdd:cd18559 94 SGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 486 SRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLLFSVSLVSFQVSTFLVALVVFAVHTLVAENA-MNA 564
Cdd:cd18559 174 PRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHSLAgLVA 253
|
250 260 270
....*....|....*....|....*....|....*..
gi 1827346401 565 EKAFVTLTVLNILNKAQAFLPFSIHSLVQARVSFDRL 601
Cdd:cd18559 254 LKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
943-1240 |
1.90e-45 |
|
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: 167.11 E-value: 1.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 943 GTPLCLYALFLFLCQQVASFCRGYWLSLWADDPAVGGQQTQAALRG----------------GIFGLLGCLQAIGLFASM 1006
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEEKLNDTTDRVQGEnstnvdiedldrdfnlGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1007 AAVLLGGARASRLLFQRLLWDVVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPL 1086
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1087 ATVAILPLFLLYAGFQSLYVVSSCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLV 1166
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 1167 ADRWLAANVELLGNGLVFAAATCAVLSKAHLSAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDYA 1240
Cdd:cd18601 241 TSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEYS 314
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
313-601 |
2.39e-45 |
|
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: 165.86 E-value: 2.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 313 LGTLSLIISDVFRFTVPKLLSLFLEFIGDPKPPA--WKGYLLAVLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITGLVY 390
Cdd:cd18593 1 LLGIFLFLEEAIRVVQPIFLGKLIRYFEGNGSSIslTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 391 RKVLALSSGSRKASAVGDVVNLVSVDVQRLTESVLYLNGLWL-PLVWIVVCFVyLWQLLGPSALTAIAVFLSLLPLNFFI 469
Cdd:cd18593 81 RKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVaPLQLIAVIYI-LWFEIGWSCLAGLAVLLILIPLQSFF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 470 SKKRNHhqeeqMRQK-----DSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLLFSVSLVSFQVSTF 544
Cdd:cd18593 160 GKLFSK-----LRRKtaartDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSK 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1827346401 545 LVALVVFAVHTLVaENAMNAEKAFVTLTVLNILNKAQA-FLPFSIHSLVQARVSFDRL 601
Cdd:cd18593 235 LILFLTFLAYILL-GNILTAERVFVTMALYNAVRLTMTlFFPFAIQFGSELSVSIRRI 291
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1265-1498 |
5.16e-45 |
|
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: 163.04 E-value: 5.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISI 1344
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1345 IPQDPILFPGSLRMNLDLLQEHSD-EAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQIL 1423
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSmERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 1424 ILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFYRLAQ 1498
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
644-840 |
7.30e-45 |
|
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: 164.26 E-value: 7.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 644 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQEAWVQNTSVVENVCFGQELDPPWLE 723
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 724 RVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVIGPggLLQ 803
Cdd:cd03291 131 SVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCK--LMA 208
|
170 180 190
....*....|....*....|....*....|....*..
gi 1827346401 804 GTTRILVTHALHILPQADWIIVLANGAIAEMGSYQEL 840
Cdd:cd03291 209 NKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
988-1503 |
2.00e-42 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 165.52 E-value: 2.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 988 GGIFGLLGCLQAIGLFASMAAVLLggAR-ASRLLFQR---LLWD----VVRSPISFFERTPIGHLLNRFSKETDTVdvdi 1059
Cdd:PRK13657 53 GDIFPLLAAWAGFGLFNIIAGVLV--ARhADRLAHRRrlaVLTEyferIIQLPLAWHSQRGSGRALHTLLRGTDAL---- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1060 pdklrsllmyaFGL-LE---------VSLVVAVATPLAT---VAILpLFLLYAGFqslYVVSSCQLRRLES------ASY 1120
Cdd:PRK13657 127 -----------FGLwLEfmrehlatlVALVVLLPLALFMnwrLSLV-LVVLGIVY---TLITTLVMRKTKDgqaaveEHY 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1121 SSVCSHMAETFQGSTVVRAFrtqapfvaqnnARVDESQRISfpRLVADRWLAANVELLG-----NGLVFAAATCAVLS-- 1193
Cdd:PRK13657 192 HDLFAHVSDAIGNVSVVQSY-----------NRIEAETQAL--RDIADNLLAAQMPVLSwwalaSVLNRAASTITMLAil 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1194 --------KAHLSAGLVGFSVSAALQVTQTLQWVVrnwtDLENSIV-SVERMQDYAWTPKEAPWRLPTCAAQPPWPQGGQ 1264
Cdd:PRK13657 259 vlgaalvqKGQLRVGEVVAFVGFATLLIGRLDQVV----AFINQVFmAAPKLEEFFEVEDAVPDVRDPPGAIDLGRVKGA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYrPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISI 1344
Cdd:PRK13657 335 VEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAV 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1345 IPQDPILFPGSLRMNLDLLQEH-SDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQIL 1423
Cdd:PRK13657 414 VFQDAGLFNRSIEDNIRVGRPDaTDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPIL 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1424 ILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFYRLAQESGLV 1503
Cdd:PRK13657 494 ILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQGML 573
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
635-846 |
1.12e-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: 150.46 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 635 TFAWSQESPpCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAYVPQEAW 701
Cdd:cd03253 7 TFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVVPQDTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 702 VQNTSVVENVCFGQELDPPwlERVLEAC---ALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDD 778
Cdd:cd03253 86 LFNDTIGYNIRYGRPDATD--EEVIEAAkaaQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827346401 779 PLAALDAHVGQHVFNQVIgpgGLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGA 846
Cdd:cd03253 164 ATSALDTHTEREIQAALR---DVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGL 228
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
629-829 |
5.03e-40 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 146.37 E-value: 5.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAY 695
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 696 VPQEAWVQNTSVVENVcfgqeldppwlervleacalqpdvdsfpegihtsigeqgmnLSGGQKQRLSLARAVYRKAAVYL 775
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 776 LDDPLAALDAHVGQHVFnQVIgpGGLLQGTTRILVTHALHILPQADWIIVLANG 829
Cdd:cd03228 120 LDEATSALDPETEALIL-EAL--RALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
629-846 |
2.03e-39 |
|
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: 146.99 E-value: 2.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAY 695
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 696 VPQEAWVQNTSVVENVCFGQ-ELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVY 774
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRpGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 775 LLDDPLAALDA---HVGQHVFNQvigpggLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGA 846
Cdd:cd03251 161 ILDEATSALDTeseRLVQAALER------LMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGV 229
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
644-845 |
2.26e-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: 146.60 E-value: 2.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 644 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAYVPQEAWVQNTSVVEN 710
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGVVLQDTFLFSGTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 711 VCFGQELDPPwlERVLEAC-ALQPD--VDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHV 787
Cdd:cd03254 97 IRLGRPNATD--EEVIEAAkEAGAHdfIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTET 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1827346401 788 GQHVFNQVigpGGLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKG 845
Cdd:cd03254 175 EKLIQEAL---EKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
644-846 |
7.29e-38 |
|
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: 142.29 E-value: 7.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 644 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-------------VAYVPQEAWVQNTSVVEN 710
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIGLVSQEPVLFDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 711 VCFGqeLDPPWLERVLEACAL---QPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAH- 786
Cdd:cd03249 97 IRYG--KPDATDEEVEEAAKKaniHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAEs 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 787 --VGQHVFNQVIgpggllQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGA 846
Cdd:cd03249 175 ekLVQEALDRAM------KGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGV 230
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1263-1477 |
2.23e-37 |
|
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: 140.68 E-value: 2.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1263 GQIEFRD--FGLRYRPELPLaVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRS 1340
Cdd:cd03248 10 GIVKFQNvtFAYPTRPDTLV-LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1341 RISIIPQDPILFPGSLRMNLDL-LQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRK 1419
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAYgLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1827346401 1420 TQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQV 1477
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
351-826 |
2.37e-37 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 148.97 E-value: 2.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 351 LLAVLMFLSACLQTLFEqqnmYRLKVLQMRLRSAITGLVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTESV-LYLNG 429
Cdd:TIGR02857 49 ALALVLLLRALLGWLQE----RAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFaRYLPQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 430 LWL----PLVWIVVCFVYLWqllgpsaLTAIAVFLSLLPLNFFISKKRNHHQEEQMRQKDSRARLTS---SILRNSKTIK 502
Cdd:TIGR02857 125 LVLavivPLAILAAVFPQDW-------ISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGhflDRLRGLPTLK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 503 FHGWEGAFLDRVLGI----RGQELGALRTSgllFSVSLVSFQVSTFLVALV-VFAVHTLVAENaMNAEKAFVTLtvlnIL 577
Cdd:TIGR02857 198 LFGRAKAQAAAIRRSseeyRERTMRVLRIA---FLSSAVLELFATLSVALVaVYIGFRLLAGD-LDLATGLFVL----LL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 578 nKAQAFLPF-----SIHSLVQARVSFDRLVTFLCLEE-VDPGVVDSSSSGSAAgkdcITIHSATFAWsQESPPCLHRINL 651
Cdd:TIGR02857 270 -APEFYLPLrqlgaQYHARADGVAAAEALFAVLDAAPrPLAGKAPVTAAPASS----LEFSGVSVAY-PGRRPALRPVSF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 652 TVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-------------VAYVPQEAWVQNTSVVENVCFGQ-EL 717
Cdd:TIGR02857 344 TVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVpladadadswrdqIAWVPQHPFLFAGTIAENIRLARpDA 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 718 DPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVIg 797
Cdd:TIGR02857 424 SDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALR- 502
|
490 500
....*....|....*....|....*....
gi 1827346401 798 pgGLLQGTTRILVTHALHILPQADWIIVL 826
Cdd:TIGR02857 503 --ALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1265-1490 |
7.74e-37 |
|
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: 139.39 E-value: 7.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLA---SGLLRLQEaaeGGIWIDGVPIAHVGLHTLRSR 1341
Cdd:COG1122 1 IELENLSFSYPGGTP-ALDDVSLSIEKGEFVAIIGPNGSGKSTLLrllNGLLKPTS---GEVLVDGKDITKKNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1342 ISIIPQDP------------ILFpgSLRmNLDLLQEHSDEAIWAALETVQLKALvaslpgqlqykcADRG-EDLSVGQKQ 1408
Cdd:COG1122 77 VGLVFQNPddqlfaptveedVAF--GPE-NLGLPREEIRERVEEALELVGLEHL------------ADRPpHELSGGQKQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1409 LLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ-CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQL 1486
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTHDLDLVAELAdRVIVLDDGRIVADGTPREV 221
|
....
gi 1827346401 1487 LAQK 1490
Cdd:COG1122 222 FSDY 225
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1011-1460 |
9.68e-37 |
|
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: 147.12 E-value: 9.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1011 LGGARASrlLFQRLlwdvVRSPISFFERTPIGHLLNRFSKETDTVD-----VDIPDKLRSLLMYAFGLLEVSLVVAVATP 1085
Cdd:TIGR02868 85 LGALRVR--VYERL----ARQALAGRRRLRRGDLLGRLGADVDALQdlyvrVIVPAGVALVVGAAAVAAIAVLSVPAALI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1086 LATVAILPLFLLYAGFQSLYVVSSCQLRRLESASYSSVcshmAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRL 1165
Cdd:TIGR02868 159 LAAGLLLAGFVAPLVSLRAARAAEQALARLRGELAAQL----TDALDGAAELVASGALPAALAQVEEADRELTRAERRAA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1166 VADRWLAAnVELLGNGLV----FAAATCAVLSKAHLSAGL--VGFSVSAALQVTQTLQWVVRNWTdleNSIVSVERMqdY 1239
Cdd:TIGR02868 235 AATALGAA-LTLLAAGLAvlgaLWAGGPAVADGRLAPVTLavLVLLPLAAFEAFAALPAAAQQLT---RVRAAAERI--V 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1240 AWTPKEAPWRLPTCAAQPPWPQGG-QIEFRDFGLRYrPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEA 1318
Cdd:TIGR02868 309 EVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1319 AEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLDLLQ-EHSDEAIWAALETVQLKALVASLPGQLQYKCAD 1397
Cdd:TIGR02868 388 LQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARpDATDEELWAALERVGLADWLRALPDGLDTVLGE 467
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 1398 RGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRL 1460
Cdd:TIGR02868 468 GGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1285-1503 |
1.25e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 147.68 E-value: 1.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1285 VSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQeAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLDLLQ 1364
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1365 EH-SDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTE-LQMQA 1442
Cdd:PRK11174 448 PDaSDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEqLVMQA 527
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 1443 MLGSWFAQcTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFYR-LAQESGLV 1503
Cdd:PRK11174 528 LNAASRRQ-TTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATlLAHRQEEI 588
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1254-1498 |
9.96e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 144.97 E-value: 9.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1254 AAQPPWPQGGQIEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHV 1333
Cdd:PRK11160 328 TTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADY 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1334 GLHTLRSRISIIPQDPILFPGSLRMNLDLLQEH-SDEAIWAALETVQLKALVASLPGqLQYKCADRGEDLSVGQKQLLCL 1412
Cdd:PRK11160 408 SEAALRQAISVVSQRVHLFSATLRDNLLLAAPNaSDEALIEVLQQVGLEKLLEDDKG-LNAWLGEGGRQLSGGEQRRLGI 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1413 ARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSV--MDcaRVLVMDKGQVAESGSPAQLLAQK 1490
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLeqFD--RICVMDNGQIIEQGTHQELLAQQ 564
|
....*...
gi 1827346401 1491 GLFYRLAQ 1498
Cdd:PRK11160 565 GRYYQLKQ 572
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
374-814 |
4.50e-35 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 142.11 E-value: 4.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 374 LKVLQmRLRSAitglVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTEsvLYLNGLWLPLVWIVV-------CFVYLWQ 446
Cdd:TIGR02868 82 LRSLG-ALRVR----VYERLARQALAGRRRLRRGDLLGRLGADVDALQD--LYVRVIVPAGVALVVgaaavaaIAVLSVP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 447 LlGPSALTAIAVFLSLLPLnFFISKKRNHHQEEQmRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRV---------LGI 517
Cdd:TIGR02868 155 A-ALILAAGLLLAGFVAPL-VSLRAARAAEQALA-RLRGELAAQLTDALDGAAELVASGALPAALAQVeeadreltrAER 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 518 RGQELGALRTSGLLFSVSLVsfqvstflVALVVFAVHTLVAENAMNAekAFVTLTVLNILNKAQAFLPFS--IHSLVQAR 595
Cdd:TIGR02868 232 RAAAATALGAALTLLAAGLA--------VLGALWAGGPAVADGRLAP--VTLAVLVLLPLAAFEAFAALPaaAQQLTRVR 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 596 VSFDRLVTFLCLEEVDPGVVDSSSSGSAAGKDCITIHSATFAWSQeSPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSA 675
Cdd:TIGR02868 302 AAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYPG-APPVLDGVSLDLPPGERVAILGPSGSGKSTLLAT 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 676 LLGELSKVEGFVSIEGA-------------VAYVPQEAWVQNTSVVENVCFGQ-ELDPPWLERVLEACALQPDVDSFPEG 741
Cdd:TIGR02868 381 LAGLLDPLQGEVTLDGVpvssldqdevrrrVSVCAQDAHLFDTTVRENLRLARpDATDEELWAALERVGLADWLRALPDG 460
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 742 IHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVIGPgglLQGTTRILVTHAL 814
Cdd:TIGR02868 461 LDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA---LSGRTVVLITHHL 530
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1020-1496 |
6.20e-35 |
|
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: 144.11 E-value: 6.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1020 LFQRLLWDVVRS--------PISFFERTPIGHLLNRFSketdtvDVD-IPDKLRSLLMYAFglLEVSLVVAVATPLATVA 1090
Cdd:TIGR01193 223 LGQRLSIDIILSyikhlfelPMSFFSTRRTGEIVSRFT------DASsIIDALASTILSLF--LDMWILVIVGLFLVRQN 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1091 ILpLFLLYAGFQSLYVVSSCQLRR---------LESASYSSvcSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRIS 1161
Cdd:TIGR01193 295 ML-LFLLSLLSIPVYAVIIILFKRtfnklnhdaMQANAVLN--SSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKS 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1162 FPRLVAD---RWLAANVELLGNGLVFAAATCAVLSKaHLSAG-LVGFSVSAALqVTQTLQWVVRNWTDLENSIVSVERMQ 1237
Cdd:TIGR01193 372 FKYQKADqgqQAIKAVTKLILNVVILWTGAYLVMRG-KLTLGqLITFNALLSY-FLTPLENIINLQPKLQAARVANNRLN 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1238 DYAWTPKE-APWRLPTCAAQPpwpqGGQIEFRDFGLRYRPELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQ 1316
Cdd:TIGR01193 450 EVYLVDSEfINKKKRTELNNL----NGDIVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFF 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1317 EAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLdLLQEH---SDEAIWAALETVQLKALVASLPGQLQY 1393
Cdd:TIGR01193 525 QARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENL-LLGAKenvSQDEIWAACEIAEIKDDIENMPLGYQT 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1394 KCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSwFAQCTVLLIAHRLRSVMDCARVLVMD 1473
Cdd:TIGR01193 604 ELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLD 682
|
490 500
....*....|....*....|...
gi 1827346401 1474 KGQVAESGSPAQLLAQKGLFYRL 1496
Cdd:TIGR01193 683 HGKIIEQGSHDELLDRNGFYASL 705
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1255-1472 |
1.93e-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: 140.11 E-value: 1.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1255 AQPPWPQGGQIEFRDFGLRYRPELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG 1334
Cdd:TIGR02857 312 APVTAAPASSLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1335 LHTLRSRISIIPQDPILFPGSLRMNLDLLQ-EHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLA 1413
Cdd:TIGR02857 391 ADSWRDQIAWVPQHPFLFAGTIAENIRLARpDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALA 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 1414 RALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVM 1472
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
649-856 |
4.39e-34 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 139.98 E-value: 4.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELsKVEGFVSIEG-------AVAYVPQEAWV-QNT-----SVVENVCFGQ 715
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGielreldPESWRKHLSWVgQNPqlphgTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 716 -ELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHV--- 791
Cdd:PRK11174 448 pDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVmqa 527
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 792 FNQVIgpggllQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGALMCLLDQARQ 856
Cdd:PRK11174 528 LNAAS------RRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQE 586
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
333-845 |
4.62e-34 |
|
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: 141.42 E-value: 4.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 333 SLFLEFIGDPK-PPAWKGYL--LAVLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITGLVYRKVLALSSGSRKASAVGDV 409
Cdd:TIGR01193 176 SYYLQKIIDTYiPHKMMGTLgiISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEI 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 410 VNLVSvDVQRLTESV------LYLNgLWLpLVWIVVCFVYLWQLLGPSALTAIAVFLSLLPLNFFISKKRNHhqeEQMRq 483
Cdd:TIGR01193 256 VSRFT-DASSIIDALastilsLFLD-MWI-LVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNH---DAMQ- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 484 kdSRARLTSSILRN---SKTIKFHGWE-----------GAFLDR--VLGIRGQELGALRTsGLLFSVSLVSFQVSTFLVA 547
Cdd:TIGR01193 329 --ANAVLNSSIIEDlngIETIKSLTSEaeryskidsefGDYLNKsfKYQKADQGQQAIKA-VTKLILNVVILWTGAYLVM 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 548 LVVFAVHTLVAENAMnaeKAFVTLTVLNILN---KAQAflpfsihslvqARVSFDRL--VTFLCLEEVDPGVVDSSSSGS 622
Cdd:TIGR01193 406 RGKLTLGQLITFNAL---LSYFLTPLENIINlqpKLQA-----------ARVANNRLneVYLVDSEFINKKKRTELNNLN 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 623 AAgkdcITIHSATFAWSQESPpCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG----------- 691
Cdd:TIGR01193 472 GD----IVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslkdidrhtl 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 692 --AVAYVPQEAWVQNTSVVENVCFG--QELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAV 767
Cdd:TIGR01193 547 rqFINYLPQEPYIFSGSILENLLLGakENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARAL 626
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827346401 768 YRKAAVYLLDDPLAALDAHVGQHVFNQVIGpgglLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKG 845
Cdd:TIGR01193 627 LTDSKVLILDESTSNLDTITEKKIVNNLLN----LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNG 700
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1265-1489 |
1.36e-33 |
|
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: 137.34 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLA---SGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSR 1341
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLAlalMGLLPHGGRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1342 ISIIPQDPI--LFPGSLR-------MNLDLLQEHSDEAIWAALETVQLKALVASLPGQlqykcadrgedLSVGQKQLLCL 1412
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGdqiaealENLGLSRAEARARVLELLEAVGLERRLDRYPHQ-----------LSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1413 ARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQ 1489
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVVAEIAdRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
629-845 |
3.12e-33 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 129.14 E-value: 3.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAY 695
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 696 VPQEAWVQNTSVVENVCFGQELDPpwLERVLEACALQpDVDSF----PEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKA 771
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMS--MERVIEAAKLA-GAHDFiselPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 772 AVYLLDDPLAALDaHVGQHVFNQVIgpGGLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKG 845
Cdd:cd03252 158 RILIFDEATSALD-YESEHAIMRNM--HDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
307-845 |
5.90e-33 |
|
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: 136.38 E-value: 5.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 307 FHSTFLLGTLSLIISDVFRFTVPKLLSLFLE--FIGDPKPPAWKGYLLAVLMFLsacLQTLFEQQNMYRLKVLQMRLRSA 384
Cdd:TIGR02203 12 YKAGLVLAGVAMILVAATESTLAALLKPLLDdgFGGRDRSVLWWVPLVVIGLAV---LRGICSFVSTYLLSWVSNKVVRD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 385 ITGLVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTES------VLYLNGLWLpLVWIVVCFVYLWQLLgpsalTAIAV 458
Cdd:TIGR02203 89 IRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAatdafiVLVRETLTV-IGLFIVLLYYSWQLT-----LIVVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 459 FLSLLPLNFFISKKR----NHHQEEQMRQKdsrARLTSSILRNSKTIKFHGWEGAFLDRvlgirgqeLGALRTSGLLFSV 534
Cdd:TIGR02203 163 MLPVLSILMRRVSKRlrriSKEIQNSMGQV---TTVAEETLQGYRVVKLFGGQAYETRR--------FDAVSNRNRRLAM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 535 SLVSFQ-----VSTFLVALVVFAVHTLVAENAMNAEKAFVTLTVLnILNKAQAFLPFSIHSLVQAR-----VSFDRLVTF 604
Cdd:TIGR02203 232 KMTSAGsisspITQLIASLALAVVLFIALFQAQAGSLTAGDFTAF-ITAMIALIRPLKSLTNVNAPmqrglAAAESLFTL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 605 LCLE-EVDPGVVdssssGSAAGKDCITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKV 683
Cdd:TIGR02203 311 LDSPpEKDTGTR-----AIERARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 684 EGFVSIEGA-------------VAYVPQEAWVQNTSVVENVCFGQ--ELDPPWLERVLEACALQPDVDSFPEGIHTSIGE 748
Cdd:TIGR02203 386 SGQILLDGHdladytlaslrrqVALVSQDVVLFNDTIANNIAYGRteQADRAEIERALAAAYAQDFVDKLPLGLDTPIGE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 749 QGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVigpGGLLQGTTRILVTHALHILPQADWIIVLAN 828
Cdd:TIGR02203 466 NGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAAL---ERLMQGRTTLVIAHRLSTIEKADRIVVMDD 542
|
570
....*....|....*..
gi 1827346401 829 GAIAEMGSYQELLQRKG 845
Cdd:TIGR02203 543 GRIVERGTHNELLARNG 559
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1245-1489 |
9.49e-33 |
|
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: 134.65 E-value: 9.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1245 EAPWRLPTCAAQPPWPQGGQ--IEFRD----FGLRYRPELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEA 1318
Cdd:COG1123 239 AVPRLGAARGRAAPAAAAAEplLEVRNlskrYPVRGKGGVR-AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRP 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1319 AEGGIWIDGVPIAHVG---LHTLRSRISIIPQDPI--LFPgslRMN--------LDLLQEHSDEAIWA----ALETVQLK 1381
Cdd:COG1123 318 TSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPYssLNP---RMTvgdiiaepLRLHGLLSRAERRErvaeLLERVGLP 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1382 ALVAS-LPGQlqykcadrgedLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQM-------QAMLGswfaqCTV 1453
Cdd:COG1123 395 PDLADrYPHE-----------LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQIlnllrdlQRELG-----LTY 458
|
250 260 270
....*....|....*....|....*....|....*...
gi 1827346401 1454 LLIAHRLrSVMD--CARVLVMDKGQVAESGSPAQLLAQ 1489
Cdd:COG1123 459 LFISHDL-AVVRyiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
431-843 |
1.29e-32 |
|
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: 135.26 E-value: 1.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 431 WLPLvWIVVCFVyLWQLLGPSALTAIAVFLSLLPLNFFISKKrnhHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAF 510
Cdd:COG4618 142 WAPI-FLAVLFL-FHPLLGLLALVGALVLVALALLNERLTRK---PLKEANEAAIRANAFAEAALRNAEVIEAMGMLPAL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 511 LDRVLGIRGQELG----ALRTSGLLFSVSLV---SFQVST-----FLV------ALVVFAVHTLVA------ENAMNAEK 566
Cdd:COG4618 217 RRRWQRANARALAlqarASDRAGGFSALSKFlrlLLQSAVlglgaYLViqgeitPGAMIAASILMGralapiEQAIGGWK 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 567 AFVtltvlnilnkaqaflpfsihslvQARVSFDRLVTFLCLEEVDPGVVDSSSSGSAagkdcITIHSATFAWSQESPPCL 646
Cdd:COG4618 297 QFV-----------------------SARQAYRRLNELLAAVPAEPERMPLPRPKGR-----LSVENLTVVPPGSKRPIL 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 647 HRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-------------VAYVPQEawVQ--NTSVVENV 711
Cdd:COG4618 349 RGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAdlsqwdreelgrhIGYLPQD--VElfDGTIAENI 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 712 C-FGqELDPpwlERVLEACALQpDVD----SFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAh 786
Cdd:COG4618 427 ArFG-DADP---EKVVAAAKLA-GVHemilRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD- 500
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1827346401 787 VGQHVFNQVIgpGGL-LQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQR 843
Cdd:COG4618 501 EGEAALAAAI--RALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
339-856 |
1.71e-32 |
|
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: 136.24 E-value: 1.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 339 IGDPKPPAWKGYLLAVLMFLSACL--QTLFE--QQnmyrLKVLQM--RLRSAITGLVYRKVLALSSGSRKASAVGDVVNL 412
Cdd:TIGR03797 163 IGTAIPDADRSLLVQIALALLAAAvgAAAFQlaQS----LAVLRLetRMDASLQAAVWDRLLRLPVSFFRQYSTGDLASR 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 413 VSVDVQ---RLTESVL-YLNGLWLPLVWIVVCFVYLWQLlgpsALTAIAVFLSLLPLNFFISKKRNHHQEEQMRQKDSRA 488
Cdd:TIGR03797 239 AMGISQirrILSGSTLtTLLSGIFALLNLGLMFYYSWKL----ALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKIS 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 489 RLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQElgalrtSGLLFSVSLVSFQVSTFLVALVVFAVHTLVAenAMNAEKAF 568
Cdd:TIGR03797 315 GLTVQLINGISKLRVAGAENRAFARWAKLFSRQ------RKLELSAQRIENLLTVFNAVLPVLTSAALFA--AAISLLGG 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 569 VTLTVLNILNKAQAFLPF--SIHSLVQARVS-------FDRLVTFL-CLEEVDPGVVDSSSSGSAagkdcITIHSATFAW 638
Cdd:TIGR03797 387 AGLSLGSFLAFNTAFGSFsgAVTQLSNTLISilaviplWERAKPILeALPEVDEAKTDPGKLSGA-----IEVDRVTFRY 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 639 SQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG---------AV----AYVPQEAWVQNT 705
Cdd:TIGR03797 462 RPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGqdlagldvqAVrrqlGVVLQNGRLMSG 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 706 SVVENVCFGQELDPpwlERVLEA---CALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAA 782
Cdd:TIGR03797 542 SIFENIAGGAPLTL---DEAWEAarmAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSA 618
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827346401 783 LD----AHVGQHVfnqvigpgGLLQGtTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGALMCLLdqARQ 856
Cdd:TIGR03797 619 LDnrtqAIVSESL--------ERLKV-TRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLA--RRQ 685
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1266-1476 |
1.74e-32 |
|
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: 126.04 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1266 EFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISII 1345
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1346 PQDP------------ILFpgSLRmNLDLLQEHSDEAIWAALETVQLKALVASLPgqlqykcadrgEDLSVGQKQLLCLA 1413
Cdd:cd03225 81 FQNPddqffgptveeeVAF--GLE-NLGLPEEEIEERVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 1414 RALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQC-TVLLIAHRLRSVMDCA-RVLVMDKGQ 1476
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGkTIIIVTHDLDLLLELAdRVIVLEDGK 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1265-1481 |
5.21e-32 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 125.31 E-value: 5.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPEL--PLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTL---R 1339
Cdd:cd03257 2 LEVKNLSVSFPTGGgsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1340 SRISIIPQDPIlfpGSL--RMN-----LDLLQEHSDEAIWAALETVQLKALVA-SLPGQlqykCADR--GEdLSVGQKQL 1409
Cdd:cd03257 82 KEIQMVFQDPM---SSLnpRMTigeqiAEPLRIHGKLSKKEARKEAVLLLLVGvGLPEE----VLNRypHE-LSGGQRQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1410 LCLARALLRKTQILILDEATAAVDPGTELQ-------MQAMLGswfaqCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESG 1481
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQildllkkLQEELG-----LTLLFITHDLGVVAKIAdRVAVMYAGKIVEEG 228
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
629-845 |
5.60e-32 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 133.69 E-value: 5.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSQESPpCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAY 695
Cdd:PRK10790 341 IDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsslshsvlrqGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 696 VPQEAWVQNTSVVENVCFGQELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYL 775
Cdd:PRK10790 420 VQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILI 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 776 LDDPLAALDAHVGQHVfNQVIgpGGLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKG 845
Cdd:PRK10790 500 LDEATANIDSGTEQAI-QQAL--AAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQG 566
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
628-842 |
5.97e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 125.59 E-value: 5.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 628 CITIHSATFAWSQEspPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------VAYVPQE 699
Cdd:COG1121 6 AIELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKpprrarrrIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 700 AWVQNT---SVVENVCFGQELDPPWL--------ERVLEACAlQPDVDSFpegIHTSIGEqgmnLSGGQKQRLSLARAVY 768
Cdd:COG1121 84 AEVDWDfpiTVRDVVLMGRYGRRGLFrrpsradrEAVDEALE-RVGLEDL---ADRPIGE----LSGGQQQRVLLARALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 769 RKAAVYLLDDPLAALDAHvGQHVFNQVIgpGGLL-QGTTRILVTHALHILPQ-ADWIIVLANGAIAEmGSYQELLQ 842
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAA-TEEALYELL--RELRrEGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPEEVLT 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
629-831 |
2.79e-31 |
|
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: 123.08 E-value: 2.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-------------VAY 695
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdirqldpadlrrnIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 696 VPQEAWVQNTSVVENVCFG-QELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVY 774
Cdd:cd03245 83 VPQDVTLFYGTLRDNITLGaPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1827346401 775 LLDDPLAALDAHVGQHVFNQVigpGGLLQGTTRILVTHALHILPQADWIIVLANGAI 831
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERL---RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1264-1498 |
6.18e-31 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 130.22 E-value: 6.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1264 QIEFRDFglRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRIS 1343
Cdd:PRK10789 315 DVNIRQF--TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1344 IIPQDPILFPGSLRMNL-----DLLQEHSDEAiwAALETVQLKALvaSLPGQLQYKCADRGEDLSVGQKQLLCLARALLR 1418
Cdd:PRK10789 393 VVSQTPFLFSDTVANNIalgrpDATQQEIEHV--ARLASVHDDIL--RLPQGYDTEVGERGVMLSGGQKQRISIARALLL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1419 KTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLF---YR 1495
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYrdmYR 548
|
...
gi 1827346401 1496 LAQ 1498
Cdd:PRK10789 549 YQQ 551
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1018-1496 |
1.06e-30 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 129.37 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1018 RLLFQRLLwdvvRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLL---MYAFGLL--------EVSLVVAVATPL 1086
Cdd:PRK11176 102 RRLFGHMM----GMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVregASIIGLFimmfyyswQLSLILIVIAPI 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1087 ATVAIlplfllyagfqslYVVSScQLRRLE---SASYSSVCSHMAETFQGSTVVRAFRTQ----------APFVAQNNAR 1153
Cdd:PRK11176 178 VSIAI-------------RVVSK-RFRNISknmQNTMGQVTTSAEQMLKGHKEVLIFGGQevetkrfdkvSNRMRQQGMK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1154 VDESQRISFP--RLVADRWLAAnvellgngLVFAAATCAVlsKAHLSAG--LVGFS--------------VSAALQ---- 1211
Cdd:PRK11176 244 MVSASSISDPiiQLIASLALAF--------VLYAASFPSV--MDTLTAGtiTVVFSsmialmrplksltnVNAQFQrgma 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1212 VTQTLQWVVRNWTDLENSIVSVERMQdyawtpkeapwrlptcaaqppwpqgGQIEFRDFGLRYRPELPLAVQGVSFKIHA 1291
Cdd:PRK11176 314 ACQTLFAILDLEQEKDEGKRVIERAK-------------------------GDIEFRNVTFTYPGKEVPALRNINFKIPA 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1292 GEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLDLLQE--HSDE 1369
Cdd:PRK11176 369 GKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTeqYSRE 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1370 AIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFA 1449
Cdd:PRK11176 449 QIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK 528
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1827346401 1450 QCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFYRL 1496
Cdd:PRK11176 529 NRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
629-836 |
1.25e-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: 121.06 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAY 695
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 696 VPQEAWVQNTSVVENVCFGQELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYL 775
Cdd:cd03244 83 IPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 776 LDDPLAALDAHVGQHVfNQVIgpGGLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGS 836
Cdd:cd03244 163 LDEATASVDPETDALI-QKTI--REAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1265-1481 |
1.78e-30 |
|
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: 118.95 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGlHTLRSRISI 1344
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1345 IPQDPILFPGSLRMNLdllqehsdeaiwaaletvqlkalvaslpgqlqykcadrGEDLSVGQKQLLCLARALLRKTQILI 1424
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1827346401 1425 LDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESG 1481
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
282-851 |
1.88e-30 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 129.84 E-value: 1.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 282 APETEPFLRQEGSQWRPLL-------KAIWQVFHSTFLLgtlsLIISDVFRFTVPKLLSLFLEFI-GDPKPPAWKG--YL 351
Cdd:TIGR00958 131 AGASEKEAEQGQSETADLLfrllglsGRDWPWLISAFVF----LTLSSLGEMFIPFYTGRVIDTLgGDKGPPALASaiFF 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 352 LAVLMFLSACLQTLFEQQNMYRLKVLQMRLRsaitGLVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTESV-LYLNGL 430
Cdd:TIGR00958 207 MCLLSIASSVSAGLRGGSFNYTMARINLRIR----EDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLsLNVNVL 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 431 WLPLVwIVVCFVYLWQLLGPSaLTAIAVFLslLPLNFFISKKRN-HHQEEQMRQKDSRARLTS---SILRNSKTIKFHGW 506
Cdd:TIGR00958 283 LRNLV-MLLGLLGFMLWLSPR-LTMVTLIN--LPLVFLAEKVFGkRYQLLSEELQEAVAKANQvaeEALSGMRTVRSFAA 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 507 EGAFLDRVLGIRGQELGALRTSGLLFSVSLVSFQVSTFLVALVVFA--VHtLVAENAMNAEK--AFVtLTVLNILNKAQA 582
Cdd:TIGR00958 359 EEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYygGQ-LVLTGKVSSGNlvSFL-LYQEQLGEAVRV 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 583 FLpfSIHSLVQARVSFDRLVtfLCLEEVDPGVVDSSSSGSAAGKDCITIHSATFAW-SQESPPCLHRINLTVPQGCLLAV 661
Cdd:TIGR00958 437 LS--YVYSGMMQAVGASEKV--FEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYpNRPDVPVLKGLTFTLHPGEVVAL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 662 VGPVGAGKSSLLSALLGELSKVEGFVSIEGA-------------VAYVPQEAWVQNTSVVENVCFGqeLDPPWLERVLEA 728
Cdd:TIGR00958 513 VGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplvqydhhylhrqVALVGQEPVLFSGSVRENIAYG--LTDTPDEEIMAA 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 729 cALQPDVDSF----PEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVgqhvfNQVIGPGGLLQG 804
Cdd:TIGR00958 591 -AKAANAHDFimefPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC-----EQLLQESRSRAS 664
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1827346401 805 TTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGALMCLL 851
Cdd:TIGR00958 665 RTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
434-846 |
3.90e-29 |
|
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: 124.93 E-value: 3.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 434 LVWIVVCFVYLWQLLGPS--ALTAIAVFLSLLpLNFFISKKRNHHQEEqMRQKDSRA--RLTSSILrNSKTIKFHG---W 506
Cdd:COG5265 163 LLEIALVAGILLVKYDWWfaLITLVTVVLYIA-FTVVVTEWRTKFRRE-MNEADSEAntRAVDSLL-NYETVKYFGneaR 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 507 EGAFLDRVLgiRGQELGALRTSGLLFSVSLV-SFQVSTFLVALVVFAVHTlVAENAMNAeKAFVTLTVLNIlnkaQAFLP 585
Cdd:COG5265 240 EARRYDEAL--ARYERAAVKSQTSLALLNFGqALIIALGLTAMMLMAAQG-VVAGTMTV-GDFVLVNAYLI----QLYIP 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 586 FSIHSLV-----QARVSFDRLVTFLcleEVDPGVVDSSSSGSAAGKDC-ITIHSATFAWSQESPpCLHRINLTVPQGCLL 659
Cdd:COG5265 312 LNFLGFVyreirQALADMERMFDLL---DQPPEVADAPDAPPLVVGGGeVRFENVSFGYDPERP-ILKGVSFEVPAGKTV 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 660 AVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAYVPQEAWVQNTSVVENVCFGQ-ELDPPWLERV 725
Cdd:COG5265 388 AIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdirdvtqaslraAIGIVPQDTVLFNDTIAYNIAYGRpDASEEEVEAA 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 726 LEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVG---QHVFNQVIgpggll 802
Cdd:COG5265 468 ARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTEraiQAALREVA------ 541
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1827346401 803 QGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGA 846
Cdd:COG5265 542 RGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGL 585
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
635-829 |
7.85e-29 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 115.64 E-value: 7.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 635 TFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-------------VAYVPQEAW 701
Cdd:cd03225 6 SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKdltklslkelrrkVGLVFQNPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 702 VQ--NTSVVENVCFGQE---LDPPWLER----VLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAA 772
Cdd:cd03225 86 DQffGPTVEEEVAFGLEnlgLPEEEIEErveeALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 773 VYLLDDPLAALDAHVGQHVFNQVIGpgglL--QGTTRILVTHALH-ILPQADWIIVLANG 829
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKK----LkaEGKTIIIVTHDLDlLLELADRVIVLEDG 210
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1265-1488 |
9.73e-29 |
|
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: 116.44 E-value: 9.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRP--ELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRI 1342
Cdd:COG1124 2 LEVRNLSVSYGQggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1343 SIIPQDPilfPGSL--RMNLD-----LLQEH----SDEAIWAALETVQLKALVAS-LPGQLqykcadrgedlSVGQKQLL 1410
Cdd:COG1124 82 QMVFQDP---YASLhpRHTVDrilaePLRIHglpdREERIAELLEQVGLPPSFLDrYPHQL-----------SGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1411 CLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRsVMD--CARVLVMDKGQVAESGSPAQL 1486
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErgLTYLFVSHDLA-VVAhlCDRVAVMQNGRIVEELTVADL 226
|
..
gi 1827346401 1487 LA 1488
Cdd:COG1124 227 LA 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
635-831 |
1.25e-28 |
|
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: 113.47 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 635 TFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-------------VAYVPQEAW 701
Cdd:cd03246 7 SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGYLPQDDE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 702 VQNTSVVENVcfgqeldppwlervleacalqpdvdsfpegihtsigeqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLA 781
Cdd:cd03246 87 LFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNS 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 782 ALDaHVGQHVFNQVIgpGGL-LQGTTRILVTHALHILPQADWIIVLANGAI 831
Cdd:cd03246 126 HLD-VEGERALNQAI--AALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
635-845 |
1.99e-27 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 119.43 E-value: 1.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 635 TFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFV-------------SIEGAVAYVPQEAW 701
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdipltklqldSWRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 702 VQNTSVVENVCFGQ-ELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPL 780
Cdd:PRK10789 400 LFSDTVANNIALGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 781 AALDAHVGQHVFNQVIGPGgllQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKG 845
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWG---EGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
631-832 |
3.36e-27 |
|
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: 110.70 E-value: 3.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 631 IHSATFAWSQEspPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------VAYVPQEA-- 700
Cdd:cd03235 2 VEDLTVSYGGH--PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerkrIGYVPQRRsi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 701 -WVQNTSVVENVCFGQELDPPWL--------ERVLEACALqpdVDSFpEGIHTSIGEqgmnLSGGQKQRLSLARAVYRKA 771
Cdd:cd03235 80 dRDFPISVRDVVLMGLYGHKGLFrrlskadkAKVDEALER---VGLS-ELADRQIGE----LSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827346401 772 AVYLLDDPLAALDAHVGQHVFnqvigpgGLL-----QGTTRILVTHALH-ILPQADWIIVLANGAIA 832
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIY-------ELLrelrrEGMTILVVTHDLGlVLEYFDRVLLLNRTVVA 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
646-781 |
3.60e-27 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 108.50 E-value: 3.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-------------VAYVPQEAWVQN-TSVVENV 711
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrkeIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827346401 712 CFGQELDPP-------WLERVLEACALqpdvdsfPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLA 781
Cdd:pfam00005 81 RLGLLLKGLskrekdaRAEEALEKLGL-------GDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1282-1430 |
3.71e-27 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 108.50 E-value: 3.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1282 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPG-SLRMNL 1360
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827346401 1361 -------DLLQEHSDEAIWAALETVQLKALVASLPGqlqykcaDRGEDLSVGQKQLLCLARALLRKTQILILDEATA 1430
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKLGLGDLADRPVG-------ERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1265-1477 |
3.75e-27 |
|
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: 109.23 E-value: 3.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISI 1344
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1345 IPQDPILFPGSLRMNLdllqehsdeaiwaaletvqlkalvaslpgqlqykcadrgedLSVGQKQLLCLARALLRKTQILI 1424
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 1425 LDEATAAVDPGTE-LQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQV 1477
Cdd:cd03246 120 LDEPNSHLDVEGErALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1265-1489 |
5.26e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 110.92 E-value: 5.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELplAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHvGLHTLRSRISI 1344
Cdd:COG1131 1 IEVRGLTKRYGDKT--ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1345 IPQDPILFPG-SLRMNLDLL-------QEHSDEAIWAALETVQLKAlvaslpgqlqyKCADRGEDLSVGQKQLLCLARAL 1416
Cdd:COG1131 78 VPQEPALYPDlTVRENLRFFarlyglpRKEARERIDELLELFGLTD-----------AADRKVGTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 1417 LRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ-CTVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQLLAQ 1489
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
948-1216 |
5.40e-27 |
|
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: 112.35 E-value: 5.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 948 LYALFLFLCQQVASFCRGYWLSLWADDPAVGGQQ--TQAALRGGIFGLLGCLQAIGLFASMAAVLLGGARASRLLFQRLL 1025
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDPetQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1026 WDVVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLLYAGFQSLY 1105
Cdd:pfam00664 82 KKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1106 VVSSCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANVELLGNGLVFA 1185
Cdd:pfam00664 162 AKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYAL 241
|
250 260 270
....*....|....*....|....*....|...
