|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1-1388 |
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: 1398.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1 MSFAVFLIHTERKKGVQSSGVLFGYWLLCFV---LPATNAAQQASGAGFQSDPVRHLSTYLCLSLVVAQFVLSCLADQPP 77
Cdd:TIGR00957 111 MLLATFLIQLERRKGVQSSGIMLTFWLVALVcalAILRSKILLALKEDAIVDPFRDTTFYIYFALVLSQLVLSCFSDKSP 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 78 FFPEDPQQSNPCPETGAAFPSKATFWWVSGLVWRGYRRPLRPKDLWSLGRENSSEELVSRLEKEWMRNRSAARRHNKAIA 157
Cdd:TIGR00957 191 LFSETNHDPNPCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKTRKQPVSAV 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 158 F------KRKGGSGMKAPETEPFL--RQEGSQWRP-LLKAIWQVFHSTFLLGTLSLIISDVFRFTVPKLLSLFLEFIGDP 228
Cdd:TIGR00957 271 YgkkdpsKPKGSSQLDANEEVEALivKSPHKPRKPsLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVNDP 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 229 KPPAWKGYLLAVLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITGLVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTE 308
Cdd:TIGR00957 351 MAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMD 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 309 SVLYLNGLWLPLVWIVVCFVYLWQLLGPSALTAIAVFLSLLPLNFFISKKRNHHQEEQMRQKDSRARLTSSILRNSKTIK 388
Cdd:TIGR00957 431 LATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLK 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 389 FHGWEGAFLDRVLGIRGQELGALRTSGLLFSVSLVSFQVSTFLVALVVFAVHTLVAE-NAMNAEKAFVTLTVLNILNKAQ 467
Cdd:TIGR00957 511 LYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDEnNILDAEKAFVSLALFNILRFPL 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 468 AFLPFSIHSLVQARVSFDRLVTFLCLEEVDPGVVDSSSSGSAAGkDCITIHSATFAWSQESPPCLHRINLTVPQGCLLAV 547
Cdd:TIGR00957 591 NILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEG-NSITVHNATFTWARDLPPTLNGITFSIPEGALVAV 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 548 VGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQEAWVQNTSVVENVCFGQELDPPWLERVLEACALQPDVDSFPEG 627
Cdd:TIGR00957 670 VGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSG 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 628 IHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVIGPGGLLQGTTRILVTHALHILPQAD 707
Cdd:TIGR00957 750 DRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLKNKTRILVTHGISYLPQVD 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 708 WIIVLANGAIAEMGSYQELLQRKGALVCLL-------DQARQPGDRGEGETEPGTSTKDPRGT-----SAGRrpELRRER 775
Cdd:TIGR00957 830 VIIVMSGGKISEMGSYQELLQRDGAFAEFLrtyapdeQQGHLEDSWTALVSGEGKEAKLIENGmlvtdVVGK--QLQRQL 907
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 776 SIKSVPEKDRTTSEAQT-EVPLDDPDRAGWP-AGKDSIQYGRVKATVHLAYLRAVGTPLCLYALFLFLCQQVASFCRGYW 853
Cdd:TIGR00957 908 SASSSDSGDQSRHHGSSaELQKAEAKEETWKlMEADKAQTGQVELSVYWDYMKAIGLFITFLSIFLFVCNHVSALASNYW 987
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 854 LSLWADDPAVGGQQTQAALRGGIFGLLGCLQAIGLFASMAAVLLGGARASRLLFQRLLWDVVRSPISFFERTPIGHLLNR 933
Cdd:TIGR00957 988 LSLWTDDPMVNGTQNNTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNR 1067
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 934 FSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLLYAGFQSLYVVSSCQLRRLESASYSSVCSHM 1013
Cdd:TIGR00957 1068 FSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHF 1147
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1014 AETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANVELLGNGLVFAAATCAVLSKAHLSAGLVGFSVS 1093
Cdd:TIGR00957 1148 NETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVS 1227
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1094 AALQVTQTLQWVVRNWTDLENSIVSVERMQDYAWTPKEAPWRLPTCAAQPPWPQGGQIEFRDFGLRYRPELPLAVQGVSF 1173
Cdd:TIGR00957 1228 YSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINV 1307
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1174 KIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLDLLQEHS 1253
Cdd:TIGR00957 1308 TIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYS 1387
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1254 DEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSW 1333
Cdd:TIGR00957 1388 DEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQ 1467
|
1370 1380 1390 1400 1410
....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 1334 FAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFYRLAQESGL 1388
Cdd:TIGR00957 1468 FEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAKDAGL 1522
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
57-1387 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 760.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 57 YLCLSLVVAQFVLSCLA-----------DQPPFFPEDPQQS---------NPCPETGAAFPSKATFWWVSGLVWRGYRRP 116
Cdd:PLN03130 175 YLYISEVAAQVLFGILLlvyfpnldpypGYTPIGSESVDDYeyeelpggeQICPERHANIFSRIFFGWMTPLMQLGYKRP 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 117 LRPKDLWSLGRENSSEELVSRLEKEWMRNRSAARrhnkaiafkrkggsgmkapetepflrqegsQWrpLLKAIWQVFHST 196
Cdd:PLN03130 255 LTEKDVWKLDTWDQTETLYRSFQKCWDEELKKPK------------------------------PW--LLRALNNSLGGR 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 197 FLLGTLSLIISDVFRFTVPKLLSLFLEFI--GDPkppAWKGYLLAVLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITGL 274
Cdd:PLN03130 303 FWLGGFFKIGNDLSQFVGPLLLNLLLESMqnGEP---AWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLVAA 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 275 VYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTESVLYLNGLWLPLVWIVVCFVYLWQLLGPSALTAIAVFLSLLPLNFF 354
Cdd:PLN03130 380 VFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQTF 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 355 ISKKRNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLLFSVSLVSFQVSTFLVAL 434
Cdd:PLN03130 460 IISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNSIPVLVTV 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 435 VVFAVHTLVAENAMNAeKAFVTLTVLNILNKAQAFLPFSIHSLVQARVSFDRLVTFLCLEE--------VDPGVvdssss 506
Cdd:PLN03130 540 VSFGVFTLLGGDLTPA-RAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEErvllpnppLEPGL------ 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 507 gsaagkDCITIHSATFAW-SQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVE-GFVSIEGAVAYVPQ 584
Cdd:PLN03130 613 ------PAISIKNGYFSWdSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTVAYVPQ 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 585 EAWVQNTSVVENVCFGQELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDD 664
Cdd:PLN03130 687 VSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDD 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 665 PLAALDAHVGQHVFNQVIGpgGLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGALVCLLDQARQPG 744
Cdd:PLN03130 767 PLSALDAHVGRQVFDKCIK--DELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAGKME 844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 745 DRGEGETEPGTSTKDPRGTSAGRRPELRRERSIKSVPEKDRTTSEAQTEVplddpdragwpagkdsiQYGRVKATVHLAY 824
Cdd:PLN03130 845 EYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKKKSKEGKSVLIKQEER-----------------ETGVVSWKVLERY 907
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 825 LRAVGTPLCLYALFLF-LCQQVASFCRGYWLSLWADdpAVGGQQTQAALRGGIFGLLGCLQAIGLFASMAAVLLGGARAS 903
Cdd:PLN03130 908 KNALGGAWVVMILFLCyVLTEVFRVSSSTWLSEWTD--QGTPKTHGPLFYNLIYALLSFGQVLVTLLNSYWLIMSSLYAA 985
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 904 RLLFQRLLWDVVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLL 983
Cdd:PLN03130 986 KRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVL 1065
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 984 YAGFQSLYVVSSCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANVEL 1063
Cdd:PLN03130 1066 FYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLET 1145
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1064 LGNGLVFAAATCAVLSKAHLS-----AGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDYAWTPKEAPWRLPT 1138
Cdd:PLN03130 1146 LGGLMIWLTASFAVMQNGRAEnqaafASTMGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPSEAPLVIEN 1225
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1139 CAAQPPWPQGGQIEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAH 1218
Cdd:PLN03130 1226 NRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISK 1305
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1219 VGLHTLRSRISIIPQDPILFPGSLRMNLDLLQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCL 1298
Cdd:PLN03130 1306 FGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSL 1385
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1299 ARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKG- 1377
Cdd:PLN03130 1386 ARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGs 1465
|
1370
....*....|
gi 1199277034 1378 LFYRLAQESG 1387
Cdd:PLN03130 1466 AFSKMVQSTG 1475
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
83-1387 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 752.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 83 PQQSNPCPETGAAFPSKATFWWVSGLVWRGYRRPLRPKDLWSLGRENSSEELVSRLEKEWMrnrsaarrhnkaiafkrkg 162
Cdd:PLN03232 221 RGGENICPERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWT------------------- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 163 gsgmkapetepflrQEGSQWRP-LLKAIWQVFHSTFLLGTLSLIISDVFRFTVPKLLSLFLEFI--GDPkppAWKGYLLA 239
Cdd:PLN03232 282 --------------EESRRPKPwLLRALNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMqeGDP---AWVGYVYA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 240 VLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITGLVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTESVLYLNGLWLP 319
Cdd:PLN03232 345 FLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSA 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 320 LVWIVVCFVYLWQLLGPSALTAIAVFLSLLPLNFFISKKRNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDR 399
Cdd:PLN03232 425 PFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESR 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 400 VLGIRGQELGALRTSGLLFSVSlvSFQVSTF--LVALVVFAVHTLVAENAMNAeKAFVTLTVLNILNKAQAFLPFSIHSL 477
Cdd:PLN03232 505 IQGIRNEELSWFRKAQLLSAFN--SFILNSIpvVVTLVSFGVFVLLGGDLTPA-RAFTSLSLFAVLRSPLNMLPNLLSQV 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 478 VQARVSFDRLVTFLCLEE--------VDPGVvdssssgsaagkDCITIHSATFAW-SQESPPCLHRINLTVPQGCLLAVV 548
Cdd:PLN03232 582 VNANVSLQRIEELLLSEErilaqnppLQPGA------------PAISIKNGYFSWdSKTSKPTLSDINLEIPVGSLVAIV 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 549 GPVGAGKSSLLSALLGELSKVE-GFVSIEGAVAYVPQEAWVQNTSVVENVCFGQELDPPWLERVLEACALQPDVDSFPEG 627