gi 1827346401 1186 AA-TCAVLSKAH-LSAGLVGFSVSAALQVTQTL 1216
Cdd:pfam00664 242 ALwFGAYLVISGeLSVGDLVAFLSLFAQLFGPL 274
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
646-843 |
2.75e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 109.00 E-value: 2.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA------------VAYVPQEAWV-QNTSVVENVC 712
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvardpaevrrrIGYVPQEPALyPDLTVRENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 713 F-------GQELDPPWLERVLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDA 785
Cdd:COG1131 96 FfarlyglPRKEARERIDELLELFGLTDAADRKVG-----------TLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 786 hVGQHVFNQVIgpGGLL-QGTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELLQR 843
Cdd:COG1131 165 -EARRELWELL--RELAaEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
646-843 |
4.39e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 111.39 E-value: 4.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYV---PQE---AWV-QN------TSVVENVC 712
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnlpPRErrvGFVfQHyalfphMTVAENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 713 FGQELDPP-----------WLERV-LEACAlqpdvDSFPegihtsigeqgMNLSGGQKQRLSLARAVYRKAAVYLLDDPL 780
Cdd:COG1118 98 FGLRVRPPskaeirarveeLLELVqLEGLA-----DRYP-----------SQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 781 AALDAHVGQ-------HVFNQvigpgglLQGTTrILVTH----ALHIlpqADWIIVLANGAIAEMGSYQELLQR 843
Cdd:COG1118 162 GALDAKVRKelrrwlrRLHDE-------LGGTT-VFVTHdqeeALEL---ADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1265-1492 |
2.26e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 106.71 E-value: 2.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELplAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVglhtlRSRISI 1344
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1345 IPQDPIL---FPGSLR----MNLD-------LLQEHSDEAIWAALETVQLKALvaslpgqlqykcADR--GEdLSVGQKQ 1408
Cdd:COG1121 80 VPQRAEVdwdFPITVRdvvlMGRYgrrglfrRPSRADREAVDEALERVGLEDL------------ADRpiGE-LSGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1409 llclarallrKT----------QILILDEATAAVDPGTELQMQAMLGSWFAQ-CTVLLIAHRLRSVMDCA-RVLVMDKGQ 1476
Cdd:COG1121 147 ----------RVllaralaqdpDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREYFdRVLLLNRGL 216
|
250
....*....|....*.
gi 1827346401 1477 VAeSGSPAQLLAQKGL 1492
Cdd:COG1121 217 VA-HGPPEEVLTPENL 231
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
635-829 |
2.90e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 106.71 E-value: 2.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 635 TFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------VAYVPQEA----Wv 702
Cdd:COG1116 16 RFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKpvtgpgpdRGVVFQEPallpW- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 703 qnTSVVENVCFGQEL-------DPPWLERVLEACALQPDVDSFPegiHTsigeqgmnLSGGQKQRLSLARAVYRKAAVYL 775
Cdd:COG1116 95 --LTVLDNVALGLELrgvpkaeRRERARELLELVGLAGFEDAYP---HQ--------LSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 776 LDDPLAALDAHVGQHVFNQVIgpgGLLQ--GTTRILVTH----ALHIlpqADWIIVLANG 829
Cdd:COG1116 162 MDEPFGALDALTRERLQDELL---RLWQetGKTVLFVTHdvdeAVFL---ADRVVVLSAR 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
629-867 |
5.76e-25 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 111.15 E-value: 5.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGEL---SKVEGFVSIEG-------------A 692
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphgGRISGEVLLDGrdllelsealrgrR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 693 VAYVPQEAWVQ--NTSVVENVCFGQELD-------PPWLERVLEACALQPDVDSFPegiHTsigeqgmnLSGGQKQRLSL 763
Cdd:COG1123 85 IGMVFQDPMTQlnPVTVGDQIAEALENLglsraeaRARVLELLEAVGLERRLDRYP---HQ--------LSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 764 ARAVYRKAAVYLLDDPLAALDAHVGQHVFnQVIGPGGLLQGTTRILVTHALH-ILPQADWIIVLANGAIAEMGSYQELLQ 842
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEIL-DLLRELQRERGTTVLLITHDLGvVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
250 260
....*....|....*....|....*..
gi 1827346401 843 RKGALMCL--LDQARQPGDRGEGETEP 867
Cdd:COG1123 233 APQALAAVprLGAARGRAAPAAAAAEP 259
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
642-851 |
6.50e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 111.59 E-value: 6.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 642 SPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAYVPQEAWVQNTSVV 708
Cdd:PRK13657 347 SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtvtraslrrNIAVVFQDAGLFNRSIE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 709 ENVCFGQE-LDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHV 787
Cdd:PRK13657 427 DNIRVGRPdATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVET 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 788 GQHVfNQVIGPggLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGALMCLL 851
Cdd:PRK13657 507 EAKV-KAALDE--LMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALL 567
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1271-1491 |
7.53e-25 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 104.94 E-value: 7.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1271 GLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHtLRSRISIIPQDPI 1350
Cdd:COG4555 6 NLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLPDERG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1351 LFPG-SLRMNLDL---LQEHSDEAIWAALEtvqlkALVASLpgQLQyKCADRG-EDLSVGQKQLLCLARALLRKTQILIL 1425
Cdd:COG4555 85 LYDRlTVRENIRYfaeLYGLFDEELKKRIE-----ELIELL--GLE-EFLDRRvGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827346401 1426 DEATAAVDPGTELQMQAMLGSWFAQ-CTVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQLLAQKG 1491
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEgKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1266-1476 |
7.61e-25 |
|
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: 102.32 E-value: 7.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1266 EFRDFGLRYRPelPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISII 1345
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1346 PQdpilfpgslrmnldllqehsdeaiwaaletvqlkalvaslpgqlqykcadrgedLSVGQKQLLCLARALLRKTQILIL 1425
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 1426 DEATAAVDPGTELQMQAMLGSWFAQ-CTVLLIAHRLRSVMD-CARVLVMDKGQ 1476
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
646-833 |
8.59e-25 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 104.09 E-value: 8.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------VAYVPQEA----WvqnTSVVENVCF 713
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgpdRGYVFQQDallpW---LTVLDNVAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 714 GQEL----DPPWLERV---LEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAH 786
Cdd:cd03293 97 GLELqgvpKAEARERAeelLELVGLSGFENAYPH-----------QLSGGMRQRVALARALAVDPDVLLLDEPFSALDAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 787 VGQHVFNQVIgpgGLLQ--GTTRILVTH----ALHIlpqADWIIVLAN--GAIAE 833
Cdd:cd03293 166 TREQLQEELL---DIWRetGKTVLLVTHdideAVFL---ADRVVVLSArpGRIVA 214
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
629-845 |
9.56e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 111.07 E-value: 9.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAY 695
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiadyseaalrqAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 696 VPQEAWVQNTSVVENVCFGQ-ELDPPWLERVLEACALQPDVDSfPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVY 774
Cdd:PRK11160 419 VSQRVHLFSATLRDNLLLAApNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLL 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 775 LLDDPLAALDAHVGQHVFNqvigpggLL----QGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKG 845
Cdd:PRK11160 498 LLDEPTEGLDAETERQILE-------LLaehaQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQG 565
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
629-845 |
1.28e-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: 104.55 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSqeSPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG------------AVAYV 696
Cdd:COG4555 2 IEVENLSKKYG--KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 697 PQE-AWVQNTSVVENVCFGQELDPPWLERVLEACALQPDVDSFPEGIHTSIGEqgmnLSGGQKQRLSLARAVYRKAAVYL 775
Cdd:COG4555 80 PDErGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGE----LSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 776 LDDPLAALDAhVGQHVFNQVIgpgGLL--QGTTRILVTHALH-ILPQADWIIVLANGAIAEMGSYQELLQRKG 845
Cdd:COG4555 156 LDEPTNGLDV-MARRLLREIL---RALkkEGKTVLFSSHIMQeVEALCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
646-829 |
1.44e-24 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 102.09 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGavayvpqeawvqnTSVVENVcfgqeldppwlERV 725
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG-------------KDIKKEP-----------EEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 726 LEACALQPDVDSFPEGIhTsiGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAhVGQHVFNQVIgpGGLL-QG 804
Cdd:cd03230 72 KRRIGYLPEEPSLYENL-T--VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREFWELL--RELKkEG 145
|
170 180
....*....|....*....|....*.
gi 1827346401 805 TTRILVTHALHILPQ-ADWIIVLANG 829
Cdd:cd03230 146 KTILLSSHILEEAERlCDRVAILNNG 171
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
636-835 |
1.54e-24 |
|
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: 103.37 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 636 FAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-----------VAYVPQE-AWVQ 703
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvpperrnIGMVFQDyALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 704 NTSVVENVCFGQEL----DPPWLERVLEACA---LQPDVDSFPEGihtsigeqgmnLSGGQKQRLSLARAVYRKAAVYLL 776
Cdd:cd03259 86 HLTVAENIAFGLKLrgvpKAEIRARVRELLElvgLEGLLNRYPHE-----------LSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 777 DDPLAALDAHVGQHVFNQVIgpgGLL--QGTTRILVTH----ALHIlpqADWIIVLANGAIAEMG 835
Cdd:cd03259 155 DEPLSALDAKLREELREELK---ELQreLGITTIYVTHdqeeALAL---ADRIAVMNEGRIVQVG 213
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
626-846 |
1.93e-24 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 110.11 E-value: 1.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 626 KDCITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSaLLGELSKV-EGFVSIEG------------- 691
Cdd:PRK11176 339 KGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIAN-LLTRFYDIdEGEILLDGhdlrdytlaslrn 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 692 AVAYVPQEAWVQNTSVVENVCFGQElDPPWLERVLEACALQPDVD---SFPEGIHTSIGEQGMNLSGGQKQRLSLARAVY 768
Cdd:PRK11176 418 QVALVSQNVHLFNDTIANNIAYART-EQYSREQIEEAARMAYAMDfinKMDNGLDTVIGENGVLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 769 RKAAVYLLDDPLAALDA---HVGQHVFNQvigpggLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKG 845
Cdd:PRK11176 497 RDSPILILDEATSALDTeseRAIQAALDE------LQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNG 570
|
.
gi 1827346401 846 A 846
Cdd:PRK11176 571 V 571
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
646-842 |
3.29e-24 |
|
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: 102.97 E-value: 3.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA----------------VAYVPQE-AWVQNTSVV 708
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrrMGMLFQSgALFDSLTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 709 ENVCFG----QELDPPWLERV----LEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPL 780
Cdd:cd03261 96 ENVAFPlrehTRLSEEEIREIvlekLEAVGLRGAEDLYPA-----------ELSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 781 AALDAhVGQHVFNQVIgpgGLLQ---GTTRILVTHALH-ILPQADWIIVLANGAIAEMGSYQELLQ 842
Cdd:cd03261 165 AGLDP-IASGVIDDLI---RSLKkelGLTSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
646-841 |
3.41e-24 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 103.58 E-value: 3.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAYVPQEAWVQ-NTSVVENV 711
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAYVPQEPPAPfGLTVRELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 712 CFG--------QELDPPWLERVLEACALQpDVDSFpegIHTSIGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAAL 783
Cdd:COG1120 97 ALGryphlglfGRPSAEDREAVEEALERT-GLEHL---ADRPVDE----LSGGERQRVLIARALAQEPPLLLLDEPTSHL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 784 DAHVGQHVFNqvigpggLL------QGTTRILVTHAL-HILPQADWIIVLANGAIAEMGSYQELL 841
Cdd:COG1120 169 DLAHQLEVLE-------LLrrlareRGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
311-578 |
3.63e-24 |
|
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: 103.88 E-value: 3.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 311 FLLGTLSLIISDVFRFTVPKLLSLFLEFI---GDPKPPAWKGYLLAVLMFLSACLQTLFEQQnmYRLKVLQMRLRSAITG 387
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLlpdGDPETQALNVYSLALLLLGLAQFILSFLQS--YLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 388 LVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTESVLYLNGLWLPLVWIVVC-----FVYLWQLlgpsALTAIAVFLSL 462
Cdd:pfam00664 79 KLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGgiivmFYYGWKL----TLVLLAVLPLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 463 LPLNFFISKKRNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLLFSVSLVSFQ-V 541
Cdd:pfam00664 155 ILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQfI 234
|
250 260 270
....*....|....*....|....*....|....*..
gi 1827346401 542 STFLVALVVFAVHTLVAENAMNAEKAFVTLTVLNILN 578
Cdd:pfam00664 235 GYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLF 271
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
629-848 |
3.86e-24 |
|
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: 102.41 E-value: 3.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSQEsPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-------------VAY 695
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKditkknlrelrrkVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 696 VPQEAWVQ--NTSVVENVCFG---QELDPPWLER----VLEACALQPDVDSFPegiHTsigeqgmnLSGGQKQRLSLARA 766
Cdd:COG1122 80 VFQNPDDQlfAPTVEEDVAFGpenLGLPREEIRErveeALELVGLEHLADRPP---HE--------LSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 767 VYRKAAVYLLDDPLAALDAHVGQHVFNQVigpGGL-LQGTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELLQRK 844
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELL---KRLnKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
....
gi 1827346401 845 GALM 848
Cdd:COG1122 226 ELLE 229
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
629-835 |
1.70e-23 |
|
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: 98.92 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG------------AVAYV 696
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvsdlekalssLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 697 PQEAWVQNTSVVENVcfgqeldppwlervleacalqpdvdsfpegihtsigeqGMNLSGGQKQRLSLARAVYRKAAVYLL 776
Cdd:cd03247 81 NQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 777 DDPLAALDAHVGQHVFNQVIgpgGLLQGTTRILVTHALHILPQADWIIVLANGAIAEMG 835
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIF---EVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1265-1487 |
2.94e-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: 100.89 E-value: 2.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELplAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISI 1344
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1345 IPQDPIL-FPGSLR----M-------NLDLLQEHSDEAIWAALETVQLKALvaslpgqlqykcADRG-EDLSVGQKQLLC 1411
Cdd:COG1120 80 VPQEPPApFGLTVRelvaLgryphlgLFGRPSAEDREAVEEALERTGLEHL------------ADRPvDELSGGERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 1412 LARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLL 1487
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErgRTVVMVLHDLNLAARYAdRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
635-831 |
3.02e-23 |
|
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: 99.85 E-value: 3.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 635 TFAWSQESP-PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAYVPQEA 700
Cdd:cd03248 18 TFAYPTRPDtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyehkylhsKVSLVGQEP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 701 WVQNTSVVENVCFGQELDPpwLERVLEAcALQPDVDSF----PEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLL 776
Cdd:cd03248 98 VLFARSLQDNIAYGLQSCS--FECVKEA-AQKAHAHSFiselASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 777 DDPLAALDAHvGQHVFNQVIGPGglLQGTTRILVTHALHILPQADWIIVLANGAI 831
Cdd:cd03248 175 DEATSALDAE-SEQQVQQALYDW--PERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
646-831 |
3.17e-23 |
|
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: 98.28 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAYVPQeawvqntsvvenvc 712
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGkdlaslspkelarKIAYVPQ-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 713 fgqeldppWLERVleacalqpDVDSFpegIHTSIGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDahvgqhVF 792
Cdd:cd03214 81 --------ALELL--------GLAHL---ADRPFNE----LSGGERQRVLLARALAQEPPILLLDEPTSHLD------IA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1827346401 793 NQVIgpggLLQ---------GTTRILVTHAL-HILPQADWIIVLANGAI 831
Cdd:cd03214 132 HQIE----LLEllrrlarerGKTVVMVLHDLnLAARYADRVILLKDGRI 176
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
642-829 |
3.68e-23 |
|
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: 97.32 E-value: 3.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 642 SPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-AVAYVPQEAWVQNTSVVenvcfgqeldpp 720
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGkDIAKLPLEELRRRIGYV------------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 721 wlervleacaLQpdvdsfpegihtsigeqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVIGPgg 800
Cdd:cd00267 79 ----------PQ--------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLREL-- 126
|
170 180 190
....*....|....*....|....*....|
gi 1827346401 801 LLQGTTRILVTHAL-HILPQADWIIVLANG 829
Cdd:cd00267 127 AEEGRTVIIVTHDPeLAELAADRVIVLKDG 156
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
636-831 |
5.09e-23 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 98.73 E-value: 5.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 636 FAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-------------VAYVPQE-AW 701
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKplsampppewrrqVAYVPQEpAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 702 VQNTsVVENVCF-----GQELDPPWLERVLEACALQPDVdsfpegIHTSIGEqgmnLSGGQKQRLSLARAVYRKAAVYLL 776
Cdd:COG4619 86 WGGT-VRDNLPFpfqlrERKFDRERALELLERLGLPPDI------LDKPVER----LSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 777 DDPLAALDAHVGQHVFNqvigpggLLQ------GTTRILVTH-ALHILPQADWIIVLANGAI 831
Cdd:COG4619 155 DEPTSALDPENTRRVEE-------LLReylaeeGRAVLWVSHdPEQIERVADRVLTLEAGRL 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1281-1489 |
6.63e-23 |
|
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: 104.77 E-value: 6.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEaAEGGIWIDGVPIAHVG---LHTLRSRISIIPQDPilFpGSL- 1356
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--F-GSLs 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1357 -RMN--------LDLLQEHSDEA-----IWAALETVQLKAlvaslpgqlqyKCADR--GEdLSVGQKQLLCLARALLRKT 1420
Cdd:COG4172 377 pRMTvgqiiaegLRVHGPGLSAAerrarVAEALEEVGLDP-----------AARHRypHE-FSGGQRQRIAIARALILEP 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827346401 1421 QILILDEATAAVDPGTELQM-------QAMLGswfaqCTVLLIAHRLRSV--MdCARVLVMDKGQVAESGSPAQLLAQ 1489
Cdd:COG4172 445 KLLVLDEPTSALDVSVQAQIldllrdlQREHG-----LAYLFISHDLAVVraL-AHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
646-843 |
7.49e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 102.07 E-value: 7.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGeLSKV-EGFVSIEGA-----------VAYVPQE-AWVQNTSVVENVC 712
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG-LEDPtSGEILIGGRdvtdlppkdrnIAMVFQSyALYPHMTVYENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 713 FG--------QELDppwlERVLEACA---LQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLA 781
Cdd:COG3839 98 FPlklrkvpkAEID----RRVREAAEllgLEDLLDRKPK-----------QLSGGQRQRVALGRALVREPKVFLLDEPLS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 782 ALDAHvgqhvfnqvigpggL----------LQ---GTTRILVTH----ALHIlpqADWIIVLANGAIAEMGSYQELLQR 843
Cdd:COG3839 163 NLDAK--------------LrvemraeikrLHrrlGTTTIYVTHdqveAMTL---ADRIAVMNDGRIQQVGTPEELYDR 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
646-833 |
1.76e-22 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 97.81 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSaLLGELSKV-EGFVSIEG-----------------AVAYVPQEA-WVQNTS 706
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVLIDGqdisslserelarlrrrHIGFVFQFFnLLPELT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 707 VVENVCFGQEL-------DPPWLERVLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDP 779
Cdd:COG1136 103 ALENVALPLLLagvsrkeRRERARELLERVGLGDRLDHRPS-----------QLSGGQQQRVAIARALVNRPKLILADEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 780 LAALDAHVGQHVFNqvigpggLLQ------GTTRILVTHALHILPQADWIIVLANGAIAE 833
Cdd:COG1136 172 TGNLDSKTGEEVLE-------LLRelnrelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1265-1489 |
1.76e-22 |
|
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: 98.04 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRY--RPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHV---GLHTLR 1339
Cdd:cd03258 2 IELKNVSKVFgdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1340 SRISIIPQ-----------DPILFPgslrmnLDLL---QEHSDEAIWAALETVQLKALVASLPGQLqykcadrgedlSVG 1405
Cdd:cd03258 82 RRIGMIFQhfnllssrtvfENVALP------LEIAgvpKAEIEERVLELLELVGLEDKADAYPAQL-----------SGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1406 QKQLLCLARALLRKTQILILDEATAAVDPGT-----EL--QMQAMLGswfaqCTVLLIAHRLRSVMD-CARVLVMDKGQV 1477
Cdd:cd03258 145 QKQRVGIARALANNPKVLLCDEATSALDPETtqsilALlrDINRELG-----LTIVLITHEMEVVKRiCDRVAVMEKGEV 219
|
250
....*....|..
gi 1827346401 1478 AESGSPAQLLAQ 1489
Cdd:cd03258 220 VEEGTVEEVFAN 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1281-1476 |
2.68e-22 |
|
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: 95.72 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHT--LRSRISIIPQDPILFPgslRM 1358
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIGMVFQDFALFP---HL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1359 NldllqehsdeaiwaALETVQLKalvaslpgqlqykcadrgedLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTEL 1438
Cdd:cd03229 92 T--------------VLENIALG--------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1827346401 1439 QMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQ 1476
Cdd:cd03229 138 EVRALLKSLQAQlgITVVLVTHDLDEAARLAdRVVVLRDGK 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1265-1486 |
8.07e-22 |
|
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: 95.71 E-value: 8.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELplAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEA-----AEGGIWIDGVPIAHVGLH--T 1337
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1338 LRSRISIIPQDPILFPGSLRMNLDL--------LQEHSDEAIWAALETVQLKALVAslpgqlqykcaDR--GEDLSVGQK 1407
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYglrlhgikLKEELDERVEEALRKAALWDEVK-----------DRlhALGLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1408 QLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQL 1486
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVAdRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
646-835 |
1.02e-21 |
|
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: 95.01 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYVPQE----AWV-QN------TSVVENVCF 713
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdVTDLPPKdrdiAMVfQNyalyphMTVYDNIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 714 G--------QELDppwlERVLEACALQpdvdsfpeGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDA 785
Cdd:cd03301 96 GlklrkvpkDEID----ERVREVAELL--------QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1827346401 786 HVGQHVFNQVIGpgglLQ---GTTRILVTH----ALHIlpqADWIIVLANGAIAEMG 835
Cdd:cd03301 164 KLRVQMRAELKR----LQqrlGTTTIYVTHdqveAMTM---ADRIAVMNDGQIQQIG 213
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1205-1459 |
1.10e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 101.42 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1205 SVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDYAWTPKEAPwRLPTCAAQPPWPQGGQIEFRDFGLRYRPELPLaVQG 1284
Cdd:COG4178 304 AASAFGQVQGALSWFVDNYQSLAEWRATVDRLAGFEEALEAAD-ALPEAASRIETSEDGALALEDLTLRTPDGRPL-LED 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1285 VSFKIHAGEKVGIVGRTGAGKSSLasglLRlqeaAEGGIWidgvPIA--HVGLHTLrSRISIIPQDPILFPGSLRMNL-- 1360
Cdd:COG4178 382 LSLSLKPGERLLITGPSGSGKSTL----LR----AIAGLW----PYGsgRIARPAG-ARVLFLPQRPYLPLGTLREALly 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1361 -DLLQEHSDEAIWAALETVQLKALVASLpgqlqykcaDRGED----LSVGQKQLLCLARALLRKTQILILDEATAAVDPG 1435
Cdd:COG4178 449 pATAEAFSDAELREALEAVGLGHLAERL---------DEEADwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
250 260
....*....|....*....|....
gi 1827346401 1436 TELQMQAMLGSWFAQCTVLLIAHR 1459
Cdd:COG4178 520 NEAALYQLLREELPGTTVISVGHR 543
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
646-812 |
1.54e-21 |
|
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: 94.47 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG------------AVAYV-PQEAWVQNTSVVENVC 712
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYLgHADGLKPELTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 713 F-----GQELDPPWLERVLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHv 787
Cdd:COG4133 98 FwaalyGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA- 165
|
170 180
....*....|....*....|....*....
gi 1827346401 788 GQHVFNQVI----GPGGLLqgttrILVTH 812
Cdd:COG4133 166 GVALLAELIaahlARGGAV-----LLTTH 189
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
646-843 |
2.24e-21 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 97.48 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-----------VAYVPQE-AWVQNTSVVENVCF 713
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppekrnVGMVFQDyALFPHLTVAENVAF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 714 G--------QELDppwlERVLEACALqpdvdsfpegihTSIGEQG----MNLSGGQKQRLSLARAVYRKAAVYLLDDPLA 781
Cdd:COG3842 101 GlrmrgvpkAEIR----ARVAELLEL------------VGLEGLAdrypHQLSGGQQQRVALARALAPEPRVLLLDEPLS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827346401 782 ALDAHVGQHVFNQVIgpgGLLQ--GTTRILVTH----ALHIlpqADWIIVLANGAIAEMGSYQELLQR 843
Cdd:COG3842 165 ALDAKLREEMREELR---RLQRelGITFIYVTHdqeeALAL---ADRIAVMNDGRIEQVGTPEEIYER 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1266-1481 |
2.59e-21 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 92.88 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1266 EFRDFGLRYRPelPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISII 1345
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1346 PQdpilfpgslrmnldllqehsdeaiwaALETVQLKALvaslpgqlqykcADRG-EDLSVGQKQLLCLARALLRKTQILI 1424
Cdd:cd03214 79 PQ--------------------------ALELLGLAHL------------ADRPfNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1425 LDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESG 1481
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARErgKTVVMVLHDLNLAARYAdRVILLKDGRIVAQG 180
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1265-1476 |
3.08e-21 |
|
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: 93.30 E-value: 3.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRP---ELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGvpiahvglhtlrsR 1341
Cdd:cd03250 1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1342 ISIIPQDPILFPGSLRMNLDLLQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQ 1421
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1827346401 1422 ILILDEATAAVDPGTELQM--QAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQ 1476
Cdd:cd03250 148 IYLLDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1281-1489 |
4.34e-21 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 96.30 E-value: 4.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHV---GLHTLRSRISIIPQ---------- 1347
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALserELRAARRKIGMIFQhfnllssrtv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1348 -DPILFPgsLRmnldlLQEHSDEAIWAA----LETVQLKALVASLPGQLqykcadrgedlSVGQKQllclarallrktQI 1422
Cdd:COG1135 100 aENVALP--LE-----IAGVPKAEIRKRvaelLELVGLSDKADAYPSQL-----------SGGQKQrvgiaralannpKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 1423 LILDEATAAVDPGT-----EL--QMQAMLGSwfaqcTVLLIAHRlrsvMD-----CARVLVMDKGQVAESGSPAQLLAQ 1489
Cdd:COG1135 162 LLCDEATSALDPETtrsilDLlkDINRELGL-----TIVLITHE----MDvvrriCDRVAVLENGRIVEQGPVLDVFAN 231
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
646-831 |
5.69e-21 |
|
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: 92.94 E-value: 5.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSaLLGELSKV-EGFVSIEGA-----------------VAYVPQE-AWVQNTS 706
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVRVDGTdisklsekelaafrrrhIGFVFQSfNLLPDLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 707 VVENVCFGQEL----DPPWLERVLEACALqpdVDsFPEGIHTSIGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAA 782
Cdd:cd03255 99 ALENVELPLLLagvpKKERRERAEELLER---VG-LGDRLNHYPSE----LSGGQQQRVAIARALANDPKIILADEPTGN 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 783 LDAHVGQHVFNqvigpggLLQ------GTTRILVTHALHILPQADWIIVLANGAI 831
Cdd:cd03255 171 LDSETGKEVME-------LLRelnkeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
646-840 |
5.88e-21 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 93.40 E-value: 5.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSAL-----LGELSKVEGFVSIEGA---------------VAYVPQEAWVQNT 705
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKdiydldvdvlelrrrVGMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 706 SVVENVCFGqeldpPWL-------------ERVLEACALQPDVDSFPEGIHtsigeqgmnLSGGQKQRLSLARAVYRKAA 772
Cdd:cd03260 96 SIYDNVAYG-----LRLhgiklkeeldervEEALRKAALWDEVKDRLHALG---------LSGGQQQRLCLARALANEPE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 773 VYLLDDPLAALDAhVGQHVFNQVIgpGGLLQGTTRILVTHALHilpQA----DWIIVLANGAIAEMGSYQEL 840
Cdd:cd03260 162 VLLLDEPTSALDP-ISTAKIEELI--AELKKEYTIVIVTHNMQ---QAarvaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1266-1478 |
6.78e-21 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 92.60 E-value: 6.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1266 EFRDFGLRYRPELplAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVglhtlRSRISII 1345
Cdd:cd03235 1 EVEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1346 PQDPIL---FPGSLR----------MNLDLLQEHSD-EAIWAALETVQLKALvaslpgqlqykcADR--GEdLSVGQKQL 1409
Cdd:cd03235 74 PQRRSIdrdFPISVRdvvlmglyghKGLFRRLSKADkAKVDEALERVGLSEL------------ADRqiGE-LSGGQQQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 1410 LCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ-CTVLLIAHRLRSVMD-CARVLVMDKGQVA 1478
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEyFDRVLLLNRTVVA 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1265-1488 |
6.97e-21 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 93.34 E-value: 6.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELPLavQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG---LHTLRSR 1341
Cdd:cd03261 1 IELRGLTKSFGGRTVL--KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1342 ISIIPQDPILF-----------PgsLRMNLDLLQEHSDEAIWAALETVQLKALVASLPGQlqykcadrgedLSVGQKQLL 1410
Cdd:cd03261 79 MGMLFQSGALFdsltvfenvafP--LREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAE-----------LSGGMKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1411 CLARALLRKTQILILDEATAAVDPGTE-------LQMQAMLGswfaqCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGS 1482
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDPIASgviddliRSLKKELG-----LTSIMVTHDLDTAFAIAdRIAVLYDGKIVAEGT 220
|
....*.
gi 1827346401 1483 PAQLLA 1488
Cdd:cd03261 221 PEELRA 226
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1265-1489 |
7.20e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 94.31 E-value: 7.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLA---SGLLRLQEaaeGGIWIDGVPIAHVGLHTLRSR 1341
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAkllNGLLLPEA---GTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1342 ISIIPQDP------------ILFpgSLRmNLDLLQEHSDEAIWAALETVQLKALVASLPGQLqykcadrgedlSVGQKQL 1409
Cdd:PRK13635 83 VGMVFQNPdnqfvgatvqddVAF--GLE-NIGVPREEMVERVDQALRQVGMEDFLNREPHRL-----------SGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1410 LCLARALLRKTQILILDEATAAVDP-------GT--ELQMQAMLgswfaqcTVLLIAHRLRSVMDCARVLVMDKGQVAES 1480
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPrgrrevlETvrQLKEQKGI-------TVLSITHDLDEAAQADRVIVMNKGEILEE 221
|
....*....
gi 1827346401 1481 GSPAQLLAQ 1489
Cdd:PRK13635 222 GTPEEIFKS 230
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
633-843 |
8.08e-21 |
|
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: 93.33 E-value: 8.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 633 SATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAYVPQE 699
Cdd:COG1124 8 SVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGrpvtrrrrkafrrRVQMVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 700 AWvqnTSV-----VENV------CFGQELDPPWLERVLEACALQPDV-DSFPegiHTsigeqgmnLSGGQKQRLSLARAV 767
Cdd:COG1124 88 PY---ASLhprhtVDRIlaeplrIHGLPDREERIAELLEQVGLPPSFlDRYP---HQ--------LSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 768 YRKAAVYLLDDPLAALDAHVGQHVFNqvigpggLLQ------GTTRILVTH----ALHIlpqADWIIVLANGAIAEMGSY 837
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILN-------LLKdlreerGLTYLFVSHdlavVAHL---CDRVAVMQNGRIVEELTV 223
|
....*.
gi 1827346401 838 QELLQR 843
Cdd:COG1124 224 ADLLAG 229
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1265-1490 |
9.21e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 93.90 E-value: 9.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISI 1344
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1345 IPQDP------------ILFpgSLRmNLDLLQEHSDEAIWAALETVQLKALVASLPgqlqykcadrgEDLSVGQKQLLCL 1412
Cdd:PRK13632 88 IFQNPdnqfigatveddIAF--GLE-NKKVPPKKMKDIIDDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1413 ARALLRKTQILILDEATAAVDPG---------TELQMQamlgswfAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSP 1483
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKgkreikkimVDLRKT-------RKKTLISITHDMDEAILADKVIVFSEGKLIAQGKP 226
|
....*..
gi 1827346401 1484 AQLLAQK 1490
Cdd:PRK13632 227 KEILNNK 233
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1265-1479 |
1.43e-20 |
|
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: 91.76 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELP--LAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGlhtlrSRI 1342
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1343 SIIPQDPILFP-GSLRMNLDL---LQEHSD----EAIWAALETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLAR 1414
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALgleLQGVPKaearERAEELLELVGLSGFENAYPHQL-----------SGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1415 ALLRKTQILILDEATAAVDPGTELQMQA-MLGSWFAQC-TVLLIAHRLR-SVMDCARVLVMDK--GQVAE 1479
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEeLLDIWRETGkTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
644-826 |
1.61e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.76 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 644 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--VAYVPQEAWVQNT---SVVENVCFGQELD 718
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGarVAYVPQRSEVPDSlplTVRDLVAMGRWAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 719 PPWLER-------VLEACALQPDVDSFPegiHTSIGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHV 791
Cdd:NF040873 86 RGLWRRltrddraAVDDALERVGLADLA---GRQLGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1827346401 792 FnqvigpgGLL-----QGTTRILVTHALHILPQADWIIVL 826
Cdd:NF040873 159 I-------ALLaeehaRGATVVVVTHDLELVRRADPCVLL 191
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1282-1489 |
2.87e-20 |
|
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: 96.74 E-value: 2.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1282 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLD 1361
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1362 LLQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQ 1441
Cdd:COG4618 428 RFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALA 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1827346401 1442 AMLGSWFAQ-CTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQ 1489
Cdd:COG4618 508 AAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1265-1483 |
3.24e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 92.12 E-value: 3.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISI 1344
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1345 IPQDPI-LFPGSLrMNLDL---LQEHS------DEAIWAALETVQLKALVASLPgqlqykcadrgEDLSVGQKQLLCLAR 1414
Cdd:PRK13648 88 VFQNPDnQFVGSI-VKYDVafgLENHAvpydemHRRVSEALKQVDMLERADYEP-----------NALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 1415 ALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCARVLVMDKGQVAESGSP 1483
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhnITIISITHDLSEAMEADHVIVMNKGTVYKEGTP 226
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1281-1486 |
4.20e-20 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 93.26 E-value: 4.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG---LHTLRSRISIIPQDPIlfpGSL- 1356
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDPY---ASLn 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1357 -RMNL-DLLQE----HS-------DEAIWAALETVQLKALVAS-LPGQlqykcadrgedLSVGQKQLLCLARALLRKTQI 1422
Cdd:COG4608 110 pRMTVgDIIAEplriHGlaskaerRERVAELLELVGLRPEHADrYPHE-----------FSGGQRQRIGIARALALNPKL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 1423 LILDEATAAVDPGTELQ-------MQAMLGswfaqCTVLLIAHRL---RSVMDcaRVLVMDKGQVAESGSPAQL 1486
Cdd:COG4608 179 IVCDEPVSALDVSIQAQvlnlledLQDELG-----LTYLFISHDLsvvRHISD--RVAVMYLGKIVEIAPRDEL 245
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1276-1477 |
4.23e-20 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 90.01 E-value: 4.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1276 PELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAhvgLHTLRSRISIIPQDP--ILFP 1353
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGYVMQDVdyQLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1354 GS----LRMNLDLLQEhSDEAIWAALETVQLKALVASLPgqlqykcadrgEDLSVGQKQLLCLARALLRKTQILILDEAT 1429
Cdd:cd03226 87 DSvreeLLLGLKELDA-GNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 1430 AAVDPGtelQMQAmLGSWFAQC-----TVLLIAHRLRSVMDCA-RVLVMDKGQV 1477
Cdd:cd03226 155 SGLDYK---NMER-VGELIRELaaqgkAVIVITHDYEFLAKVCdRVLLLANGAI 204
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1281-1489 |
4.25e-20 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 93.19 E-value: 4.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEA---AEGGIWIDGVPIAHVGLHTLR----SRISIIPQDPIlfp 1353
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRkirgREIQMIFQDPM--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1354 GSL--RMNL-----DLLQEH---SDEAIWA----ALETVQL---KALVASLPGQlqykcadrgedLSVGQKQLLCLARAL 1416
Cdd:COG0444 97 TSLnpVMTVgdqiaEPLRIHgglSKAEAREraieLLERVGLpdpERRLDRYPHE-----------LSGGMRQRVMIARAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1417 LRKTQILILDEATAAVDPGTELQ-------MQAMLGswfaqCTVLLIAHRLRSV--MdCARVLVMDKGQVAESGSPAQLL 1487
Cdd:COG0444 166 ALEPKLLIADEPTTALDVTIQAQilnllkdLQRELG-----LAILFITHDLGVVaeI-ADRVAVMYAGRIVEEGPVEELF 239
|
..
gi 1827346401 1488 AQ 1489
Cdd:COG0444 240 EN 241
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1281-1488 |
6.31e-20 |
|
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: 90.19 E-value: 6.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTlRSR--ISIIPQDPILFPG-SLR 1357
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARagIGYVPEGRRIFPElTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1358 MNLDL-LQEHSDEAIWAALETVqlkalVASLPgQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGT 1436
Cdd:cd03224 94 ENLLLgAYARRRAKRKARLERV-----YELFP-RLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 1437 ELQMQAMLGSWFAQ-CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLA 1488
Cdd:cd03224 168 VEEIFEAIRELRDEgVTILLVEQNARFALEIAdRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
644-840 |
1.31e-19 |
|
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: 89.71 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 644 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-----------AVAYVPQE-AWVQNTSVVENV 711
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatdvpvqerNVGFVFQHyALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 712 CFGQEL-----DPPWLE------RVLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPL 780
Cdd:cd03296 96 AFGLRVkprseRPPEAEirakvhELLKLVQLDWLADRYPA-----------QLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 781 AALDAHVGQH-------VFNQVigpggllqGTTRILVTH----ALHIlpqADWIIVLANGAIAEMGSYQEL 840
Cdd:cd03296 165 GALDAKVRKElrrwlrrLHDEL--------HVTTVFVTHdqeeALEV---ADRVVVMNKGRIEQVGTPDEV 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
648-843 |
1.39e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 89.43 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 648 RINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-----------VAYVPQEawvqNT-----SVVENV 711
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltalppaerpVSMLFQE----NNlfphlTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 712 CFGQE----LDPPWLERVLEACA---LQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 784
Cdd:COG3840 93 GLGLRpglkLTAEQRAQVEQALErvgLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 785 -----------AHVGQHvfnqvigpggllQGTTRILVTH----ALHIlpqADWIIVLANGAIAEMGSYQELLQR 843
Cdd:COG3840 162 palrqemldlvDELCRE------------RGLTVLMVTHdpedAARI---ADRVLLVADGRIAADGPTAALLDG 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1274-1485 |
1.85e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 90.49 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1274 YRPELPL---AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIA--HVGLHTLRSRISIIPQD 1348
Cdd:PRK13637 12 YMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1349 P------------ILFPGSlrmNLDLLQEHSDEAIWAALETVQLKALVaslpgqlqYKcaDRGE-DLSVGQKQLLCLARA 1415
Cdd:PRK13637 92 PeyqlfeetiekdIAFGPI---NLGLSEEEIENRVKRAMNIVGLDYED--------YK--DKSPfELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 1416 LLRKTQILILDEATAAVDPGT--EL--QMQAMLGSWfaQCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQ 1485
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGrdEIlnKIKELHKEY--NMTIILVSHSMEDVAKLAdRIIVMNKGKCELQGTPRE 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
643-833 |
2.59e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 88.19 E-value: 2.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 643 PPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG---------AVAY-------VPQEAW-VQNT 705
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlkrrEIPYlrrrigvVFQDFRlLPDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 706 SVVENVCFGQELD-----------PPWLERV-LEACAlqpdvDSFPegihtsigeqgMNLSGGQKQRLSLARAVYRKAAV 773
Cdd:COG2884 95 TVYENVALPLRVTgksrkeirrrvREVLDLVgLSDKA-----KALP-----------HELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827346401 774 YLLDDPLAALDAHVGQHV------FNQVigpggllqGTTRILVTHALHILPQADW-IIVLANGAIAE 833
Cdd:COG2884 159 LLADEPTGNLDPETSWEImelleeINRR--------GTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
644-842 |
3.45e-19 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 87.87 E-value: 3.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 644 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------------VAYVPQEAWV-QNTSVV 708
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEGRRIfPELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 709 ENV----CFGQELDPPW-LERVLEAcalqpdvdsFPEgIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAAL 783
Cdd:cd03224 94 ENLllgaYARRRAKRKArLERVYEL---------FPR-LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 784 DAHVGQHVFNQVIGpgglL--QGTTRILV----THALHIlpqADWIIVLANGAIAEMGSYQELLQ 842
Cdd:cd03224 164 APKIVEEIFEAIRE----LrdEGVTILLVeqnaRFALEI---ADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1265-1481 |
3.53e-19 |
|
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: 87.57 E-value: 3.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELplAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHtlRSRISI 1344
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1345 IPQDPILFP----------GsLRMNLDLLQEHSDEAIWAaLETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLAR 1414
Cdd:cd03259 77 VFQDYALFPhltvaeniafG-LKLRGVPKAEIRARVREL-LELVGLEGLLNRYPHEL-----------SGGQQQRVALAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1415 ALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESG 1481
Cdd:cd03259 144 ALAREPSLLLLDEPLSALDAKLREELREELKELQRElgITTIYVTHDQEEALALAdRIAVMNEGRIVQVG 213
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1281-1489 |
3.73e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 89.13 E-value: 3.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHvGLHTLRSR-ISIIPQDP---------- 1349
Cdd:COG4167 28 AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY-GDYKYRCKhIRMIFQDPntslnprlni 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1350 --IL-FPgsLRMNLDLLQEHSDEAIWAALETVQLkalvasLPGQLQYKCadrgEDLSVGQKQLLCLARALLRKTQILILD 1426
Cdd:COG4167 107 gqILeEP--LRLNTDLTAEEREERIFATLRLVGL------LPEHANFYP----HMLSSGQKQRVALARALILQPKIIIAD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 1427 EATAAVDPGTELQM-------QAMLGSWFaqctvLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQ 1489
Cdd:COG4167 175 EALAALDMSVRSQIinlmlelQEKLGISY-----IYVSQHLGIVKHISdKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1281-1477 |
3.83e-19 |
|
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: 86.30 E-value: 3.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGlHTLRSRISIIPQDPILFPG-SLRMN 1359
Cdd:cd03230 15 ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGYLPEEPSLYENlTVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1360 LDLlqehsdeaiwaaletvqlkalvaslpgqlqykcadrgedlSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQ 1439
Cdd:cd03230 94 LKL----------------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGLDPESRRE 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1827346401 1440 MQAMLGSWFAQ-CTVLLIAHRLRSVMD-CARVLVMDKGQV 1477
Cdd:cd03230 134 FWELLRELKKEgKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1265-1488 |
3.96e-19 |
|
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: 88.51 E-value: 3.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYrPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISI 1344
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1345 IPQDPILFPG-SLRMNLDL---LQEHSDEAIWA-ALEtvqLKALVASLPGQLqykcADRGED-LSVGQKQLLCLARALLR 1418
Cdd:cd03295 80 VIQQIGLFPHmTVEENIALvpkLLKWPKEKIRErADE---LLALVGLDPAEF----ADRYPHeLSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1419 KTQILILDEATAAVDPGT--ELQ-----MQAMLGSwfaqcTVLLIAHRlrsvMDCA-----RVLVMDKGQVAESGSPAQL 1486
Cdd:cd03295 153 DPPLLLMDEPFGALDPITrdQLQeefkrLQQELGK-----TIVFVTHD----IDEAfrladRIAIMKNGEIVQVGTPDEI 223
|
..
gi 1827346401 1487 LA 1488
Cdd:cd03295 224 LR 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1264-1473 |
8.18e-19 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 86.38 E-value: 8.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1264 QIEFRDFGLRYRPELPLAvqGVSFKIHAGEKVGIVGRTGAGKSSLasglLR----LQEAAEGGIWIDGVPIAHVGLHtLR 1339
Cdd:COG4133 2 MLEAENLSCRRGERLLFS--GLSFTLAAGEALALTGPNGSGKTTL----LRilagLLPPSAGEVLWNGEPIRDARED-YR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1340 SRISIIPQDPILFPG-SLRMNLDLLQ-----EHSDEAIWAALETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLA 1413
Cdd:COG4133 75 RRLAYLGHADGLKPElTVRENLRFWAalyglRADREAIDEALEAVGLAGLADLPVRQL-----------SAGQKRRVALA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 1414 RALLRKTQILILDEATAAVDPgtelQMQAMLGSWFAQ-----CTVLLIAHRLRSVmDCARVLVMD 1473
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDA----AGVALLAELIAAhlargGAVLLTTHQPLEL-AAARVLDLG 203
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
641-859 |
9.36e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 93.12 E-value: 9.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 641 ESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSAL--LGELSKVE-----------GFVSIEGAVAYVPQEAWVQNTSV 707
Cdd:PLN03232 1247 GLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALfrIVELEKGRimiddcdvakfGLTDLRRVLSIIPQSPVLFSGTV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 708 VENVCFGQELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHV 787
Cdd:PLN03232 1327 RFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT 1406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 788 GqhvfnqvigpgGLLQGTTR--------ILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGALMCLLDQARQPGD 859
Cdd:PLN03232 1407 D-----------SLIQRTIReefksctmLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPAN 1475
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
646-843 |
1.01e-18 |
|
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: 91.50 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG----------------AVAYVPQEAWVQ---NTS 706
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkdltklsrrslrelrrRVQMVFQDPYSSlnpRMT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 707 VVENVCFG----QELDPPWLER----VLEACALQPDV-DSFPegiHTsigeqgmnLSGGQKQRLSLARAVYRKAAVYLLD 777
Cdd:COG1123 361 VGDIIAEPlrlhGLLSRAERRErvaeLLERVGLPPDLaDRYP---HE--------LSGGQRQRVAIARALALEPKLLILD 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 778 DPLAALDAHVGQHVFNqvigpggLLQ------GTTRILVTH----ALHIlpqADWIIVLANGAIAEMGSYQELLQR 843
Cdd:COG1123 430 EPTSALDVSVQAQILN-------LLRdlqrelGLTYLFISHdlavVRYI---ADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
646-839 |
1.14e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 90.01 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYVPQEAWVQNT-----------SVVENVCF 713
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdITHVPAENRHVNTvfqsyalfphmTVFENVAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 714 G--------QELDPpwleRVLEACA---LQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLAA 782
Cdd:PRK09452 110 GlrmqktpaAEITP----RVMEALRmvqLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 783 LDAHVGQHVFNQVIGpgglLQ---GTTRILVTH----ALHIlpqADWIIVLANGAIAEMGSYQE 839
Cdd:PRK09452 175 LDYKLRKQMQNELKA----LQrklGITFVFVTHdqeeALTM---SDRIVVMRDGRIEQDGTPRE 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1281-1488 |
1.33e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 91.31 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQeAAEGGIWIDGVPIAHVG---LHTLRSRISIIPQDPilfPGSLR 1357
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP---NSSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1358 MNLDLLQ---------------EHSDEAIWAALETVQLKAlvaslpgqlqykcADRGE---DLSVGQKQLLCLARALLRK 1419
Cdd:PRK15134 377 PRLNVLQiieeglrvhqptlsaAQREQQVIAVMEEVGLDP-------------ETRHRypaEFSGGQRQRIAIARALILK 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 1420 TQILILDEATAAVDPGTELQMQAMLGSWFA--QCTVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQLLA 1488
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQILALLKSLQQkhQLAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
646-842 |
1.43e-18 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 86.57 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYVPQEAWV----------QN----TS--VV 708
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQdITGLSEKELYelrrrigmlfQGgalfDSltVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 709 ENVCFG----QELDPPWLER----VLEACALQPDVDSFPegihtsiGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPL 780
Cdd:COG1127 101 ENVAFPlrehTDLSEAEIRElvleKLELVGLPGAADKMP-------SE----LSGGMRKRVALARALALDPEILLYDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827346401 781 AALDAhVGQHVFNQVIgpgglLQ-----GTTRILVTHALH-ILPQADWIIVLANGAIAEMGSYQELLQ 842
Cdd:COG1127 170 AGLDP-ITSAVIDELI-----RElrdelGLTSVVVTHDLDsAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
646-829 |
3.18e-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: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGavayvpqeawvqntsvvENVCFGQELDPPWLERV 725
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDG-----------------EDLTDLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 726 leACALQpDVDSFPegiHTSIGEQ-GMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVfnqvigpGGLLQ- 803
Cdd:cd03229 79 --GMVFQ-DFALFP---HLTVLENiALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREV-------RALLKs 145
|
170 180 190
....*....|....*....|....*....|..
gi 1827346401 804 -----GTTRILVTHALH-ILPQADWIIVLANG 829
Cdd:cd03229 146 lqaqlGITVVLVTHDLDeAARLADRVVVLRDG 177
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
646-842 |
4.09e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 85.94 E-value: 4.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGavayVPQEAW----------V--QNTSV-----V 708
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNG----RPLAAWspwelarrraVlpQHSSLafpftV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 709 ENV--------CFGQELDPPWLERVLEACALQPDVD-SFPEgihtsigeqgmnLSGGQKQRLSLARA-------VYRKAA 772
Cdd:COG4559 93 EEVvalgraphGSSAAQDRQIVREALALVGLAHLAGrSYQT------------LSGGEQQRVQLARVlaqlwepVDGGPR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827346401 773 VYLLDDPLAALD-AHVgQHVFNqvigpggLL-----QGTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELLQ 842
Cdd:COG4559 161 WLFLDEPTSALDlAHQ-HAVLR-------LArqlarRGGGVVAVLHDLNLAAQyADRILLLHQGRLVAQGTPEEVLT 229
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
1015-1236 |
4.48e-18 |
|
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: 87.16 E-value: 4.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1015 RASRLLFQRLLWDVVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPL 1094
Cdd:cd18600 100 TVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVVSILQPYIFLATVPV 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1095 FLLYAGFQSLYVVSSCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAAN 1174
Cdd:cd18600 180 IIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMR 259
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 1175 VELLGNGLVFAAATCAVLSKAHlSAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERM 1236
Cdd:cd18600 260 IEMIFVIFFTAVTFISIGTTGD-GEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRI 320
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
644-813 |
4.63e-18 |
|
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: 84.38 E-value: 4.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 644 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG---------AVAYVPQEAWV--------QNTS 706
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgrAIPYLRRKIGVvfqdfrllPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 707 VVENVCFGQEL--DPP--WLERV---LEACALQPDVDSFPEGihtsigeqgmnLSGGQKQRLSLARAVYRKAAVYLLDDP 779
Cdd:cd03292 95 VYENVAFALEVtgVPPreIRKRVpaaLELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 1827346401 780 LAALDAHVGQHVFNqvigpggLLQ-----GTTRILVTHA 813
Cdd:cd03292 164 TGNLDPDTTWEIMN-------LLKkinkaGTTVVVATHA 195
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1286-1489 |
4.88e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 84.81 E-value: 4.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1286 SFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTlrsR-ISIIPQDPILFPG-SLRMNLDL- 1362
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE---RpVSMLFQENNLFPHlTVAQNIGLg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1363 ------LQEHSDEAIWAALETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLARALLRKTQILILDEATAAVDPGT 1436
Cdd:COG3840 96 lrpglkLTAEQRAQVEQALERVGLAGLLDRLPGQL-----------SGGQRQRVALARCLVRKRPILLLDEPFSALDPAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 1437 ELQMQAMLGSWFA--QCTVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQLLAQ 1489
Cdd:COG3840 165 RQEMLDLVDELCRerGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
646-833 |
6.88e-18 |
|
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: 84.41 E-value: 6.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-----------------VAYVPQ-EAWVQNTSV 707
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQdlfaldedararlrarhVGFVFQsFQLLPTLTA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 708 VENV-----------CFGQELDppWLERVleacALQPDVDSFPEGihtsigeqgmnLSGGQKQRLSLARAVYRKAAVYLL 776
Cdd:COG4181 108 LENVmlplelagrrdARARARA--LLERV----GLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 777 DDPLAALDAHVGQHVFnqvigpgGLL------QGTTRILVTHALHILPQADWIIVLANGAIAE 833
Cdd:COG4181 171 DEPTGNLDAATGEQII-------DLLfelnreRGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1265-1489 |
7.38e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 85.55 E-value: 7.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELP-LAVQGVSFKIHAGEKVGIVGRTGAGKSS---LASGLLrlqEAAEGGIWIDGVPIAHVGLHTLRS 1340
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLL---EAESGQIIIDGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1341 RISIIPQDPI-LFPGSL------------RMNLDLLQEHSDEaiwaALETVQLKALVASLPGQlqykcadrgedLSVGQK 1407
Cdd:PRK13650 82 KIGMVFQNPDnQFVGATveddvafglenkGIPHEEMKERVNE----ALELVGMQDFKEREPAR-----------LSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1408 QLLCLARALLRKTQILILDEATAAVDPGTELQM----QAMLGSWfaQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSP 1483
Cdd:PRK13650 147 QRVAIAGAVAMRPKIIILDEATSMLDPEGRLELiktiKGIRDDY--QMTVISITHDLDEVALSDRVLVMKNGQVESTSTP 224
|
....*.
gi 1827346401 1484 AQLLAQ 1489
Cdd:PRK13650 225 RELFSR 230
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1281-1488 |
9.18e-18 |
|
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: 84.03 E-value: 9.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSL---ASGLLRlqeAAEGGIWIDGVPIAHVGLHtLRSRISIIP--QDPILFPG- 1354
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLfnlISGFLR---PTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFPEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1355 SLRMNLDL-LQEHSDEAIWAA----------------LETVQLKALVASLPGqlqykcadrgeDLSVGQKQLLCLARALL 1417
Cdd:cd03219 91 TVLENVMVaAQARTGSGLLLArarreereareraeelLERVGLADLADRPAG-----------ELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 1418 RKTQILILDEATAAVDPGTELQMQAMLGSWFAQ-CTVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQLLA 1488
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERgITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1265-1486 |
1.13e-17 |
|
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: 83.71 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIaHVGLHTLRSRISI 1344
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1345 IPQDPILFPGslrMN-LDLLQehsdeaIWAAL---ETVQLKALVASLPGQLQ-YKCADR-GEDLSVGQKQLLCLARALLR 1418
Cdd:cd03263 80 CPQFDALFDE---LTvREHLR------FYARLkglPKSEIKEEVELLLRVLGlTDKANKrARTLSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 1419 KTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRlrsvMD-----CARVLVMDKGQVAESGSPAQL 1486
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHS----MDeaealCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
633-835 |
1.54e-17 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 83.32 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 633 SATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG----------------AVAYV 696
Cdd:cd03257 8 SVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirrkEIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 697 PQEAwvqNTS----------VVENVCFGQELDPPWLERV---LEACALQPD---VDSFPegiHTsigeqgmnLSGGQKQR 760
Cdd:cd03257 88 FQDP---MSSlnprmtigeqIAEPLRIHGKLSKKEARKEavlLLLVGVGLPeevLNRYP---HE--------LSGGQRQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 761 LSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNqvigpggLLQ------GTTRILVTHALHILPQ-ADWIIVLANGAIAE 833
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILD-------LLKklqeelGLTLLFITHDLGVVAKiADRVAVMYAGKIVE 226
|
..
gi 1827346401 834 MG 835
Cdd:cd03257 227 EG 228
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1265-1482 |
1.57e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 86.01 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYR---PELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHV---GLHTL 1338
Cdd:PRK11153 2 IELKNISKVFPqggRTIH-ALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1339 RSRISIIPQ-----------DPILFPgsLRmnldlLQEHSDEAIWAA----LETVQLKALVASLPGQLqykcadrgedlS 1403
Cdd:PRK11153 81 RRQIGMIFQhfnllssrtvfDNVALP--LE-----LAGTPKAEIKARvtelLELVGLSDKADRYPAQL-----------S 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1404 VGQKQLLCLARALLRKTQILILDEATAAVDPGT-----EL--QMQAMLGswfaqCTVLLIAHRlrsvMD-----CARVLV 1471
Cdd:PRK11153 143 GGQKQRVAIARALASNPKVLLCDEATSALDPATtrsilELlkDINRELG-----LTIVLITHE----MDvvkriCDRVAV 213
|
250
....*....|.
gi 1827346401 1472 MDKGQVAESGS 1482
Cdd:PRK11153 214 IDAGRLVEQGT 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1263-1493 |
1.57e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 89.32 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1263 GQIEFRDFGLRY--RPELPLaVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLR-------------------------- 1314
Cdd:PTZ00265 1164 GKIEIMDVNFRYisRPNVPI-YKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfknehtndmtneqdy 1242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1315 ---------LQEAAE-------------------GGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLDLLQEH 1366
Cdd:PTZ00265 1243 qgdeeqnvgMKNVNEfsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKED 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1367 SD-EAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLG 1445
Cdd:PTZ00265 1323 ATrEDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1402
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 1446 SW--FAQCTVLLIAHRLRSVMDCARVLVMDKGQ-----VAESGSPAQLL-AQKGLF 1493
Cdd:PTZ00265 1403 DIkdKADKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLsVQDGVY 1458
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
629-836 |
1.68e-17 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 82.85 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYVPQEAWVQNTSV 707
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 708 VENvcfgqelDPpwlerVLEACALQPDVDSFPE----GIHT--SIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLA 781
Cdd:cd03369 87 IPQ-------DP-----TLFSGTIRSNLDPFDEysdeEIYGalRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 782 ALDAHVgQHVFNQVIGPggLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGS 836
Cdd:cd03369 155 SIDYAT-DALIQKTIRE--EFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1260-1479 |
1.88e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 83.99 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1260 PQGGQIEFRDFGLRYRPEL--PLAVQGVSFKIHAGEKVGIVGRTGAGKSSL---ASGLLRlqeAAEGGIWIDGVPIAHVG 1334
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGggVTALDDVSLTVAAGEFVALVGPSGCGKSTLlrlIAGLEK---PTSGEVLVDGKPVTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1335 lhtlrSRISIIPQDPILFP----------GsLRMNlDLLQEHSDEAIWAALETVQLKALVASLPGQLqykcadrgedlSV 1404
Cdd:COG1116 80 -----PDRGVVFQEPALLPwltvldnvalG-LELR-GVPKAERRERARELLELVGLAGFEDAYPHQL-----------SG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1405 GQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHrlrSVM------DcaRVLVMDK-- 1474
Cdd:COG1116 142 GMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQEtgKTVLFVTH---DVDeavflaD--RVVVLSArp 216
|
....*
gi 1827346401 1475 GQVAE 1479
Cdd:COG1116 217 GRIVE 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1265-1485 |
2.07e-17 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 82.79 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHV---GLHTLRSR 1341
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1342 ISIIPQDPILFPG-SLRMNLDL---LQEHSDEAIW----AALETVQLKALVASLPGQlqykcadrgedLSVGQKQLLCLA 1413
Cdd:COG2884 81 IGVVFQDFRLLPDrTVYENVALplrVTGKSRKEIRrrvrEVLDLVGLSDKAKALPHE-----------LSGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 1414 RALLRKTQILILDEATAAVDPGTELQ-MQAM-----LGswfaqCTVLLIAHRLRSVMDC-ARVLVMDKGQVAESGSPAQ 1485
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEiMELLeeinrRG-----TTVLIATHDLELVDRMpKRVLELEDGRLVRDEARGV 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1265-1486 |
2.44e-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: 83.00 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYrPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG---LHTLRSR 1341
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1342 ISIIPQDPILFP----------GSL-RMN-----LDLLQEHSDEAIWAALETVQLKALVaslpgqlqYKCADRgedLSVG 1405
Cdd:cd03256 80 IGMIFQQFNLIErlsvlenvlsGRLgRRStwrslFGLFPKEEKQRALAALERVGLLDKA--------YQRADQ---LSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1406 QKQLLCLARALLRKTQILILDEATAAVDPGTELQ-MQAMLGswFAQ---CTVLLIAHRLRSVMD-CARVLVMDKGQVAES 1480
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQvMDLLKR--INReegITVIVSLHQVDLAREyADRIVGLKDGRIVFD 226
|
....*.
gi 1827346401 1481 GSPAQL 1486
Cdd:cd03256 227 GPPAEL 232
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1281-1477 |
2.89e-17 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 82.19 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPI--AHVGLHTLRSRISIIPQDPILFPgslrm 1358
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFP----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1359 NLDLLQ-----------EHSDEAIWAA---LETVQLKALVASLPGQlqykcadrgedLSVGQKQLLCLARALLRKTQILI 1424
Cdd:cd03262 90 HLTVLEnitlapikvkgMSKAEAEERAlelLEKVGLADKADAYPAQ-----------LSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 1425 LDEATAAVDP---GTELQ-MQAMlgswfAQ--CTVLLIAHRL---RSVMDcaRVLVMDKGQV 1477
Cdd:cd03262 159 FDEPTSALDPelvGEVLDvMKDL-----AEegMTMVVVTHEMgfaREVAD--RVIFMDDGRI 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1281-1481 |
3.23e-17 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 81.86 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGeKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGlHTLRSRISIIPQDPILFPG-SLRMN 1359
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGYLPQEFGVYPNfTVREF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1360 LDLL-------QEHSDEAIWAALETVQLkalvaslpgqlqykcADRGED----LSVGQKQLLCLARALLRKTQILILDEA 1428
Cdd:cd03264 93 LDYIawlkgipSKEVKARVDEVLELVNL---------------GDRAKKkigsLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 1429 TAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMD-CARVLVMDKGQVAESG 1481
Cdd:cd03264 158 TAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1281-1478 |
3.84e-17 |
|
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: 80.17 E-value: 3.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG-LHTLRSRISIIPQdpilfpgslrmn 1359
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1360 ldllqehsdeaiwaaletvqlkalvaslpgqlqykcadrgedLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQ 1439
Cdd:cd03216 83 ------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1827346401 1440 MQAMLGSWFAQ-CTVLLIAHRLRSVMD-CARVLVMDKGQVA 1478
Cdd:cd03216 121 LFKVIRRLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
646-840 |
6.06e-17 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 81.90 E-value: 6.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYVPQEAWVQNT-----------SVVENVCF 713
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKdITNLPPHKRPVNTvfqnyalfphlTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 714 G--------QELDppwlERVLEACALQpDVDSFPegiHTSIGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDA 785
Cdd:cd03300 96 GlrlkklpkAEIK----ERVAEALDLV-QLEGYA---NRKPSQ----LSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 786 HVGQHvfnqvigpgglLQ----------GTTRILVTH----ALHIlpqADWIIVLANGAIAEMGSYQEL 840
Cdd:cd03300 164 KLRKD-----------MQlelkrlqkelGITFVFVTHdqeeALTM---SDRIAVMNKGKIQQIGTPEEI 218
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
646-835 |
6.35e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 81.98 E-value: 6.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSAL-LGELSKvEGFVSIEGA-------------------VAYVPQE--AWVQ 703
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPR-SGTLNIAGNhfdfsktpsdkairelrrnVGMVFQQynLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 704 NTsVVENV----CFGQELDPPWL----ERVLEACALQPDVDSFPegihtsigeqgMNLSGGQKQRLSLARAVYRKAAVYL 775
Cdd:PRK11124 97 LT-VQQNLieapCRVLGLSKDQAlaraEKLLERLRLKPYADRFP-----------LHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 776 LDDPLAALDAHVGqhvfNQVIGPGGLLQGT--TRILVTHALHILPQ-ADWIIVLANGAIAEMG 835
Cdd:PRK11124 165 FDEPTAALDPEIT----AQIVSIIRELAETgiTQVIVTHEVEVARKtASRVVYMENGHIVEQG 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1265-1477 |
6.89e-17 |
|
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: 81.30 E-value: 6.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYrPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHV---GLHTLRSR 1341
Cdd:cd03292 1 IEFINVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1342 ISIIPQDPILFPG-----SLRMNLDLLQEHSDEA---IWAALETVQLKALVASLPGQlqykcadrgedLSVGQKQLLCLA 1413
Cdd:cd03292 80 IGVVFQDFRLLPDrnvyeNVAFALEVTGVPPREIrkrVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 1414 RALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCA--RVLVMDKGQV 1477
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTrhRVIALERGKL 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1281-1477 |
7.03e-17 |
|
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: 80.79 E-value: 7.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGlhtlRSRISIIPQDPILFP------- 1353
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYPkmkvidq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1354 ----GSLR-MNLDLLQEHSDEaiWaaLETVQLkalvaslpGQLQYKcadRGEDLSVGQKQLLCLARALLRKTQILILDEA 1428
Cdd:cd03269 91 lvylAQLKgLKKEEARRRIDE--W--LERLEL--------SEYANK---RVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 1429 TAAVDP-GTELQMQAMLGSWFAQCTVLLIAHRLRSVMD-CARVLVMDKGQV 1477
Cdd:cd03269 156 FSGLDPvNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1280-1489 |
7.12e-17 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 82.31 E-value: 7.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1280 LAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG---LHTLRS-RISIIPQDPILFPG- 1354
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRkKISMVFQSFALLPHr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1355 SLRMN----LDL----LQEHSDEAIwAALETVQLKALVASLPGQlqykcadrgedLSVGQKQLLCLARALLRKTQILILD 1426
Cdd:cd03294 118 TVLENvafgLEVqgvpRAEREERAA-EALELVGLEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 1427 EATAAVDPGTELQMQAMLGSWFA--QCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQ 1489
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRLQAelQKTIVFITHDLDEALRLGdRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
646-840 |
7.61e-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: 7.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA----------------VAYVPQE-AWVQNTSVV 708
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrrqIGMIFQQfNLIERLSVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 709 ENVCFGQeLD--PPW--------LERVLEACALQPDVdsfpeGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDD 778
Cdd:cd03256 97 ENVLSGR-LGrrSTWrslfglfpKEEKQRALAALERV-----GLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 779 PLAALDAHVGQHVfnqvigpGGLL------QGTTRILVTHALHI-LPQADWIIVLANGAIAEMGSYQEL 840
Cdd:cd03256 171 PVASLDPASSRQV-------MDLLkrinreEGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
639-828 |
7.78e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 80.99 E-value: 7.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 639 SQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELS---KVEGFVSIEG-----------AVAYVPQEAWV-Q 703
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGrrltalpaeqrRIGILFQDDLLfP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 704 NTSVVENVCFGQELDPPWLER------VLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLD 777
Cdd:COG4136 90 HLSVGENLAFALPPTIGRAQRrarveqALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRALLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 778 DPLAALDAH----VGQHVFNQVIgpgglLQGTTRILVTHALHILPQADWIIVLAN 828
Cdd:COG4136 159 EPFSKLDAAlraqFREFVFEQIR-----QRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1281-1488 |
8.26e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 82.14 E-value: 8.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIaHVGLHTLRS-RISIIPQDP---------- 1349
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSYRSqRIRMIFQDPstslnprqri 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1350 --IL-FPgsLRMNLDLLQEHSDEAIWAALETVQLkalvasLPGQLQYkcadRGEDLSVGQKQLLCLARALLRKTQILILD 1426
Cdd:PRK15112 107 sqILdFP--LRLNTDLEPEQREKQIIETLRQVGL------LPDHASY----YPHMLAPGQKQRLGLARALILRPKVIIAD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 1427 EATAAVDPGTE-------LQMQAMLGSWFAQCTVLLiaHRLRSVMDcaRVLVMDKGQVAESGSPAQLLA 1488
Cdd:PRK15112 175 EALASLDMSMRsqlinlmLELQEKQGISYIYVTQHL--GMMKHISD--QVLVMHQGEVVERGSTADVLA 239
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
646-843 |
8.46e-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: 81.23 E-value: 8.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-----------VAYVPQE-AWVQNTSVVENVCF 713
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 714 G---QELDPPWLER-VLEACALQpdvdsfpeGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQ 789
Cdd:cd03299 95 GlkkRKVDKKEIERkVLEIAEML--------GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 790 HVFNQVIGPGGLLqGTTRILVTHAL-HILPQADWIIVLANGAIAEMGSYQELLQR 843
Cdd:cd03299 167 KLREELKKIRKEF-GVTVLHVTHDFeEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
644-841 |
1.07e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.12 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 644 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAYVPQEAWVQ-NTSVVE 709
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASVPQDTSLSfEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 710 NVCFGQ-----ELDP--PWLERVLEACALQPDVDSFPEGIHTSigeqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAA 782
Cdd:PRK09536 97 VVEMGRtphrsRFDTwtETDRAAVERAMERTGVAQFADRPVTS-------LSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 783 LDAHVGQHVFNQVigpgGLLQGTTRILVThALHILPQA----DWIIVLANGAIAEMGSYQELL 841
Cdd:PRK09536 170 LDINHQVRTLELV----RRLVDDGKTAVA-AIHDLDLAarycDELVLLADGRVRAAGPPADVL 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
646-784 |
1.39e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 81.24 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSAL--LGEL---SKVEGFVSIEGA---------------VAYVPQEAwvqN- 704
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLipgARVEGEILLDGEdiydpdvdvvelrrrVGMVFQKP---Np 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 705 --TSVVENVCFG---------QELDppwlERV---LEACALQPDV-DSfpegIHTSigeqGMNLSGGQKQRLSLARAVYR 769
Cdd:COG1117 104 fpKSIYDNVAYGlrlhgikskSELD----EIVeesLRKAALWDEVkDR----LKKS----ALGLSGGQQQRLCIARALAV 171
|
170
....*....|....*
gi 1827346401 770 KAAVYLLDDPLAALD 784
Cdd:COG1117 172 EPEVLLMDEPTSALD 186
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1282-1479 |
1.39e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 81.66 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1282 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHV---GLHTLRSRISIIPQDPI-------- 1350
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSIsavnprkt 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1351 ---LFPGSLRMNLDLLQEHSDEAIWAALETVQLKALVAS-LPGQlqykcadrgedLSVGQKQLLCLARALLRKTQILILD 1426
Cdd:PRK10419 108 vreIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDkRPPQ-----------LSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 1427 EATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMD-CARVLVMDKGQVAE 1479
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQQfgTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
649-814 |
1.61e-16 |
|
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: 80.03 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGcLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-----------------AVAYVPQE-AWVQNTSVVEN 710
Cdd:cd03297 17 IDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrkkinlppqqrKIGLVFQQyALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 711 VCFGQELDPPWLER-----VLEACALQPDVDSFPEGihtsigeqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDA 785
Cdd:cd03297 96 LAFGLKRKRNREDRisvdeLLDLLGLDHLLNRYPAQ-----------LSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180
....*....|....*....|....*....
gi 1827346401 786 HVGQHVFNQVIGPGGLLQGTTrILVTHAL 814
Cdd:cd03297 165 ALRLQLLPELKQIKKNLNIPV-IFVTHDL 192
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1265-1490 |
1.62e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 81.82 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYrPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHV--GLHTLRSRI 1342
Cdd:PRK13636 6 LKVEELNYNY-SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSrkGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1343 SIIPQDP--ILFPGSLR-------MNLDLLQEHSDEAIWAALEtvqlKALVASLPGQLQYKcadrgedLSVGQKQLLCLA 1413
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYqdvsfgaVNLKLPEDEVRKRVDNALK----RTGIEHLKDKPTHC-------LSFGQKKRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1414 RALLRKTQILILDEATAAVDP-GTE------LQMQAMLGswfaqCTVLLIAHRLRSV-MDCARVLVMDKGQVAESGSPAQ 1485
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPmGVSeimkllVEMQKELG-----LTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKE 228
|
....*
gi 1827346401 1486 LLAQK 1490
Cdd:PRK13636 229 VFAEK 233
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1265-1477 |
1.69e-16 |
|
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: 80.23 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELP--LAVQGVSFKIHAGEKVGIVGRTGAGKSSL---ASGLLRLQeaaEGGIWIDGVPIAHVGLHTL- 1338
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLlniLGGLDRPT---SGEVRVDGTDISKLSEKELa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1339 ---RSRISIIPQDPILFPG-SLRMNLDLLQEHS-------DEAIWAALETVQLKALVASLPGQlqykcadrgedLSVGQK 1407
Cdd:cd03255 78 afrRRHIGFVFQSFNLLPDlTALENVELPLLLAgvpkkerRERAEELLERVGLGDRLNHYPSE-----------LSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 1408 QLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSwFAQ---CTVLLIAHRLRSVMDCARVLVMDKGQV 1477
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRE-LNKeagTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
646-842 |
2.07e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 80.97 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAvayvPQEAW----------V--QNTSV-----V 708
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGR----PLADWspaelarrraVlpQHSSLsfpftV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 709 ENV--------CFGQELDPPWLERVLEACALQPDVD-SFPEgihtsigeqgmnLSGGQKQRLSLARA------VYRKAAV 773
Cdd:PRK13548 94 EEVvamgraphGLSRAEDDALVAAALAQVDLAHLAGrDYPQ------------LSGGEQQRVQLARVlaqlwePDGPPRW 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 774 YLLDDPLAALDAHVGQHVFNqvigpggLL------QGTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELLQ 842
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLR-------LArqlaheRGLAVIVVLHDLNLAARyADRIVLLHQGRLVADGTPAEVLT 230
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1289-1481 |
3.32e-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: 79.07 E-value: 3.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1289 IHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHvgLHTLRSRISIIPQDPILFPG-SLRMNLDL----- 1362
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA--APPADRPVSMLFQENNLFAHlTVEQNVGLglspg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1363 --LQEHSDEAIWAALETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQM 1440
Cdd:cd03298 99 lkLTAEDRQAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1827346401 1441 QAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESG 1481
Cdd:cd03298 168 LDLVLDLHAEtkMTVLMVTHQPEDAKRLAqRVVFLDNGRIAAQG 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
633-841 |
4.93e-16 |
|
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: 79.16 E-value: 4.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 633 SATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA----------------VAYV 696
Cdd:cd03258 8 SKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltllsgkelrkarrrIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 697 PQE-AWVQNTSVVENVCFGQELD-------PPWLERVLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVY 768
Cdd:cd03258 88 FQHfNLLSSRTVFENVALPLEIAgvpkaeiEERVLELLELVGLEDKADAYPA-----------QLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 769 RKAAVYLLDDPLAALDAHVGQHVFNqvigpggLLQ------GTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELL 841
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILA-------LLRdinrelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
648-835 |
4.96e-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: 4.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 648 RINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-----------VAYVPQEAWV-QNTSVVENVCFGQ 715
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdvtaappadrpVSMLFQENNLfAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 716 EldpPWLErvleacaLQPDVDSFPEGIHTSIGEQGM------NLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQ 789
Cdd:cd03298 96 S---PGLK-------LTAEDRQAIEVALARVGLAGLekrlpgELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1827346401 790 HVFNQVIGPGGlLQGTTRILVTH----ALHIlpqADWIIVLANGAIAEMG 835
Cdd:cd03298 166 EMLDLVLDLHA-ETKMTVLMVTHqpedAKRL---AQRVVFLDNGRIAAQG 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
646-841 |
5.50e-16 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 78.87 E-value: 5.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------------VAYVPQEAWV-QNTSVVEN 710
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarlgIGYVPEGRRIfPSLTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 711 -----VCFGQELDPPW-LERVLEAcalqpdvdsFPEgIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 784
Cdd:COG0410 99 lllgaYARRDRAEVRAdLERVYEL---------FPR-LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 785 AHVGQHVFNQVigpgGLL--QGTTRILV----THALHIlpqADWIIVLANGAIAEMGSYQELL 841
Cdd:COG0410 169 PLIVEEIFEII----RRLnrEGVTILLVeqnaRFALEI---ADRAYVLERGRIVLEGTAAELL 224
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
629-851 |
6.25e-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: 79.57 E-value: 6.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYVPQEAWVQNTSV 707
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIdISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 708 V--ENVCFGQ----ELDPPW------LERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYL 775
Cdd:cd03288 100 IlqDPILFSGsirfNLDPECkctddrLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 776 LDDPLAALDAHVgQHVFNQVIGPGglLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGALMCLL 851
Cdd:cd03288 180 MDEATASIDMAT-ENILQKVVMTA--FADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASL 252
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
633-785 |
6.50e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 79.52 E-value: 6.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 633 SATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAV--------AYVPQE----A 700
Cdd:COG4525 10 SVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVFQKdallP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 701 WVqntSVVENVCFGQELDP-PWLERVLEACALQPDVdsfpeGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDP 779
Cdd:COG4525 90 WL---NVLDNVAFGLRLRGvPKAERRARAEELLALV-----GLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEP 161
|
....*.
gi 1827346401 780 LAALDA 785
Cdd:COG4525 162 FGALDA 167
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1265-1490 |
8.69e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 79.49 E-value: 8.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELPLAVQG---VSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPI----AHVGLHT 1337
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGldnISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1338 LRSRISIIPQDP--ILFPGSLRMNLDL----LQEHSDEAIWAALETVQLKALVASLPGQLQYkcadrgeDLSVGQKQLLC 1411
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTVLKDVEFgpknFGFSEDEAKEKALKWLKKVGLSEDLISKSPF-------ELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1412 LARALLRKTQILILDEATAAVDPGTELQM-QAMLGSWFAQCTVLLIAHRLRSVMDCAR-VLVMDKGQVAESGSPAQLLAQ 1489
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMmQLFKDYQKAGHTVILVTHNMDDVAEYADdVLVLEHGKLIKHASPKEIFSD 235
|
.
gi 1827346401 1490 K 1490
Cdd:PRK13641 236 K 236
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
649-831 |
1.32e-15 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 77.30 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG----------AVAYVPQEAWVQ--NTSVVENVCFGQE 716
Cdd:cd03226 19 LSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQDVDYQlfTDSVREELLLGLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 717 L---DPPWLERVLEACALQPDVDSFPegihtsigeqgMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHV-- 791
Cdd:cd03226 99 EldaGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVge 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1827346401 792 -FNQVIGpggllQGTTRILVTHALHILPQ-ADWIIVLANGAI 831
Cdd:cd03226 168 lIRELAA-----QGKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
629-860 |
1.37e-15 |
|
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: 83.04 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLgELSKVEGFVSIEG-------------AVAY 695
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGvswnsvtlqtwrkAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 696 VPQEAWVQNTSvvenvcFGQELDP--PW----LERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYR 769
Cdd:TIGR01271 1297 IPQKVFIFSGT------FRKNLDPyeQWsdeeIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILS 1370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 770 KAAVYLLDDPLAALDAhVGQHVFNQVIGPGglLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGalmc 849
Cdd:TIGR01271 1371 KAKILLLDEPSAHLDP-VTLQIIRKTLKQS--FSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETS---- 1443
|
250
....*....|.
gi 1827346401 850 LLDQARQPGDR 860
Cdd:TIGR01271 1444 LFKQAMSAADR 1454
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
646-832 |
1.63e-15 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 75.54 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVayvpqeawVQNTSVVEnvcfgqeldppwlerv 725
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE--------VSFASPRD---------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 726 leacALQpdvdsfpEGIhtsigeqGM--NLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVigpgGLL- 802
Cdd:cd03216 72 ----ARR-------AGI-------AMvyQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVI----RRLr 129
|
170 180 190
....*....|....*....|....*....|..
gi 1827346401 803 -QGTTRILVTHAL-HILPQADWIIVLANGAIA 832
Cdd:cd03216 130 aQGVAVIFISHRLdEVFEIADRVTVLRDGRVV 161
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
629-860 |
1.85e-15 |
|
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: 78.36 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLgELSKVEGFVSIEGaVAY--VPQEAWVQNTS 706
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDG-VSWnsVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 707 VVENVCF------GQELDP--PW----LERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVY 774
Cdd:cd03289 81 VIPQKVFifsgtfRKNLDPygKWsdeeIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 775 LLDDPLAALDAhVGQHVFNQVIGPGglLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGalmcLLDQA 854
Cdd:cd03289 161 LLDEPSAHLDP-ITYQVIRKTLKQA--FADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKS----HFKQA 233
|
....*.
gi 1827346401 855 RQPGDR 860
Cdd:cd03289 234 ISPSDR 239
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
646-835 |
1.90e-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: 76.44 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELS--KVEGFVSIEG----------AVAYVPQEAWVQNT-SVVENVC 712
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGrpldkrsfrkIIGYVPQDDILHPTlTVRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 713 FGQELdppwlervleacalqpdvdsfpegihtsigeQGmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVF 792
Cdd:cd03213 105 FAAKL-------------------------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1827346401 793 nqvigpgGLL-----QGTTRILVTHAL--HILPQADWIIVLANGAIAEMG 835
Cdd:cd03213 152 -------SLLrrladTGRTIICSIHQPssEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
649-842 |
2.03e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 77.96 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLSAL-----LGELSKVEGFVSIEGAVAYVPQEAWVQ----------------NTSV 707
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIEvrrevgmvfqypnpfpHLTI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 708 VENVCFG----------QELDppwlERV---LEACALQPDVDSfpegihtSIGEQGMNLSGGQKQRLSLARAVYRKAAVY 774
Cdd:PRK14267 103 YDNVAIGvklnglvkskKELD----ERVewaLKKAALWDEVKD-------RLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 775 LLDDPLAALDAhVGQHVFNQVIGPggLLQGTTRILVTHA-LHILPQADWIIVLANGAIAEMGSYQELLQ 842
Cdd:PRK14267 172 LMDEPTANIDP-VGTAKIEELLFE--LKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
649-843 |
2.37e-15 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 79.37 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-----------------AVAYVPQEAwvq-ntSVVEN 710
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargiflpphrrRIGYVFQEArlfphlSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 711 VCFGQ-----ELDPPWLERVLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDA 785
Cdd:COG4148 98 LLYGRkraprAERRISFDEVVELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827346401 786 HVGQHVfnqvigpggL-----LQGTTRI---LVTHALH-ILPQADWIIVLANGAIAEMGSYQELLQR 843
Cdd:COG4148 167 ARKAEI---------LpylerLRDELDIpilYVSHSLDeVARLADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
649-812 |
2.77e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.07 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG----------AVAYV-PQEAWVQNTSVVENVCFGQEL 717
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpdvaeACHYLgHRNAMKPALTVAENLEFWAAF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 718 ---DPPWLERVLEACALQPdVDSFPEGihtsigeqgmNLSGGQKQRLSLAR--AVYRkaAVYLLDDPLAALDAHvGQHVF 792
Cdd:PRK13539 101 lggEELDIAAALEAVGLAP-LAHLPFG----------YLSAGQKRRVALARllVSNR--PIWILDEPTAALDAA-AVALF 166
|
170 180
....*....|....*....|
gi 1827346401 793 NQVIGpGGLLQGTTRILVTH 812
Cdd:PRK13539 167 AELIR-AHLAQGGIVIAATH 185
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1265-1488 |
2.94e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 77.83 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELPL-AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRIS 1343
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1344 IIPQDP--ILFPGSLRMNLDLLQEHSDEAIWAALETVQLKALVASLpgqLQYKCADRGEdLSVGQKQLLCLARALLRKTQ 1421
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNM---LDFKTREPAR-LSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 1422 ILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLA 1488
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
631-815 |
3.97e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 77.00 E-value: 3.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 631 IHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALlGELSKVEGFVSIEGAVAYVPQEAWVQNT----- 705
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEFFNQNIYERRVnlnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 706 ----------------SVVENVCFGQELdPPW-----LERVLEACALQPDV-DSFPEGIHTSigeqGMNLSGGQKQRLSL 763
Cdd:PRK14258 87 rrqvsmvhpkpnlfpmSVYDNVAYGVKI-VGWrpkleIDDIVESALKDADLwDEIKHKIHKS----ALDLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 764 ARAVYRKAAVYLLDDPLAALDAHVGQHVfNQVIGPGGLLQGTTRILVTHALH 815
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKV-ESLIQSLRLRSELTMVIVSHNLH 212
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
644-839 |
4.61e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 75.91 E-value: 4.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 644 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-AVAYVPQEAWVQNTS------------VVEN 710
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGeDISTLKPEIYRQQVSycaqtptlfgdtVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 711 VCFgqeldpPWLER--VLEACALQPDVDSFpeGIHTSIGEQGMN-LSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHV 787
Cdd:PRK10247 101 LIF------PWQIRnqQPDPAIFLDDLERF--ALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 788 GQHVfNQVIGPGGLLQGTTRILVTHALHILPQADWIIVLAngaiAEMGSYQE 839
Cdd:PRK10247 173 KHNV-NEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQ----PHAGEMQE 219
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
646-840 |
5.85e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 78.20 E-value: 5.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-----------VAYVPQE-AWVQNTSVVENVCF 713
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHyALFRHMTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 714 GQELDP-----------PWLERVLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLAA 782
Cdd:PRK10851 98 GLTVLPrrerpnaaaikAKVTQLLEMVQLAHLADRYPA-----------QLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 783 LDAHVGQHVFNQVIGPGGLLQGTTrILVTH----ALHIlpqADWIIVLANGAIAEMGSYQEL 840
Cdd:PRK10851 167 LDAQVRKELRRWLRQLHEELKFTS-VFVTHdqeeAMEV---ADRVVVMSQGNIEQAGTPDQV 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1265-1499 |
6.99e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 76.76 E-value: 6.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLA---SGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSR 1341
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISkliNGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1342 ISIIPQDPI-LFPGSlRMNLDLLQEHSDEAIwAALETVQLKALVASLPGQLQYKCADRgEDLSVGQKQLLCLARALLRKT 1420
Cdd:PRK13640 86 VGIVFQNPDnQFVGA-TVGDDVAFGLENRAV-PRPEMIKIVRDVLADVGMLDYIDSEP-ANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1421 QILILDEATAAVDPGTELQMQAMLGSWFA--QCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQ------LLAQKGL 1492
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEifskveMLKEIGL 242
|
250
....*....|.