Cdd:PLN03232 650 GGTGEGKTSLISAMLGELSHAEtSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGR 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 628 IHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVIGPGglLQGTTRILVTHALHILPQAD 707
Cdd:PLN03232 730 DLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDE--LKGKTRVLVTNQLHFLPLMD 807
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 708 WIIVLANGAIAEMGSYQELLQRKGALVCLLDQArqpgdrGEGETEPGTSTKDPRGTSAGRRPELR-RERSIKSVPEKDRT 786
Cdd:PLN03232 808 RIILVSEGMIKEEGTFAELSKSGSLFKKLMENA------GKMDATQEVNTNDENILKLGPTVTIDvSERNLGSTKQGKRG 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 787 TSeaqteVPLDDPDRagwpagkdsiQYGRVKATVHLAYLRAVGTPLCLYALFL-FLCQQVASFCRGYWLSLWADdpavgg 865
Cdd:PLN03232 882 RS-----VLVKQEER----------ETGIISWNVLMRYNKAVGGLWVVMILLVcYLTTEVLRVSSSTWLSIWTD------ 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 866 QQTQAALRGG----IFGLLGCLQAIGLFASMAAVLLGGARASRLLFQRLLWDVVRSPISFFERTPIGHLLNRFSKETDTV 941
Cdd:PLN03232 941 QSTPKSYSPGfyivVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDI 1020
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 942 DVDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLLYAGFQSLYVVSSCQLRRLESASYSSVCSHMAETFQGST 1021
Cdd:PLN03232 1021 DRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLS 1100
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1022 VVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANVELLGNGLVFAAATCAVLSKAHLS-----AGLVGFSVSAAL 1096
Cdd:PLN03232 1101 SIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLRNGNAEnqagfASTMGLLLSYTL 1180
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1097 QVTQTLQWVVRNWTDLENSIVSVERMQDYAWTPKEAPWRLPTCAAQPPWPQGGQIEFRDFGLRYRPELPLAVQGVSFKIH 1176
Cdd:PLN03232 1181 NITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVS 1260
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1177 AGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLDLLQEHSDEA 1256
Cdd:PLN03232 1261 PSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDAD 1340
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1257 IWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ 1336
Cdd:PLN03232 1341 LWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKS 1420
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 1337 CTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKG-LFYRLAQESG 1387
Cdd:PLN03232 1421 CTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVHSTG 1472
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
183-1372 |
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 1199277034 183 RPLLKAIWQVFHSTFLLgtlsLIISDVFRFTVPKLLSLFLEFIGDPkPPAW-KGYLLAVLMFLSACLQTLFEQQNMYRLK 261
Cdd:PTZ00243 236 RTLFAALPYYVWWQIPF----KLLSDVCTLTLPVLLKYFVKFLDAD-NATWgRGLGLVLTLFLTQLIQSVCLHRFYYISI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 262 VLQMRLRSAITGLVYRKVLALSSGS--RKASAVGDVVNLVSVDVQRLTESVLYLNGLWLPLVWIVVCFVYLWQLLGPSAL 339
Cdd:PTZ00243 311 RCGLQYRSALNALIFEKCFTISSKSlaQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCAL 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 340 TAIAVFLSLLPLNFFISKKRNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALR---TSGL 416
Cdd:PTZ00243 391 MAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRdvqLARV 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 417 LFSvsLVSFQVSTFLVAlVVFAVHTLVAeNAMNAEKAFVTLTVLNILNKAQAFLPFSIHSLVQARVSFDRLVTFL----- 491
Cdd:PTZ00243 471 ATS--FVNNATPTLMIA-VVFTVYYLLG-HELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLecdna 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 492 -----------------------------------------------------------CLEEVDP--------GVVDSS 504
Cdd:PTZ00243 547 tcstvqdmeeywreqrehstacqlaavlenvdvtafvpvklprapkvktsllsralrmlCCEQCRPtkrhpspsVVVEDT 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 505 SSGSAAGKDCITIHSATFAWSQESPP----------------------CLHRINLTVPQGCLLAVVGPVGAGKSSLLSAL 562
Cdd:PTZ00243 627 DYGSPSSASRHIVEGGTGGGHEATPTsersaktpkmktddffelepkvLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSL 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 563 LGELSKVEGFVSIEGAVAYVPQEAWVQNTSVVENVCFGQELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGG 642
Cdd:PTZ00243 707 LSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGG 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 643 QKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVIgpGGLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGS 722
Cdd:PTZ00243 787 QKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF--LGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGS 864
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 723 YQellqrkgalvcllDQARQPGDrgEGETEPGTSTKDPRGTSAGRR-PELRRERSIKSVPEKDRTTSEAQTEVplDDPDR 801
Cdd:PTZ00243 865 SA-------------DFMRTSLY--ATLAAELKENKDSKEGDADAEvAEVDAAPGGAVDHEPPVAKQEGNAEG--GDGAA 927
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 802 AGWPAGKDSIQ----YGRVKATVHLAYLRAV-GTPLCLYALFLFLCQQVASFCRGYWLSLWADDPavggqqtqaalrggi 876
Cdd:PTZ00243 928 LDAAAGRLMTReekaSGSVPWSTYVAYLRFCgGLHAAGFVLATFAVTELVTVSSGVWLSMWSTRS--------------- 992
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 877 fglLGCLQAIGLFASMAAVLLGGA--------------RASRLLFQRLLWDVVRSPISFFERTPIGHLLNRFSKETDTVD 942