gi 1827346401 1493 ----FYRLAQE 1499
Cdd:PRK13640 243 dipfVYKLKNK 253
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1265-1502 |
7.30e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 76.70 E-value: 7.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISI 1344
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1345 IPQDP--ILFPGSLR-------MNLDLLQEHSDEAIWAALETVQLKALVASLPGQLQYkcadrgedlsvGQKQLLCLARA 1415
Cdd:PRK13647 84 VFQDPddQVFSSTVWddvafgpVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSY-----------GQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1416 LLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIA-HRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQKglf 1493
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEWAdQVIVLKEGRVLAEGDKSLLTDED--- 229
|
....*....
gi 1827346401 1494 yrLAQESGL 1502
Cdd:PRK13647 230 --IVEQAGL 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1281-1481 |
8.69e-15 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 75.26 E-value: 8.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHT-LRSRISIIpqDPILFPGSLR-M 1358
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGGgFNPELTGR--ENIYLNGRLLgL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1359 NLDLLQEHSDEAI-WAALETVQlkalvaslpgQLQYKcadrgeDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTE 1437
Cdd:cd03220 115 SRKEIDEKIDEIIeFSELGDFI----------DLPVK------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1827346401 1438 LQMQAMLGSWFAQC-TVLLIAHRLRSVMD-CARVLVMDKGQVAESG 1481
Cdd:cd03220 179 EKCQRRLRELLKQGkTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1278-1487 |
8.77e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 78.15 E-value: 8.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1278 LPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRS----RISIIPQDPILFP 1353
Cdd:PRK10070 40 LSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1354 gslRMNLDLLQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVD 1433
Cdd:PRK10070 120 ---HMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1827346401 1434 PGTELQMQAMLGSWFA--QCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLL 1487
Cdd:PRK10070 197 PLIRTEMQDELVKLQAkhQRTIVFISHDLDEAMRIGdRIAIMQNGEVVQVGTPDEIL 253
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
629-847 |
9.58e-15 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 75.93 E-value: 9.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQEAW------- 701
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeirkkvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 702 -V-QN-------TSVVENVCFGQE---LDPPWLER----VLEACALQPDVDSFPegiHtsigeqgmNLSGGQKQRLSLAR 765
Cdd:TIGR04520 81 mVfQNpdnqfvgATVEDDVAFGLEnlgVPREEMRKrvdeALKLVGMEDFRDREP---H--------LLSGGQKQRVAIAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 766 AVYRKAAVYLLDDPLAALDahvgqhvfnqvigPGG---LL---------QGTTRILVTHALHILPQADWIIVLANGAIAE 833
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLD-------------PKGrkeVLetirklnkeEGITVISITHDMEEAVLADRVIVMNKGKIVA 216
|
250
....*....|....
gi 1827346401 834 MGSYQELLQRKGAL 847
Cdd:TIGR04520 217 EGTPREIFSQVELL 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1281-1489 |
1.28e-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: 78.57 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRL----QEAAEGGIWIDGVPIAHVGLHTLR----SRISIIPQDPI-- 1350
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLLGLSERELRrirgNRIAMIFQEPMts 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1351 LFP----G-----SLRMNLDLLQEHSDEAIWAALETVQL---KALVASLPGQlqykcadrgedLSVGQKQLLCLARALLR 1418
Cdd:COG4172 105 LNPlhtiGkqiaeVLRLHRGLSGAAARARALELLERVGIpdpERRLDAYPHQ-----------LSGGQRQRVMIAMALAN 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 1419 KTQILILDEATAAVDPGTELQM-------QAMLGSwfaqcTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQ 1489
Cdd:COG4172 174 EPDLLIADEPTTALDVTVQAQIldllkdlQRELGM-----ALLLITHDLGVVRRFAdRVAVMRQGEIVEQGPTAELFAA 247
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
649-847 |
1.61e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 76.68 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-----------VAYVPQE-AWVQNTSVVENVCFG-Q 715
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvthrsiqqrdICMVFQSyALFPHMSLGENVGYGlK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 716 ELDPPWLE---RVLEACALQpDVDSFPEGIHTSIgeqgmnlSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVF 792
Cdd:PRK11432 105 MLGVPKEErkqRVKEALELV-DLAGFEDRYVDQI-------SGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMR 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 793 NQVIGpgglLQ---GTTRILVTH----ALHIlpqADWIIVLANGAIAEMGSYQELLQRKGAL 847
Cdd:PRK11432 177 EKIRE----LQqqfNITSLYVTHdqseAFAV---SDTVIVMNKGKIMQIGSPQELYRQPASR 231
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
661-844 |
1.93e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 79.05 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 661 VVGPVGAGKSSLLSALLGELSKVEGFVSIEG--AVAY-----------VPQEAWVQNTSVVENVCFGQELDPPWLERVLE 727
Cdd:PTZ00243 1341 IVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGreIGAYglrelrrqfsmIPQDPVLFDGTVRQNVDPFLEASSAEVWAALE 1420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 728 ACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVY-LLDDPLAALDAHVGQHVFNQVIGPgglLQGTT 806
Cdd:PTZ00243 1421 LVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFiLMDEATANIDPALDRQIQATVMSA---FSAYT 1497
|
170 180 190
....*....|....*....|....*....|....*...
gi 1827346401 807 RILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRK 844
Cdd:PTZ00243 1498 VITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1279-1489 |
1.95e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.51 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1279 PLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG-LHTLRSRISIIPQDP-------- 1349
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQNPdnqivati 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1350 ----ILF-PGSLRMNLDLLQEHSDEAiwaaletvqLKALvaslpGQLQYKcadRGED--LSVGQKQLLCLARALLRKTQI 1422
Cdd:PRK13633 103 veedVAFgPENLGIPPEEIRERVDES---------LKKV-----GMYEYR---RHAPhlLSGGQKQRVAIAGILAMRPEC 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1423 LILDEATAAVDP-GTELQMQAM--LGSWFAqCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQ 1489
Cdd:PRK13633 166 IIFDEPTAMLDPsGRREVVNTIkeLNKKYG-ITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1286-1490 |
1.96e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 74.23 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1286 SFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPiahvglHTL----RSRISIIPQDPILF--------- 1352
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD------HTTtppsRRPVSMLFQENNLFshltvaqni 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1353 -----PGsLRMNLDllQEHSDEAIwaaLETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLARALLRKTQILILDE 1427
Cdd:PRK10771 93 glglnPG-LKLNAA--QREKLHAI---ARQMGIEDLLARLPGQL-----------SGGQRQRVALARCLVREQPILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 1428 ATAAVDPGTELQMQAMLGSWFA--QCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQK 1490
Cdd:PRK10771 156 PFSALDPALRQEMLTLVSQVCQerQLTLLMVSHSLEDAARIApRSLVVADGRIAWDGPTDELLSGK 221
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1282-1490 |
2.95e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.02 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1282 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPI-AHVGLhtLRSRISIIPQ-DPILFPGSLRMN 1359
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARL--ARARIGVVPQfDNLDLEFTVREN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1360 LDLLQEhsdeaiWAALETVQLKALVASLP--GQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTE 1437
Cdd:PRK13536 135 LLVFGR------YFGMSTREIEAVIPSLLefARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHAR 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1438 LQMQAMLGSWFAQC-TVLLIAH------RLrsvmdCARVLVMDKGQVAESGSPAQLLAQK 1490
Cdd:PRK13536 209 HLIWERLRSLLARGkTILLTTHfmeeaeRL-----CDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1281-1479 |
3.08e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 73.54 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSL---ASGLLRlqeAAEGGIWIDGVPIAHVG---LHTLRSR-ISIIPQDPILFP 1353
Cdd:COG1136 23 ALRGVSLSIEAGEFVAIVGPSGSGKSTLlniLGGLDR---PTSGEVLIDGQDISSLSereLARLRRRhIGFVFQFFNLLP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1354 gSL------RMNLDLLQEHSDEA---IWAALETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLARALLRKTQILI 1424
Cdd:COG1136 100 -ELtalenvALPLLLAGVSRKERrerARELLERVGLGDRLDHRPSQL-----------SGGQQQRVAIARALVNRPKLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 1425 LDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAH--RLRSVMDcaRVLVMDKGQVAE 1479
Cdd:COG1136 168 ADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHdpELAARAD--RVIRLRDGRIVS 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1282-1488 |
3.51e-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: 73.73 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1282 VQGVSFKIHAGEKVGIVGRTGAGKSSL---ASGLLRlqeAAEGGIWIDGVPIAHVGLHTlRSRISII--PQDPILFPG-S 1355
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTfymIVGLVK---PDSGKILLDGQDITKLPMHK-RARLGIGylPQEASIFRKlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1356 LRMNLDLLQE--HSDEAIWAALetvqLKALVASLpgQLQyKCADR-GEDLSVGQKQLLCLARALLRKTQILILDEATAAV 1432
Cdd:cd03218 92 VEENILAVLEirGLSKKEREEK----LEELLEEF--HIT-HLRKSkASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1433 DPGTELQMQAM---LGSWfaQCTVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQLLA 1488
Cdd:cd03218 165 DPIAVQDIQKIikiLKDR--GIGVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
648-840 |
3.63e-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: 73.31 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 648 RINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA------------VAYVPQE-AWVQNTSVVENVCF- 713
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsirtdrkaarqsLGYCPQFdALFDELTVREHLRFy 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 714 ----------GQELDppwlERVLEACALQPDvdsfpegIHTSIGeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLAAL 783
Cdd:cd03263 100 arlkglpkseIKEEV----ELLLRVLGLTDK-------ANKRAR----TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 784 DAHVGQHVFNQVIgpgGLLQGTTRILVTHALH---ILpqADWIIVLANGAIAEMGSYQEL 840
Cdd:cd03263 165 DPASRRAIWDLIL---EVRKGRSIILTTHSMDeaeAL--CDRIAIMSDGKLRCIGSPQEL 219
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
997-1479 |
3.84e-14 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 77.15 E-value: 3.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 997 LQAIGLFASMAAVLLGGARASRLLF------------QRLLWDVVRSPISFFERTPIGHLLNRFSKETDTVdvdipdkLR 1064
Cdd:COG4615 48 ARLLLLFAGLLVLLLLSRLASQLLLtrlgqhavarlrLRLSRRILAAPLERLERIGAARLLAALTEDVRTI-------SQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1065 SLLMYAFGLLEVSLVVAVATPLATVAiLPLFLLYAGFQSLYVVSSCQL-----RRLESASyssvcshMAET--FQG-STV 1136
Cdd:COG4615 121 AFVRLPELLQSVALVLGCLAYLAWLS-PPLFLLTLVLLGLGVAGYRLLvrrarRHLRRAR-------EAEDrlFKHfRAL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1137 VRAF--------RTQAPFVAQNNARVDESQRIsfpRLVADRWLAANVeLLGNGLVFAAATCAVLSKAHLSAG----LVGF 1204
Cdd:COG4615 193 LEGFkelklnrrRRRAFFDEDLQPTAERYRDL---RIRADTIFALAN-NWGNLLFFALIGLILFLLPALGWAdpavLSGF 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1205 sVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDYAWTPKEAPWRLPTCAAQPPWPQGGQIEFRDFGLRYRPEL---PLA 1281
Cdd:COG4615 269 -VLVLLFLRGPLSQLVGALPTLSRANVALRKIEELELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDgdeGFT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1282 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGslrmNLD 1361
Cdd:COG4615 348 LGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR----LLG 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1362 LLQEHSDEAIWAALETVQLKALVAslpgqlqykcADRGE----DLSVGQKQLLCLARALLRKTQILILDEATAAVDPG-- 1435
Cdd:COG4615 424 LDGEADPARARELLERLELDHKVS----------VEDGRfsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEfr 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 1436 ----TEL--QMQAMlGSwfaqcTVLLIAH--RLRSVMDcaRVLVMDKGQVAE 1479
Cdd:COG4615 494 rvfyTELlpELKAR-GK-----TVIAISHddRYFDLAD--RVLKMDYGKLVE 537
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
646-843 |
4.24e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 73.79 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSAL--LGEL---SKVEGFVSIEGA----------------VAYVPQEawVQN 704
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELypeARVSGEVYLDGQdifkmdvielrrrvqmVFQIPNP--IPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 705 TSVVENVCFGQELD------PPWLERVLEACalqpDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDD 778
Cdd:PRK14247 97 LSIFENVALGLKLNrlvkskKELQERVRWAL----EKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 779 PLAALDAHVGQHVFNQVIgpgGLLQGTTRILVThalHILPQA----DWIIVLANGAIAEMGSYQELLQR 843
Cdd:PRK14247 173 PTANLDPENTAKIESLFL---ELKKDMTIVLVT---HFPQQAarisDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
646-831 |
4.60e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 73.94 E-value: 4.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGeLSKVEGFVSIEGAVAYVP---------QEA----WvqnTSVVENVC 712
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-LETPSAGELLAGTAPLAEaredtrlmfQDArllpW---KKVIDNVG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 713 FGqeLDPPWLERVLEACAlqpdvdsfPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAhVGQHVF 792
Cdd:PRK11247 104 LG--LKGQWRDAALQALA--------AVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA-LTRIEM 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1827346401 793 NQVIGPGGLLQGTTRILVTHAL-HILPQADWIIVLANGAI 831
Cdd:PRK11247 173 QDLIESLWQQHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1281-1488 |
4.99e-14 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 73.09 E-value: 4.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTL-RSRISIIPQDPILFPG-SLRM 1358
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1359 NLDL--LQEHSDEAIWAALETV-----QLKALVASlpgqlqykcadRGEDLSVGQKQLLCLARALLRKTQILILDEATAA 1431
Cdd:COG0410 98 NLLLgaYARRDRAEVRADLERVyelfpRLKERRRQ-----------RAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 1432 VDPgtelQMQAMLGSWFAQ-----CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLA 1488
Cdd:COG0410 167 LAP----LIVEEIFEIIRRlnregVTILLVEQNARFALEIAdRAYVLERGRIVLEGTAAELLA 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1281-1493 |
5.81e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 74.89 E-value: 5.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAH-------VGLHT---------LRSRISI 1344
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDkknnhelITNPYskkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1345 IPQDP--ILFPGSLRMNLDL----LQEHSDEAiwaaletVQLKALVASLPGqLQYKCADRGE-DLSVGQKQLLCLARALL 1417
Cdd:PRK13631 121 VFQFPeyQLFKDTIEKDIMFgpvaLGVKKSEA-------KKLAKFYLNKMG-LDDSYLERSPfGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827346401 1418 RKTQILILDEATAAVDP-GTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQKGLF 1493
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPkGEHEMMQLILDAKANNKTVFVITHTMEHVLEVAdEVIVMDKGKILKTGTPYEIFTDQHII 270
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1281-1488 |
6.00e-14 |
|
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: 73.53 E-value: 6.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSL---ASGLLRlqeAAEGGIWIDGVPIAHVGLHtLRSRISI-----IPQdpiLF 1352
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLfnlITGFYR---PTSGRILFDGRDITGLPPH-RIARLGIartfqNPR---LF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1353 PG-SLRMNLDL-----------------------LQEHSDEAiWAALETVQLKALVASLPGqlqykcadrgeDLSVGQKQ 1408
Cdd:COG0411 92 PElTVLENVLVaaharlgrgllaallrlprarreEREARERA-EELLERVGLADRADEPAG-----------NLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1409 LLCLARALLRKTQILILDEATAAVDPG-----TEL--QMQAMLGswfaqCTVLLIAHRLRSVMD-CARVLVMDKGQVAES 1480
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEeteelAELirRLRDERG-----ITILLIEHDMDLVMGlADRIVVLDFGRVIAE 234
|
....*...
gi 1827346401 1481 GSPAQLLA 1488
Cdd:COG0411 235 GTPAEVRA 242
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1265-1490 |
7.28e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 73.57 E-value: 7.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYrPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAH--VGLHTLRSRI 1342
Cdd:PRK13639 2 LETRDLKYSY-PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYdkKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1343 SIIPQDP--ILFPGSLR-------MNLDLLQEHSDEAIWAALETVQLKALVASLPgqlqykcadrgEDLSVGQKQLLCLA 1413
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEedvafgpLNLGLSKEEVEKRVKEALKAVGMEGFENKPP-----------HHLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 1414 RALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ-CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQK 1490
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEgITIIISTHDVDLVPVYAdKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1280-1485 |
7.57e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.22 E-value: 7.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1280 LAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAhvgLHT----LRSRISIIPQDPILFP-- 1353
Cdd:COG3845 19 VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR---IRSprdaIALGIGMVHQHFMLVPnl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1354 -----------GSLRMNLDL------LQEHSDEAiwaALEtVQLKALVaslpgqlqykcadrgEDLSVGQKQllclaral 1416
Cdd:COG3845 96 tvaenivlglePTKGGRLDRkaararIRELSERY---GLD-VDPDAKV---------------EDLSVGEQQ-------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1417 lrK----------TQILILDEATAAVDPG--TEL-----QMQAmlgswfAQCTVLLIAHRLRSVMDCA-RVLVMDKGQVA 1478
Cdd:COG3845 149 --RveilkalyrgARILILDEPTAVLTPQeaDELfeilrRLAA------EGKSIIFITHKLREVMAIAdRVTVLRRGKVV 220
|
....*..
gi 1827346401 1479 ESGSPAQ 1485
Cdd:COG3845 221 GTVDTAE 227
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
626-784 |
9.36e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.38 E-value: 9.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 626 KDCITIHSATFAWsQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA----------VAY 695
Cdd:PRK15056 4 QAGIVVNDVTVTW-RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 696 VPQEA---WVQNTSVVENVCFGQELDPPWLER-------VLEACALQPDVDSFPegiHTSIGEqgmnLSGGQKQRLSLAR 765
Cdd:PRK15056 83 VPQSEevdWSFPVLVEDVVMMGRYGHMGWLRRakkrdrqIVTAALARVDMVEFR---HRQIGE----LSGGQKKRVFLAR 155
|
170
....*....|....*....
gi 1827346401 766 AVYRKAAVYLLDDPLAALD 784
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVD 174
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1265-1492 |
9.47e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 73.52 E-value: 9.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELP---LAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWI-DGVPIAHV---GLHT 1337
Cdd:PRK13634 3 ITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVITAGKknkKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1338 LRSRISIIPQDP------------ILF-PgslrMNLDLLQEhsdEAIWAALETVQLKALVASLPGQLQYkcadrgeDLSV 1404
Cdd:PRK13634 83 LRKKVGIVFQFPehqlfeetvekdICFgP----MNFGVSEE---DAKQKAREMIELVGLPEELLARSPF-------ELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1405 GQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMlgswFAQC------TVLLIAHrlrSVMDCAR----VLVMDK 1474
Cdd:PRK13634 149 GQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEM----FYKLhkekglTTVLVTH---SMEDAARyadqIVVMHK 221
|
250 260
....*....|....*....|....
gi 1827346401 1475 GQVAESGSPAQL------LAQKGL 1492
Cdd:PRK13634 222 GTVFLQGTPREIfadpdeLEAIGL 245
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1280-1486 |
9.60e-14 |
|
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: 72.02 E-value: 9.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1280 LAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGlHTLRSRISIIPQDPILfpgslrmn 1359
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP-REVRRRIGIVFQDLSV-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1360 ldllqehsDEAIwAALETVQLKALVASLPGQLQYKCADRGEDL--------------SVGQKQLLCLARALLRKTQILIL 1425
Cdd:cd03265 85 --------DDEL-TGWENLYIHARLYGVPGAERRERIDELLDFvglleaadrlvktySGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 1426 DEATAAVDPGTELQM----QAMLGSWfaQCTVLLIAHRLRSV-MDCARVLVMDKGQVAESGSPAQL 1486
Cdd:cd03265 156 DEPTIGLDPQTRAHVweyiEKLKEEF--GMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1282-1481 |
1.09e-13 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 71.43 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1282 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGL--LRLQEAAEGGIWIDGVPIahvGLHTLRSRISIIPQDPILFPgslrmN 1359
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKRSFRKIIGYVPQDDILHP-----T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1360 LdllqehsdeaiwAALETVQLKALVASLPGqlqykcadrgedlsvGQKQLLCLARALLRKTQILILDEATAAVDPGTELQ 1439
Cdd:cd03213 97 L------------TVRETLMFAAKLRGLSG---------------GERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1827346401 1440 -MQAMLGSWFAQCTVLLIAHRLRSVM--DCARVLVMDKGQVAESG 1481
Cdd:cd03213 150 vMSLLRRLADTGRTIICSIHQPSSEIfeLFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1269-1488 |
1.10e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.12 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1269 DFGLRYRPELPLAVQGVSFKIHAgeKVGIVGRTGAGKSSL---ASGLLRLQEAAEggIWiDGVPIAHV--GLHTLRSRIS 1343
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSP--VTGLVGANGCGKSTLfmnLSGLLRPQKGAV--LW-QGKPLDYSkrGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1344 IIPQDP------------ILFpgSLRmNLDLLQEHSDEAIWAALETVQLKALvaslpGQLQYKCadrgedLSVGQKQLLC 1411
Cdd:PRK13638 81 TVFQDPeqqifytdidsdIAF--SLR-NLGVPEAEITRRVDEALTLVDAQHF-----RHQPIQC------LSHGQKKRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 1412 LARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCT-VLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLA 1488
Cdd:PRK13638 147 IAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNhVIISSHDIDLIYEISdAVYVLRQGQILTHGAPGEVFA 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
646-831 |
1.12e-13 |
|
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: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGeLSKV-EGFVSIEGAVAYVPQEAWVQ----------------NTSVV 708
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINL-LEEPdSGTIIIDGLKLTDDKKNINElrqkvgmvfqqfnlfpHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 709 ENVCFGqeldPPWL------------ERVLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLL 776
Cdd:cd03262 95 ENITLA----PIKVkgmskaeaeeraLELLEKVGLADKADAYPA-----------QLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 777 DDPLAALDAHVGQHVFNQVIgpgGLLQ-GTTRILVTH----ALHIlpqADWIIVLANGAI 831
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMK---DLAEeGMTMVVVTHemgfAREV---ADRVIFMDDGRI 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
646-843 |
1.17e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 72.43 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSAL--LGELSK----VEGFVSIEGAVA--YVPQEA---------WVQNTSVv 708
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITSgdliVDGLKVNDPKVDerLIRQEAgmvfqqfylFPHLTAL- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 709 ENVCFG------------QELDPPWLERVleacALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLL 776
Cdd:PRK09493 96 ENVMFGplrvrgaskeeaEKQARELLAKV----GLAERAHHYPS-----------ELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 777 DDPLAALDAHVGQHVFNqvigpggLLQ-----GTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELLQR 843
Cdd:PRK09493 161 DEPTSALDPELRHEVLK-------VMQdlaeeGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
311-601 |
1.19e-13 |
|
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: 73.35 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 311 FLLGTLSLIISDVFRFTVPKLLSLFLEFIGdPKPPAWKGYLLAVLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITGLVY 390
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVI-PAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 391 RKVLALSSGSRKASAVGDVVNLVSVDVQRLTESV-LYLNGLWLPLVWIVVCFVYL----WQLlgpsaltAIAVFLsLLPL 465
Cdd:cd07346 80 RHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVsSGLLQLLSDVLTLIGALVILfylnWKL-------TLVALL-LLPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 466 NFFISKK-RNHHQEEQMRQKDSRARLTSSI---LRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLLFSVSLVSFQV 541
Cdd:cd07346 152 YVLILRYfRRRIRKASREVRESLAELSAFLqesLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 542 STFLVALVVFAVHT-LVAENAMNAEKAFVTLTVLNILNKAQAFLPFSIHSLVQARVSFDRL 601
Cdd:cd07346 232 LTALGTALVLLYGGyLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
646-841 |
1.22e-13 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 72.33 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGeLSKV-EGFVSIEGAVAYVPQEAWVQ----------------NTSVV 708
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINL-LEEPdSGTITVDGEDLTDSKKDINKlrrkvgmvfqqfnlfpHLTVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 709 ENVCFGQ----------------ELdppwLERV-LEACAlqpdvDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKA 771
Cdd:COG1126 96 ENVTLAPikvkkmskaeaeeramEL----LERVgLADKA-----DAYPA-----------QLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 772 AVYLLDDPLAALDahvgqhvfnqvigP---GGLLQ--------GTTRILVTH----ALHIlpqADWIIVLANGAIAEMGS 836
Cdd:COG1126 156 KVMLFDEPTSALD-------------PelvGEVLDvmrdlakeGMTMVVVTHemgfAREV---ADRVVFMDGGRIVEEGP 219
|
....*
gi 1827346401 837 YQELL 841
Cdd:COG1126 220 PEEFF 224
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1265-1490 |
1.68e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 72.89 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELPL---AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG----LHT 1337
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1338 LRSRISIIPQDP------------ILF-PGSLRMNLDllqEHSDEAIWAALETVQLKALVASLPGQlqykcadrgedLSV 1404
Cdd:PRK13646 83 VRKRIGMVFQFPesqlfedtvereIIFgPKNFKMNLD---EVKNYAHRLLMDLGFSRDVMSQSPFQ-----------MSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1405 GQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESG 1481
Cdd:PRK13646 149 GQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARYAdEVIVMKEGSIVSQT 228
|
....*....
gi 1827346401 1482 SPAQLLAQK 1490
Cdd:PRK13646 229 SPKELFKDK 237
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
649-844 |
1.69e-13 |
|
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: 73.61 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-----------------AVAYVPQEAWV-QNTSVVEN 710
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrkgiflppekrRIGYVFQEARLfPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 711 VCFG-QELDPPWL----ERVLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDa 785
Cdd:TIGR02142 96 LRYGmKRARPSERrisfERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD- 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 786 hvgQHVFNQVIGPGGLLQGTTRI---LVTHAL-HILPQADWIIVLANGAIAEMGSYQELLQRK 844
Cdd:TIGR02142 164 ---DPRKYEILPYLERLHAEFGIpilYVSHSLqEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1280-1481 |
2.43e-13 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 71.15 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1280 LAVQGVSFKIHAGEKVGIVGRTGAGKSSL---ASGLLRLQEAAEGGIWIDGVPIAHvglHTLRSRISIIPQDPILFPG-- 1354
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLldaISGRVEGGGTTSGQILFNGQPRKP---DQFQKCVAYVRQDDILLPGlt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1355 ---SLR-MNLDLLQEHSDEAIWAAL-ETVQLKALVASLPGQlqykcaDRGEDLSVGQKQLLCLARALLRKTQILILDEAT 1429
Cdd:cd03234 98 vreTLTyTAILRLPRKSSDAIRKKRvEDVLLRDLALTRIGG------NLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1827346401 1430 AAVDPGTELQMQAMLgSWFAQ--CTVLLIAHRLRS----VMDcaRVLVMDKGQVAESG 1481
Cdd:cd03234 172 SGLDSFTALNLVSTL-SQLARrnRIVILTIHQPRSdlfrLFD--RILLLSSGEIVYSG 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
649-835 |
2.44e-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: 70.68 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGcLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG------------AVAYVPQE-AWVQNTSVVENV---C 712
Cdd:cd03264 19 VSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQEfGVYPNFTVREFLdyiA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 713 FGQELDPPWLERvlEACALQPDVDSFPEGiHTSIGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDahVGQ-HV 791
Cdd:cd03264 98 WLKGIPSKEVKA--RVDEVLELVNLGDRA-KKKIGS----LSGGMRRRVGIAQALVGDPSILIVDEPTAGLD--PEErIR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1827346401 792 FNQVIgpGGLLQGTTRILVTHALH-ILPQADWIIVLANGAIAEMG 835
Cdd:cd03264 169 FRNLL--SELGEDRIVILSTHIVEdVESLCNQVAVLNKGKLVFEG 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
648-842 |
2.60e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 71.15 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 648 RINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-----------VAYVPQEawvqNT-----SVVENV 711
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsrrpVSMLFQE----NNlfshlTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 712 CFGqeLDPPW---------LERVLEACALQPDVDSFPegihtsiGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAA 782
Cdd:PRK10771 93 GLG--LNPGLklnaaqrekLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 783 LDAHVGQHVFNqvigpggLL------QGTTRILVTH----ALHILPQAdwiIVLANGAIAEMGSYQELLQ 842
Cdd:PRK10771 160 LDPALRQEMLT-------LVsqvcqeRQLTLLMVSHsledAARIAPRS---LVVADGRIAWDGPTDELLS 219
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
644-785 |
2.93e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 71.27 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 644 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVP---------QEAWVQNTSVVENVCFG 714
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPgaergvvfqNEGLLPWRNVQDNVAFG 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 715 QEL-DPPWLERVLEACALQPDVDSfpEGIHTSIGEQgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDA 785
Cdd:PRK11248 95 LQLaGVEKMQRLEIAHQMLKKVGL--EGAEKRYIWQ---LSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1281-1482 |
3.21e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 72.82 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGI-WI--DGVPIAHVGLHTLRSRISIIPQDPIlfpGSL- 1356
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVaWLgkDLLGMKDDEWRAVRSDIQMIFQDPL---ASLn 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1357 -RMNL-DLLQEH--------SDEAIWAALETVQLKalVASLPGQL-QYKcadrgEDLSVGQKQLLCLARALLRKTQILIL 1425
Cdd:PRK15079 113 pRMTIgEIIAEPlrtyhpklSRQEVKDRVKAMMLK--VGLLPNLInRYP-----HEFSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 1426 DEATAAVDPGTELQ-------MQAMLGswfaqCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGS 1482
Cdd:PRK15079 186 DEPVSALDVSIQAQvvnllqqLQREMG-----LSLIFIAHDLAVVKHISdRVLVMYLGHAVELGT 245
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
696-841 |
3.44e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.07 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 696 VPQEAWVQNTSVVENVCFGQEldPPWLERVLEAC---ALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAA 772
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGKE--DATREDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPK 1378
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 773 VYLLDDPLAALDAHvGQHVFNQVIGPGGLLQGTTRILVTHALHILPQADWIIVLAN----GAIAEM-GSYQELL 841
Cdd:PTZ00265 1379 ILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAhGTHEELL 1451
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1265-1488 |
3.55e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.15 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELplAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTlRSRISI 1344
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1345 IPQDPILFPG-SLRMNLDLLQEhsdeaiWAALETVQLKALVASLP--GQLQYKCADRGEDLSVGQKQLLCLARALLRKTQ 1421
Cdd:PRK13537 85 VPQFDNLDPDfTVRENLLVFGR------YFGLSAAAARALVPPLLefAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 1422 ILILDEATAAVDPGTELQMQAMLGSWFAQC-TVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQLLA 1488
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGkTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1283-1486 |
4.01e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.93 E-value: 4.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1283 QGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAH---VGLHTLRsrISIIPQDPILFPG-SLRM 1358
Cdd:PRK15439 28 KGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARltpAKAHQLG--IYLVPQEPLLFPNlSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1359 NLDL-LQEHSDEaiwaaleTVQLKALVASLPGQLqyKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPG-T 1436
Cdd:PRK15439 106 NILFgLPKRQAS-------MQKMKQLLAALGCQL--DLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAeT 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 1437 EL---QMQAMLGSWFAqctVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQL 1486
Cdd:PRK15439 177 ERlfsRIRELLAQGVG---IVFISHKLPEIRQLAdRISVMRDGTIALSGKTADL 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1280-1486 |
4.28e-13 |
|
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: 70.34 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1280 LAVQGVSFKIHAGEKVGIVGRTGAGKSSLasglLRL----QEAAEGGIWIDGVPIAHVGLHtlRSRISIIPQDPILFPG- 1354
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLiagfETPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALFPHl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1355 --------SLRMnLDLLQEHSDEAIWAALETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLARALLRKTQILILD 1426
Cdd:cd03300 88 tvfeniafGLRL-KKLPKAEIKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827346401 1427 EATAAVDPG--TELQ-----MQAMLGSwfaqcTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQL 1486
Cdd:cd03300 156 EPLGALDLKlrKDMQlelkrLQKELGI-----TFVFVTHDQEEALTMSdRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1265-1481 |
4.29e-13 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 70.09 E-value: 4.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELP--LAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTlRSRI 1342
Cdd:cd03266 2 ITADALTKRFRDVKKtvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEA-RRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1343 SIIPQDPILFPG-SLRMNLDLLqehsdeAIWAALETVQLKALVASLPGQLQYK-CAD-RGEDLSVGQKQLLCLARALLRK 1419
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYF------AGLYGLKGDELTARLEELADRLGMEeLLDrRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 1420 TQILILDEATAAVD-PGTELQMQAMLGSWFAQCTVLLIAHRLRSVMD-CARVLVMDKGQVAESG 1481
Cdd:cd03266 155 PPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
633-784 |
4.92e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.81 E-value: 4.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 633 SATFAWSQesppCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGEL-------SKVEGF---VSIEGAVA-------- 694
Cdd:PRK09984 11 AKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdksagSHIELLgrtVQREGRLArdirksra 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 695 ---YVPQE-AWVQNTSVVENVCFGQELDPP-------WLERVLEACALQPDVDSfpeGIHTSIGEQGMNLSGGQKQRLSL 763
Cdd:PRK09984 87 ntgYIFQQfNLVNRLSVLENVLIGALGSTPfwrtcfsWFTREQKQRALQALTRV---GMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180
....*....|....*....|.
gi 1827346401 764 ARAVYRKAAVYLLDDPLAALD 784
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLD 184
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1281-1486 |
6.16e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.13 E-value: 6.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLA---SGLLRlqeAAEGGIWIDGVPIAHVG-LHTLRSRISIIPQDPILFP--- 1353
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMkilSGVYQ---PDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPnls 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1354 -------GSLRMNLDLLQehsdeaiWAALETvQLKALVASLpgQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILD 1426
Cdd:COG1129 96 vaeniflGREPRRGGLID-------WRAMRR-RARELLARL--GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 1427 EATAAVDPG---------TELQmqamlgswfAQ-CTVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQL 1486
Cdd:COG1129 166 EPTASLTEReverlfriiRRLK---------AQgVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
646-842 |
6.51e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 70.43 E-value: 6.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAYVPQEAWV-QNTSVVENV 711
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTpEGITVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 712 CFGQEldpPWL-----------ERVLEACAlQPDVDSFPEGIHTSigeqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPL 780
Cdd:PRK11231 98 AYGRS---PWLslwgrlsaednARVNQAME-QTRINHLADRRLTD-------LSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 781 AALDahvgqhvFNQVIGPGGLL-----QGTTRILVthaLHILPQA----DWIIVLANGAIAEMGSYQELLQ 842
Cdd:PRK11231 167 TYLD-------INHQVELMRLMrelntQGKTVVTV---LHDLNQAsrycDHLVVLANGHVMAQGTPEEVMT 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
646-840 |
6.78e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.13 E-value: 6.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------------VAYVPQE-AWVQNTSVVEN 710
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvrfrsprdaqaagIAIIHQElNLVPNLSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 711 VCFGQELDPPWL-------ERVLEACA-LQPDVDsfPegiHTSIGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAA 782
Cdd:COG1129 100 IFLGREPRRGGLidwramrRRARELLArLGLDID--P---DTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 783 LDAHVGQHVFNQVigpgGLL--QGTTRILVTHALH-ILPQADWIIVLANGAIAEMGSYQEL 840
Cdd:COG1129 171 LTEREVERLFRII----RRLkaQGVAIIYISHRLDeVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1265-1495 |
7.83e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 70.60 E-value: 7.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISI 1344
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1345 I---PQDPILFP--------GSLRMNLDllQEHSDEAIWAALETVQLKALVASLPgqlqykcadrgEDLSVGQKQLLCLA 1413
Cdd:PRK13652 83 VfqnPDDQIFSPtveqdiafGPINLGLD--EETVAHRVSSALHMLGLEELRDRVP-----------HHLSGGEKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1414 RALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCAR-VLVMDKGQVAESGSPAQLLAQK 1490
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMADyIYVMDKGRIVAYGTVEEIFLQP 229
|
....*
gi 1827346401 1491 GLFYR 1495
Cdd:PRK13652 230 DLLAR 234
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
646-844 |
8.77e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 70.82 E-value: 8.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIE--------------------GAVAYVPQEAWVQNT 705
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGervitagkknkklkplrkkvGIVFQFPEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 706 sVVENVCFG------QELDPpwLERVLEACALqpdVDSFPEGIHTSIGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDP 779
Cdd:PRK13634 103 -VEKDICFGpmnfgvSEEDA--KQKAREMIEL---VGLPEELLARSPFE----LSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 780 LAALDAHvGQH----VFNQVIGPGGLlqgtTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELLQRK 844
Cdd:PRK13634 173 TAGLDPK-GRKemmeMFYKLHKEKGL----TTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
648-784 |
9.00e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.22 E-value: 9.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 648 RINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEgavayVPQEAWVQNTSVVEnvCFGQELDPPWLERVLE 727
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----VPDNQFGREASLID--AIGRKGDFKDAVELLN 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 728 ACALqpdVD------SFPEgihtsigeqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 784
Cdd:COG2401 121 AVGL---SDavlwlrRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1282-1477 |
1.11e-12 |
|
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: 72.16 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1282 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAA-EGGIWIDGVPIA-HVGLHTLRSRISIIPQD-------PILF 1352
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDiRNPAQAIRAGIAMVPEDrkrhgivPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1353 PG-----------SLRMNLDLLQEhsDEAIWAALETVQLKALVASLPGQlqykcadrgeDLSVGQKQLLCLARALLRKTQ 1421
Cdd:TIGR02633 356 VGknitlsvlksfCFKMRIDAAAE--LQIIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNPR 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1827346401 1422 ILILDEATAAVDPGTELQMQAMLGSWFAQ-CTVLLIAHRLRSVMDCA-RVLVMDKGQV 1477
Cdd:TIGR02633 424 VLILDEPTRGVDVGAKYEIYKLINQLAQEgVAIIVVSSELAEVLGLSdRVLVIGEGKL 481
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
629-829 |
1.28e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 66.70 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWsqESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--VAYVPQeawvqnts 706
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTvkIGYFEQ-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 707 vvenvcfgqeldppwlervleacalqpdvdsfpegihtsigeqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAH 786
Cdd:cd03221 71 ----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1827346401 787 vGQHVFNQVIG--PGGLlqgttrILVTHALHILPQ-ADWIIVLANG 829
Cdd:cd03221 105 -SIEALEEALKeyPGTV------ILVSHDRYFLDQvATKIIELEDG 143
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1282-1490 |
1.53e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.15 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1282 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTlRSR--ISIIPQDPILFP------ 1353
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA-RARrgIGYLPQEASIFRrlsvyd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1354 ---GSLRMNLDLLQEHSDEAIWAALETVQLKALVASLpgqlqykcadrGEDLSVGQKQLLCLARALLRKTQILILDEATA 1430
Cdd:PRK10895 98 nlmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 1431 AVDPGTELQMQAMLGSWF-AQCTVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQLLAQK 1490
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1273-1477 |
1.76e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 69.32 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1273 RYRPELPLAVQGVS-------------FKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPiahvgLHTLR 1339
Cdd:PRK11247 6 RLNQGTPLLLNAVSkrygertvlnqldLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAP-----LAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1340 SRISIIPQDPILFP-GSLRMNLDL-LQEHSDEAIWAALETVQLkalvaslpgqlqykcADRGED----LSVGQKQLLCLA 1413
Cdd:PRK11247 81 EDTRLMFQDARLLPwKKVIDNVGLgLKGQWRDAALQALAAVGL---------------ADRANEwpaaLSGGQKQRVALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827346401 1414 RALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQV 1477
Cdd:PRK11247 146 RALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhgFTVLLVTHDVSEAVAMAdRVLLIEEGKI 212
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
946-1235 |
1.80e-12 |
|
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: 69.90 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 946 LCLYALFLFLCQQVASFCRGYWLSLWaddpavgGQQTQAALRggifgllgclqaiglfasmaavllggarasRLLFQRLL 1025
Cdd:cd18557 38 LALILLAIYLLQSVFTFVRYYLFNIA-------GERIVARLR------------------------------RDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1026 wdvvRSPISFFERTPIGHLLNRFSKET----DTVDVDIPDKLRSLLMYAFGLLeVSLVVAVATPLATVAILPLFLLYAGF 1101
Cdd:cd18557 81 ----RQEIAFFDKHKTGELTSRLSSDTsvlqSAVTDNLSQLLRNILQVIGGLI-ILFILSWKLTLVLLLVIPLLLIASKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1102 QSLYVVsscQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANVELLGNG 1181
Cdd:cd18557 156 YGRYIR---KLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1827346401 1182 LVFAAATCA---VLSKaHLSAG-LVGFSVsAALQVTQTLQWVVRNWTDLENSIVSVER 1235
Cdd:cd18557 233 SLLLVLWYGgylVLSG-QLTVGeLTSFIL-YTIMVASSVGGLSSLLADIMKALGASER 288
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1281-1486 |
1.81e-12 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 68.91 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVglhTLRSR-ISIIPQDPILF------- 1352
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV---PVQERnVGFVFQHYALFrhmtvfd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1353 ---------PGSLRMNLDLLQEHSDEaiwaALETVQLKALVASLPGQlqykcadrgedLSVGQKQLLCLARALLRKTQIL 1423
Cdd:cd03296 94 nvafglrvkPRSERPPEAEIRAKVHE----LLKLVQLDWLADRYPAQ-----------LSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1424 ILDEATAAVDPgtelQMQAMLGSWFAQ------CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQL 1486
Cdd:cd03296 159 LLDEPFGALDA----KVRKELRRWLRRlhdelhVTTVFVTHDQEEALEVAdRVVVMNKGRIEQVGTPDEV 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1281-1486 |
2.17e-12 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 70.51 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLasglLR----LQEAAEGGIWIDGVPIAHVGLHtlRSRISIIPQDPILFP--- 1353
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTL----LRmiagFETPDSGRILLDGRDVTGLPPE--KRNVGMVFQDYALFPhlt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1354 -------GsLRMnldllQEHSDEAIWA----ALETVQLKALVASLPGQLqykcadrgedlSVGQKQllclarallrktQI 1422
Cdd:COG3842 94 vaenvafG-LRM-----RGVPKAEIRArvaeLLELVGLEGLADRYPHQL-----------SGGQQQrvalaralapepRV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 1423 LILDEATAAVDPGTELQMQAMLGSWFAQC--TVLLIAHRLR---SVMDcaRVLVMDKGQVAESGSPAQL 1486
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHDQEealALAD--RIAVMNDGRIEQVGTPEEI 223
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1281-1489 |
2.25e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 69.37 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHT---------LRSRISIIPQdpIL 1351
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpeergLYPKMKVGEQ--LV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1352 FPGSLR-MNLDLLQEHSDEaiWaaLETVQLKAlvaslpgqlqYKcADRGEDLSVGQKQllclarallrKTQI-------- 1422
Cdd:COG4152 94 YLARLKgLSKAEAKRRADE--W--LERLGLGD----------RA-NKKVEELSKGNQQ----------KVQLiaallhdp 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 1423 --LILDEATAAVDP-GTELQMQAML-----GSwfaqcTVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQLLAQ 1489
Cdd:COG4152 149 elLILDEPFSGLDPvNVELLKDVIRelaakGT-----TVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
646-831 |
2.43e-12 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 67.63 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGavayvpqEAWVQNTSVVENVcfGQELDPPWL--- 722
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG-------KSYQKNIEALRRI--GALIEAPGFypn 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 723 ---ERVLEACALQPDVDSfpEGIHTSIGEQGM---------NLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDahvgqh 790
Cdd:cd03268 87 ltaRENLRLLARLLGIRK--KRIDEVLDVVGLkdsakkkvkGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD------ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 791 vfnqvigPGGLL-----------QGTTRILVTHALHILPQ-ADWIIVLANGAI 831
Cdd:cd03268 159 -------PDGIKelrelilslrdQGITVLISSHLLSEIQKvADRIGIINKGKL 204
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
629-843 |
2.44e-12 |
|
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: 68.48 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSqESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAY 695
Cdd:cd03295 1 IEFENVTKRYG-GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 696 VPQEAWV-QNTSVVENVcfgqELDPPWL--------ERVLEACALqpdVDSFPEGIHTSIGEQgmnLSGGQKQRLSLARA 766
Cdd:cd03295 80 VIQQIGLfPHMTVEENI----ALVPKLLkwpkekirERADELLAL---VGLDPAEFADRYPHE---LSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 767 VYRKAAVYLLDDPLAALDAHVGQHVFNQVIGpgglLQ---GTTRILVTH----ALHIlpqADWIIVLANGAIAEMGSYQE 839
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKR----LQqelGKTIVFVTHdideAFRL---ADRIAIMKNGEIVQVGTPDE 222
|
....