Cdd:PTZ00243 993 ---FKLSAATYLYVYLGIVLLGTFsvplrfflsyeamrRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILD 1069
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 943 VDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLLYAGFQSLYVVSSCQLRRLESASYSSVCSHMAETFQGSTV 1022
Cdd:PTZ00243 1070 NTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSAT 1149
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1023 VRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANVELLGNGLVFAAA----TCAVLSKAHLSAGLVGFSVSAALQV 1098
Cdd:PTZ00243 1150 ITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIAligvIGTMLRATSQEIGLVSLSLTMAMQT 1229
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1099 TQTLQWVVRNWTDLENSIVSVERMQDYA-WTPKEAPWRL---------------------------PTCAAqPPWPQGGQ 1150
Cdd:PTZ00243 1230 TATLNWLVRQVATVEADMNSVERLLYYTdEVPHEDMPELdeevdalerrtgmaadvtgtvviepasPTSAA-PHPVQAGS 1308
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISI 1230
Cdd:PTZ00243 1309 LVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSM 1388
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1231 IPQDPILFPGSLRMNLDLLQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILI 1310
Cdd:PTZ00243 1389 IPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFI 1468
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 1311 L-DEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQL 1372
Cdd:PTZ00243 1469 LmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
90-1379 |
1.42e-141 |
|
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: 470.55 E-value: 1.42e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 90 PETGAAFPSKATFWWVSGLVWRGYRRPLRPKDLWSLGRENSSEELVSRLEKEWMRNRSAARRHNKaiafkrkggsgmkap 169
Cdd:TIGR01271 5 PVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAKKNPK--------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 170 etepflrqegsqwrpLLKAIWQVFHSTFLLGTLSLIISDVFRFTVPKLLS-LFLEFIGDPKPPAWKGYLLAVLMFLSACL 248
Cdd:TIGR01271 70 ---------------LLNALRRCFFWRFVFYGILLYFGEATKAVQPLLLGrIIASYDPFNAPEREIAYYLALGLCLLFIV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 249 QTLFEQQNMYRLKVLQMRLRSAITGLVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTESVLYLNGLWLPLVWIVVCFV 328
Cdd:TIGR01271 135 RTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 329 YLWQLLGPSALTAIAVFLSLLPLNFFISKKRNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQEL 408
Cdd:TIGR01271 215 LIWELLEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDEL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 409 GALRTSGLLFSVSLVSFQVSTFLVALVVFAVHTLVaeNAMNAEKAFVTLT---VLNILNKAQafLPFSIHSLVQARVSFD 485
Cdd:TIGR01271 295 KLTRKIAYLRYFYSSAFFFSGFFVVFLSVVPYALI--KGIILRRIFTTISyciVLRMTVTRQ--FPGAIQTWYDSLGAIT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 486 RLVTFLCLEEV---------------------DPGVVDSSSSGSAAGKDCITIH---SATFA-WSQESPPCLHRINLTVP 540
Cdd:TIGR01271 371 KIQDFLCKEEYktleynltttevemvnvtaswDEGIGELFEKIKQNNKARKQPNgddGLFFSnFSLYVTPVLKNISFKLE 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 541 QGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQEAWVQNTSVVENVCFGQELDPPWLERVLEACALQPD 620
Cdd:TIGR01271 451 KGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEED 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 621 VDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVIGPggLLQGTTRILVTHAL 700
Cdd:TIGR01271 531 IALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCK--LMSNKTRILVTSKL 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 701 HILPQADWIIVLANGAIAEMGSYQELL----------------------------------------------------- 727
Cdd:TIGR01271 609 EHLKKADKILLLHEGVCYFYGTFSELQakrpdfsslllgleafdnfsaerrnsiltetlrrvsidgdstvfsgpetikqs 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 728 ----------QRKGALVC-----------------------LLDQARQPGDRGEG---ETEPGTSTKdPRG--------- 762
Cdd:TIGR01271 689 fkqpppefaeKRKQSIILnpiasarkfsfvqmgpqkaqattIEDAVREPSERKFSlvpEDEQGEESL-PRGnqyhhglqh 767
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 763 ------------TSAGRRPELRRE-----RSIKSVPEKDRTTSEA-------------QTEVPLDDPDRAGWPAGKDSIQ 812
Cdd:TIGR01271 768 qaqrrqsvlqlmTHSNRGENRREQlqtsfRKKSSITQQNELASELdiysrrlskdsvyEISEEINEEDLKECFADERENV 847
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 813 YgrvKATVHLAYLRAVGTP-----LCLYALFLFLCQQVASFCrGYWLslWADDPAVGGQQTQAALRGG------------ 875
Cdd:TIGR01271 848 F---ETTTWNTYLRYITTNrnlvfVLIFCLVIFLAEVAASLL-GLWL--ITDNPSAPNYVDQQHANASspdvqkpviitp 921
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 876 -----IF----GLLGCLQAIGLFASMAAV--LLggaRASRLLFQRLLWDVVRSPISFFERTPIGHLLNRFSKETDTVDVD 944
Cdd:TIGR01271 922 tsayyIFyiyvGTADSVLALGFFRGLPLVhtLL---TVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDM 998
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 945 IPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLLYAGFQSLYVVSSCQLRRLESASYSSVCSHMAETFQGSTVVR 1024
Cdd:TIGR01271 999 LPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIR 1078
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1025 AFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANVELLGNgLVFAAATCAVLSKAHLSAGLVGFSVSAALQVTQTLQW 1104
Cdd:TIGR01271 1079 AFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFV-FFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQW 1157