gi 1827346401 840 LLQR 843
Cdd:cd03295 223 ILRS 226
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
644-843 |
2.85e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 69.87 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 644 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVayV----PQE---AWV-QN------TSVVE 709
Cdd:PRK11650 18 QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRV--VnelePADrdiAMVfQNyalyphMSVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 710 NVCFG--------QELDppwlERVLEACA---LQPDVDSFPegihtsigeqgMNLSGGQKQRLSLARAVYRKAAVYLLDD 778
Cdd:PRK11650 96 NMAYGlkirgmpkAEIE----ERVAEAARileLEPLLDRKP-----------RELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 779 PLAALDAHvgqhvfnqvigpggL----------LQ---GTTRILVTH-ALHILPQADWIIVLANGAIAEMGSYQELLQR 843
Cdd:PRK11650 161 PLSNLDAK--------------LrvqmrleiqrLHrrlKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEVYEK 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1276-1494 |
2.86e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 68.86 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1276 PELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLA---SGLLRLQEaaeGGIWIDGVPIAHVG-LHTLRSRISIIPQDP-I 1350
Cdd:PRK13644 12 PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLAlhlNGLLRPQK---GKVLVSGIDTGDFSkLQGIRKLVGIVFQNPeT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1351 LFPGslRMNLDLLQEHSDEAIWAALETVQL--KALVASLPGQLQYKCAdrgEDLSVGQKQLLCLARALLRKTQILILDEA 1428
Cdd:PRK13644 89 QFVG--RTVEEDLAFGPENLCLPPIEIRKRvdRALAEIGLEKYRHRSP---KTLSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827346401 1429 TAAVDPGTELQMQAMLGSWFAQC-TVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFY 1494
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQT 230
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
629-847 |
3.22e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 68.89 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVaYVPQEAW------- 701
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV-LSEETVWdvrrqvg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 702 --VQN-------TSVVENVCFGQELD----PPWLERVLEACAlQPDVDSFPEgihtsigEQGMNLSGGQKQRLSLARAVY 768
Cdd:PRK13635 85 mvFQNpdnqfvgATVQDDVAFGLENIgvprEEMVERVDQALR-QVGMEDFLN-------REPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 769 RKAAVYLLDDPLAALDAHVGQHVFNQVigpgGLL---QGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKG 845
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETV----RQLkeqKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGH 232
|
..
gi 1827346401 846 AL 847
Cdd:PRK13635 233 ML 234
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
646-840 |
3.54e-12 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 67.88 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVP---QEAWVQNTSVVenvcfgqeldpPWL 722
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpdRMVVFQNYSLL-----------PWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 723 ErVLEACALQPD--VDSFPEGIHTSIGEQGMNL--------------SGGQKQRLSLARAVYRKAAVYLLDDPLAALDAH 786
Cdd:TIGR01184 70 T-VRENIALAVDrvLPDLSKSERRAIVEEHIALvglteaadkrpgqlSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 787 VGQHVFNQvigpggLLQ-----GTTRILVTHAL-HILPQADWIIVLANGAIAEMGSYQEL 840
Cdd:TIGR01184 149 TRGNLQEE------LMQiweehRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1282-1463 |
3.66e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 68.52 E-value: 3.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1282 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAaEGGIWIDG--------VPIAHVGLHTLRSRISIIPQDPILFP 1353
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGrveffnqnIYERRVNLNRLRRQVSMVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1354 GSLRMNL----DLLQEHSDEAIWAALETVqLKAlvASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEAT 1429
Cdd:PRK14258 102 MSVYDNVaygvKIVGWRPKLEIDDIVESA-LKD--ADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPC 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 1827346401 1430 AAVDPGTELQMQAMLGSWF--AQCTVLLIAHRLRSV 1463
Cdd:PRK14258 179 FGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQV 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1282-1487 |
3.72e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 68.26 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1282 VQGVSFKIHAGEKVGIVGRTGAGKSSlasgLLRL----QEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPIL-FPGSL 1356
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKST----LLRAlsgeLSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1357 -------RMNLDLLQEHSDEAIWAALETVQLKALvaslpgqlqykcADRG-EDLSVGQKQ------LLCLARALLRKTQI 1422
Cdd:PRK13548 94 eevvamgRAPHGLSRAEDDALVAAALAQVDLAHL------------AGRDyPQLSGGEQQrvqlarVLAQLWEPDGPPRW 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 1423 LILDEATAAVDPGTELQMQAMLGSwFAQ---CTVLLIAHRLR-SVMDCARVLVMDKGQVAESGSPAQLL 1487
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQ-LAHergLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
646-844 |
4.09e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.22 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQEAWVQN---------------TSVVEN 710
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSkvglvfqdpddqvfsSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 711 VCFG---QELDPPWLERVLEACALQPDVDSFPEgihtsigEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHv 787
Cdd:PRK13647 101 VAFGpvnMGLDKDEVERRVEEALKAVRMWDFRD-------KPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR- 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 788 GQHVFNQVIgpGGL-LQGTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELLQRK 844
Cdd:PRK13647 173 GQETLMEIL--DRLhNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
646-841 |
6.00e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 67.76 E-value: 6.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQEAW--------------------VQNT 705
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFqidaiklrkevgmvfqqpnpFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 706 SVVENVCFGQEL----DPPWLERVLEACALQpdVDSFPEgIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLA 781
Cdd:PRK14246 106 SIYDNIAYPLKShgikEKREIKKIVEECLRK--VGLWKE-VYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 782 ALDAhVGQHVFNQVIGPggLLQGTTRILVTHAlhilPQ-----ADWIIVLANGAIAEMGSYQELL 841
Cdd:PRK14246 183 MIDI-VNSQAIEKLITE--LKNEIAIVIVSHN----PQqvarvADYVAFLYNGELVEWGSSNEIF 240
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1281-1489 |
7.01e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 68.45 E-value: 7.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIA---HVGLHTLRSRISIIPQDPI--LFP-- 1353
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNPYgsLNPrk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1354 --GS-----LRMNLDLLQEHSDEAIWAALETVQLKAlvaslpgqlqyKCADRGEDL-SVGQKQLLCLARALLRKTQILIL 1425
Cdd:PRK11308 110 kvGQileepLLINTSLSAAERREKALAMMAKVGLRP-----------EHYDRYPHMfSGGQRQRIAIARALMLDPDVVVA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 1426 DEATAAVDPGTELQ-------MQAMLGSWFaqctvLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQ 1489
Cdd:PRK11308 179 DEPVSALDVSVQAQvlnlmmdLQQELGLSY-----VFISHDLSVVEHIAdEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1264-1472 |
8.30e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.44 E-value: 8.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1264 QIEFRDFGLRYRPELPLAV-QGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWI-DGVPIAHVGLHTLRSR 1341
Cdd:PTZ00265 382 KIQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1342 ISIIPQDPILFPGSLRMN----------LDLLQEHSDEAIWAALE----------------------------------- 1376
Cdd:PTZ00265 462 IGVVSQDPLLFSNSIKNNikyslyslkdLEALSNYYNEDGNDSQEnknkrnscrakcagdlndmsnttdsneliemrkny 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1377 ---------TVQLKAL----VASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAM 1443
Cdd:PTZ00265 542 qtikdsevvDVSKKVLihdfVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
|
250 260 270
....*....|....*....|....*....|.
gi 1827346401 1444 LGSWFAQCT--VLLIAHRLRSVMDCARVLVM 1472
Cdd:PTZ00265 622 INNLKGNENriTIIIAHRLSTIRYANTIFVL 652
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1265-1487 |
9.17e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 66.65 E-value: 9.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELPLavQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPI--AHVGLHTLRSRI 1342
Cdd:PRK09493 2 IEFKNVSKHFGPTQVL--HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1343 SIIPQDPILFP----------GSLRMNLDLLQEHSDEAIwAALETVQLKALVASLPGQlqykcadrgedLSVGQKQLLCL 1412
Cdd:PRK09493 80 GMVFQQFYLFPhltalenvmfGPLRVRGASKEEAEKQAR-ELLAKVGLAERAHHYPSE-----------LSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1413 ARALLRKTQILILDEATAAVDPgtELQ------MQAMlgswfAQ--CTVLLIAHRL---RSVmdCARVLVMDKGQVAESG 1481
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDP--ELRhevlkvMQDL-----AEegMTMVIVTHEIgfaEKV--ASRLIFIDKGRIAEDG 218
|
....*.
gi 1827346401 1482 SPAQLL 1487
Cdd:PRK09493 219 DPQVLI 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
626-779 |
1.09e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 69.32 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 626 KDCITIHSATFAWsqESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIeGA---VAYVPQEawv 702
Cdd:COG0488 313 KKVLELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GEtvkIGYFDQH--- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 703 qntsvvenvcfGQELDPPWleRVLEA-CALQPDVD---------SF---PEGIHTSIGeqgmNLSGGQKQRLSLARAVYR 769
Cdd:COG0488 387 -----------QEELDPDK--TVLDElRDGAPGGTeqevrgylgRFlfsGDDAFKPVG----VLSGGEKARLALAKLLLS 449
|
170
....*....|
gi 1827346401 770 KAAVYLLDDP 779
Cdd:COG0488 450 PPNVLLLDEP 459
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1281-1477 |
1.23e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 66.65 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSL---ASGLLRLQEaaeGGIWIDGVPIAHVGLHTlRSR-ISIIPQDPIL--FPG 1354
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLlnaIAGSLPPDS---GSILIDGKDVTKLPEYK-RAKyIGRVFQDPMMgtAPS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1355 -------SL------RMNLDLLQEHSDEAiwaaletvQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQ 1421
Cdd:COG1101 97 mtieenlALayrrgkRRGLRRGLTKKRRE--------LFRELLATLGLGLENRLDTKVGLLSGGQRQALSLLMATLTKPK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 1422 ILILDEATAAVDPGT-----ELQMQAMLGSwfaQCTVLLIAHRLRSVMDCA-RVLVMDKGQV 1477
Cdd:COG1101 169 LLLLDEHTAALDPKTaalvlELTEKIVEEN---NLTTLMVTHNMEQALDYGnRLIMMHEGRI 227
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1265-1489 |
1.23e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.07 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELPLAVQG---VSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG----LHT 1337
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRAlfdIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1338 LRSRISIIPQdpilFPGSLRMNLDLLQE----------HSDEAIWAALETVQLKALVASLPGQLQYkcadrgeDLSVGQK 1407
Cdd:PRK13643 82 VRKKVGVVFQ----FPESQLFEETVLKDvafgpqnfgiPKEKAEKIAAEKLEMVGLADEFWEKSPF-------ELSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1408 QLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQC-TVLLIAHRLRSVMDCAR-VLVMDKGQVAESGSPAQ 1485
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGqTVVLVTHLMDDVADYADyVYLLEKGHIISCGTPSD 230
|
....
gi 1827346401 1486 LLAQ 1489
Cdd:PRK13643 231 VFQE 234
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
649-840 |
1.36e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 68.32 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYVP-----------QEAWVQNTSVVENVCFGQE 716
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdLSHVPpyqrpinmmfqSYALFPHMTVEQNIAFGLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 717 LDP-PWLE---RVLEACALqpdvdsfpegIHTS--IGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQH 790
Cdd:PRK11607 118 QDKlPKAEiasRVNEMLGL----------VHMQefAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDR 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 791 VFNQVIgpgGLLQ--GTTRILVTH-ALHILPQADWIIVLANGAIAEMGSYQEL 840
Cdd:PRK11607 188 MQLEVV---DILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
646-854 |
1.54e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 68.98 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSaLLGELSK-VEGFVSIEG---------AVAYVPQEAW---VQNTSVVENVC 712
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKpTSGTYRVAGqdvatldadALAQLRREHFgfiFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 713 FGQELDPPWL-------ERVLEACALQPDVdsfpeGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDA 785
Cdd:PRK10535 103 AAQNVEVPAVyaglerkQRLLRAQELLQRL-----GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 786 HVGQHVFNqvigpggLL-----QGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGALMCLLDQA 854
Cdd:PRK10535 178 HSGEEVMA-------ILhqlrdRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVAGGTEPVVNTA 244
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
646-842 |
1.59e-11 |
|
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: 66.51 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-AVAYVPQEAWVQ-----------------NTSV 707
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqDIAAMSRKELRElrrkkismvfqsfallpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 708 VENVCFGQELDP-PWLER------VLEACALQPDVDSFPegihtsiGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPL 780
Cdd:cd03294 120 LENVAFGLEVQGvPRAEReeraaeALELVGLEGWEHKYP-------DE----LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 781 AALDAHVGQHVFNQVIGPGGLLQGTTrILVTH----ALHIlpqADWIIVLANGAIAEMGSYQELLQ 842
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAELQKTI-VFITHdldeALRL---GDRIAIMKDGRLVQVGTPEEILT 250
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
646-841 |
1.84e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 66.40 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-AVAY------------VPQEAwvqNTSVVENVC 712
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhKLEYgdykyrckhirmIFQDP---NTSLNPRLN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 713 FGQELDPPWL-----------ERV---LEACALQPDVDSFPegIHTsigeqgmnLSGGQKQRLSLARAVYRKAAVYLLDD 778
Cdd:COG4167 106 IGQILEEPLRlntdltaeereERIfatLRLVGLLPEHANFY--PHM--------LSSGQKQRVALARALILQPKIIIADE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 779 PLAALDAHVGQHVFNqvigpggLL------QGTTRILVTHAL----HIlpqADWIIVLANGAIAEMGSYQELL 841
Cdd:COG4167 176 ALAALDMSVRSQIIN-------LMlelqekLGISYIYVSQHLgivkHI---SDKVLVMHQGEVVEYGKTAEVF 238
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
629-844 |
2.36e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 66.17 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVayVPQEAW------- 701
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGIT--ISKENLkeirkki 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 702 ---VQN-------TSVVENVCFGQE---LDPPWLERVLEACALQPDVDSFpegihtsIGEQGMNLSGGQKQRLSLARAVY 768
Cdd:PRK13632 86 giiFQNpdnqfigATVEDDIAFGLEnkkVPPKKMKDIIDDLAKKVGMEDY-------LDKEPQNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 769 RKAAVYLLDDPLAALDAHvGQHVFNQVIGPgglLQGT---TRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRK 844
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPK-GKREIKKIMVD---LRKTrkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
641-831 |
2.53e-11 |
|
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: 65.43 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 641 ESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQEAWVQNTSVVenvcFGQELDPP 720
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVV----FGQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 721 WLERVLEACALQPDVDSFPEGIHTS----------IGE----QGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAh 786
Cdd:cd03267 108 WDLPVIDSFYLLAAIYDLPPARFKKrldelselldLEElldtPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV- 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1827346401 787 VGQHVFNQVIGPGGLLQGTTRILVTHALH-ILPQADWIIVLANGAI 831
Cdd:cd03267 187 VAQENIRNFLKEYNRERGTTVLLTSHYMKdIEALARRVLVIDKGRL 232
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
629-830 |
3.18e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 63.33 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAwSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSI--EGAVAYVPQEAWVQNTS 706
Cdd:cd03223 1 IELENLSLA-TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpeGEDLLFLPQRPYLPLGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 707 VVENVCFgqeldpPWlervleacalqpdvdsfpegihtsigeqGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAH 786
Cdd:cd03223 80 LREQLIY------PW----------------------------DDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1827346401 787 VGQHVFNQVigpggLLQGTTRILVTHALHILPQADWIIVLANGA 830
Cdd:cd03223 126 SEDRLYQLL-----KELGITVISVGHRPSLWKFHDRVLDLDGEG 164
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1246-1479 |
3.81e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 67.69 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1246 APWR--LPTCAAQPPWPQggqIEFRDFGLRYrPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGI 1323
Cdd:PRK10522 305 APYKaeFPRPQAFPDWQT---LELRNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1324 WIDGVPIAHVGLHTLRSRISIIPQDPILFPgslRMNLDLLQEHSDEAIWAALETVQLKALVASLPGQLqykcadRGEDLS 1403
Cdd:PRK10522 381 LLDGKPVTAEQPEDYRKLFSAVFTDFHLFD---QLLGPEGKPANPALVEKWLERLKMAHKLELEDGRI------SNLKLS 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1404 VGQKQLLCLARALLRKTQILILDEATAAVDPG------TEL--QMQAMlGSwfaqcTVLLIAHRLRSVMDCARVLVMDKG 1475
Cdd:PRK10522 452 KGQKKRLALLLALAEERDILLLDEWAADQDPHfrrefyQVLlpLLQEM-GK-----TIFAISHDDHYFIHADRLLEMRNG 525
|
....
gi 1827346401 1476 QVAE 1479
Cdd:PRK10522 526 QLSE 529
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
646-779 |
4.29e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.40 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--VAYVPQEA-WVQNTSVVENVCFG-QELDpPW 721
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGlrIGYLPQEPpLDDDLTVLDTVLDGdAELR-AL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 722 LERVLEACALQPDVDSFPE----------------------------GIHTSIGEQGM-NLSGGQKQRLSLARAVYRKAA 772
Cdd:COG0488 93 EAELEELEAKLAEPDEDLErlaelqeefealggweaearaeeilsglGFPEEDLDRPVsELSGGWRRRVALARALLSEPD 172
|
....*..
gi 1827346401 773 VYLLDDP 779
Cdd:COG0488 173 LLLLDEP 179
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1278-1477 |
4.86e-11 |
|
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: 63.22 E-value: 4.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1278 LPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHT-LRSRISIIPQDPI---LFP 1353
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDRKregLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1354 G-SLRMNLDLlqehsdeaiwaaleTVQL------KALVAslpgqlqyKCADRGedlsvgqkqllclarallrkTQILILD 1426
Cdd:cd03215 92 DlSVAENIAL--------------SSLLsggnqqKVVLA--------RWLARD--------------------PRVLILD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 1427 EATAAVDPGTELQMQAMLGSwFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQV 1477
Cdd:cd03215 130 EPTRGVDVGAKAEIYRLIRE-LADagKAVLLISSELDELLGLCdRILVMYEGRI 182
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
646-839 |
5.48e-11 |
|
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: 64.67 E-value: 5.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYVPQEAWV--------QNT------SVVEN 710
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRdITGLPPHRIArlgiartfQNPrlfpelTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 711 V----------CFGQELDPPWL------------ERVLEACALQPDVDsfpegihtsigEQGMNLSGGQKQRLSLARAVY 768
Cdd:COG0411 100 VlvaaharlgrGLLAALLRLPRarreereareraEELLERVGLADRAD-----------EPAGNLSYGQQRRLEIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 769 RKAAVYLLDDPLAALDAHVGQHVfnqvigpGGLLQ------GTTRILVTHALHILPQ-ADWIIVLANGA-IAEmGSYQE 839
Cdd:COG0411 169 TEPKLLLLDEPAAGLNPEETEEL-------AELIRrlrderGITILLIEHDMDLVMGlADRIVVLDFGRvIAE-GTPAE 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
646-841 |
7.21e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 64.39 E-value: 7.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSA--LLGELS----KVeGFVSIEGAVAYVPQEAWV-----------QN---- 704
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCinLLEQPEagtiRV-GDITIDTARSLSQQKGLIrqlrqhvgfvfQNfnlf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 705 --TSVVENVCFGQEL--DPPWLERVLEACALQPDV------DSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVY 774
Cdd:PRK11264 98 phRTVLENIIEGPVIvkGEPKEEATARARELLAKVglagkeTSYPR-----------RLSGGQQQRVAIARALAMRPEVI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 775 LLDDPLAALDAHVGQHVFNQVigpGGLLQ-GTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELL 841
Cdd:PRK11264 167 LFDEPTSALDPELVGEVLNTI---RQLAQeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALF 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
646-814 |
7.85e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 64.03 E-value: 7.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSAL--LGELS---KVEGFVSIEGAVAYVPQEAWVQ---------------NT 705
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNpevTITGSIVYNGHNIYSPRTDTVDlrkeigmvfqqpnpfPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 706 SVVENVCFGQEL----DPPWLERVLEACALQPDV-DSFPEGIHTSigeqGMNLSGGQKQRLSLARAVYRKAAVYLLDDPL 780
Cdd:PRK14239 101 SIYENVVYGLRLkgikDKQVLDEAVEKSLKGASIwDEVKDRLHDS----ALGLSGGQQQRVCIARVLATSPKIILLDEPT 176
|
170 180 190
....*....|....*....|....*....|....
gi 1827346401 781 AALDAHVGQHVFNQVIgpgGLLQGTTRILVTHAL 814
Cdd:PRK14239 177 SALDPISAGKIEETLL---GLKDDYTMLLVTRSM 207
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1281-1489 |
9.26e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 63.95 E-value: 9.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSL---ASGLLrlqEAAEGGIWIDG---VPIAH-VGLH---TLRsrisiipqDPI 1350
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLlklIAGIL---EPTSGRVEVNGrvsALLELgAGFHpelTGR--------ENI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1351 LFPGS-LRMNLDLLQEHSDEAIW-AALE--------------TVQLK-ALVASLPgqlqykcADrgedlsvgqkqllcla 1413
Cdd:COG1134 110 YLNGRlLGLSRKEIDEKFDEIVEfAELGdfidqpvktyssgmRARLAfAVATAVD-------PD---------------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1414 rallrktqILILDEATAAVDPgtELQ------MQAMLGSwfaQCTVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQL 1486
Cdd:COG1134 167 --------ILLVDEVLAVGDA--AFQkkclarIRELRES---GRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEV 233
|
...
gi 1827346401 1487 LAQ 1489
Cdd:COG1134 234 IAA 236
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
646-820 |
9.32e-11 |
|
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: 62.90 E-value: 9.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQEAWVQNT-------------SVVENVC 712
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLlylghapgikttlSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 713 FgqeldppWlervleaCALQPDvdsfpEGIHTSIGEQGMN---------LSGGQKQRLSLARAVYRKAAVYLLDDPLAAL 783
Cdd:cd03231 96 F-------W-------HADHSD-----EQVEEALARVGLNgfedrpvaqLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 1827346401 784 DAHvGQHVFNQVIGpGGLLQGTTRILVTHalHILPQA 820
Cdd:cd03231 157 DKA-GVARFAEAMA-GHCARGGMVVLTTH--QDLGLS 189
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1281-1481 |
1.01e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.13 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLrsrISIIPQD-------PILFP 1353
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSeevdwsfPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1354 GSLRMN-------LDLLQEHSDEAIWAALETVQLkalvaslpgqLQYKCADRGEdLSVGQKQLLCLARALLRKTQILILD 1426
Cdd:PRK15056 99 DVVMMGryghmgwLRRAKKRDRQIVTAALARVDM----------VEFRHRQIGE-LSGGQKKRVFLARAIAQQGQVILLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 1427 EATAAVDPGTELQMQAMLGSWFAQ-CTVLLIAHRLRSVMDCARVLVMDKGQVAESG 1481
Cdd:PRK15056 168 EPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1282-1488 |
1.03e-10 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.51 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1282 VQGVSFKIHAGEKVGIVGRTGAGKS---SLASGLLRlqeAAEGGIWIDGVPIAHVGLHtLRSR--ISIIPQDPILFPG-S 1355
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTttfYMIVGLVK---PDSGRIFLDGEDITHLPMH-KRARlgIGYLPQEASIFRKlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1356 LRMNldllqehsdeaIWAALETVQL-----KALVASLPGQLQ-YKCAD-RGEDLSVGQKQllclarallrKTQI------ 1422
Cdd:COG1137 95 VEDN-----------ILAVLELRKLskkerEERLEELLEEFGiTHLRKsKAYSLSGGERR----------RVEIaralat 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 1423 ----LILDEATAAVDPGTELQMQAM--------LGswfaqctVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQLLA 1488
Cdd:COG1137 154 npkfILLDEPFAGVDPIAVADIQKIirhlkergIG-------VLITDHNVRETLGiCDRAYIISEGKVLAEGTPEEILN 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
644-841 |
1.23e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 63.85 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 644 PCLHRINLTVPQGCLLAVVGPVGAGKSSL---LSALL--------------GELSKVEGFVSIEGAVAYVPQEAWVQNTs 706
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLalhLNGLLrpqkgkvlvsgidtGDFSKLQGIRKLVGIVFQNPETQFVGRT- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 707 VVENVCFGQE---LDPPWLERVLEACALQPDVDSFPegiHTSigeqGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAAL 783
Cdd:PRK13644 95 VEEDLAFGPEnlcLPPIEIRKRVDRALAEIGLEKYR---HRS----PKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1827346401 784 DAHVGQHVFNQVIGPGGllQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELL 841
Cdd:PRK13644 168 DPDSGIAVLERIKKLHE--KGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1292-1481 |
1.27e-10 |
|
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: 62.70 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1292 GEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPI----AHVGLHTLRSRISIIPQDPILFPG-SLRMNLDL-LQE 1365
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFPHlNVRENLAFgLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1366 HSDEAIwaaleTVQLKALVASLpgQLQyKCADRGED-LSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAML 1444
Cdd:cd03297 103 KRNRED-----RISVDELLDLL--GLD-HLLNRYPAqLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1827346401 1445 GSWFA--QCTVLLIAHRLRSV-MDCARVLVMDKGQVAESG 1481
Cdd:cd03297 175 KQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
649-784 |
1.33e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 63.65 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLSAL-----LGELSKVEGFVSIEGAVAYVPQEAWVQ---------------NTSVV 708
Cdd:PRK14243 29 VWLDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYAPDVDPVEvrrrigmvfqkpnpfPKSIY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 709 ENVCFGQ-------ELDPpWLERVLEACALQPDVDSfpegihtSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLA 781
Cdd:PRK14243 109 DNIAYGAringykgDMDE-LVERSLRQAALWDEVKD-------KLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCS 180
|
...
gi 1827346401 782 ALD 784
Cdd:PRK14243 181 ALD 183
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1275-1458 |
1.44e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 62.38 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1275 RPELPLaVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPG 1354
Cdd:TIGR01189 10 RGERML-FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1355 SLRMNLDLLQE-HSDE--AIWAALETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLARALLRKTQILILDEATAA 1431
Cdd:TIGR01189 89 SALENLHFWAAiHGGAqrTIEDALAAVGLTGFEDLPAAQL-----------SAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*...
gi 1827346401 1432 VDP-GTELQMQAMLGSWFAQCTVLLIAH 1458
Cdd:TIGR01189 158 LDKaGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
646-835 |
1.49e-10 |
|
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: 62.94 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYV--PQEAWVQNTSVVENVCFG-------QE 716
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLlgLGGGFNPELTGRENIYLNgrllglsRK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 717 LDPPWLERVLEACALqpdvdsfPEGIHTSIGeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVG---QHVFN 793
Cdd:cd03220 118 EIDEKIDEIIEFSEL-------GDFIDLPVK----TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQekcQRRLR 186
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1827346401 794 QVIgpgglLQGTTRILVTHALHILPQ-ADWIIVLANGAIAEMG 835
Cdd:cd03220 187 ELL-----KQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
649-839 |
1.49e-10 |
|
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: 62.84 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYVPQEAWV--------QNT------SVVENV-- 711
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEdITGLPPHEIArlgigrtfQIPrlfpelTVLENVmv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 712 -CFGQELDPPWL--------------ERVLEACALQPDvdsfpegIHTSIGeqgmNLSGGQKQRLSLARAVYRKAAVYLL 776
Cdd:cd03219 99 aAQARTGSGLLLararreereareraEELLERVGLADL-------ADRPAG----ELSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 777 DDPLAALDAHVGQHVfnqvigpGGLL-----QGTTRILVTHALHILPQ-ADWIIVLANGA-IAEmGSYQE 839
Cdd:cd03219 168 DEPAAGLNPEETEEL-------AELIrelreRGITVLLVEHDMDVVMSlADRVTVLDQGRvIAE-GTPDE 229
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
644-840 |
1.51e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.46 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 644 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------------VAYVPQEAWV-QNTSVV 708
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLfPNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 709 ENVCFGQELDPPWLERVLE-----ACALQPDVdsfpegihtsigeQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAAL 783
Cdd:PRK15439 105 ENILFGLPKRQASMQKMKQllaalGCQLDLDS-------------SAGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 784 DAHVGQHVFNQVigpGGLL-QGTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQEL 840
Cdd:PRK15439 172 TPAETERLFSRI---RELLaQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1265-1459 |
1.62e-10 |
|
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: 61.40 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLrYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLasglLRlqeaAEGGIWidgvPIA--HVGLHTlRSRI 1342
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSL----FR----ALAGLW----PWGsgRIGMPE-GEDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1343 SIIPQDPILFPGSLRmnldllqehsdeaiwaaletvqlkalvaslpGQLQYKCADRgedLSVGQKQLLCLARALLRKTQI 1422
Cdd:cd03223 67 LFLPQRPYLPLGTLR-------------------------------EQLIYPWDDV---LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*..
gi 1827346401 1423 LILDEATAAVDPGTELQMQAMLGSwfAQCTVLLIAHR 1459
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
648-812 |
1.81e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 61.99 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 648 RINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQEAWVQNT-------------SVVENVCFg 714
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENIlylghlpglkpelSALENLHF- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 715 qeldppwlervleacaLQPDVDSFPEGIHTSIGEQGMN---------LSGGQKQRLSLARAVYRKAAVYLLDDPLAALDA 785
Cdd:TIGR01189 97 ----------------WAAIHGGAQRTIEDALAAVGLTgfedlpaaqLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180
....*....|....*....|....*..
gi 1827346401 786 HvGQHVFNQVIGpGGLLQGTTRILVTH 812
Cdd:TIGR01189 161 A-GVALLAGLLR-AHLARGGIVLLTTH 185
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1283-1472 |
2.36e-10 |
|
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: 61.74 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1283 QGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLDL 1362
Cdd:cd03231 17 SGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1363 LQE-HSDEAIWAALETVQLKALVASLPGQlqykcadrgedLSVGQKQLLCLARALLRKTQILILDEATAAVD-PGTELQM 1440
Cdd:cd03231 97 WHAdHSDEQVEEALARVGLNGFEDRPVAQ-----------LSAGQQRRVALARLLLSGRPLWILDEPTTALDkAGVARFA 165
|
170 180 190
....*....|....*....|....*....|...
gi 1827346401 1441 QAMLGSWFAQCTVLLIAHR-LRSVMDCARVLVM 1472
Cdd:cd03231 166 EAMAGHCARGGMVVLTTHQdLGLSEAGARELDL 198
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
649-839 |
2.50e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 64.13 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAV-----------------AYVPQEAWV-QNTSVVEN 710
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgiclppekrriGYVFQDARLfPHYKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 711 VCFG-QELDPPWLERVLEACALQPDVDSFPegihtsigeqgMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQ 789
Cdd:PRK11144 97 LRYGmAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1827346401 790 HVFNqvigpggLLQGTTR-----IL-VTHAL-HILPQADWIIVLANGAIAEMGSYQE 839
Cdd:PRK11144 166 ELLP-------YLERLAReinipILyVSHSLdEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1281-1486 |
2.51e-10 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 63.94 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLasglLR----LQEAAEGGIWIDGVPIAHvgLHTLRSRISIIPQDPILFPG-- 1354
Cdd:COG3839 18 ALKDIDLDIEDGEFLVLLGPSGCGKSTL----LRmiagLEDPTSGEILIGGRDVTD--LPPKDRNIAMVFQSYALYPHmt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1355 -------SLRMNlDLLQEHSDEAIWAALETVQLKALVASLPGQLqykcadrgedlSVGQKQllclarallRKTQILILDE 1427
Cdd:COG3839 92 vyeniafPLKLR-KVPKAEIDRRVREAAELLGLEDLLDRKPKQL-----------SGGQRQrvalgralvREPKVFLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 1428 ATAAVDPG------TEL-QMQAMLGSwfaqcTVLLIAHRLRSVM---DcaRVLVMDKGQVAESGSPAQL 1486
Cdd:COG3839 160 PLSNLDAKlrvemrAEIkRLHRRLGT-----TTIYVTHDQVEAMtlaD--RIAVMNDGRIQQVGTPEEL 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1281-1489 |
2.66e-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: 64.82 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWI----DGVPIAHVGLhTLRSR----ISIIPQDPILF 1352
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGP-DGRGRakryIGILHQEYDLY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1353 PGslRMNLDLLQehsdEAIWAAL--ETVQLKALVASLPGQLQYKCA----DRGED-LSVGQKQLLCLARALLRKTQILIL 1425
Cdd:TIGR03269 378 PH--RTVLDNLT----EAIGLELpdELARMKAVITLKMVGFDEEKAeeilDKYPDeLSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827346401 1426 DEATAAVDPGTELQM-QAMLGSWFA-QCTVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQLLAQ 1489
Cdd:TIGR03269 452 DEPTGTMDPITKVDVtHSILKAREEmEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1282-1492 |
2.70e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 62.72 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1282 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPG-SLR--- 1357
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRelv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1358 -------MNL-DLLQEHSDEAIWAALETVQLKALvaslpgqlqykcADRG-EDLSVGQKQLLCLARALLRKTQILILDEA 1428
Cdd:PRK11231 98 aygrspwLSLwGRLSAEDNARVNQAMEQTRINHL------------ADRRlTDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 1429 TAAVDPGTELQMQAMLGSWFAQC-TVLLIAHRL-RSVMDCARVLVMDKGQVAESGSPAQLLAQKGL 1492
Cdd:PRK11231 166 TTYLDINHQVELMRLMRELNTQGkTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVMTPGLL 231
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
644-814 |
3.28e-10 |
|
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: 65.42 E-value: 3.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 644 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG------------AVAYVPQEAWV-QNTSVVEN 710
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldavrqSLGMCPQHNILfHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 711 VCFGQELD-PPWLERVLEACALQPDVdsfpeGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQ 789
Cdd:TIGR01257 1024 ILFYAQLKgRSWEEAQLEMEAMLEDT-----GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180
....*....|....*....|....*
gi 1827346401 790 HVFNQVIgpgGLLQGTTRILVTHAL 814
Cdd:TIGR01257 1099 SIWDLLL---KYRSGRTIIMSTHHM 1120
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
639-840 |
3.82e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 62.41 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 639 SQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQEAW---------VQN----- 704
Cdd:PRK13633 19 ESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdirnkagmvFQNpdnqi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 705 --TSVVENVCFGQE---LDPPWL-ERV---LEACALQPDVDSFPegiHTsigeqgmnLSGGQKQRLSLARAVYRKAAVYL 775
Cdd:PRK13633 99 vaTIVEEDVAFGPEnlgIPPEEIrERVdesLKKVGMYEYRRHAP---HL--------LSGGQKQRVAIAGILAMRPECII 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 776 LDDPLAALDAHVGQHVFNqVIGPGGLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQEL 840
Cdd:PRK13633 168 FDEPTAMLDPSGRREVVN-TIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
646-843 |
4.18e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 62.51 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-------------VAYVPQEAWVQ--NTSVVEN 710
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfVGLVFQNPDDQifSPTVEQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 711 VCFGQ---ELDPPWLE-RVLEACALQpdvdsfpeGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAH 786
Cdd:PRK13652 100 IAFGPinlGLDEETVAhRVSSALHML--------GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQ 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1827346401 787 VGQHVFnQVIGPGGLLQGTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELLQR 843
Cdd:PRK13652 172 GVKELI-DFLNDLPETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
646-841 |
4.19e-10 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 62.02 E-value: 4.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGF-----------VSIE------GAVAYVPQEAWVQNTSVV 708
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgerrggEDVWelrkriGLVSPALQLRFPRDETVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 709 ENVCFG--------QELDPP-------WLERV-LEACALQPdvdsfpegIHTsigeqgmnLSGGQKQRLSLARAVYRKAA 772
Cdd:COG1119 99 DVVLSGffdsiglyREPTDEqrerareLLELLgLAHLADRP--------FGT--------LSQGEQRRVLIARALVKDPE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 773 VYLLDDPLAALDAHvGQHVFNQVIgpGGLLQ--GTTRILVTHALHILPQA-DWIIVLANGAIAEMGSYQELL 841
Cdd:COG1119 163 LLILDEPTAGLDLG-ARELLLALL--DKLAAegAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVL 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
649-840 |
5.97e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.12 E-value: 5.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLS--ALLGELSKVEGFVS---------IEGAVAYVPQE-AWVQNTSVVENVCFGQE 716
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRmiAGLEDITSGDLFIGekrmndvppAERGVGMVFQSyALYPHLSVAENMSFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 717 L---DPPWLERVLEACA--LQPD--VDSFPEGihtsigeqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQ 789
Cdd:PRK11000 102 LagaKKEEINQRVNQVAevLQLAhlLDRKPKA-----------LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 790 HVFNQVigpgGLLQ---GTTRILVTH-ALHILPQADWIIVLANGAIAEMGSYQEL 840
Cdd:PRK11000 171 QMRIEI----SRLHkrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
646-849 |
7.26e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 63.53 E-value: 7.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSK---VEGFVSIEGAV----------AYVPQ-EAWVQNTSVVENV 711
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPidakemraisAYVQQdDLFIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 712 CFGQEL----DPPWLER------VLEACALQPdvdsfpeGIHTSIGEQGM--NLSGGQKQRLSLARAVYRKAAVYLLDDP 779
Cdd:TIGR00955 121 MFQAHLrmprRVTKKEKrervdeVLQALGLRK-------CANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 780 LAALDAHVGQHVFnQVIgpGGLLQ-GTTRILVTH--ALHILPQADWIIVLANGAIAEMGSYQELLQ--RKGALMC 849
Cdd:TIGR00955 194 TSGLDSFMAYSVV-QVL--KGLAQkGKTIICTIHqpSSELFELFDKIILMAEGRVAYLGSPDQAVPffSDLGHPC 265
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
649-786 |
7.34e-10 |
|
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: 60.75 E-value: 7.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLSALLG---ELSKVEGFVSIEGA----------VAYVPQ-EAWVQNTSVVENVCF- 713
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQprkpdqfqkcVAYVRQdDILLPGLTVRETLTYt 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 714 ----------GQELDPPWLERVLEACAlqpdvdsfpegiHTSIGEQGM-NLSGGQKQRLSLARAVYRKAAVYLLDDPLAA 782
Cdd:cd03234 106 ailrlprkssDAIRKKRVEDVLLRDLA------------LTRIGGNLVkGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
....
gi 1827346401 783 LDAH 786
Cdd:cd03234 174 LDSF 177
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
649-840 |
8.83e-10 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 60.46 E-value: 8.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG------------AVAYVPQEAWVQNT-SVVENV-CFG 714
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGWENLyIHA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 715 QELDPPWLER------VLEACALQPDVDsfpegihtsigEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVG 788
Cdd:cd03265 99 RLYGVPGAERrerideLLDFVGLLEAAD-----------RLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 789 QHVFnQVIGPGGLLQGTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQEL 840
Cdd:cd03265 168 AHVW-EYIEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
434-829 |
9.65e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 62.90 E-value: 9.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 434 LVWIVVCFVylwqLLGpsalTAIAVFLS--LLPLNFfiskkrnhhqEEQMRQKDSRARLTSsILRNSKTIKFHGWEGA-- 509
Cdd:COG4178 184 MVWAALIYA----IIG----TLLTHLIGrpLIRLNF----------EQQRREADFRFALVR-VRENAESIALYRGEAAer 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 510 -----FLDRVLG-----IRGQelgaLRTSGLLFSVSLVSFQVSTFLVALVVFA-------VHTLVAenamnaekAFvtlt 572
Cdd:COG4178 245 rrlrrRFDAVIAnwrrlIRRQ----RNLTFFTTGYGQLAVIFPILVAAPRYFAgeitlggLMQAAS--------AF---- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 573 vlNILNKAQAFLPFSIHSLVQARVSFDRLVTFL-CLEEVDPgVVDSSSSGSAAGKDCITIHSATFAwSQESPPCLHRINL 651
Cdd:COG4178 309 --GQVQGALSWFVDNYQSLAEWRATVDRLAGFEeALEAADA-LPEAASRIETSEDGALALEDLTLR-TPDGRPLLEDLSL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 652 TVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSI--EGAVAYVPQEAWVQNTSVVENVCFGQ---ELDPPWLERVL 726
Cdd:COG4178 385 SLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQRPYLPLGTLREALLYPAtaeAFSDAELREAL 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 727 EACALQPDVDSFPEGIHTSigeqgMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVIgpgGLLQGTT 806
Cdd:COG4178 465 EAVGLGHLAERLDEEADWD-----QVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR---EELPGTT 536
|
410 420
....*....|....*....|...
gi 1827346401 807 RILVTHALHILPQADWIIVLANG 829
Cdd:COG4178 537 VISVGHRSTLAAFHDRVLELTGD 559
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1271-1372 |
1.05e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 62.74 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1271 GLRYRPELPL-AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSR-ISIIPQD 1348
Cdd:COG3845 262 NLSVRDDRGVpALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPED 341
|
90 100
....*....|....*....|....*...