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1105 VVRNWTDLENSIVSVERMQDYAWTPKEAPwrLPTCAAQPP----------------WPQGGQIEFRDFGLRYRPELPLAV 1168
Cdd:TIGR01271 1158 AVNSSIDVDGLMRSVSRVFKFIDLPQEEP--RPSGGGGKYqlstvlvienphaqkcWPSGGQMDVQGLTAKYTEAGRAVL 1235
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1169 QGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQeAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLDL 1248
Cdd:TIGR01271 1236 QDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDP 1314
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1249 LQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQA 1328
Cdd:TIGR01271 1315 YEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRK 1394
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 1329 MLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLF 1379
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, ... |
833-1126 |
1.16e-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: 391.07 E-value: 1.16e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 833 CLYALFLFLCQQVASFCRGYWLSLWADDPAVGGQQT--QAALRGGIFGLLGCLQAIGLFASMAAVLLGGARASRLLFQRL 910
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDteQRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 911 LWDVVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLLYAGFQSL 990
Cdd:cd18603 81 LHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 991 YVVSSCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANVELLGNGLVF 1070
Cdd:cd18603 161 YVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 1071 AAATCAVLSKAHLSAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDYA 1126
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, ... |
199-487 |
2.99e-118 |
|
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: 371.03 E-value: 2.99e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 199 LGTLSLIISDVFRFTVPKLLSLFLEFIGDPKPPAWKGYLLAVLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITGLVYRK 278
Cdd:cd18595 1 LAALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 279 VLALSSGSRKASAVGDVVNLVSVDVQRLTESVLYLNGLWLPLVWIVVCFVYLWQLLGPSALTAIAVFLSLLPLNFFISKK 358
Cdd:cd18595 81 ALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 359 RNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLLFSVSLVSFQVSTFLVALVVFA 438
Cdd:cd18595 161 IKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1199277034 439 VHTLVAE-NAMNAEKAFVTLTVLNILNKAQAFLPFSIHSLVQARVSFDRL 487
Cdd:cd18595 241 TYVLSDPdNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1149-1369 |
2.25e-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: 352.18 E-value: 2.25e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1149 GQIEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRI 1228
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1229 SIIPQDPILFPGSLRMNLDLLQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQI 1308
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 1309 LILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSP 1369
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
515-715 |
8.99e-107 |
|
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: 336.36 E-value: 8.99e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAW---SQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQEAWVQNT 591
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 592 SVVENVCFGQELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDA 671
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1199277034 672 HVGQHVFNQVIGpGGLLQGTTRILVTHALHILPQADWIIVLANG 715
Cdd:cd03250 161 HVGRHIFENCIL-GLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
822-1384 |
9.21e-99 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 328.66 E-value: 9.21e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 822 LAYLRAVGTPLCLyALFLFLCQQVASFCRGYWLSLWADDPAVGGQQTQAALRGGIFGLLGCLQAIGLFASMAAVLLGGAR 901
Cdd:COG1132 13 LRYLRPYRGLLIL-ALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 902 ASRLLFQRLLWDVVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLeVSLVVAVAT-PLATVAILPL 980
Cdd:COG1132 92 VVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLI-GALVVLFVIdWRLALIVLLV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 981 FLLYAGFQSLYVVSSCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAAN 1060
Cdd:COG1132 171 LPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1061 VELLGNGLVFAAATCAVL--SKAHLSAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDYAWTPKEAPwrlPT 1138
Cdd:COG1132 251 MELLGNLGLALVLLVGGLlvLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP---DP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1139 CAAQPPWPQGGQIEFRDFGLRYRPELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAH 1218
Cdd:COG1132 328 PGAVPLPPVRGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRD 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1219 VGLHTLRSRISIIPQDPILFPGSLRMNLDL-LQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQ--- 1294
Cdd:COG1132 407 LTLESLRRQIGVVPQDTFLFSGTIRENIRYgRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQria 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1295 ------LlclarallrKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGS 1368
Cdd:COG1132 487 iarallK---------DPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
570
....*....|....*.
gi 1199277034 1369 PAQLLAQKGLFYRLAQ 1384
Cdd:COG1132 558 HEELLARGGLYARLYR 573
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
199-487 |
1.04e-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: 295.55 E-value: 1.04e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 199 LGTLSLIISDVFRFTVPKLLSLFLEFIGD-PKPPAWKGYLLAVLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITGLVYR 277
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSyPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 278 KVLALSSGSRKASAVGDVVNLVSVDVQRLTESVLYLNGLWLPLVWIVVCFVYLWQLLGPSALTAIAVFLSLLPLNFFISK 357
Cdd:cd18579 81 KALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 358 KRNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLLFSVSLVSFQVSTFLVALVVF 437
Cdd:cd18579 161 LISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1199277034 438 AVHTLVAeNAMNAEKAFVTLTVLNILNKAQAFLPFSIHSLVQARVSFDRL 487
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 ... |
837-1126 |
1.60e-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: 280.93 E-value: 1.60e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 837 LFLFLCQQVASFCRGYWLSLWADDPAVGGQQTQAALRGGIFGLLGCLQAIGLFASMAAVLLGGARASRLLFQRLLWDVVR 916
Cdd:cd18580 5 LLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 917 SPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLLYAGFQSLYVVSSC 996
Cdd:cd18580 85 APMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYLRTSR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 997 QLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANVELLGNGLVFAAATCA 1076
Cdd:cd18580 165 QLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALVVALLA 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1077 VLSKAHLSAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDYA 1126
Cdd:cd18580 245 VLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
874-1385 |
3.62e-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: 288.66 E-value: 3.62e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 874 GGIFGLLGCLQAIGLFASMAAVLLGGARASRLLFQRLLWDVVRSPISFFERTPIGHLLNRFSkETDTVDVDIPDKLRSLL 953
Cdd:COG2274 199 AIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTAL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 954 MYAFGLLeVSLVV--AVATPLATVAILpLFLLYAGfqsLYVVSSCQLRRL---ESASYSSVCSHMAETFQGSTVVRAFRT 1028
Cdd:COG2274 278 LDLLFVL-IFLIVlfFYSPPLALVVLL-LIPLYVL---LGLLFQPRLRRLsreESEASAKRQSLLVETLRGIETIKALGA 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1029 QAPFVAQNNARVDESQRISFPRLVADRWL---AANVELLGNGLVFAAATCAVLSKaHLSAG-LVGFSvSAALQVTQTLQW 1104
Cdd:COG2274 353 ESRFRRRWENLLAKYLNARFKLRRLSNLLstlSGLLQQLATVALLWLGAYLVIDG-QLTLGqLIAFN-ILSGRFLAPVAQ 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1105 VVRNWTDLENSIVSVERMQDYAWTPKEapwRLPTCAAQPPWPQGGQIEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIV 1184
Cdd:COG2274 431 LIGLLQRFQDAKIALERLDDILDLPPE---REEGRSKLSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIV 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1185 GRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLDLLQEH-SDEAIWAALET 1263
Cdd:COG2274 508 GRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDaTDEEIIEAARL 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1264 VQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIA 1343
Cdd:COG2274 588 AGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIA 667
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1199277034 1344 HRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFYRLAQE 1385
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 ... |
1145-1369 |
4.58e-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: 4.58e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1145 WPQGGQIEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTL 1224
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1225 RSRISIIPQDPILFPGSLRMNLDLLQEHSDEAIWAALetvqlkalvaslpgqlqyKCADRGEDLSVGQKQLLCLARALLR 1304
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 1305 KTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSP 1369
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 ... |
836-1126 |
1.41e-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: 244.31 E-value: 1.41e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 836 ALFLFLCQQVASFCRGYWLSLWADD-PAVGGQQTQaalrgGIFGLLGCLQAIGLFASMAAVLLGGARASRLLFQRLLWDV 914
Cdd:cd18606 4 LLLLLILSQFAQVFTNLWLSFWTEDfFGLSQGFYI-----GIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 915 VRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLLYAGFQSLYVVS 994
Cdd:cd18606 79 LRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 995 SCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANVELLGNGLVFAAAT 1074
Cdd:cd18606 159 SRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLIVAL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 1075 CAVLSKAHLSAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDYA 1126