gi 1827346401 1349 PI---LFPG-SLRMNLdLLQEHSDEAIW 1372
Cdd:COG3845 342 RLgrgLVPDmSVAENL-ILGRYRRPPFS 368
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
646-831 |
1.09e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 60.66 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG--------------AVAYVPQEAWV-QNTSVVEN 710
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditdwqtakimreAVAIVPEGRRVfSRMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 711 VCFG-----QELDPPWLERVLeacalqpdvDSFPEgIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDA 785
Cdd:PRK11614 101 LAMGgffaeRDQFQERIKWVY---------ELFPR-LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1827346401 786 HVGQHVFNQVigPGGLLQGTTRILV-THALHILPQADWIIVLANGAI 831
Cdd:PRK11614 171 IIIQQIFDTI--EQLREQGMTIFLVeQNANQALKLADRGYVLENGHV 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
646-843 |
1.14e-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: 62.90 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGelskVEGFVSIEGA----VAYVPQEAWVQNTSVVENVC--FGQELDP 719
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRG----MDQYEPTSGRiiyhVALCEKCGYVERPSKVGEPCpvCGGTLEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 720 P----W------------------------------LERVLEAC---------ALQPDVDSFpEGIHTS--IGEQGMNLS 754
Cdd:TIGR03269 92 EevdfWnlsdklrrrirkriaimlqrtfalygddtvLDNVLEALeeigyegkeAVGRAVDLI-EMVQLShrITHIARDLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 755 GGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVIgPGGLLQGTTRILVTHALHILPQ-ADWIIVLANGAIAE 833
Cdd:TIGR03269 171 GGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALE-EAVKASGISMVLTSHWPEVIEDlSDKAIWLENGEIKE 249
|
250
....*....|
gi 1827346401 834 MGSYQELLQR 843
Cdd:TIGR03269 250 EGTPDEVVAV 259
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1285-1500 |
1.14e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 63.64 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1285 VSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDgvpiahvglhtlRSrISIIPQDPILFPGSLRMNLDLLQ 1364
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE------------RS-IAYVPQQAWIMNATVRGNILFFD 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1365 EHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGT-ELQMQAM 1443
Cdd:PTZ00243 746 EEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgERVVEEC 825
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1827346401 1444 LGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQlLAQKGLFYRLAQES 1500
Cdd:PTZ00243 826 FLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSAD-FMRTSLYATLAAEL 881
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1280-1469 |
1.51e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 60.57 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1280 LAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQE-----AAEGGIWIDGVPI--AHVGLHTLRSRISIIPQDPILF 1352
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1353 PGSLRMNLDL------LQEHSDEAIWAALETvqlkalvASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILD 1426
Cdd:PRK14243 104 PKSIYDNIAYgaringYKGDMDELVERSLRQ-------AALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1827346401 1427 EATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVmdcARV 1469
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQA---ARV 216
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
655-784 |
1.92e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.13 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 655 QGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQ----------EAWV-QNTSVVENVCFGQEL-DPPWL 722
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQyikpdydgtvEDLLrSITDDLGSSYYKSEIiKPLQL 443
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 723 ERVLEAcalqpDVDsfpegihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 784
Cdd:PRK13409 444 ERLLDK-----NVK---------------DLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1281-1489 |
1.94e-09 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 61.32 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLasglLR----LQEAAEGGIWIDGVpIAHVGLHTLRSRISIIPQDPILFP--- 1353
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTL----LRiiagLETPDSGRIVLNGR-DLFTNLPPRERRVGFVFQHYALFPhmt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1354 -------GsLRMnldllQEHSDEAI------WaaLETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLARALLRKT 1420
Cdd:COG1118 92 vaeniafG-LRV-----RPPSKAEIrarveeL--LELVQLEGLADRYPSQL-----------SGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 1421 QILILDEATAAVDPGTELQMQAMLGSWFA--QCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQ 1489
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRRLHDelGGTTVFVTHDQEEALELAdRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1266-1440 |
2.09e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 59.03 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1266 EFRDFGLRYRPElPLaVQGVSFKIHAGEKVGIVGRTGAGKSSLAS---GLLRLQEAAEGGIWIDGVPIAHvgLHTLRSRI 1342
Cdd:COG4136 3 SLENLTITLGGR-PL-LAPLSLTVAPGEILTLMGPSGSGKSTLLAaiaGTLSPAFSASGEVLLNGRRLTA--LPAEQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1343 SIIPQDPILFP-----GSLRMNL--DLLQEHSDEAIWAALETVQLKALVASLPGQlqykcadrgedLSVGQKQLLCLARA 1415
Cdd:COG4136 79 GILFQDDLLFPhlsvgENLAFALppTIGRAQRRARVEQALEEAGLAGFADRDPAT-----------LSGGQRARVALLRA 147
|
170 180
....*....|....*....|....*
gi 1827346401 1416 LLRKTQILILDEATAAVDPGTELQM 1440
Cdd:COG4136 148 LLAEPRALLLDEPFSKLDAALRAQF 172
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
646-840 |
2.13e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 60.09 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYvpqeawvQNTSVVE-----NVCFGQELDP 719
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpIKY-------DKKSLLEvrktvGIVFQNPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 720 PWLERVLEACALQP-----DVDSFPEGIHTSIGEQGM---------NLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDA 785
Cdd:PRK13639 91 LFAPTVEEDVAFGPlnlglSKEEVEKRVKEALKAVGMegfenkpphHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 786 HVGQHVFNqvigpggLL-----QGTTRILVTHALHILP-QADWIIVLANGAIAEMGSYQEL 840
Cdd:PRK13639 171 MGASQIMK-------LLydlnkEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEV 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
646-831 |
2.36e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 60.10 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYVPQE---AWV----QNT--------SVVE 709
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdVTKLPEYkraKYIgrvfQDPmmgtapsmTIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 710 NVC----------FGQELDPPWLERVLEACAlqpdvdSFPEG----IHTSIGeqgmNLSGGQKQRLSLARAVYRKAAVYL 775
Cdd:COG1101 102 NLAlayrrgkrrgLRRGLTKKRRELFRELLA------TLGLGlenrLDTKVG----LLSGGQRQALSLLMATLTKPKLLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 776 LDDPLAALDAHVGQHVF---NQVIGPGGLlqgTTrILVTHALHilpQA----DWIIVLANGAI 831
Cdd:COG1101 172 LDEHTAALDPKTAALVLeltEKIVEENNL---TT-LMVTHNME---QAldygNRLIMMHEGRI 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
626-853 |
2.90e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 59.75 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 626 KDCITIHSATFAWSQESP-PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAvAYVPQEAW--- 701
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-LLTEENVWdir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 702 ------VQN-------TSVVENVCFG--------QELdppwLERVLEACALQpDVDSFPEgihtsigEQGMNLSGGQKQR 760
Cdd:PRK13650 81 hkigmvFQNpdnqfvgATVEDDVAFGlenkgiphEEM----KERVNEALELV-GMQDFKE-------REPARLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 761 LSLARAVYRKAAVYLLDDPLAALDahvgqhvfnqvigPGGLLQ------------GTTRILVTHALHILPQADWIIVLAN 828
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLD-------------PEGRLEliktikgirddyQMTVISITHDLDEVALSDRVLVMKN 215
|
250 260
....*....|....*....|....*.
gi 1827346401 829 GAIAEMGSYQELLQRKGALMCL-LDQ 853
Cdd:PRK13650 216 GQVESTSTPRELFSRGNDLLQLgLDI 241
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
649-829 |
3.09e-09 |
|
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: 58.45 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA---------VAYVPQE-AWVQNTSVVEN-VCFGQ-- 715
Cdd:cd03269 19 ISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarnrIGYLPEErGLYPKMKVIDQlVYLAQlk 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 716 ---------ELDpPWLERV-LEACALQPDvdsfpegihtsigEQgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDA 785
Cdd:cd03269 99 glkkeearrRID-EWLERLeLSEYANKRV-------------EE---LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1827346401 786 hVGQHVFNQVIGPggLL-QGTTRILVTHAL-HILPQADWIIVLANG 829
Cdd:cd03269 162 -VNVELLKDVIRE--LArAGKTVILSTHQMeLVEELCDRVLLLNKG 204
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1271-1489 |
3.11e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.26 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1271 GLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAA-----EGGIWIDGVPIAHVGLHTLR----SR 1341
Cdd:PRK15134 14 AFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRgvrgNK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1342 ISIIPQDPI--LFP---------GSLRMNLDLLQEHSDEAIWAALETVQLKalvaslpgQLQYKCADRGEDLSVGQKQLL 1410
Cdd:PRK15134 94 IAMIFQEPMvsLNPlhtlekqlyEVLSLHRGMRREAARGEILNCLDRVGIR--------QAAKRLTDYPHQLSGGERQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1411 CLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQC--TVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLL 1487
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELnmGLLFITHNLSIVRKLAdRVAVMQNGRCVEQNRAATLF 245
|
..
gi 1827346401 1488 AQ 1489
Cdd:PRK15134 246 SA 247
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1275-1486 |
3.22e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.41 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1275 RPELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVpiahvgLHTLRSR------------- 1341
Cdd:PRK10261 26 QQKIA-AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKM------LLRRRSRqvielseqsaaqm 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1342 -------ISIIPQDPI-----LFP------GSLRMNLDLLQEHSDEAIWAALETVQL---KALVASLPGQlqykcadrge 1400
Cdd:PRK10261 99 rhvrgadMAMIFQEPMtslnpVFTvgeqiaESIRLHQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQ---------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1401 dLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTE---LQMQAMLGSWFAQcTVLLIAHRLRSVMDCA-RVLVMDKGQ 1476
Cdd:PRK10261 169 -LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQaqiLQLIKVLQKEMSM-GVIFITHDMGVVAEIAdRVLVMYQGE 246
|
250
....*....|
gi 1827346401 1477 VAESGSPAQL 1486
Cdd:PRK10261 247 AVETGSVEQI 256
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1281-1486 |
3.34e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 60.62 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHtlRSRISIIPQDPILFPG-SLRMN 1359
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPINMMFQSYALFPHmTVEQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1360 L--DLLQEHsdeaiwaaLETVQLKALVASLPG--QLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPG 1435
Cdd:PRK11607 112 IafGLKQDK--------LPKAEIASRVNEMLGlvHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 1436 TELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQL 1486
Cdd:PRK11607 184 LRDRMQLEVVDILERvgVTCVMVTHDQEEAMTMAgRIAIMNRGKFVQIGEPEEI 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1283-1354 |
3.77e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 61.23 E-value: 3.77e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 1283 QGVSFKIHAGEKVGIVGRTGAGKSSlasgLLRL---QEAAEGG-IWIDGvpiahvGLhtlrsRISIIPQDPILFPG 1354
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKST----LLKIlagELEPDSGeVSIPK------GL-----RIGYLPQEPPLDDD 75
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1285-1480 |
4.07e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.83 E-value: 4.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1285 VSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHT-LRSRISIIPQDP----ILFPGSLRMN 1359
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDRqssgLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1360 LDLLQeHSDEAIWaaLETVQLKALVASLPGQLQYKCADRGED---LSVGQKQLLCLARALLRKTQILILDEATAAVDPGT 1436
Cdd:PRK15439 362 VCALT-HNRRGFW--IKPARENAVLERYRRALNIKFNHAEQAartLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1827346401 1437 ELQMQAMLGSWFAQCT-VLLIAHRLRSVMDCA-RVLVMDKGQVAES 1480
Cdd:PRK15439 439 RNDIYQLIRSIAAQNVaVLFISSDLEEIEQMAdRVLVMHQGEISGA 484
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
646-831 |
4.32e-09 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 57.44 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------------VAYVP----QEAWVQNTSV 707
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairagIAYVPedrkREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 708 VENVCFGQELdppwlervleacalqpdvdsfpegihtsigeqgmnlSGGQKQRLSLARAVYRKAAVYLLDDPLAALDahV 787
Cdd:cd03215 96 AENIALSSLL------------------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGVD--V 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1827346401 788 G--QHVFNQVIgpggLL--QGTTRILVTHALH-ILPQADWIIVLANGAI 831
Cdd:cd03215 138 GakAEIYRLIR----ELadAGKAVLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1282-1477 |
4.59e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.71 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1282 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLL-RLQEAAEGGIWIDGVPIA-HVGLHTLRSRISIIPQD-------PILF 1352
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFgAYPGRWEGEIFIDGKPVKiRNPQQAIAQGIAMVPEDrkrdgivPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1353 PGSlRMNLDLLQEHSD-EAIWAALEtvqLKALVASLpGQLQYKCAD---RGEDLSVGQKQLLCLARALLRKTQILILDEA 1428
Cdd:PRK13549 358 VGK-NITLAALDRFTGgSRIDDAAE---LKTILESI-QRLKVKTASpelAIARLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 1429 TAAVDPGTELQMQAMLGSWFAQ-CTVLLIAHRLRSVMD-CARVLVMDKGQV 1477
Cdd:PRK13549 433 TRGIDVGAKYEIYKLINQLVQQgVAIIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1282-1487 |
4.89e-09 |
|
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: 58.50 E-value: 4.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1282 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAhvGLHTLRSRISIIPQDPILFPG------- 1354
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFPHmtvykni 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1355 --SLRMNLDLLQEHSDEAIWAAlETVQLKALVASLPgqlqykcadrgEDLSVGQKQLLCLARALLRKTQILILDEATAAV 1432
Cdd:cd03299 93 ayGLKKRKVDKKEIERKVLEIA-EMLGIDHLLNRKP-----------ETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1827346401 1433 DPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLL 1487
Cdd:cd03299 161 DVRTKEKLREELKKIRKEfgVTVLHVTHDFEEAWALAdKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
973-1235 |
5.22e-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: 59.10 E-value: 5.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 973 DDPAVGGQQTQAALRGGIFGLLGCLQAI-GLFASMAAVLLGGARASRL---LFQRLLwdvvRSPISFFERTPIGHLLNRF 1048
Cdd:cd07346 27 DDVIPAGDLSLLLWIALLLLLLALLRALlSYLRRYLAARLGQRVVFDLrrdLFRHLQ----RLSLSFFDRNRTGDLMSRL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1049 SKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLLYAGFQSLYVVSSCQLRRLESASYSSVCSHMA 1128
Cdd:cd07346 103 TSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1129 ETFQGSTVVRAFRTQ----APFVAQNNARVDESQRISfprlvadRWLAANVELLgnGLVFAAATCAVL-------SKAHL 1197
Cdd:cd07346 183 ESLSGIRVVKAFAAEereiERFREANRDLRDANLRAA-------RLSALFSPLI--GLLTALGTALVLlyggylvLQGSL 253
|
250 260 270
....*....|....*....|....*....|....*....
gi 1827346401 1198 SAG-LVGFsVSAALQVTQTLQWVVRNWTDLENSIVSVER 1235
Cdd:cd07346 254 TIGeLVAF-LAYLGMLFGPIQRLANLYNQLQQALASLER 291
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1281-1482 |
5.32e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 59.74 E-value: 5.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQeAAEG---------GIWIDGVPIAHvgLHTLRS-RISIIPQDPI 1350
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGriggsatfnGREILNLPEKE--LNKLRAeQISMIFQDPM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1351 --LFP----GSLRMNLDLLQEHSDEAIwAALETVQLKALVaSLPgQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILI 1424
Cdd:PRK09473 108 tsLNPymrvGEQLMEVLMLHKGMSKAE-AFEESVRMLDAV-KMP-EARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 1425 LDEATAAVDpgTELQMQAM-----LGSWFaQCTVLLIAHRLRSVMD-CARVLVMDKGQVAESGS 1482
Cdd:PRK09473 185 ADEPTTALD--VTVQAQIMtllneLKREF-NTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGN 245
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
646-826 |
5.68e-09 |
|
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: 58.78 E-value: 5.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLL---------SALLGELSKVEGFVSIEGA-----VAYVPQEAWVQN------- 704
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalaRRLHLKKEQPGNHDRIEGLehidkVIVIDQSPIGRTprsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 705 -TSVVE-------NVCFGQELDPPWLE---------RVL-----EACALQPDVDSFPEGIHT---------SIGEQGMNL 753
Cdd:cd03271 91 yTGVFDeirelfcEVCKGKRYNRETLEvrykgksiaDVLdmtveEALEFFENIPKIARKLQTlcdvglgyiKLGQPATTL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 754 SGGQKQRLSLARAVYRKA---AVYLLDDPLAALDAHVGQH---VFNQVIGpggllQGTTRILVTHALHILPQADWIIVL 826
Cdd:cd03271 171 SGGEAQRIKLAKELSKRStgkTLYILDEPTTGLHFHDVKKlleVLQRLVD-----KGNTVVVIEHNLDVIKCADWIIDL 244
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1281-1481 |
5.75e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.64 E-value: 5.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG---LHTLRSRISIIPQDP-------- 1349
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPyasldprq 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1350 -----ILFPgsLRMNLDLLQEHSDEAIWAALETVQLKALVAslpgqLQYKcadrgEDLSVGQKQLLCLARALLRKTQILI 1424
Cdd:PRK10261 419 tvgdsIMEP--LRVHGLLPGKAAAARVAWLLERVGLLPEHA-----WRYP-----HEFSGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 1425 LDEATAAVDPGTE-------LQMQAMLGSWFaqctvLLIAHRLRSVMDCA-RVLVMDKGQVAESG 1481
Cdd:PRK10261 487 ADEAVSALDVSIRgqiinllLDLQRDFGIAY-----LFISHDMAVVERIShRVAVMYLGQIVEIG 546
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
646-784 |
7.07e-09 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 57.94 E-value: 7.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------------VAYVPQEAWV-QNTSVVEN 710
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarlgIGYLPQEASIfRKLTVEEN 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 711 V-CFGQELDPPWLERVLEACALqpdVDSFpeGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 784
Cdd:cd03218 96 IlAVLEIRGLSKKEREEKLEEL---LEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
647-851 |
7.34e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 58.46 E-value: 7.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 647 HRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--VAYVPQEA------WVQNTS------VVENVC 712
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiQHYASKEVarriglLAQNATtpgditVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 713 FGQELDPPWLERvleacALQPDVDSFPEGIH----TSIGEQGMN-LSGGQKQRLSLARAVYRKAAVYLLDDPLAALD-AH 786
Cdd:PRK10253 104 RGRYPHQPLFTR-----WRKEDEEAVTKAMQatgiTHLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDiSH 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 787 vgQHVFNQVIGPGGLLQGTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQE-----LLQRKGALMCLL 851
Cdd:PRK10253 179 --QIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEivtaeLIERIYGLRCMI 247
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1265-1487 |
7.39e-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: 58.17 E-value: 7.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELPLavQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGG-IWIDGVPIAHVGLHTLRSRIS 1343
Cdd:COG1119 4 LELRNVTVRRGGKTIL--DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1344 IIpqDPIL---FPGSLRM----------NLDLLQEHSDEAI---WAALETVQLKALvaslpgqlqykcADRG-EDLSVGQ 1406
Cdd:COG1119 82 LV--SPALqlrFPRDETVldvvlsgffdSIGLYREPTDEQReraRELLELLGLAHL------------ADRPfGTLSQGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1407 KQllclarallrKTQI----------LILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDC-ARVLVMD 1473
Cdd:COG1119 148 QR----------RVLIaralvkdpelLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEIPPGiTHVLLLK 217
|
250
....*....|....
gi 1827346401 1474 KGQVAESGSPAQLL 1487
Cdd:COG1119 218 DGRVVAAGPKEEVL 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1283-1462 |
8.96e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 57.19 E-value: 8.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1283 QGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIahvGLHTLRSRISII-PQD---PILfpgSLRM 1358
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHYLgHRNamkPAL---TVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1359 NLDLLQE---HSDEAIWAALETVQLkALVASLPGQlqykcadrgeDLSVGQKQLLCLARALLRKTQILILDEATAAVDPG 1435
Cdd:PRK13539 93 NLEFWAAflgGEELDIAAALEAVGL-APLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
170 180
....*....|....*....|....*..
gi 1827346401 1436 TelqmQAMLGSwfaqctvlLIAHRLRS 1462
Cdd:PRK13539 162 A----VALFAE--------LIRAHLAQ 176
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
646-785 |
1.01e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.56 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGelskV------EGFVSIEGA--------------VAYVPQE-AWVQN 704
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG----VyphgtyEGEIIFEGEelqasnirdteragIAIIHQElALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 705 TSVVENVCFGQELDP----PWLERVLEACALQPDVdsfpeGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPL 780
Cdd:PRK13549 97 LSVLENIFLGNEITPggimDYDAMYLRAQKLLAQL-----KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
....*
gi 1827346401 781 AALDA 785
Cdd:PRK13549 172 ASLTE 176
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
629-844 |
1.08e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 58.25 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSQESP---PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIE--------------- 690
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDditithktkdkyirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 691 -----GAVAYVPqEAWVQNTSVVENVCFGQELDPPWLERVLE-ACALQPDVdSFPEGIHTSIGEQgmnLSGGQKQRLSLA 764
Cdd:PRK13646 83 vrkriGMVFQFP-ESQLFEDTVEREIIFGPKNFKMNLDEVKNyAHRLLMDL-GFSRDVMSQSPFQ---MSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 765 RAVYRKAAVYLLDDPLAALDAHVGQHVFnQVIGPGGLLQGTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELLQR 843
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVM-RLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKD 236
|
.
gi 1827346401 844 K 844
Cdd:PRK13646 237 K 237
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1265-1479 |
1.09e-08 |
|
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: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRY-RPELPLAV-QGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHV---GLHTLR 1339
Cdd:COG4181 9 IELRGLTKTVgTGAGELTIlKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedARARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1340 SR-ISIIPQDPILFPgSLRM--NLDL---LQEHSD--EAIWAALETVQLKALVASLPGQlqykcadrgedLSVGQKQLLC 1411
Cdd:COG4181 89 ARhVGFVFQSFQLLP-TLTAleNVMLpleLAGRRDarARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 1412 LARALLRKTQILILDEATAAVDPGTELQMQAMLgswFA-----QCTVLLIAHRLRSVMDCARVLVMDKGQVAE 1479
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATGEQIIDLL---FElnrerGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
646-843 |
1.22e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 58.55 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLS--ALLGELSkvEGFVSIEGA----------------VAYVPQEAwvqN--- 704
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRciNLLERPT--SGSVLVDGVdltalserelraarrkIGMIFQHF---Nlls 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 705 --TsVVENVCF-----G----------QELdppwLERV-LEACAlqpdvDSFPEgihtsigeqgmNLSGGQKQRLSLARA 766
Cdd:COG1135 96 srT-VAENVALpleiaGvpkaeirkrvAEL----LELVgLSDKA-----DAYPS-----------QLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 767 VYRKAAVYLLDDPLAALDAHVGQHVFNqvigpggLLQ------GTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQE 839
Cdd:COG1135 155 LANNPKVLLCDEATSALDPETTRSILD-------LLKdinrelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVLD 227
|
....
gi 1827346401 840 LLQR 843
Cdd:COG1135 228 VFAN 231
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1267-1493 |
1.23e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 57.94 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1267 FRDFGLRYRPELplavQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGgiwidgvPIAHVGlhtlrsRISIIP 1346
Cdd:cd03291 42 FSNLCLVGAPVL----KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG-------KIKHSG------RISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1347 QDPILFPGSLRMNLDLLQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILD 1426
Cdd:cd03291 105 QFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827346401 1427 EATAAVDPGTELQM-QAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLF 1493
Cdd:cd03291 185 SPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDF 252
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
659-784 |
1.38e-08 |
|
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: 59.41 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 659 LAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQ------EAWVQntSVVENVCfGQELDPPWLE-RVLEACAL 731
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQyispdyDGTVE--EFLRSAN-TDDFGSSYYKtEIIKPLGL 445
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 732 QPDVDSfpegihtSIGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 784
Cdd:COG1245 446 EKLLDK-------NVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
658-784 |
1.47e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 57.42 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 658 LLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYVPQEAWVQNTSVVENVCFGQeldppwLERVLEACALQPDVD 736
Cdd:cd03237 27 VIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDtVSYKPQYIKADYEGTVRDLLSSI------TKDFYTHPYFKTEIA 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1827346401 737 SfPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 784
Cdd:cd03237 101 K-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
646-842 |
1.61e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 57.49 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-------------VAYVPQE-AWVQNTSVVENV 711
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafarkVAYLPQQlPAAEGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 712 CFGQEldpPW-----------LERVLEACAL-------QPDVDSfpegihtsigeqgmnLSGGQKQRLSLARAVYRKAAV 773
Cdd:PRK10575 107 AIGRY---PWhgalgrfgaadREKVEEAISLvglkplaHRLVDS---------------LSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 774 YLLDDPLAALD-AHvgQHVFNQVIGPGGLLQGTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELLQ 842
Cdd:PRK10575 169 LLLDEPTSALDiAH--QVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMR 237
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1268-1477 |
1.69e-08 |
|
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: 56.96 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1268 RDFGLRYRPELPlAVQGVSFKIHAGEKVGIVGRTGAGKSS---LASGLLRlqeAAEGGIWIDG-VP----IAHVglhtlr 1339
Cdd:cd03267 24 KSLFKRKYREVE-ALKGISFTIEKGEIVGFIGPNGAGKTTtlkILSGLLQ---PTSGEVRVAGlVPwkrrKKFL------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1340 SRISII------------PQDpilfpgSLRMNLDLLQEHSDEAiwaaleTVQLKALVASLP-GQLQYKCADRgedLSVGQ 1406
Cdd:cd03267 94 RRIGVVfgqktqlwwdlpVID------SFYLLAAIYDLPPARF------KKRLDELSELLDlEELLDTPVRQ---LSLGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 1407 KQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFA--QCTVLLIAHRLRSVMDCA-RVLVMDKGQV 1477
Cdd:cd03267 159 RMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRerGTTVLLTSHYMKDIEALArRVLVIDKGRL 232
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1276-1475 |
2.11e-08 |
|
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: 56.19 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1276 PELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSR----ISIIPQDPIL 1351
Cdd:cd03290 12 SGLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1352 FPGSLRMNLDLLQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAA 1431
Cdd:cd03290 91 LNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1827346401 1432 VDPG-TELQMQAMLGSWFA--QCTVLLIAHRLRSVMDCARVLVMDKG 1475
Cdd:cd03290 171 LDIHlSDHLMQEGILKFLQddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
629-839 |
2.73e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 56.98 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSQESP---PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------- 691
Cdd:PRK13637 3 IKIENLTHIYMEGTPfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 692 -AVAYVPQ--EAWVQNTSVVENVCFG-QEL---DPPWLERVLEACAL-QPDVDSFPEgihtsigEQGMNLSGGQKQRLSL 763
Cdd:PRK13637 83 kKVGLVFQypEYQLFEETIEKDIAFGpINLglsEEEIENRVKRAMNIvGLDYEDYKD-------KSPFELSGGQKRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 764 ARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVigpgGLLQ---GTTRILVTHALH-ILPQADWIIVLANGAIAEMGSYQE 839
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKI----KELHkeyNMTIILVSHSMEdVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1282-1487 |
2.97e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 57.93 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1282 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPilfpgSLRMNLD 1361
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDT-----SLSFEFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1362 LLQ-------------EHSDEAIWAALETVQLKALVASLpgqlqykcADRGED-LSVGQKQLLCLARALLRKTQILILDE 1427
Cdd:PRK09536 94 VRQvvemgrtphrsrfDTWTETDRAAVERAMERTGVAQF--------ADRPVTsLSGGERQRVLLARALAQATPVLLLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 1428 ATAAVDPGTELQMQAMLGSWFAQC-TVLLIAHRLR-SVMDCARVLVMDKGQVAESGSPAQLL 1487
Cdd:PRK09536 166 PTASLDINHQVRTLELVRRLVDDGkTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
646-817 |
3.14e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 56.28 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--VAYVPQEAWVQNTSVVENVCFGQeLDP---- 719
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlrIGYVPQKLYLDTTLPLTVNRFLR-LRPgtkk 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 720 ----PWLERVLEACALQpdvdsfpegihtsigeQGMN-LSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHvGQHVFNQ 794
Cdd:PRK09544 99 edilPALKRVQAGHLID----------------APMQkLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN-GQVALYD 161
|
170 180
....*....|....*....|...
gi 1827346401 795 VIGPGGLLQGTTRILVTHALHIL 817
Cdd:PRK09544 162 LIDQLRRELDCAVLMVSHDLHLV 184
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1281-1478 |
3.38e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.11 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDG--VPIAHVGlHTLRSRISIIPQDpilfpgslRM 1358
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPR-DAIRAGIAYVPED--------RK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1359 NLDLLQEHS--DEAIWAALETV---------QLKALVASLPGQLQYKCADRGE---DLSVGQKQllclarallrK----- 1419
Cdd:COG1129 338 GEGLVLDLSirENITLASLDRLsrgglldrrRERALAEEYIKRLRIKTPSPEQpvgNLSGGNQQ----------Kvvlak 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 1420 -----TQILILDEATAAVDPGTELQMQAMLGSwFAQ--CTVLLIAhrlrSVMD-----CARVLVMDKGQVA 1478
Cdd:COG1129 408 wlatdPKVLILDEPTRGIDVGAKAEIYRLIRE-LAAegKAVIVIS----SELPellglSDRILVMREGRIV 473
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
629-847 |
3.45e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 56.68 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIE----------------GA 692
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNnqaitddnfeklrkhiGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 693 VAYVPQEAWVQNTsVVENVCFGQELDP-PWLERVLEACALQPDVDSFPEGIHtsigeQGMNLSGGQKQRLSLARAVYRKA 771
Cdd:PRK13648 88 VFQNPDNQFVGSI-VKYDVAFGLENHAvPYDEMHRRVSEALKQVDMLERADY-----EPNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 772 AVYLLDDPLAALDAHVGQHVFNQVigpgGLLQGT---TRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGAL 847
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLV----RKVKSEhniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1282-1489 |
4.14e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 56.13 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1282 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHV-------------GLHTLRSRISIIPQD 1348
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1349 PILFpgSLRMNLDLLQEHSDEAIWAALETVQLKALV----ASLPGQLQYKCAdrgEDLSVGQKQLLCLARALLRKTQILI 1424
Cdd:PRK10619 101 FNLW--SHMTVLENVMEAPIQVLGLSKQEARERAVKylakVGIDERAQGKYP---VHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 1425 LDEATAAVDP---GTELQMQAMLGSwfAQCTVLLIAHRlrsvMDCAR-----VLVMDKGQVAESGSPAQLLAQ 1489
Cdd:PRK10619 176 FDEPTSALDPelvGEVLRIMQQLAE--EGKTMVVVTHE----MGFARhvsshVIFLHQGKIEEEGAPEQLFGN 242
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1280-1486 |
4.85e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 55.77 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1280 LAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLrSRISIIP--QDPILFPgslR 1357
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVRtfQHVRLFR---E 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1358 M----NLdLLQEH--------------------SDEAI-WAA--LETVQLKALVASLPGQLQYkcadrgedlsvGQKQLL 1410
Cdd:PRK11300 95 MtvieNL-LVAQHqqlktglfsgllktpafrraESEALdRAAtwLERVGLLEHANRQAGNLAY-----------GQQRRL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 1411 CLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQL 1486
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhnVTVLLIEHDMKLVMGISdRIYVVNQGTPLANGTPEEI 241
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1260-1440 |
4.89e-08 |
|
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: 57.84 E-value: 4.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1260 PQGGQIEFRDFGLRYRpELPLA-------VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLlrlqeaaeGGIWidgvPIaH 1332
Cdd:TIGR00954 440 PGRGIVEYQDNGIKFE-NIPLVtpngdvlIESLSFEVPSGNNLLICGPNGCGKSSLFRIL--------GELW----PV-Y 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1333 VGLHTL--RSRISIIPQDPILFPGSLR------MNLDLLQEH--SDEAIWAALETVQLKALVASLPGQlqYKCADRGEDL 1402
Cdd:TIGR00954 506 GGRLTKpaKGKLFYVPQRPYMTLGTLRdqiiypDSSEDMKRRglSDKDLEQILDNVQLTHILEREGGW--SAVQDWMDVL 583
|
170 180 190
....*....|....*....|....*....|....*...
gi 1827346401 1403 SVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQM 1440
Cdd:TIGR00954 584 SGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYM 621
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
629-835 |
5.07e-08 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 55.07 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSQESPPC--LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-AVAYVPQEAwVQNT 705
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEA-RRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 706 SVVenvcFGQELDPPWL---ERV--------LEACALQPDVDSFPE--GIHTSIGEQGMNLSGGQKQRLSLARAVYRKAA 772
Cdd:cd03266 81 GFV----SDSTGLYDRLtarENLeyfaglygLKGDELTARLEELADrlGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 773 VYLLDDPLAALDAhVGQHVFNQVIGPgglL--QGTTRILVTHALH-ILPQADWIIVLANGAIAEMG 835
Cdd:cd03266 157 VLLLDEPTTGLDV-MATRALREFIRQ---LraLGKCILFSTHIMQeVERLCDRVVVLHRGRVVYEG 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
649-843 |
5.71e-08 |
|
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: 57.39 E-value: 5.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLSALLGeLSKVEGFVSIEG-AVAYVPQEAW------VQntsVVenvcFgQE----L 717
Cdd:COG4172 305 VSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGqDLDGLSRRALrplrrrMQ---VV----F-QDpfgsL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 718 DP----------------PWL------ERVLEACA---LQPDV-DSFPegiHtsigEqgmnLSGGQKQRLSLARAVYRKA 771
Cdd:COG4172 376 SPrmtvgqiiaeglrvhgPGLsaaerrARVAEALEevgLDPAArHRYP---H----E----FSGGQRQRIAIARALILEP 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 772 AVYLLDDPLAALDAHVgQHvfnQVIgpgGLLQ------GTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELLQR 843
Cdd:COG4172 445 KLLVLDEPTSALDVSV-QA---QIL---DLLRdlqrehGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1285-1486 |
5.75e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 56.63 E-value: 5.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1285 VSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVglHTLRSRISIIPQDPILFP-----GSLRMN 1359
Cdd:PRK10851 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL--HARDRKVGFVFQHYALFRhmtvfDNIAFG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1360 LDLLQEHS-------DEAIWAALETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLARALLRKTQILILDEATAAV 1432
Cdd:PRK10851 99 LTVLPRRErpnaaaiKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 1433 DPgtelQMQAMLGSWFAQC------TVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQL 1486
Cdd:PRK10851 168 DA----QVRKELRRWLRQLheelkfTSVFVTHDQEEAMEVAdRVVVMSQGNIEQAGTPDQV 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1265-1434 |
5.99e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 55.43 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELplAVQGVSFKIHAGEKVGIVGRTGAGKSSLasglLR-------LQEAA--EGGIWIDGVPI--AHV 1333
Cdd:COG1117 12 IEVRNLNVYYGDKQ--ALKDINLDIPENKVTALIGPSGCGKSTL----LRclnrmndLIPGArvEGEILLDGEDIydPDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1334 GLHTLRSRISIIPQDPILFPGS--------LRMNLDLLQEHSDEAIWAALETVQL----KAlvaslpgQLQykcaDRGED 1401
Cdd:COG1117 86 DVVELRRRVGMVFQKPNPFPKSiydnvaygLRLHGIKSKSELDEIVEESLRKAALwdevKD-------RLK----KSALG 154
|
170 180 190
....*....|....*....|....*....|...
gi 1827346401 1402 LSVGQKQLLCLARALLRKTQILILDEATAAVDP 1434
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDP 187
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
646-816 |
6.11e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.21 E-value: 6.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-----------------AVAYVPQ-EAWVQNTSV 707
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklssaakaelrnqKLGFIYQfHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 708 VENVCF----GQELDPPWLERVLEACAlqpdvdsfPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAAL 783
Cdd:PRK11629 105 LENVAMplliGKKKPAEINSRALEMLA--------AVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190
....*....|....*....|....*....|...
gi 1827346401 784 DAHVGQHVFnQVIGPGGLLQGTTRILVTHALHI 816
Cdd:PRK11629 177 DARNADSIF-QLLGELNRLQGTAFLVVTHDLQL 208
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1282-1481 |
6.55e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 55.30 E-value: 6.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1282 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQE-----AAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPG-- 1354
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPNls 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1355 -----SLRMNLDLL---QEHSDEAIWAALETVQLKALVASLPGqlqykcADRGEdLSVGQKQLLCLARALLRKTQILILD 1426
Cdd:PRK14247 99 ifenvALGLKLNRLvksKKELQERVRWALEKAQLWDEVKDRLD------APAGK-LSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1827346401 1427 EATAAVDPGTELQMQAMLGSWFAQCTVLLIAH---RLRSVMDcaRVLVMDKGQVAESG 1481
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqQAARISD--YVAFLYKGQIVEWG 227
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1282-1433 |
6.66e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 55.11 E-value: 6.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1282 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNL- 1360
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNLi 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 1361 ---DLLQEHSDEAIWAAlETVQLkalvaSLPGQLQYKcadRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVD 1433
Cdd:PRK10247 103 fpwQIRNQQPDPAIFLD-DLERF-----ALPDTILTK---NIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
644-784 |
6.83e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.57 E-value: 6.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 644 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA------VAYVPQEAWV-------QNTSVVEN 710
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlCTYQKQLCFVghrsginPYLTLREN 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827346401 711 VCFGQELDPPWLErVLEAC---ALQPDVDsFPEGIhtsigeqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 784
Cdd:PRK13540 95 CLYDIHFSPGAVG-ITELCrlfSLEHLID-YPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
644-844 |
1.10e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 55.61 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 644 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA------------VAYVPQ-EAWVQNTSVVEN 710
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVpvpararlararIGVVPQfDNLDLEFTVREN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 711 -VCFGQ--ELDPPWLERV----LEACALQPDVDsfpegihTSIGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAAL 783
Cdd:PRK13536 135 lLVFGRyfGMSTREIEAVipslLEFARLESKAD-------ARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 784 DAHVGQHVFNQVigPGGLLQGTTRILVThalHILPQA----DWIIVLANG-AIAEmGSYQELLQRK 844
Cdd:PRK13536 204 DPHARHLIWERL--RSLLARGKTILLTT---HFMEEAerlcDRLCVLEAGrKIAE-GRPHALIDEH 263
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
649-841 |
1.46e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.41 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIE------GAVAYVPQEAWV----QNTSVVENVCFGQELD 718
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDdhplhfGDYSYRSQRIRMifqdPSTSLNPRQRISQILD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 719 PPW-LERVLEACALQpdvdsfpEGIHTSIGEQGM----------NLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHV 787
Cdd:PRK15112 112 FPLrLNTDLEPEQRE-------KQIIETLRQVGLlpdhasyyphMLAPGQKQRLGLARALILRPKVIIADEALASLDMSM 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 788 GQHVFNQVIGpgglLQ---GTTRILVTHAL----HIlpqADWIIVLANGAIAEMGSYQELL 841
Cdd:PRK15112 185 RSQLINLMLE----LQekqGISYIYVTQHLgmmkHI---SDQVLVMHQGEVVERGSTADVL 238
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
629-845 |
1.94e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 54.42 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSS---LLSALLGELSKVEGFVSIEGA------------- 692
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGItltaktvwdirek 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 693 VAYV---PQEAWVQNTsVVENVCFGQE---LDPPWL----ERVLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLS 762
Cdd:PRK13640 86 VGIVfqnPDNQFVGAT-VGDDVAFGLEnraVPRPEMikivRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 763 LARAVYRKAAVYLLDDPLAALDAHvGQHVFNQVIGPGGLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGS------ 836
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPA-GKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSpveifs 232
|
....*....
gi 1827346401 837 YQELLQRKG 845
Cdd:PRK13640 233 KVEMLKEIG 241
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
650-841 |
2.09e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 55.04 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 650 NLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-----------------VAYVPQE-AWVQNTSVVENV 711
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVdiakisdaelrevrrkkIAMVFQSfALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 712 CFGQELDP-PWLER------VLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 784
Cdd:PRK10070 128 AFGMELAGiNAEERrekaldALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1827346401 785 AHVGQHVFNQVIGPGGLLQGTTrILVTHAL-HILPQADWIIVLANGAIAEMGSYQELL 841
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKHQRTI-VFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
632-818 |
2.11e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.31 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 632 HSATFawSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA----------VAYVPQ-EA 700
Cdd:PRK13543 15 HALAF--SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsrfMAYLGHlPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 701 WVQNTSVVENVCFgqeldppwlervleACALQP-DVDSFPEGIHTSIGEQGM------NLSGGQKQRLSLARAVYRKAAV 773
Cdd:PRK13543 93 LKADLSTLENLHF--------------LCGLHGrRAKQMPGSALAIVGLAGYedtlvrQLSAGQKKRLALARLWLSPAPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1827346401 774 YLLDDPLAALDAHvGQHVFNQVIGPGGLLQGTTrILVTHALHILP 818
Cdd:PRK13543 159 WLLDEPYANLDLE-GITLVNRMISAHLRGGGAA-LVTTHGAYAAP 201
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
648-793 |
2.14e-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: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 648 RINLTVPQGCLLAVVGPVGAGKSSLLSaLLGELSKVEG---FVSIEGAVAYVPQEAWVQNTSVVENVCFgqeldPPWLER 724
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIY-----PDSSED 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 725 VLEACALQPDVDSFPEGIH-TSIGEQGMN----------LSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFN 793
Cdd:TIGR00954 544 MKRRGLSDKDLEQILDNVQlTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYR 623
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
646-829 |
2.15e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.42 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG----------AVAY----VPQE-AWVQNTSVVEN 710
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpvrirsprdAIALgigmVHQHfMLVPNLTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 711 VCFGQELDPPWL-------ERVLEACA---LQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPL 780
Cdd:COG3845 101 IVLGLEPTKGGRldrkaarARIRELSErygLDVDPDAKVE-----------DLSVGEQQRVEILKALYRGARILILDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 781 AALDAHVGQHVFnqvigpgGLL-----QGTTRILVTHALH-ILPQADWIIVLANG 829
Cdd:COG3845 170 AVLTPQEADELF-------EILrrlaaEGKSIIFITHKLReVMAIADRVTVLRRG 217
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1283-1487 |
2.42e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.84 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1283 QGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILfPGSLRMN--- 1359
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATT-PGDITVQelv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1360 ----------LDLLQEHSDEAIWAALETVQLKALvaslpgqlqykcADRGED-LSVGQKQLLCLARALLRKTQILILDEA 1428
Cdd:PRK10253 103 argryphqplFTRWRKEDEEAVTKAMQATGITHL------------ADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 1429 TAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCARVLV-MDKGQVAESGSPAQLL 1487
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREkgYTLAAVLHDLNQACRYASHLIaLREGKIVAQGAPKEIV 232
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
646-843 |
2.50e-07 |
|
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: 52.91 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGelskVEGFVSIEGAVAYvpqeawvQNTSVvenvcfgqeLDPPWLERV 725
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG----HPKYEVTEGEILF-------KGEDI---------TDLPPEERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 726 LEAC--ALQ--PDVdsfpEGIHTS--IGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVigpG 799
Cdd:cd03217 76 RLGIflAFQypPEI----PGVKNAdfLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVI---N 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1827346401 800 GLL-QGTTRILVTHALHIL--PQADWIIVLANGAIAEMGSyQELLQR 843
Cdd:cd03217 149 KLReEGKSVLIITHYQRLLdyIKPDRVHVLYDGRIVKSGD-KELALE 194
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1265-1486 |
3.15e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.59 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELPL---AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG----LHT 1337
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1338 LRSRISIIPQdpilFPGSLRMNLDLLQE----------HSDEAIWAALETVQLKALVASLPGQLQYkcadrgeDLSVGQK 1407
Cdd:PRK13649 83 IRKKVGLVFQ----FPESQLFEETVLKDvafgpqnfgvSQEEAEALAREKLALVGISESLFEKNPF-------ELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1408 QLLCLARALLRKTQILILDEATAAVDP-GTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCAR-VLVMDKGQVAESGSPAQ 1485
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPkGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADfVYVLEKGKLVLSGKPKD 231
|
.