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; ... |
836-1125 |
4.19e-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: 237.37 E-value: 4.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 836 ALFLFLCQQVASFCRGYWLSLWADDPAVGGQQTQAALR----GGIFGLLGCLQAIGLFASMAAVLLGGARASRLLFQRLL 911
Cdd:cd18604 4 LLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVSvlyyLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 912 WDVVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLLYAGFQSLY 991
Cdd:cd18604 84 HSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGRLY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 992 VVSSCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANVELLGnGLVFA 1071
Cdd:cd18604 164 LRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLG-ALFSF 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 1072 AATCAVLSKAHLSAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDY 1125
Cdd:cd18604 243 ATAALLVYGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEY 296
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
183-739 |
1.96e-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: 248.60 E-value: 1.96e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 183 RPLLKAIWQVFHSTFLLGTLSLIISDVFRFTVPK-LLSLFLEFIgdpkppawkgYLLAVLMFLSACLQTLFEQQNMYRLK 261
Cdd:COG2274 152 RRYRRLLLQVLLASLLINLLALATPLFTQVVIDRvLPNQDLSTL----------WVLAIGLLLALLFEGLLRLLRSYLLL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 262 VLQMRLRSAITGLVYRKVLALSSGSRKASAVGDVVNLVSvDVQR----LTESVL--YLNGLWLpLVWIVVCFVYLWQLLG 335
Cdd:COG2274 222 RLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESirefLTGSLLtaLLDLLFV-LIFLIVLFFYSPPLAL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 336 PSALTAIAVFLsllpLNFFISKKRNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQ----ELGAL 411
Cdd:COG2274 300 VVLLLIPLYVL----LGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKylnaRFKLR 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 412 RTSGLLFSVSLVSFQVSTflVALVVFAVHtLVAENAMnaekafvTLTVL---NILnKAQAFLPFS-----IHSLVQARVS 483
Cdd:COG2274 376 RLSNLLSTLSGLLQQLAT--VALLWLGAY-LVIDGQL-------TLGQLiafNIL-SGRFLAPVAqliglLQRFQDAKIA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 484 FDRLVTFLCLE-EVDPGvvdSSSSGSAAGKDCITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSAL 562
Cdd:COG2274 445 LERLDDILDLPpEREEG---RSKLSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 563 LGELSKVEGFVSIEG-------------AVAYVPQEAWVQNTSVVENVCFG-QELDPPWLERVLEACALQPDVDSFPEGI 628
Cdd:COG2274 522 LGLYEPTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGTIRENITLGdPDATDEEIIEAARLAGLHDFIEALPMGY 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 629 HTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVigpGGLLQGTTRILVTHALHILPQADW 708
Cdd:COG2274 602 DTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENL---RRLLKGRTVIIIAHRLSTIRLADR 678
|
570 580 590
....*....|....*....|....*....|.
gi 1199277034 709 IIVLANGAIAEMGSYQELLQRKGALVCLLDQ 739
Cdd:COG2274 679 IIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
183-731 |
6.19e-68 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 240.45 E-value: 6.19e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 183 RPLLKAIWQVFHS---TFLLGTLSLIISDVFRFTVPKLLSLFLEFIGDPKPPAwKGYLLAVLMFLSACLQTLFEQQNMYR 259
Cdd:COG1132 6 RKLLRRLLRYLRPyrgLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLS-ALLLLLLLLLGLALLRALLSYLQRYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 260 LKVLQMRLRSAITGLVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTESVLY-LNGLWLPLVWIVVCFVYL----WQLl 334
Cdd:COG1132 85 LARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHgLPQLVRSVVTLIGALVVLfvidWRL- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 335 gpsALTAIAVFLSLLPLNFFISKKRNHHQEEQMRQkdsRARLTSSI---LRNSKTIKFHGWEGAFLDRVLGI----RGQE 407
Cdd:COG1132 164 ---ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEA---LAELNGRLqesLSGIRVVKAFGREERELERFREAneelRRAN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 408 LGALRTSGLLFSVSLVSFQVSTFLVALVVFAvhtLVAENAMNAEK--AFVTLtVLNILNKAQAFLpFSIHSLVQARVSFD 485
Cdd:COG1132 238 LRAARLSALFFPLMELLGNLGLALVLLVGGL---LVLSGSLTVGDlvAFILY-LLRLFGPLRQLA-NVLNQLQRALASAE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 486 RLVTFLcleEVDPGVVDSS-SSGSAAGKDCITIHSATFAWsQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLG 564
Cdd:COG1132 313 RIFELL---DEPPEIPDPPgAVPLPPVRGEIEFENVSFSY-PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 565 ELSKVEGFVSIEG-------------AVAYVPQEAWVQNTSVVENVCFGQ-ELDPPWLERVLEACALQPDVDSFPEGIHT 630
Cdd:COG1132 389 FYDPTSGRILIDGvdirdltleslrrQIGVVPQDTFLFSGTIRENIRYGRpDATDEEVEEAAKAAQAHEFIEALPDGYDT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 631 SIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVigpGGLLQGTTRILVTHALHILPQADWII 710
Cdd:COG1132 469 VVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL---ERLMKGRTTIVIAHRLSTIRNADRIL 545
|
570 580
....*....|....*....|.