gi 1827346401 1486 L 1486
Cdd:PRK13649 232 I 232
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
649-843 |
3.20e-07 |
|
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: 53.90 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLSALLG---ELSKVEGFVSIEGA-----------------VAYVPQEAWvqnTSvv 708
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEdllklsekelrkirgreIQMIFQDPM---TS-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 709 envcfgqeLDP---------------------PWLERVLEACAL----QPD--VDSFPegiHtsigeqgmNLSGGQKQRL 761
Cdd:COG0444 99 --------LNPvmtvgdqiaeplrihgglskaEARERAIELLERvglpDPErrLDRYP---H--------ELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 762 SLARAVYRKAAVYLLDDPLAALDAHVgQHvfnQVIgpgGLLQ------GTTRILVTH----ALHIlpqADWIIVLANGAI 831
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTI-QA---QIL---NLLKdlqrelGLAILFITHdlgvVAEI---ADRVAVMYAGRI 229
|
250
....*....|..
gi 1827346401 832 AEMGSYQELLQR 843
Cdd:COG0444 230 VEEGPVEELFEN 241
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1281-1491 |
3.52e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.13 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSS---LASGLLrlqEAAEGGIWIDGVPIAHVGLHTlRSRISIIPQDpilFpgSL- 1356
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTtmkMLTGLL---PASEGEAWLFGQPVDAGDIAT-RRRVGYMSQA---F--SLy 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1357 -----RMNLDL---L----QEHSDEAIWAALETVQLKALVASLPgqlqykcadrgEDLSVGQKQLLCLARALLRKTQILI 1424
Cdd:NF033858 352 geltvRQNLELharLfhlpAAEIAARVAEMLERFDLADVADALP-----------DSLPLGIRQRLSLAVAVIHKPELLI 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 1425 LDEATAAVDPGTELQMQAMLG--SWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKG 1491
Cdd:NF033858 421 LDEPTSGVDPVARDMFWRLLIelSREDGVTIFISTHFMNEAERCDRISLMHAGRVLASDTPAALVAARG 489
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
649-842 |
4.04e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 52.92 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKvEGFVSIEGA--VAYVPQE-----AWvqntsvvenvcFGQELDPPW 721
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRplSDWSAAElarhrAY-----------LSQQQSPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 722 LERVLEACAL-QPDVDSFPEGIHT------------SIGEQGMNLSGGQKQRLSLARAVYR-------KAAVYLLDDPLA 781
Cdd:COG4138 83 AMPVFQYLALhQPAGASSEAVEQLlaqlaealgledKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 782 ALD-AHvgQHVFNQVIgpGGL-LQGTTRILVTHAL-HILPQADWIIVLANGAIAEMGSYQELLQ 842
Cdd:COG4138 163 SLDvAQ--QAALDRLL--RELcQQGITVVMSSHDLnHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
644-829 |
4.15e-07 |
|
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: 52.26 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 644 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGelsKVEGFVSIEGAVAY---VPQEAWVQNTSvveNVCFGQELD-- 718
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSVEGDIHYngiPYKEFAEKYPG---EIIYVSEEDvh 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 719 PPWL--ERVLEAcALQPDVDSFPEGIhtsigeqgmnlSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQvi 796
Cdd:cd03233 95 FPTLtvRETLDF-ALRCKGNEFVRGI-----------SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKC-- 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1827346401 797 gpgglLQGTTRILVTHALHILPQA--------DWIIVLANG 829
Cdd:cd03233 161 -----IRTMADVLKTTTFVSLYQAsdeiydlfDKVLVLYEG 196
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
640-843 |
4.27e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 53.16 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 640 QESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGEL----SKVEGFVSIEGaVAYVPQE------AWV-QN---- 704
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDG-KPVAPCAlrgrkiATImQNprsa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 705 --------TSVVENV-CFGQELDPPWLERVLEACALQPD---VDSFPegihtsigeqgMNLSGGQKQRLSLARAVYRKAA 772
Cdd:PRK10418 92 fnplhtmhTHARETClALGKPADDATLTAALEAVGLENAarvLKLYP-----------FEMSGGMLQRMMIALALLCEAP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827346401 773 VYLLDDPLAALDAHVGQHVFN------QVIGPGGLlqgttriLVTHALHILPQ-ADWIIVLANGAIAEMGSYQELLQR 843
Cdd:PRK10418 161 FIIADEPTTDLDVVAQARILDllesivQKRALGML-------LVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
629-843 |
4.74e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.09 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSQESP---PCLHRINLTVPQGCLLAVVGPVGAGKSSLLS------------ALLGELSKVEGFVSIE--- 690
Cdd:PRK13645 7 IILDNVSYTYAKKTPfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqTIVGDYAIPANLKKIKevk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 691 ------GAVAYVPQEAWVQNTsVVENVCFGqeldPPWL----ERVLEACALQPDVDSFPEgihTSIGEQGMNLSGGQKQR 760
Cdd:PRK13645 87 rlrkeiGLVFQFPEYQLFQET-IEKDIAFG----PVNLgenkQEAYKKVPELLKLVQLPE---DYVKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 761 LSLARAVYRKAAVYLLDDPLAALDAHvGQHVFNQVIGPGGLLQGTTRILVTHAL-HILPQADWIIVLANGAIAEMG---- 835
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPK-GEEDFINLFERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGspfe 237
|
250
....*....|
gi 1827346401 836 --SYQELLQR 843
Cdd:PRK13645 238 ifSNQELLTK 247
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1285-1488 |
5.25e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 53.18 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1285 VSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEG-----GIWIDGVPI-AHVGLHTLRSRISIIPQDPILFPGSLRM 1358
Cdd:PRK14271 40 VSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFPMSIMD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1359 N-LDLLQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTE 1437
Cdd:PRK14271 120 NvLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTT 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 1438 LQMQAMLGSWFAQCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLA 1488
Cdd:PRK14271 200 EKIEEFIRSLADRLTVIIVTHNLAQAARISdRAALFFDGRLVEEGPTEQLFS 251
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
629-843 |
5.67e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 52.82 E-value: 5.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSQESP---PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA------------- 692
Cdd:PRK13649 3 INLQNVSYTYQAGTPfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitstsknkdikq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 693 ----VAYVPQ--EAWVQNTSVVENVCFGQE---LDPPWLERV-LEACALQpdvdsfpeGIHTSIGEQG-MNLSGGQKQRL 761
Cdd:PRK13649 83 irkkVGLVFQfpESQLFEETVLKDVAFGPQnfgVSQEEAEALaREKLALV--------GISESLFEKNpFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 762 SLARAVYRKAAVYLLDDPLAALDAHVGQH---VFNQVigpggLLQGTTRILVTHAL-HILPQADWIIVLANGAIAEMGSY 837
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKElmtLFKKL-----HQSGMTIVLVTHLMdDVANYADFVYVLEKGKLVLSGKP 229
|
....*.
gi 1827346401 838 QELLQR 843
Cdd:PRK13649 230 KDIFQD 235
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1281-1481 |
6.89e-07 |
|
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: 51.87 E-value: 6.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGlhtLRSR-ISIIPQDPILFPgslRMN 1359
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLP---PKDRdIAMVFQNYALYP---HMT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1360 ------LDLLQEHSDEAI------WAAlETVQLKALVASLPGQlqykcadrgedLSVGQKQLLCLARALLRKTQILILDE 1427
Cdd:cd03301 89 vydniaFGLKLRKVPKDEidervrEVA-ELLQIEHLLDRKPKQ-----------LSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 1428 ATAAVDPGTELQM-------QAMLGSwfaqcTVLLIAHRLRSVMDCA-RVLVMDKGQVAESG 1481
Cdd:cd03301 157 PLSNLDAKLRVQMraelkrlQQRLGT-----TTIYVTHDQVEAMTMAdRIAVMNDGQIQQIG 213
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1265-1333 |
6.89e-07 |
|
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: 50.14 E-value: 6.89e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYrPELPLaVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGI-WIDGVPIAHV 1333
Cdd:cd03221 1 IELENLSKTY-GGKLL-LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVtWGSTVKIGYF 68
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1269-1501 |
7.57e-07 |
|
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: 53.18 E-value: 7.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1269 DFGLRyRPELPLAVQgvsFKIHAGEKVGIVGRTGAGKSSLA---SGLLRLQE---AAEGGIWIDGVPIAHVGLHtlRSRI 1342
Cdd:COG4148 6 DFRLR-RGGFTLDVD---FTLPGRGVTALFGPSGSGKTTLLraiAGLERPDSgriRLGGEVLQDSARGIFLPPH--RRRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1343 SIIPQDPILFPG-SLRMNLD-----LLQEHSDEAIWAALETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLARAL 1416
Cdd:COG4148 80 GYVFQEARLFPHlSVRGNLLygrkrAPRAERRISFDEVVELLGIGHLLDRRPATL-----------SGGERQRVAIGRAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1417 LRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQKGLF 1493
Cdd:COG4148 149 LSSPRLLLMDEPLAALDLARKAEILPYLERLRDEldIPILYVSHSLDEVARLAdHVVLLEQGRVVASGPLAEVLSRPDLL 228
|
....*...
gi 1827346401 1494 yRLAQESG 1501
Cdd:COG4148 229 -PLAGGEE 235
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
649-836 |
9.64e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 52.66 E-value: 9.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-AVAYVPQEAWVQNTSVVENVcF-------------G 714
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqDLLKADPEAQKLLRQKIQIV-FqnpygslnprkkvG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 715 QELDPPWL-----------ERVLEACA---LQPD-VDSFPegiHtsigeqgMnLSGGQKQRLSLARAVYRKAAVYLLDDP 779
Cdd:PRK11308 113 QILEEPLLintslsaaerrEKALAMMAkvgLRPEhYDRYP---H-------M-FSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 780 LAALDAHVGQHVFNQVIGpgglLQ---GTTRILVTHAL----HIlpqADWIIVLANGAIAEMGS 836
Cdd:PRK11308 182 VSALDVSVQAQVLNLMMD----LQqelGLSYVFISHDLsvveHI---ADEVMVMYLGRCVEKGT 238
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1282-1487 |
9.96e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.97 E-value: 9.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1282 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGV------PIAHVGLHTLRSRISIIPQDPILFPG- 1354
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPHl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1355 SLRMNLDL-LQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVD 1433
Cdd:PRK14246 106 SIYDNIAYpLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 1434 PGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCAR-VLVMDKGQVAESGSPAQLL 1487
Cdd:PRK14246 186 IVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADyVAFLYNGELVEWGSSNEIF 240
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
649-784 |
9.99e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 51.82 E-value: 9.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG--------------AVAYVPQEAWV-QNTSVVENVCF 713
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllplhararrGIGYLPQEASIfRRLSVYDNLMA 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 714 GQELdppwlERVLEACALQPDVDSFPEGIHTS--IGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 784
Cdd:PRK10895 102 VLQI-----RDDLSAEQREDRANELMEEFHIEhlRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
646-836 |
1.05e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 52.50 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSA--LLGELSkvEGFVSIEGA--VAYVPQE--AWVQNT-------------S 706
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCinLLERPT--SGRVLVDGQdlTALSEKElrKARRQIgmifqhfnllssrT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 707 VVENVCFGQELD-----------PPWLERV-LEACAlqpdvDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVY 774
Cdd:PRK11153 99 VFDNVALPLELAgtpkaeikarvTELLELVgLSDKA-----DRYPA-----------QLSGGQKQRVAIARALASNPKVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 775 LLDDPLAALDAHVGQHVFNqvigpggLLQ------GTTRILVTHALHILPQ-ADWIIVLANGAIAEMGS 836
Cdd:PRK11153 163 LCDEATSALDPATTRSILE-------LLKdinrelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1264-1488 |
1.06e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.40 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1264 QIEFRDFGLRYRPELPL---AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGI-WI--DGVPIAHVGLHT 1337
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIfkDEKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1338 ---------------------LRSRISIIPQ------------DPILFpGSLRMNLDllqehSDEAIWAALETVQLKALV 1384
Cdd:PRK13651 82 kvleklviqktrfkkikkikeIRRRVGVVFQfaeyqlfeqtieKDIIF-GPVSMGVS-----KEEAKKRAAKYIELVGLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1385 ASLpgqLQykcadRGE-DLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQC-TVLLIAHRLRS 1462
Cdd:PRK13651 156 ESY---LQ-----RSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGkTIILVTHDLDN 227
|
250 260
....*....|....*....|....*..
gi 1827346401 1463 VMDCA-RVLVMDKGQVAESGSPAQLLA 1488
Cdd:PRK13651 228 VLEWTkRTIFFKDGKIIKDGDTYDILS 254
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
646-779 |
1.17e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 53.10 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------------VAYVP----QEAWVQNTSV 707
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVPedrkGEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 708 VENVCFgqeldpPWLERVLEACALQPD---------VDSF---PEGIHTSIGeqgmNLSGGQKQRLSLARAVYRKAAVYL 775
Cdd:COG1129 348 RENITL------ASLDRLSRGGLLDRRreralaeeyIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLI 417
|
....
gi 1827346401 776 LDDP 779
Cdd:COG1129 418 LDEP 421
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
747-841 |
1.38e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 51.51 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 747 GEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAH-VGQ--HVFNQVIGpggllQGTTRILVTH----ALHIlpq 819
Cdd:PRK10619 147 GKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElVGEvlRIMQQLAE-----EGKTMVVVTHemgfARHV--- 218
|
90 100
....*....|....*....|..
gi 1827346401 820 ADWIIVLANGAIAEMGSYQELL 841
Cdd:PRK10619 219 SSHVIFLHQGKIEEEGAPEQLF 240
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1281-1492 |
1.52e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 51.03 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAH-VGLHTLRSRISIIPQDPILFPgslRMN 1359
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMREAVAIVPEGRRVFS---RMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1360 LDllQEHSDEAIWAALETVQLK-ALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTEL 1438
Cdd:PRK11614 97 VE--ENLAMGGFFAERDQFQERiKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 1439 QMQAMLGSWFAQ-CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQKGL 1492
Cdd:PRK11614 175 QIFDTIEQLREQgMTIFLVEQNANQALKLAdRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
746-826 |
1.56e-06 |
|
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: 53.09 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 746 IGEQGMNLSGGQKQRLSLARAVYRKA---AVYLLDDPLAALDAH-VGQ--HVFNQVIGpggllQGTTRILVTHALHILPQ 819
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLHFDdIKKllEVLQRLVD-----KGNTVVVIEHNLDVIKT 897
|
....*..
gi 1827346401 820 ADWIIVL 826
Cdd:TIGR00630 898 ADYIIDL 904
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1281-1431 |
1.58e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.62 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAA--EGGIWIDGVPIAHVGLH-TLRSRISIIPQDPILFPG-SL 1356
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRdTERAGIAIIHQELALVKElSV 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827346401 1357 RMNLDLLQEHSDEAI--WAALeTVQLKALVASLpgQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAA 1431
Cdd:PRK13549 100 LENIFLGNEITPGGImdYDAM-YLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
646-879 |
1.72e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 51.65 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA---------VAYVPQE-AWVQNTSVVEN-VCFG 714
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEpldpedrrrIGYLPEErGLYPKMKVGEQlVYLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 715 Q--ELDPP--------WLERVleacalqpdvdsfpeGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 784
Cdd:COG4152 97 RlkGLSKAeakrradeWLERL---------------GLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 785 AhVGQHVFNQVIgpgglL----QGTTRILVThalHILPQA----DWIIVLANGAIAEMGSYQELLQRKGALMCLLdqaRQ 856
Cdd:COG4152 162 P-VNVELLKDVI-----RelaaKGTTVIFSS---HQMELVeelcDRIVIINKGRKVLSGSVDEIRRQFGRNTLRL---EA 229
|
250 260
....*....|....*....|...
gi 1827346401 857 PGDRGEGETEPGTSTKDPRGTSA 879
Cdd:COG4152 230 DGDAGWLRALPGVTVVEEDGDGA 252
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1282-1469 |
1.78e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.00 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1282 VQGVSFKIHAGEKVGIVGRTGAGKSSLASG---LLRLQEAA--EGGIWIDGVPI--AHVGLHTLRSRISIIPQDPILFPG 1354
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEArvEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1355 ---------SLRMN-LDLLQEHSDEAIWAALETvqlkalvASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILI 1424
Cdd:PRK14267 100 ltiydnvaiGVKLNgLVKSKKELDERVEWALKK-------AALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1827346401 1425 LDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHrlrSVMDCARV 1469
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH---SPAQAARV 214
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1277-1326 |
1.80e-06 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 50.90 E-value: 1.80e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1277 ELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWID 1326
Cdd:COG4778 23 RLP-VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR 71
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
990-1162 |
1.83e-06 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 51.32 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 990 IFGLLGCLQAIGLFASMAAVLLGGARASRLLFQRLLWDVVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMY 1069
Cdd:cd18577 52 YFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1070 AFGLLeVSLVVA------VAtpLATVAILPLFLLYAGFQSLYVVSSCQlrrLESASYSSVCSHMAETFQGSTVVRAFRTQ 1143
Cdd:cd18577 132 LSTFI-AGFIIAfiyswkLT--LVLLATLPLIAIVGGIMGKLLSKYTK---KEQEAYAKAGSIAEEALSSIRTVKAFGGE 205
|
170
....*....|....*....
gi 1827346401 1144 APFVAQNNARVDESQRISF 1162
Cdd:cd18577 206 EKEIKRYSKALEKARKAGI 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1281-1461 |
1.95e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 50.93 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQE-----AAEGGIWIDGVPIAHVGLHT--LRSRISIIPQDPILFP 1353
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1354 GSLRMN----LDLLQEHSDEAIWAALETvQLKAlvASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEAT 1429
Cdd:PRK14239 100 MSIYENvvygLRLKGIKDKQVLDEAVEK-SLKG--ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPT 176
|
170 180 190
....*....|....*....|....*....|..
gi 1827346401 1430 AAVDPGTELQMQAMLGSWFAQCTVLLIAHRLR 1461
Cdd:PRK14239 177 SALDPISAGKIEETLLGLKDDYTMLLVTRSMQ 208
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1281-1444 |
2.07e-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: 52.13 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAA--EGGIWIDGVPIAHVGLH-TLRSRISIIPQDPILFPG-SL 1356
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRdTERAGIVIIHQELTLVPElSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1357 RMNLDLLQE--------HSDEAIWAA---LETVQLKALVASLPGQlqykcadrgeDLSVGQKQLLCLARALLRKTQILIL 1425
Cdd:TIGR02633 96 AENIFLGNEitlpggrmAYNAMYLRAknlLRELQLDADNVTRPVG----------DYGGGQQQLVEIAKALNKQARLLIL 165
|
170
....*....|....*....
gi 1827346401 1426 DEATAAVdpgTELQMQAML 1444
Cdd:TIGR02633 166 DEPSSSL---TEKETEILL 181
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1260-1488 |
2.13e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.85 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1260 PQGGQIEfrdfGLRYRPELPLaVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAA----EGGIWIDGVPIAhvgL 1335
Cdd:PRK10418 2 PQQIELR----NIALQAAQPL-VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVA---P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1336 HTLRSR-ISIIPQDPILFPGSLR-MN-------LDLLQEHSDEAIWAALETVQL---KALVASLPGQlqykcadrgedLS 1403
Cdd:PRK10418 74 CALRGRkIATIMQNPRSAFNPLHtMHtharetcLALGKPADDATLTAALEAVGLenaARVLKLYPFE-----------MS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1404 VGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQVAES 1480
Cdd:PRK10418 143 GGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKraLGMLLVTHDMGVVARLAdDVAVMSHGRIVEQ 222
|
....*...
gi 1827346401 1481 GSPAQLLA 1488
Cdd:PRK10418 223 GDVETLFN 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
753-840 |
2.23e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 51.39 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 753 LSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHvGQHVFNQVIGPGGlLQGTTRILVTHAL-HILPQADWIIVLANGAI 831
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK-GEHEMMQLILDAK-ANNKTVFVITHTMeHVLEVADEVIVMDKGKI 254
|
....*....
gi 1827346401 832 AEMGSYQEL 840
Cdd:PRK13631 255 LKTGTPYEI 263
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1282-1488 |
2.25e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 50.90 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1282 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLlRLQEAAEGG------IWIDG-VPIAHVG--LHTLRSRISIIPQDPILF 1352
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLEQPEAGtirvgdITIDTaRSLSQQKglIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1353 PGslRMNLD--------LLQEHSDEAIWAALEtvqLKALVAsLPGQlqykcadrgED-----LSVGQKQLLCLARALLRK 1419
Cdd:PRK11264 98 PH--RTVLEniiegpviVKGEPKEEATARARE---LLAKVG-LAGK---------ETsyprrLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 1420 TQILILDEATAAVDP---GTELQMQAMLGSwfAQCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLA 1488
Cdd:PRK11264 163 PEVILFDEPTSALDPelvGEVLNTIRQLAQ--EKRTMVIVTHEMSFARDVAdRAIFMDQGRIVEQGPAKALFA 233
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
646-785 |
2.56e-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: 51.75 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLG--ELSKVEGFVSIEGA--------------VAYVPQE-AWVQNTSVV 708
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSplkasnirdteragIVIIHQElTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 709 ENVCFGQELDPP-----WLERVLEACAL--QPDVDSFPEGIHTsigeqgMNLSGGQKQRLSLARAVYRKAAVYLLDDPLA 781
Cdd:TIGR02633 97 ENIFLGNEITLPggrmaYNAMYLRAKNLlrELQLDADNVTRPV------GDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
....
gi 1827346401 782 ALDA 785
Cdd:TIGR02633 171 SLTE 174
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1248-1487 |
2.81e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 51.97 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1248 WR---LPTCAAQP-PWPQGGQIEFRDFGlRYRPELPLaVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAA---E 1320
Cdd:TIGR00955 5 WRnsdVFGRVAQDgSWKQLVSRLRGCFC-RERPRKHL-LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1321 GGIWIDGVPIahvGLHTLRSRISIIPQDPILFP-----------GSLRMNLDLLQEHSDEAIWAALETVQLKalvaslpg 1389
Cdd:TIGR00955 83 GSVLLNGMPI---DAKEMRAISAYVQQDDLFIPtltvrehlmfqAHLRMPRRVTKKEKRERVDEVLQALGLR-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1390 qlqyKCAD-------RGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQ-MQAMLGswFAQ--CTVLLIAH- 1458
Cdd:TIGR00955 152 ----KCANtrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSvVQVLKG--LAQkgKTIICTIHq 225
|
250 260 270
....*....|....*....|....*....|..
gi 1827346401 1459 ---RLRSVMDcaRVLVMDKGQVAESGSPAQLL 1487
Cdd:TIGR00955 226 pssELFELFD--KIILMAEGRVAYLGSPDQAV 255
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
647-820 |
3.44e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.42 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 647 HRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQEAWVQNT-------------SVVENVCF 713
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLlylghqpgiktelTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 714 gqeldppwlervleACALQPDVDsfPEGIHTSIGEQGM---------NLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 784
Cdd:PRK13538 98 --------------YQRLHGPGD--DEALWEALAQVGLagfedvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1827346401 785 --------AHVGQHvfnqvigpggLLQGTTRILVTHA-LHILPQA 820
Cdd:PRK13538 162 kqgvarleALLAQH----------AEQGGMVILTTHQdLPVASDK 196
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
646-830 |
3.57e-06 |
|
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: 48.86 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEgfvSIEGAVAYVPQEAwvqntsvvenVCFGQeldppwLERV 725
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKAR---LISFLPKFSRNKL----------IFIDQ------LQFL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 726 LEAcalqpdvdsfpeGI-HTSIGEQGMNLSGGQKQRLSLARAVYR--KAAVYLLDDPLAALDAHVGQHVFNQVigpGGLL 802
Cdd:cd03238 72 IDV------------GLgYLTLGQKLSTLSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQDINQLLEVI---KGLI 136
|
170 180
....*....|....*....|....*....
gi 1827346401 803 -QGTTRILVTHALHILPQADWIIVLANGA 830
Cdd:cd03238 137 dLGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
629-841 |
3.61e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 50.48 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 629 ITIHSATFAWSQESP-PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAvAYVPQEAW------ 701
Cdd:PRK13642 5 LEVENLVFKYEKESDvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVWnlrrki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 702 ---VQN-------TSVVENVCFGQELD----PPWLERVLEACaLQPDVDSFPEgihtsigEQGMNLSGGQKQRLSLARAV 767
Cdd:PRK13642 84 gmvFQNpdnqfvgATVEDDVAFGMENQgiprEEMIKRVDEAL-LAVNMLDFKT-------REPARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 768 YRKAAVYLLDDPLAALDAhVGQHVFNQVIGPGGLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELL 841
Cdd:PRK13642 156 ALRPEIIILDESTSMLDP-TGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1281-1483 |
4.08e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.94 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIaHVGLHTLRSRISIIPQDPILFPGSLRMNL 1360
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1361 DLLQEHSDEAIWaalETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQM 1440
Cdd:TIGR01257 1024 ILFYAQLKGRSW---EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1827346401 1441 QAMLGSWFAQCTVLLIAHRlrsvMDCA-----RVLVMDKGQVAESGSP 1483
Cdd:TIGR01257 1101 WDLLLKYRSGRTIIMSTHH----MDEAdllgdRIAIISQGRLYCSGTP 1144
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
646-844 |
5.22e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 49.83 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-----------------AVAYVPQ--EAWVQNTS 706
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkKVSLVFQfpEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 707 VVENVCFG-----------QELDPPWLERVleacalqpdvdsfpeGIHTSIGEQG-MNLSGGQKQRLSLARAVYRKAAVY 774
Cdd:PRK13641 103 VLKDVEFGpknfgfsedeaKEKALKWLKKV---------------GLSEDLISKSpFELSGGQMRRVAIAGVMAYEPEIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 775 LLDDPLAALDAHvGQHVFNQVIgPGGLLQGTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELLQRK 844
Cdd:PRK13641 168 CLDEPAAGLDPE-GRKEMMQLF-KDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1264-1458 |
6.30e-06 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 49.48 E-value: 6.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1264 QIEFRDFGLRY--RPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGlhtlrSR 1341
Cdd:COG4525 3 MLTVRHVSVRYpgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG-----AD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1342 ISIIPQDPILFPG---------SLRM--------------NLDL--LQEHSDEAIWAaletvqlkalvaslpgqlqykca 1396
Cdd:COG4525 78 RGVVFQKDALLPWlnvldnvafGLRLrgvpkaerraraeeLLALvgLADFARRRIWQ----------------------- 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 1397 drgedLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQC--TVLLIAH 1458
Cdd:COG4525 135 -----LSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTgkGVFLITH 193
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1283-1485 |
6.63e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 50.88 E-value: 6.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1283 QGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTL----RSRISIIPQDPILFPgslrm 1358
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLS----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1359 nlDLLQEHSDE--AIWAALETVQLKALVASLPGQLqyKCADRGE----DLSVGQKQLLCLARALLRKTQILILDEATAAV 1432
Cdd:PRK10535 100 --HLTAAQNVEvpAVYAGLERKQRLLRAQELLQRL--GLEDRVEyqpsQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 1433 DPGTELQMQAMLGSWFAQC-TVLLIAHRLRSVMDCARVLVMDKGQVAeSGSPAQ 1485
Cdd:PRK10535 176 DSHSGEEVMAILHQLRDRGhTVIIVTHDPQVAAQAERVIEIRDGEIV-RNPPAQ 228
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1281-1488 |
7.67e-06 |
|
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: 50.57 E-value: 7.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASgLLRLQEAAEGgiwIDGVPIAHVGL------------------------- 1335
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMH-VLRGMDQYEP---TSGRIIYHVALcekcgyverpskvgepcpvcggtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1336 --------------HTLRSRISIIPQDPILFPGSLRMnLDLLQEHSDEAIWAALETVQlKALVASLPGQLQYKCADRGED 1401
Cdd:TIGR03269 91 peevdfwnlsdklrRRIRKRIAIMLQRTFALYGDDTV-LDNVLEALEEIGYEGKEAVG-RAVDLIEMVQLSHRITHIARD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1402 LSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAML--GSWFAQCTVLLIAHRLRSVMDCA-RVLVMDKGQVA 1478
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeeAVKASGISMVLTSHWPEVIEDLSdKAIWLENGEIK 248
|
250
....*....|
gi 1827346401 1479 ESGSPAQLLA 1488
Cdd:TIGR03269 249 EEGTPDEVVA 258
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1281-1496 |
8.13e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 49.62 E-value: 8.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSS---LASGLLrlqeAAEGGIWIDGVPIAHVGLHT------LRSRISIIPQDP-- 1349
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTmiqLTNGLI----ISETGQTIVGDYAIPANLKKikevkrLRKEIGLVFQFPey 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1350 ILFPGSLRMNLDL----LQEHSDEAIWAALETVQLkalvASLPGQLqykcADRGE-DLSVGQKQLLCLARALLRKTQILI 1424
Cdd:PRK13645 102 QLFQETIEKDIAFgpvnLGENKQEAYKKVPELLKL----VQLPEDY----VKRSPfELSGGQKRRVALAGIIAMDGNTLV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 1425 LDEATAAVDPGTE---LQMQAMLGSWFAQcTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQKGLFYRL 1496
Cdd:PRK13645 174 LDEPTGGLDPKGEedfINLFERLNKEYKK-RIIMVTHNMDQVLRIAdEVIVMHEGKVISIGSPFEIFSNQELLTKI 248
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1283-1380 |
8.26e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 48.26 E-value: 8.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1283 QGVSFKIHAGEKVGIVGRTGAGKSSL---ASGLLRlqeAAEGGIWIDGVPIAHVGLHTLRSrisiipqdpILFPG----- 1354
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLlriLAGLAR---PDAGEVLWQGEPIRRQRDEYHQD---------LLYLGhqpgi 85
|
90 100 110
....*....|....*....|....*....|....
gi 1827346401 1355 --------SLRMNLDLLQEHSDEAIWAALETVQL 1380
Cdd:PRK13538 86 kteltaleNLRFYQRLHGPGDDEALWEALAQVGL 119
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
644-844 |
8.54e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 50.32 E-value: 8.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 644 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEG-FVSIEGA-VAYVPQEAWVQNT-SVVENVCFG-QEL-- 717
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGeARPQPGIkVGYLPQEPQLDPTkTVRENVEEGvAEIkd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 718 -------------DPPWLERVL--EACALQPDVDSfpEGIHT--SIGEQGM-------------NLSGGQKQRLSLARAV 767
Cdd:TIGR03719 99 aldrfneisakyaEPDADFDKLaaEQAELQEIIDA--ADAWDldSQLEIAMdalrcppwdadvtKLSGGERRRVALCRLL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 768 YRKAAVYLLDDPLAALDAH----VGQHVFNQvigPGgllqgtTRILVTHALHILPQ-ADWIIVLANG-AIAEMGSYQELL 841
Cdd:TIGR03719 177 LSKPDMLLLDEPTNHLDAEsvawLERHLQEY---PG------TVVAVTHDRYFLDNvAGWILELDRGrGIPWEGNYSSWL 247
|
...
gi 1827346401 842 QRK 844
Cdd:TIGR03719 248 EQK 250
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1282-1479 |
9.50e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.17 E-value: 9.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1282 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIA-HVGLHTLRSRISIIPQ---DPILFPG-SL 1356
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITEsrrDNGFFPNfSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1357 RMNLDLLQEHSD---EAIWAALETVQLKALVASLPGQLQYKCADRGE---DLSVGQKQLLCLARALLRKTQILILDEATA 1430
Cdd:PRK09700 359 AQNMAISRSLKDggyKGAMGLFHEVDEQRTAENQRELLALKCHSVNQnitELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 1431 AVDPGTELQMQAMLGSWFAQC-TVLLIAHRLRSVMD-CARVLVMDKGQVAE 1479
Cdd:PRK09700 439 GIDVGAKAEIYKVMRQLADDGkVILMVSSELPEIITvCDRIAVFCEGRLTQ 489
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1281-1314 |
1.15e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 49.32 E-value: 1.15e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSS---LASGLLR 1314
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTtikMLTGILV 73
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
646-833 |
1.16e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 48.24 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-----------------VAYVPQE-AWVQNTSV 707
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQplhqmdeearaklrakhVGFVFQSfMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 708 VENVcfgqELdpPWLER-------------VLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVY 774
Cdd:PRK10584 106 LENV----EL--PALLRgessrqsrngakaLLEQLGLGKRLDHLPA-----------QLSGGEQQRVALARAFNGRPDVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 775 LLDDPLAALDAHVGQHVFNqvigpggLL------QGTTRILVTHALHILPQADWIIVLANGAIAE 833
Cdd:PRK10584 169 FADEPTGNLDRQTGDKIAD-------LLfslnreHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
649-843 |
1.29e-05 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 48.96 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYVPQEAWV----------QN--TS--------- 706
Cdd:COG4608 37 VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQdITGLSGRELRplrrrmqmvfQDpyASlnprmtvgd 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 707 ------VVENVCFGQELDppwlERV---LEACALQPD-VDSFPegiHTsigeqgmnLSGGQKQRLSLARAVYRKAAVYLL 776
Cdd:COG4608 117 iiaeplRIHGLASKAERR----ERVaelLELVGLRPEhADRYP---HE--------FSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827346401 777 DDPLAALDAHVGQHVFNqvigpggLLQ------GTTRILVTHAL----HIlpqADWIIVLANGAIAEMGSYQELLQR 843
Cdd:COG4608 182 DEPVSALDVSIQAQVLN-------LLEdlqdelGLTYLFISHDLsvvrHI---SDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
646-907 |
1.35e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAV--AYVPQ---------EAWVQNTSVVENvcfg 714
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIklGYFAQhqleflradESPLQHLARLAP---- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 715 QELDPPwLERVLEACALQPDvdsfpegihtSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQ 794
Cdd:PRK10636 404 QELEQK-LRDYLGGFGFQGD----------KVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEA 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 795 VIGPGGLLqgttrILVTHALHIL-PQADWIIVLANGAIA----EMGSYQELlqrkgalmcLLDQARQpgdrgegETEPGT 869
Cdd:PRK10636 473 LIDFEGAL-----VVVSHDRHLLrSTTDDLYLVHDGKVEpfdgDLEDYQQW---------LSDVQKQ-------ENQTDE 531
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1827346401 870 STKDPRGTSA-GRRPELRRERSIKSVPE---KDRTTSEAQTE 907
Cdd:PRK10636 532 APKENNANSAqARKDQKRREAELRTQTQplrKEIARLEKEME 573
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
649-841 |
1.43e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 48.39 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKvEGFVSIEGAvayvPQEAWVQNTSVVENVCFGQELDPPWLERVLEA 728
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQ----PLEAWSAAELARHRAYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 729 CALqpdvdSFPEGIHTSIGEQGMN------------------LSGGQKQRLSLARA---VYRKAAVY----LLDDPLAAL 783
Cdd:PRK03695 90 LTL-----HQPDKTRTEAVASALNevaealglddklgrsvnqLSGGEWQRVRLAAVvlqVWPDINPAgqllLLDEPMNSL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 784 DahVGQHV-----FNQVIGpggllQGTTRILVTHAL-HILPQADWIIVLANGAIAEMGSYQELL 841
Cdd:PRK03695 165 D--VAQQAaldrlLSELCQ-----QGIAVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
646-792 |
1.47e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFV--------------SIEGAVAYVPQEA-WVQNTSVVEN 710
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSIlfqgkeidfksskeALENGISMVHQELnLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 711 VCFGQE------LDPPWLERVLEACALQPDVDSFPEgihtsigEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 784
Cdd:PRK10982 94 MWLGRYptkgmfVDQDKMYRDTKAIFDELDIDIDPR-------AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
....*...
gi 1827346401 785 AHVGQHVF 792
Cdd:PRK10982 167 EKEVNHLF 174
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
646-826 |
1.47e-05 |
|
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: 48.13 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRinLTVPQ-GCLLAVVGPVGAGKSSLLSALLGELSKVEGfvsiegavAYVPQEAWvqnTSVVENvcF-GQELDPpWLE 723
Cdd:cd03236 17 LHR--LPVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLG--------KFDDPPDW---DEILDE--FrGSELQN-YFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 724 RVLEA---CALQPD-VDSFPEGIHTSIG-------EQGM-------------------NLSGGQKQRLSLARAVYRKAAV 773
Cdd:cd03236 81 KLLEGdvkVIVKPQyVDLIPKAVKGKVGellkkkdERGKldelvdqlelrhvldrnidQLSGGELQRVAIAAALARDADF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 774 YLLDDPLAALDahVGQHvFNQVIGPGGLLQGTTRILVT-HALHILPQ-ADWIIVL 826
Cdd:cd03236 161 YFFDEPSSYLD--IKQR-LNAARLIRELAEDDNYVLVVeHDLAVLDYlSDYIHCL 212
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1281-1433 |
2.20e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 47.56 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG---LHTLRSRISIIPQD-PILFPGSL 1356
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRRQIGMIFQDhHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1357 RMNLDL---LQEHSDEAIW----AALETVQLKALVASLPGQlqykcadrgedLSVGQKQLLCLARALLRKTQILILDEAT 1429
Cdd:PRK10908 97 YDNVAIpliIAGASGDDIRrrvsAALDKVGLLDKAKNFPIQ-----------LSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
....
gi 1827346401 1430 AAVD 1433
Cdd:PRK10908 166 GNLD 169
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1270-1487 |
2.37e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.75 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1270 FGLRYRP--ELPLAVQG---------VSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIA-HVGLHT 1337
Cdd:PRK11288 246 YGYRPRPlgEVRLRLDGlkgpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1338 LRSRISIIPQD----PILFPGSLRMNLDL-LQEHSDEAIWaALETVQLKALVASLPGQLQYKCADRGED---LSVGQKQL 1409
Cdd:PRK11288 326 IRAGIMLCPEDrkaeGIIPVHSVADNINIsARRHHLRAGC-LINNRWEAENADRFIRSLNIKTPSREQLimnLSGGNQQK 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1410 LCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ-CTVLLIAHRLRSVMDCA-RVLVMDKGQVA-----ESGS 1482
Cdd:PRK11288 405 AILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQgVAVLFVSSDLPEVLGVAdRIVVMREGRIAgelarEQAT 484
|
....*
gi 1827346401 1483 PAQLL 1487
Cdd:PRK11288 485 ERQAL 489
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1282-1491 |
2.60e-05 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 46.75 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1282 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQ--EAAEGGIWIDGVPIAHVGLHtLRSR--ISIIPQDPILFPGslr 1357
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPE-ERARlgIFLAFQYPPEIPG--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1358 mnldllqehsdeaiwaaletVQLKALVASLpgqlqykcadrGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPgTE 1437
Cdd:cd03217 92 --------------------VKNADFLRYV-----------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI-DA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1438 LQMQAMLGSWFAQ--CTVLLIAH--RLRSVMDCARVLVMDKGQVAESGSP--AQLLAQKG 1491
Cdd:cd03217 140 LRLVAEVINKLREegKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKelALEIEKKG 199
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
644-786 |
2.71e-05 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 47.04 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 644 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGelskveGFVSIEGAVAYVPQEAWV--------------------- 702
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG------NYLPDSGSILVRHDGGWVdlaqaspreilalrrrtigyv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 703 -QNTSVVENVcfgqeldpPWLERVLEAcALQPDVDSfpegiHTSIGEQG-----MNL------------SGGQKQRLSLA 764
Cdd:COG4778 99 sQFLRVIPRV--------SALDVVAEP-LLERGVDR-----EEARARARellarLNLperlwdlppatfSGGEQQRVNIA 164
|
170 180
....*....|....*....|..
gi 1827346401 765 RAVYRKAAVYLLDDPLAALDAH 786
Cdd:COG4778 165 RGFIADPPLLLLDEPTASLDAA 186
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
754-840 |
2.76e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 48.16 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 754 SGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNqvigpggLLQ------GTTRILVTHAL----HIlpqADWI 823
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVN-------LLQqlqremGLSLIFIAHDLavvkHI---SDRV 232
|
90
....*....|....*..
gi 1827346401 824 IVLANGAIAEMGSYQEL 840
Cdd:PRK15079 233 LVMYLGHAVELGTYDEV 249
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
646-784 |
3.05e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.48 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------------VAYVPQE----AWVQNTSV 707
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsprerrrlgVAYIPEDrlgrGLVPDMSV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 708 VENVCFGQELDPPWLERVLeacaLQPD---------VDSF---PEGIHTSIGeqgmNLSGGQKQRLSLARAVYRKAAVYL 775
Cdd:COG3845 354 AENLILGRYRRPPFSRGGF----LDRKairafaeelIEEFdvrTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLI 425
|
....*....
gi 1827346401 776 LDDPLAALD 784
Cdd:COG3845 426 AAQPTRGLD 434
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
646-763 |
3.22e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.58 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------------VAYVPQ---EAWVQNTSVV 708
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGdmadarhrravcprIAYMPQglgKNLYPTLSVF 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 709 ENV-----CFGQelDPPW----LERVLEACALQPDVDSfPEGihtsigeqgmNLSGGQKQRLSL 763
Cdd:NF033858 97 ENLdffgrLFGQ--DAAErrrrIDELLRATGLAPFADR-PAG----------KLSGGMKQKLGL 147
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1265-1479 |
3.29e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 48.52 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYrPELPLaVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIwidgvpiaHVGlHTLrsRISI 1344
Cdd:COG0488 316 LELEGLSKSY-GDKTL-LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV--------KLG-ETV--KIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1345 IPQDPILFPGSLRMnLDLLQEHSDEAiwaalETVQLKALVASL--PGQLQYKcadRGEDLSVGQKQLLCLARALLRKTQI 1422
Cdd:COG0488 383 FDQHQEELDPDKTV-LDELRDGAPGG-----TEQEVRGYLGRFlfSGDDAFK---PVGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1423 LILDEATAAVDPGTELQMQAMLGSWfaQCTVLLIAH-R--LRSVmdCARVLVMDKGQVAE 1479
Cdd:COG0488 454 LLLDEPTNHLDIETLEALEEALDDF--PGTVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
752-841 |
3.71e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.39 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 752 NLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNqvIGPGGLLQGTTRILVTHAL-HILPQADWIIVLANGA 830
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLdNVLEWTKRTIFFKDGK 242
|
90
....*....|.
gi 1827346401 831 IAEMGSYQELL 841
Cdd:PRK13651 243 IIKDGDTYDIL 253
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1286-1497 |
3.93e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1286 SFKIHAGEKVGIVGRTGAGKSSLA---SGLLRLqeaAEGGIWIDGVPIAHVGLHTLRSRISIIPQdpilfpgslRMNLDL 1362
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALAralAGELPL---LSGERQSQFSHITRLSFEQLQKLVSDEWQ---------RNNTDM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1363 LQEHSDEAIWAALETVQLK----ALVASLPGQLQYK--CADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGT 1436
Cdd:PRK10938 91 LSPGEDDTGRTTAEIIQDEvkdpARCEQLAQQFGITalLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 1437 ELQMQAMLGSWFAQ-CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQkGLFYRLA 1497
Cdd:PRK10938 171 RQQLAELLASLHQSgITLVLVLNRFDEIPDFVqFAGVLADCTLAETGEREEILQQ-ALVAQLA 232
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
649-832 |
4.75e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.98 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------------VAYVP----QEAWVQNTSVVEN 710
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpidirsprdairagIMLCPedrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 711 V---C------FGQELDPPWlERVLeacalqpdVDSFPE--GIHTSIGEQG-MNLSGGQKQRLSLARAVYRKAAVYLLDD 778
Cdd:PRK11288 352 InisArrhhlrAGCLINNRW-EAEN--------ADRFIRslNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1827346401 779 PLAALDahVG-QHVFNQVIgpGGLL-QGTTRILVTHAL-HILPQADWIIVLANGAIA 832
Cdd:PRK11288 423 PTRGID--VGaKHEIYNVI--YELAaQGVAVLFVSSDLpEVLGVADRIVVMREGRIA 475
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
648-784 |
4.93e-05 |
|
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: 48.01 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 648 RINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAV--AYVPQ--EAWVQNTSVVENVCFGQEldppwle 723
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVklAYVDQsrDALDPNKTVWEEISGGLD------- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 724 rvleacalqpdvdsfpegiHTSIGEQGMN---------------------LSGGQKQRLSLARAVYRKAAVYLLDDPLAA 782
Cdd:TIGR03719 413 -------------------IIKLGKREIPsrayvgrfnfkgsdqqkkvgqLSGGERNRVHLAKTLKSGGNVLLLDEPTND 473
|
..
gi 1827346401 783 LD 784
Cdd:TIGR03719 474 LD 475
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
591-843 |
4.95e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 47.66 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 591 LVQARVSFDRLVTFlCLEEVDPGVvdsssSGSAAGKDCITIH--SATFAWsQESPPCLHRINLTVPQGCLLAVVGPVGAG 668
Cdd:PRK10522 289 LLSAQVAFNKLNKL-ALAPYKAEF-----PRPQAFPDWQTLElrNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSG 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 669 KSSLLSALLGELSKVEGFVSIEGA-VAYVPQEAWVQNTSVVenvcF-------------GQELDPPWLERVLEACALQPD 734
Cdd:PRK10522 362 KSTLAMLLTGLYQPQSGEILLDGKpVTAEQPEDYRKLFSAV----FtdfhlfdqllgpeGKPANPALVEKWLERLKMAHK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 735 VdSFPEGIHTSIgeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQhVFNQVIGPggLLQ--GTTRILVTH 812
Cdd:PRK10522 438 L-ELEDGRISNL-----KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRR-EFYQVLLP--LLQemGKTIFAISH 508
|
250 260 270
....*....|....*....|....*....|..
gi 1827346401 813 ALHILPQADWIIVLANGAIAEM-GSYQELLQR 843
Cdd:PRK10522 509 DDHYFIHADRLLEMRNGQLSELtGEERDAASR 540
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1281-1331 |
5.09e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.60 E-value: 5.09e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIA 1331
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR 69
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
985-1191 |
5.76e-05 |
|
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: 46.86 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 985 ALRGGIFGLLGCLQAIGLFASMAAVL--LGG----ARASRLLFQRLlwdvVRSPISFFERTPIGHLLNRFSKET----DT 1054
Cdd:cd18780 40 ALNQAVLILLGVVLIGSIATFLRSWLftLAGervvARLRKRLFSAI----IAQEIAFFDVTRTGELLNRLSSDTqvlqNA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1055 VDVDIPDKLRSLLMyAFGLLEVSLVVAVATPLATVAILPLFLLYAGFQSLYVVsscQLRRL---ESASYSSVCShmaETF 1131
Cdd:cd18780 116 VTVNLSMLLRYLVQ-IIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVR---KLSKKfqdALAAASTVAE---ESI 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1132 QGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLaanvellgNGLVFAAATCAV 1191
Cdd:cd18780 189 SNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGF--------NGFMGAAAQLAI 240
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
646-830 |
5.77e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.48 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSAllgeLSKVEGFVSIEGAVAY--------------------VPQE-AWVQN 704
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKV----LSGVYPHGSYEGEILFdgevcrfkdirdsealgiviIHQElALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 705 TSVVENVCFGQE------LDppWLERVLEACALQPDVdsfpeGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDD 778
Cdd:NF040905 93 LSIAENIFLGNErakrgvID--WNETNRRARELLAKV-----GLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1827346401 779 PLAALDAHVGQHVFNqvigpggLL-----QGTTRILVTHALH-ILPQADWIIVLANGA 830
Cdd:NF040905 166 PTAALNEEDSAALLD-------LLlelkaQGITSIIISHKLNeIRRVADSITVLRDGR 216
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
649-844 |
6.05e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 46.72 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA------------VAYVPQ-EAWVQNTSVVENV-CFG 714
Cdd:PRK13537 26 LSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharqrVGVVPQfDNLDPDFTVRENLlVFG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 715 Q----------ELDPPwlerVLEACALQPDVDSfpegihtSIGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 784
Cdd:PRK13537 106 RyfglsaaaarALVPP----LLEFAKLENKADA-------KVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 785 AHVGQHVFNQVigPGGLLQGTTRILVTHALHILPQ-ADWIIVLANG-AIAEmGSYQELLQRK 844
Cdd:PRK13537 171 PQARHLMWERL--RSLLARGKTILLTTHFMEEAERlCDRLCVIEEGrKIAE-GAPHALIESE 229
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1285-1464 |
6.11e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 46.26 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1285 VSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIwidgvpiahvgLHTLRSRISIIPQ----DPILfPGSLRMNL 1360
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVPQklylDTTL-PLTVNRFL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1361 DLLQEHSDEAIWAALETVQLKALVASlPGQlqykcadrgeDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTEL-- 1438
Cdd:PRK09544 91 RLRPGTKKEDILPALKRVQAGHLIDA-PMQ----------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVal 159
|
170 180 190
....*....|....*....|....*....|.
gi 1827346401 1439 -----QMQAMLGswfaqCTVLLIAHRLRSVM 1464
Cdd:PRK09544 160 ydlidQLRRELD-----CAVLMVSHDLHLVM 185
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1285-1481 |
6.54e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 46.16 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1285 VSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDG------VPIAHVGLHTLRSRISIIPQDPILFPG-SLR 1357
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQYNLWPHlTVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1358 MNL-----DLLQEHSDEAIWAA---LETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLARALLRKTQILILDEAT 1429
Cdd:PRK11124 101 QNLieapcRVLGLSKDQALARAeklLERLRLKPYADRFPLHL-----------SGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 1430 AAVDPGTELQMQAMLGSwFAQC--TVLLIAHRLRSVMDCA-RVLVMDKGQVAESG 1481
Cdd:PRK11124 170 AALDPEITAQIVSIIRE-LAETgiTQVIVTHEVEVARKTAsRVVYMENGHIVEQG 223
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
751-829 |
6.86e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 46.02 E-value: 6.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 751 MNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHV------FNQVigpggllqGTTRILVTHALHILPQADW-I 823
Cdd:PRK10908 136 IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIlrlfeeFNRV--------GVTVLMATHDIGLISRRSYrM 207
|
....*.
gi 1827346401 824 IVLANG 829
Cdd:PRK10908 208 LTLSDG 213
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
646-843 |
7.19e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 46.62 E-value: 7.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGavaYVPQE---AWVQNTSVVenvcFGQ------- 715
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG---YVPFKrrkEFARRIGVV----FGQrsqlwwd 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 716 --------------ELDPPWLERVLEACALQPDVDSFpegIHTSIgeqgMNLSGGQKQRLSLARAVYRKAAVYLLDDPLA 781
Cdd:COG4586 111 lpaidsfrllkaiyRIPDAEYKKRLDELVELLDLGEL---LDTPV----RQLSLGQRMRCELAAALLHRPKILFLDEPTI 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827346401 782 ALDAHVGQHV------FNQVigpggllQGTTRILVTH------ALhilpqADWIIVLANGAIAEMGSYQELLQR 843
Cdd:COG4586 184 GLDVVSKEAIreflkeYNRE-------RGTTILLTSHdmddieAL-----CDRVIVIDHGRIIYDGSLEELKER 245
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
990-1140 |
8.06e-05 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 46.35 E-value: 8.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 990 IFGLLGCLQAIGLFASMAAVLL---GGARASRLLFQRLLWDVVRSPISFFERTPIGHLLNRFSKET----DTVDVDIPDK 1062
Cdd:cd18573 43 FALALLGVFVVGAAANFGRVYLlriAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTsvvgKSLTQNLSDG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1063 LRSLLMYAFGlleVSLVVAVATPLATV--AILPLFLLYAGFQSLYvVSSCQLRRLESASYSSVCShmAETFQGSTVVRAF 1140
Cdd:cd18573 123 LRSLVSGVGG---IGMMLYISPKLTLVmlLVVPPIAVGAVFYGRY-VRKLSKQVQDALADATKVA--EERLSNIRTVRAF 196
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
1020-1236 |
9.97e-05 |
|
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: 45.88 E-value: 9.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1020 LFQRLLwdvvRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLL---MYAFGLLEV--------SLVVAVATPLAT 1088
Cdd:cd18552 78 LFDKLL----RLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVrdpLTVIGLLGVlfyldwklTLIALVVLPLAA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1089 VAIlplflLYAGfqslyvvsscqlRRLESASYSS------VCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISF 1162
Cdd:cd18552 154 LPI-----RRIG------------KRLRKISRRSqesmgdLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSM 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 1163 PRLVADRWLAANVELLGnGLVFAA----ATCAVLSkAHLSAG-LVGFsVSAALQVTQTLQWVVRNWTDLENSIVSVERM 1236
Cdd:cd18552 217 KIARARALSSPLMELLG-AIAIALvlwyGGYQVIS-GELTPGeFISF-ITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1281-1483 |
1.03e-04 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 46.48 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLasglLRL----QEAAEGGIWIDGVPIAHV-----GLHTlrsrisiIPQDPIL 1351
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTV----LRLiagfETPDSGRIMLDGQDITHVpaenrHVNT-------VFQSYAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1352 FPG---------SLRMnldllQEHSDEAIWA----ALETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLARALLR 1418
Cdd:PRK09452 98 FPHmtvfenvafGLRM-----QKTPAAEITPrvmeALRMVQLEEFAQRKPHQL-----------SGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1419 KTQILILDEATAAVDPGTELQMQAMLGSWFAQC--TVLLIAHRLR---SVMDcaRVLVMDKGQVAESGSP 1483
Cdd:PRK09452 162 KPKVLLLDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEealTMSD--RIVVMRDGRIEQDGTP 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
626-843 |
1.23e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.77 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 626 KDCITIHSATFAWSQESP--PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVS--------------- 688
Cdd:PRK10261 10 RDVLAVENLNIAFMQEQQkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrrrsrqvie 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 689 -----------IEGA-VAYVPQE-------AWVQNTSVVENVCFGQELDPpwlERVLEACALQPDVDSFPEGiHTSIGEQ 749
Cdd:PRK10261 90 lseqsaaqmrhVRGAdMAMIFQEpmtslnpVFTVGEQIAESIRLHQGASR---EEAMVEAKRMLDQVRIPEA-QTILSRY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 750 GMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFnQVIgpgGLLQGTTR---ILVTHALHILPQ-ADWIIV 825
Cdd:PRK10261 166 PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQIL-QLI---KVLQKEMSmgvIFITHDMGVVAEiADRVLV 241
|
250
....*....|....*...
gi 1827346401 826 LANGAIAEMGSYQELLQR 843
Cdd:PRK10261 242 MYQGEAVETGSVEQIFHA 259
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
646-830 |
1.46e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.32 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG--------------AVAYVPQEAWVQNT-SVVEN 710
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhklaaqlGIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 711 VCFGQELDPP--------WLERVLEACALQPDVdsfpeGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAA 782
Cdd:PRK09700 101 LYIGRHLTKKvcgvniidWREMRVRAAMMLLRV-----GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 783 L-DAHVGQ--HVFNQVIGpggllQGTTRILVTHAL-HILPQADWIIVLANGA 830
Cdd:PRK09700 176 LtNKEVDYlfLIMNQLRK-----EGTAIVYISHKLaEIRRICDRYTVMKDGS 222
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
717-826 |
1.87e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 717 LDPPWLERVLEA-CALQPDvdsfpegiHTSIGEQGMNLSGGQKQRLSLAR---AVYRKAAVYLLDDPLAAL---DAHVGQ 789
Cdd:PRK00635 781 LDEPSIHEKIHAlCSLGLD--------YLPLGRPLSSLSGGEIQRLKLAYellAPSKKPTLYVLDEPTTGLhthDIKALI 852
|
90 100 110
....*....|....*....|....*....|....*..
gi 1827346401 790 HVFNQVIgpgglLQGTTRILVTHALHILPQADWIIVL 826
Cdd:PRK00635 853 YVLQSLT-----HQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
979-1210 |
2.15e-04 |
|
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: 45.17 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 979 GQQTQAALRGGIFGLLG--CLQAIGLFASMAAVLLGGARAS----RLLFQRLLwdvvRSPISFFERTPIGHLLNRFSkeT 1052
Cdd:cd18575 28 AAGNTALLNRAFLLLLAvaLVLALASALRFYLVSWLGERVVadlrKAVFAHLL----RLSPSFFETTRTGEVLSRLT--T 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1053 DT------VDVDIPDKLRSLLMYAFGL-------LEVSLVVAVATPLatvAILPLFLLyagfqslyvvsSCQLRRLESAS 1119
Cdd:cd18575 102 DTtliqtvVGSSLSIALRNLLLLIGGLvmlfitsPKLTLLVLLVIPL---VVLPIILF-----------GRRVRRLSRAS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1120 ---YSSVCSHMAETFQGSTVVRAFrTQAPFVAQN-NARVDESQRISFPRLVADRWLAANVELlgngLVFAAATC------ 1189
Cdd:cd18575 168 qdrLADLSAFAEETLSAIKTVQAF-TREDAERQRfATAVEAAFAAALRRIRARALLTALVIF----LVFGAIVFvlwlga 242
|
250 260
....*....|....*....|...
gi 1827346401 1190 -AVLSKAhLSAG-LVGFSVSAAL 1210
Cdd:cd18575 243 hDVLAGR-MSAGeLSQFVFYAVL 264
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1281-1480 |
2.25e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG-LHTLRSRISIIPQDPILFPG-SLRM 1358
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGpKSSQEAGIGIIHQELNLIPQlTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1359 NLDLLQEHSDeaIWAALETVQLKA----LVASLpgQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAV-D 1433
Cdd:PRK10762 99 NIFLGREFVN--RFGRIDWKKMYAeadkLLARL--NLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1827346401 1434 PGT--------ELQMQAmlgswfaqCTVLLIAHRLRSVMD-CARVLVMDKGQ-VAES 1480
Cdd:PRK10762 175 TETeslfrvirELKSQG--------RGIVYISHRLKEIFEiCDDVTVFRDGQfIAER 223
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
990-1192 |
2.37e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 44.79 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 990 IFGLLGCLQAIGLFASMAAVLLGGARASRLLF----------QRLlwdvvrsPISFFERTPIGHLLNRFsketdTVDVDi 1059
Cdd:cd18546 41 AAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYdlrlrvfahlQRL-------SLDFHERETSGRIMTRM-----TSDID- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1060 pdKLRSLLMYafGLleVSLVVAVATPLATVAIL-----PLFLLYAGFQSLYVVSSCQLRRLESASY-------SSVCSHM 1127
Cdd:cd18546 108 --ALSELLQT--GL--VQLVVSLLTLVGIAVVLlvldpRLALVALAALPPLALATRWFRRRSSRAYrrareriAAVNADL 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 1128 AETFQGSTVVRAFR----TQAPFVAQNNARVDESQRISfpRLVAdrWLAANVELLGNglvfaAATCAVL 1192
Cdd:cd18546 182 QETLAGIRVVQAFRrerrNAERFAELSDDYRDARLRAQ--RLVA--IYFPGVELLGN-----LATAAVL 241
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
728-784 |
2.47e-04 |
|
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: 43.71 E-value: 2.47e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1827346401 728 ACALQP--DVDSFPeGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 784
Cdd:cd03222 46 AGQLIPngDNDEWD-GITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLD 103
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
311-483 |
2.50e-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: 44.71 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 311 FLLGTLSLIISDVFRFTVPKLLSLFLEFIGDPKPPAWKGYLLAVLMFLSACLQTLFeqQNMYRLKV------LQMRLRSA 384
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTASQLLRYALLILLLALLIGIF--RFLWRYLIfgasrrIEYDLRND 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 385 ItglvYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTES----VLYL-NGLWLPLVWIVVCFVYLWQLlgpsALTAIAVF 459
Cdd:cd18541 79 L----FAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMAlgpgILYLvDALFLGVLVLVMMFTISPKL----TLIALLPL 150
|
170 180
....*....|....*....|....
gi 1827346401 460 LSLLPLNFFISKKRNHHQEEQMRQ 483
Cdd:cd18541 151 PLLALLVYRLGKKIHKRFRKVQEA 174
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1285-1489 |
2.79e-04 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 45.10 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1285 VSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHvglHTLRSR-ISIIPQDPILFPG--------- 1354
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH---RSIQQRdICMVFQSYALFPHmslgenvgy 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1355 SLRMnLDLLQEHSDEAIWAALETVQLKALvaslpgqlqykcADRGED-LSVGQKQLLCLARALLRKTQILILDEATAAVD 1433
Cdd:PRK11432 102 GLKM-LGVPKEERKQRVKEALELVDLAGF------------EDRYVDqISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827346401 1434 PG---------TELQMQAMLgswfaqcTVLLIAH---RLRSVMDcaRVLVMDKGQVAESGSPAQLLAQ 1489
Cdd:PRK11432 169 ANlrrsmrekiRELQQQFNI-------TSLYVTHdqsEAFAVSD--TVIVMNKGKIMQIGSPQELYRQ 227
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
646-841 |
3.25e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 44.32 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGF-------------------VSIEGAVAYVPQEAWVQNTS 706
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdvllggrsifnyrdvLEFRRRVGMLFQRPNPFPMS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 707 VVENVCFGQELDP--PWLERVLEACALQPDVDSFpEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 784
Cdd:PRK14271 117 IMDNVLAGVRAHKlvPRKEFRGVAQARLTEVGLW-DAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1827346401 785 AHVGQHVFNQVigpGGLLQGTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELL 841
Cdd:PRK14271 196 PTTTEKIEEFI---RSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLF 250
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1281-1479 |
3.34e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 44.31 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGlhtlrSRISIIPQDPILFP-----GS 1355
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVVFQNEGLLPwrnvqDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1356 LRMNLDLL---QEHSDEAIWAALETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLARALLRKTQILILDEATAAV 1432
Cdd:PRK11248 91 VAFGLQLAgveKMQRLEIAHQMLKKVGLEGAEKRYIWQL-----------SGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 1433 DPGTELQMQAMLGSWFAQC--TVLLIAHRLRSVMDCARVLVM---DKGQVAE 1479
Cdd:PRK11248 160 DAFTREQMQTLLLKLWQETgkQVLLITHDIEEAVFMATELVLlspGPGRVVE 211
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
646-842 |
6.32e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 43.28 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 646 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELS--------KVEGFVSIEGAV-------------AYVPQEAWVQN 704
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPlaaidaprlarlrAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 705 T-SVVENVCFGQEldpPWLERVLEACALQPDVDSFP---EGIHTSIGEQGMNLSGGQKQRLSLARAV---------YRKA 771
Cdd:PRK13547 97 AfSAREIVLLGRY---PHARRAGALTHRDGEIAWQAlalAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 772 AVYLLDDPLAALD-AHvgQHvfnqvigpggLLQGTTRIL----------VTHALHILPQ-ADWIIVLANGAIAEMGSYQE 839
Cdd:PRK13547 174 RYLLLDEPTAALDlAH--QH----------RLLDTVRRLardwnlgvlaIVHDPNLAARhADRIAMLADGAIVAHGAPAD 241
|
...
gi 1827346401 840 LLQ 842
Cdd:PRK13547 242 VLT 244
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
977-1236 |
6.65e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 43.65 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 977 VGGQQTQAALRGGIFGLLGCLQAIGLFASMA----AVLLGGARASRL---LFQRLLwdvvRSPISFFERTPIGHLLNRFS 1049
Cdd:cd18563 32 QLGPGGNTSLLLLLVLGLAGAYVLSALLGILrgrlLARLGERITADLrrdLYEHLQ----RLSLSFFDKRQTGSLMSRVT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1050 KETDTVD---VD-IPDKLRSLLMyafgLLEVSLVVAVATP-LATVAILPLFLLYAGFQSLYVVSSCQLRRLeSASYSSVC 1124
Cdd:cd18563 108 SDTDRLQdflSDgLPDFLTNILM----IIGIGVVLFSLNWkLALLVLIPVPLVVWGSYFFWKKIRRLFHRQ-WRRWSRLN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1125 SHMAETFQGSTVVRAFrtqapfvAQNNarvDESQRisFpRLVADRWLAANVEL----------------LGNGLVFAAAT 1188
Cdd:cd18563 183 SVLNDTLPGIRVVKAF-------GQEK---REIKR--F-DEANQELLDANIRAeklwatffplltfltsLGTLIVWYFGG 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1827346401 1189 CAVLSkAHLSAG-LVGFsVSAALQVTQTLQWVVRNWTDLENSIVSVERM 1236
Cdd:cd18563 250 RQVLS-GTMTLGtLVAF-LSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
754-840 |
6.86e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.93 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 754 SGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVIGpgglLQGTTR---ILVTHALHILPQ-ADWIIVLANG 829
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKS----LQQKHQlayLFISHDLHVVRAlCHQVIVLRQG 502
|
90
....*....|.
gi 1827346401 830 AIAEMGSYQEL 840
Cdd:PRK15134 503 EVVEQGDCERV 513
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
975-1185 |
8.05e-04 |
|
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: 43.24 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 975 PAVGGQQTQAALRGGIFG--------LLGCLQAIGLFASMAAVLLG--GARASRLLFQRLLWDVVRSPISFFERTPIGHL 1044
Cdd:cd18576 16 PLLAGQLIDAALGGGDTAslnqiallLLGLFLLQAVFSFFRIYLFArvGERVVADLRKDLYRHLQRLPLSFFHERRVGEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1045 LNRFSKET----DTVDVDIPDKLRSLLMYAFGlleVSLVVAVATPLATV--AILPLFLLYAgfqslyVVSSCQLRRLESA 1118
Cdd:cd18576 96 TSRLSNDVtqiqDTLTTTLAEFLRQILTLIGG---VVLLFFISWKLTLLmlATVPVVVLVA------VLFGRRIRKLSKK 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 1119 ---SYSSVCSHMAETFQGSTVVRAFrTQAPF-VAQNNARVDESQRISFPRLVADRWLAANVELLGNGLVFA 1185
Cdd:cd18576 167 vqdELAEANTIVEETLQGIRVVKAF-TREDYeIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVA 236
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
968-1192 |
8.28e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 43.27 E-value: 8.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 968 LSLWADDPAVGGQQTQAALRGGIFGLLGCLQAIGLFASMAAVLLGGARASRL---LFQRLLwdvvRSPISFFERTPIGHL 1044
Cdd:cd18564 38 LLGLAPLLGPDPLALLLLAAAALVGIALLRGLASYAGTYLTALVGQRVVLDLrrdLFAHLQ----RLSLSFHDRRRTGDL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1045 LNRFsketdTVDVDipdKLRSLLMYAFGLLEVSLVVAVAT-----------PLATVAILPLFLLYA-GFQSLYVVSSCQL 1112
Cdd:cd18564 114 LSRL-----TGDVG---AIQDLLVSGVLPLLTNLLTLVGMlgvmfwldwqlALIALAVAPLLLLAArRFSRRIKEASREQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1113 RRLESASYSSVcshmAETFQGSTVVRAF----RTQAPFVAQNNARVDESQRISfpRLVAdrWLAANVELLGnglvfAAAT 1188
Cdd:cd18564 186 RRREGALASVA----QESLSAIRVVQAFgreeHEERRFARENRKSLRAGLRAA--RLQA--LLSPVVDVLV-----AVGT 252
|
....
gi 1827346401 1189 CAVL 1192
Cdd:cd18564 253 ALVL 256
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1281-1327 |
8.52e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 43.29 E-value: 8.52e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSlasgLLR----LQEAAEGGIWIDG 1327
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKST----LLRmvagLERITSGEIWIGG 65
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
647-824 |
8.95e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.58 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 647 HRINLTV-----PQGCLLAVVGPVGAGKSSLLSAL---LGELSKVEGFVSIEGAVAYVPQEawvqntsvvenvcfgqeld 718
Cdd:cd03227 7 FPSYFVPndvtfGEGSLTIITGPNGSGKSTILDAIglaLGGAQSATRRRSGVKAGCIVAAV------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 719 ppwlervlEACalqpdvdsfpegIHTSIgeqgMNLSGGQKQRLSLARAV----YRKAAVYLLDDPLAALDAHVGQHVFNQ 794
Cdd:cd03227 68 --------SAE------------LIFTR----LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEA 123
|
170 180 190
....*....|....*....|....*....|
gi 1827346401 795 VIGPggLLQGTTRILVTHALHILPQADWII 824
Cdd:cd03227 124 ILEH--LVKGAQVIVITHLPELAELADKLI 151
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1285-1486 |
9.59e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 43.48 E-value: 9.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1285 VSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDG-----VPIAHVGlhtlrsrISIIPQDPILFPgslrmN 1359
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmndVPPAERG-------VGMVFQSYALYP-----H 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1360 LDLLQEHS-------------DEAIWAALETVQLKALVASLPgqlqykcadrgEDLSVGQKQLLCLARALLRKTQILILD 1426
Cdd:PRK11000 90 LSVAENMSfglklagakkeeiNQRVNQVAEVLQLAHLLDRKP-----------KALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 1427 EATAAVDPGTELQMQAMLGSWFA--QCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQL 1486
Cdd:PRK11000 159 EPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHDQVEAMTLAdKIVVLDAGRVAQVGKPLEL 221
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
990-1235 |
1.25e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 42.58 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 990 IFGLLGCLQAIGLFASMAAVL---LGGAR-------ASRL-------LFQRLLwdvvRSPISFFERTPIGHLLNRFSkET 1052
Cdd:cd18782 34 VQQDLATLYVIGVVMLVAALLeavLTALRtylftdtANRIdlelggtIIDHLL----RLPLGFFDKRPVGELSTRIS-EL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1053 DTVDVDIPDK-LRSLLMYAFGLLEVSLVVAVATPL--ATVAILPLFLLyagfqsLYVVSSCQLRRL---ESASYSSVCSH 1126
Cdd:cd18782 109 DTIRGFLTGTaLTTLLDVLFSVIYIAVLFSYSPLLtlVVLATVPLQLL------LTFLFGPILRRQirrRAEASAKTQSY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1127 MAETFQGSTVVRAFRTQAPFVAQNNAR----VDESQRISFPRLVADRwLAANVELLGNGLVFAAATCAVLsKAHLSAG-L 1201
Cdd:cd18782 183 LVESLTGIQTVKAQNAELKARWRWQNRyarsLGEGFKLTVLGTTSGS-LSQFLNKLSSLLVLWVGAYLVL-RGELTLGqL 260
|
250 260 270
....*....|....*....|....*....|....
gi 1827346401 1202 VGFSVSAAlQVTQTLQWVVRNWTDLENSIVSVER 1235
Cdd:cd18782 261 IAFRILSG-YVTGPILRLSTLWQQFQELRVSLER 293
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1265-1486 |
1.97e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.04 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRpelplAVQGVSFKIHAGEKVGIVGRTGAGKS--SLA-SGLLRLqeaaEGGIWIDGVPIAHVGLHTLRSR 1341
Cdd:PRK11022 11 VHFGDESAPFR-----AVDRISYSVKQGEVVGIVGESGSGKSvsSLAiMGLIDY----PGRVMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1342 ---------ISIIPQDPI--LFP----GSLRMnlDLLQEHSD-EAIWAALETVQLKALVAsLPGQlqykcADRGE----D 1401
Cdd:PRK11022 82 errnlvgaeVAMIFQDPMtsLNPcytvGFQIM--EAIKVHQGgNKKTRRQRAIDLLNQVG-IPDP-----ASRLDvyphQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1402 LSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQVA 1478
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKenMALVLITHDLALVAEAAhKIIVMYAGQVV 233
|
....*...
gi 1827346401 1479 ESGSPAQL 1486
Cdd:PRK11022 234 ETGKAHDI 241
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
660-683 |
2.07e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 39.52 E-value: 2.07e-03
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1281-1488 |
2.44e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.71 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAaEGGIWIDGVPIAHVGLHTLRSR---------ISIIPQDP-- 1349
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKD-NWRVTADRMRFDDIDLLRLSPRerrklvghnVSMIFQEPqs 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1350 ILFPgSLRMNLDLLQehsdeAI--------------WAALETVQL---------KALVASLPGQLqykcadrgedlSVGQ 1406
Cdd:PRK15093 101 CLDP-SERVGRQLMQ-----NIpgwtykgrwwqrfgWRKRRAIELlhrvgikdhKDAMRSFPYEL-----------TEGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1407 KQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSP 1483
Cdd:PRK15093 164 CQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnnTTILLISHDLQMLSQWAdKINVLYCGQTVETAPS 243
|
....*
gi 1827346401 1484 AQLLA 1488
Cdd:PRK15093 244 KELVT 248
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1292-1465 |
2.73e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.05 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1292 GEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIwidgvpiahvglhtlrsrisiipqdpilfpgsLRMNLDLLQEHSDEAI 1371
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------------IYIDGEDILEEVLDQL 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1372 WAALETVqlkalvaslpgqlqykcadRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWF--- 1448
Cdd:smart00382 50 LLIIVGG-------------------KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLlll 110
|
170 180
....*....|....*....|.
gi 1827346401 1449 ----AQCTVLLIAHRLRSVMD 1465
Cdd:smart00382 111 lkseKNLTVILTTNDEKDLGP 131
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1268-1322 |
3.11e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 41.06 E-value: 3.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 1268 RDFGLRYRPELplAVQGVSFKIHAGEKVGIVGRTGAGKSSLASgLLRLQEAAEGG 1322
Cdd:PRK11701 10 RGLTKLYGPRK--GCRDVSFDLYPGEVLGIVGESGSGKTTLLN-ALSARLAPDAG 61
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
660-679 |
3.74e-03 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 39.92 E-value: 3.74e-03
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1265-1491 |
4.64e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.65 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1265 IEFRDFGLRYRPELplAVQGVSFKIHAGEKVGIVGRTGAGKSSL---ASGLLRLQEaaeGGIWIDGVPIAHVGlH--TLR 1339
Cdd:NF033858 2 ARLEGVSHRYGKTV--ALDDVSLDIPAGCMVGLIGPDGVGKSSLlslIAGARKIQQ---GRVEVLGGDMADAR-HrrAVC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1340 SRISIIPQD------PILfpgSLRMNLD-------LLQEHSDEAIWAALETVQLKALvaslpgqlqykcADR--GEdLSV 1404
Cdd:NF033858 76 PRIAYMPQGlgknlyPTL---SVFENLDffgrlfgQDAAERRRRIDELLRATGLAPF------------ADRpaGK-LSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1405 GQKQllclarallrKT----------QILILDEATAAVDPGTELQmqamlgswFAQctvlLIAhRLR------SV----- 1463
Cdd:NF033858 140 GMKQ----------KLglccalihdpDLLILDEPTTGVDPLSRRQ--------FWE----LID-RIRaerpgmSVlvata 196
|
250 260 270
....*....|....*....|....*....|...
gi 1827346401 1464 -MDCA----RVLVMDKGQVAESGSPAQLLAQKG 1491
Cdd:NF033858 197 yMEEAerfdWLVAMDAGRVLATGTPAELLARTG 229
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1285-1492 |
4.96e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 40.30 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1285 VSFKIHAGEKVGIVGRTGAGKSSL---ASGLLrlqeAAEGGIWIDGVPIAHVGLHTL-RSRISIIPQDPILFPGSLRMNL 1360
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLlarMAGLL----PGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1361 DLLQehSDEAIWAALETVqLKALVASLpgQLQYKCADRGEDLSVGQKQLLCLAR-------ALLRKTQILILDEATAAVD 1433
Cdd:PRK03695 91 TLHQ--PDKTRTEAVASA-LNEVAEAL--GLDDKLGRSVNQLSGGEWQRVRLAAvvlqvwpDINPAGQLLLLDEPMNSLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827346401 1434 PGTELQMQAMLgSWFAQC--TVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQKGL 1492
Cdd:PRK03695 166 VAQQAALDRLL-SELCQQgiAVVMSSHDLNHTLRHAdRVWLLKQGKLLASGRRDEVLTPENL 226
|
|
| MTABC_N |
pfam16185 |
Mitochondrial ABC-transporter N-terminal five TM region; MTABC_N is the N-terminal five ... |
27-145 |
5.44e-03 |
|
Mitochondrial ABC-transporter N-terminal five TM region; MTABC_N is the N-terminal five transmembrane helices of eukaryotic mitochondrial ABC-transporters.
Pssm-ID: 465049 Cd Length: 244 Bit Score: 40.34 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 27 LSLCFLRTAGVWVPPMYLWVLGPIYLLFIHHHG----RGYLRMSPLFKAKMVLGFALIVLCtssVAVALWKI-QQGTPEA 101
Cdd:pfam16185 18 LSPCFYDTLVPSVLLGFLLLFGTIQLIMYRKYGtpmePKFIPRSRLYVLQLFLALLLPLLA---LARFILRAaLIGGGRL 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1827346401 102 PEFLI-----HPTVWlttmSFAVFLIHTERKKGVQS------SGVLFGYWLLCFV 145
Cdd:pfam16185 95 YGYMVlyaclSLLAW----PFSLALLRLERRYALPSlptrghGLVLLLFWTLAFV 145
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
651-783 |
5.49e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.14 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 651 LTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-AVAY----VPQEA----------WVQNTSVVENVCFGQ 715
Cdd:PRK10762 25 LNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkEVTFngpkSSQEAgigiihqelnLIPQLTIAENIFLGR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 716 ELDPP-----WLERVLEACALQPDVdSFPEGIHTSIGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAAL 783
Cdd:PRK10762 105 EFVNRfgridWKKMYAEADKLLARL-NLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1297-1482 |
6.09e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 40.63 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1297 IVGRTGAGKSSLA---SGLLRLQEA-----------AEGGIWidgvpiahvgLHTLRSRISIIPQDPILFPG-SLRMNLD 1361
Cdd:PRK11144 29 IFGRSGAGKTSLInaiSGLTRPQKGrivlngrvlfdAEKGIC----------LPPEKRRIGYVFQDARLFPHyKVRGNLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1362 LLQEHSDEAIWAALetVQL---KALVASLPGqlqykcadrgeDLSVGQKQLLCLARALLRKTQILILDEATAAVDpgteL 1438
Cdd:PRK11144 99 YGMAKSMVAQFDKI--VALlgiEPLLDRYPG-----------SLSGGEKQRVAIGRALLTAPELLLMDEPLASLD----L 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 1439 QMQAMLGSWFAQCT------VLLIAHRLRSVMDCA-RVLVMDKGQVAESGS 1482
Cdd:PRK11144 162 PRKRELLPYLERLAreinipILYVSHSLDEILRLAdRVVVLEQGKVKAFGP 212
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
977-1161 |
6.69e-03 |
|
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: 40.11 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 977 VGGQQTQAALRGGIFGLLGCLQAIGLFASMAAVLLG--GARASRLLfQRLLWD-VVRSPISFFERTPIGHLLNRFSKET- 1052
Cdd:cd18551 26 IDALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGrtGERVVLDL-RRRLWRrLLRLPVSFFDRRRSGDLVSRVTNDTt 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1053 ---DTVDVDIPDKLRSLLMY--AFGLLEV-----SLVVAVATPLATVAILPLfllyagfqslyvvsscqLRRLESASY-- 1120
Cdd:cd18551 105 llrELITSGLPQLVTGVLTVvgAVVLMFLldwvlTLVTLAVVPLAFLIILPL-----------------GRRIRKASKra 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1827346401 1121 ----SSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRIS 1161
Cdd:cd18551 168 qdalGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAG 212
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
352-513 |
6.84e-03 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 40.28 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 352 LAVLMFLSACLQTLFEQqnmYRLKVLQ---MRLRSAITGLVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTESVLYL- 427
Cdd:cd18586 44 LTLGMVVLLAFDGLLRQ---VRSRILQrvgLRLDVELGRRVFRAVLELPLESRPSGYWQQLLRDLDTLRNFLTGPSLFAf 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 428 -NGLWLPLVWIVVCFVYLWqlLGPSALTAIAVFLSLLPLNFFISKKRnhhQEEQMRQKDSRARLTSSILRNSKTIKFHGW 506
Cdd:cd18586 121 fDLPWAPLFLAVIFLIHPP--LGWVALVGAPVLVGLAWLNHRATRKP---LGEANEAQAARDALAAETLRNAETIKALGM 195
|
....*..
gi 1827346401 507 EGAFLDR 513
Cdd:cd18586 196 LGNLRRR 202
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
644-698 |
7.15e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.65 E-value: 7.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1827346401 644 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFV--SIEGAVAYVPQ 698
Cdd:PRK15064 333 PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwSENANIGYYAQ 389
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
1032-1235 |
7.85e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 40.24 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1032 PISFFERTPIGHLLNRFsKETDTVDVDI-PDKLRSLLMYAFGLLEVSLVVAVATPLATVAILpLFLLYAGfqsLYVVSSC 1110
Cdd:cd18568 89 PLSFFASRKVGDIITRF-QENQKIRRFLtRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLA-FIPLYVL---LTLLSSP 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1111 QLRRLESASYSS---VCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVadrwLAANVELLGNgLVFAAA 1187
Cdd:cd18568 164 KLKRNSREIFQAnaeQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQK----LSIVLQLISS-LINHLG 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1827346401 1188 TCAVLS-------KAHLSAG-LVGFSVSAALqVTQTLQWVVRNWTDLENSIVSVER 1235
Cdd:cd18568 239 TIAVLWygaylviSGQLTIGqLVAFNMLFGS-VINPLLALVGLWDELQETRISVER 293
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1281-1486 |
8.03e-03 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 40.00 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLA---SGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLR 1357
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlSGLITGDKSAGSHIELLGRTVQREGRLARDIRKSRANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1358 MNLDLLQEHSDEAI-----------WAALETVQlKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILD 1426
Cdd:PRK09984 99 NRLSVLENVLIGALgstpfwrtcfsWFTREQKQ-RALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 1427 EATAAVDP-GTELQMQAMLG-SWFAQCTVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQL 1486
Cdd:PRK09984 178 EPIASLDPeSARIVMDTLRDiNQNDGITVVVTLHQVDYALRyCERIVALRQGHVFYDGSSQQF 240
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1281-1480 |
8.36e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1281 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAA--EGGIWIDGVPiahVGLHTLRSR----ISIIPQDPILFPG 1354
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEV---CRFKDIRDSealgIVIIHQELALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1355 -SLRMNLDLLQEHSDEAI--WAA--LETVQLKALVAslpgqLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEAT 1429
Cdd:NF040905 93 lSIAENIFLGNERAKRGVidWNEtnRRARELLAKVG-----LDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827346401 1430 AA---------VDPGTELQMQAMlgswfaqcTVLLIAHRLRSVMDCA-RVLVMDKGQVAES 1480
Cdd:NF040905 168 AAlneedsaalLDLLLELKAQGI--------TSIIISHKLNEIRRVAdSITVLRDGRTIET 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
649-829 |
9.50e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 40.19 E-value: 9.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 649 INLTVPQGCLLAVVGPVGAGKSSLLSALLGEL-SKVEGFV--------------SIEGAVAYVPQEAwvQNTSVVENVCF 713
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNVfingkpvdirnpaqAIRAGIAMVPEDR--KRHGIVPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 714 GQELDPPWLER-----VLEACALQPDVDSFPEGIHTSIGEQGM---NLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDA 785
Cdd:TIGR02633 357 GKNITLSVLKSfcfkmRIDAAAELQIIGSAIQRLKVKTASPFLpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1827346401 786 HVGQHVFNQVigpGGLLQ-GTTRILVTHAL-HILPQADWIIVLANG 829
Cdd:TIGR02633 437 GAKYEIYKLI---NQLAQeGVAIIVVSSELaEVLGLSDRVLVIGEG 479
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
301-601 |
9.86e-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: 39.74 E-value: 9.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 301 KAIWQVFHSTFLLGTLSLIISDVFRFTV----PKLLSLFLefigdpkppawkgYLLAVLMFLSACLQTLFE--QQNMyrL 374
Cdd:cd18570 2 KLLILILLLSLLITLLGIAGSFFFQILIddiiPSGDINLL-------------NIISIGLILLYLFQSLLSyiRSYL--L 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 375 KVLQMRLRSAITGLVYRKVLALSS---GSRKasaVGDVVNLVSvDVQR----LTESVLylnGLWLPLVWIVVCFVYL--- 444
Cdd:cd18570 67 LKLSQKLDIRLILGYFKHLLKLPLsffETRK---TGEIISRFN-DANKireaISSTTI---SLFLDLLMVIISGIILffy 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 445 -WQLLGPSALTAIAVFLSLLPLNFFISKKrnhhQEEQMrqkDSRARLTSSI---LRNSKTIKFHGWEGAFLDRVLGIRGQ 520
Cdd:cd18570 140 nWKLFLITLLIIPLYILIILLFNKPFKKK----NREVM---ESNAELNSYLiesLKGIETIKSLNAEEQFLKKIEKKFSK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 521 ELGALRTSGLL--FSVSLVSFQVSTFLVALVVFAVH----------TLVAENAMNAekaFVTLTVLNILNkAQAflpfsi 588
Cdd:cd18570 213 LLKKSFKLGKLsnLQSSIKGLISLIGSLLILWIGSYlvikgqlslgQLIAFNALLG---YFLGPIENLIN-LQP------ 282
|
330
....*....|...
gi 1827346401 589 hSLVQARVSFDRL 601
Cdd:cd18570 283 -KIQEAKVAADRL 294
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
1032-1162 |
9.86e-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: 39.74 E-value: 9.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827346401 1032 PISFFERTPIGHLLNRFSketdtvdvDIpDKLRSLLMYAFG--LLEVSLVVAVATPLA---------TVAILPLF-LLYA 1099
Cdd:cd18570 89 PLSFFETRKTGEIISRFN--------DA-NKIREAISSTTIslFLDLLMVIISGIILFfynwklfliTLLIIPLYiLIIL 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827346401 1100 GFQSLYVvsscQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISF 1162
Cdd:cd18570 160 LFNKPFK----KKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSF 218
|
|
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