gi 1199277034 711 VLANGAIAEMGSYQELLQRKG 731
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; ... |
198-487 |
1.01e-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: 1.01e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 198 LLGTLSLIISdVFRFTVPKLLSLFLEFIGDPKPPA-WKGYLLAVLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITGLVY 276
Cdd:cd18596 1 LQALLAVLSS-VLSFAPPFFLNRLLRYLEDPGEDAtVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 277 RKVL-------------------ALSSGSRKASAVGDVVNLVSVDVQRLTESVLYLNGLWLPLVWIVVCFVYLWQLLGPS 337
Cdd:cd18596 80 EKALrrrdksgssksseskkkdkEEDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 338 ALTAIAVFLSLLPLNFFISKKRNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLL 417
Cdd:cd18596 160 ALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 418 FSVSLVSFQVSTFLVALVVFAVHTLVAENAMNAEKAFVTLTVLNILNKAQAFLPFSIHSLVQARVSFDRL 487
Cdd:cd18596 240 DLLLSLLWFLIPILVTVVTFATYTLVMGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1148-1379 |
1.80e-62 |
|
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: 214.00 E-value: 1.80e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1148 GGQIEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSR 1227
Cdd:cd03288 17 GGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1228 ISIIPQDPILFPGSLRMNLDLLQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQ 1307
Cdd:cd03288 97 LSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 1308 ILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQK-GLF 1379
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVF 249
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1149-1377 |
3.50e-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: 3.50e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1149 GQIEFRDFGLRYRPELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRI 1228
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1229 SIIPQDPILFPGSLRMNLDL-LQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQ 1307
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLgRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1308 ILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKG 1377
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
906-1384 |
4.32e-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: 4.32e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 906 LFQRLLwdvvRSPISFFERTPIGHLLNRFSKETDTVDvDIPdkLR-------SLLMYAFGLLEVSL------VVAVATPL 972
Cdd:COG4987 94 LYRRLE----PLAPAGLARLRSGDLLNRLVADVDALD-NLY--LRvllpllvALLVILAAVAFLAFfspalaLVLALGLL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 973 ATVAILPLFLLYAGFQSlyvvsSCQLRRLESASYSSVcshmAETFQGSTVVRAFRTQAPFVAqnnaRVDESQRisfpRLV 1052
Cdd:COG4987 167 LAGLLLPLLAARLGRRA-----GRRLAAARAALRARL----TDLLQGAAELAAYGALDRALA----RLDAAEA----RLA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1053 ADRWLAANVELLGNG---LVFAAATCAVL-------SKAHLSAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERM 1122
Cdd:COG4987 230 AAQRRLARLSALAQAllqLAAGLAVVAVLwlaaplvAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1123 QdyAWTPKEAPWRLPtcAAQPPWPQGGQIEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQ 1202
Cdd:COG4987 310 N--ELLDAPPAVTEP--AEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1203 EAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLdLL--QEHSDEAIWAALETVQLKALVASLPGQLQYK 1280
Cdd:COG4987 386 DPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENL-RLarPDATDEELWAALERVGLGDWLAALPDGLDTW 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1281 CADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDK 1360
Cdd:COG4987 465 LGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLED 544
|
490 500
....*....|....*....|....
gi 1199277034 1361 GQVAESGSPAQLLAQKGLFYRLAQ 1384
Cdd:COG4987 545 GRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1114-1377 |
1.02e-60 |
|
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: 218.86 E-value: 1.02e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1114 NSIVSVERMQDYAWTPKEAPwrlPTCAAQPPWPQGGQIEFRDFGLRYrPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSS 1193
Cdd:COG4988 303 NGIAAAEKIFALLDAPEPAA---PAGTAPLPAAGPPSIELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKST 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1194 LASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLDLLQEH-SDEAIWAALETVQLKALVAS 1272
Cdd:COG4988 379 LLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDaSDEELEAALEAAGLDEFVAA 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1273 LPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDC 1352
Cdd:COG4988 459 LPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQA 538
|
250 260
....*....|....*....|....*
gi 1199277034 1353 ARVLVMDKGQVAESGSPAQLLAQKG 1377
Cdd:COG4988 539 DRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
260-732 |
9.57e-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: 9.57e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 260 LKVLQmRLRSAitglVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLteSVLYLNGLwLPLVW----IVVCFVYLWQLLG 335
Cdd:COG4987 84 LRLLA-DLRVR----LYRRLEPLAPAGLARLRSGDLLNRLVADVDAL--DNLYLRVL-LPLLVallvILAAVAFLAFFSP 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 336 PSALTAIAVFLS---LLPLNFFISKKRNHHQEEQMRQkDSRARLTSsILRNSKTIKFHGWEGAFLDRVLGIRGQELGALR 412
Cdd:COG4987 156 ALALVLALGLLLaglLLPLLAARLGRRAGRRLAAARA-ALRARLTD-LLQGAAELAAYGALDRALARLDAAEARLAAAQR 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 413 TSGLL--FSVSLVSFQVSTFLVALVVFAVHtLVAENAMNAekAFVTLTVLNILNKAQAFLPFS--IHSLVQARVSFDRLV 488
Cdd:COG4987 234 RLARLsaLAQALLQLAAGLAVVAVLWLAAP-LVAAGALSG--PLLALLVLAALALFEALAPLPaaAQHLGRVRAAARRLN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 489 TflcLEEVDPGVVDSSSSGSAAGKDCITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSK 568
Cdd:COG4987 311 E---LLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 569 VEGFVSIEG-------------AVAYVPQEAWVQNTSVVENVCFG-QELDPPWLERVLEACALQPDVDSFPEGIHTSIGE 634
Cdd:COG4987 388 QSGSITLGGvdlrdldeddlrrRIAVVPQRPHLFDTTLRENLRLArPDATDEELWAALERVGLGDWLAALPDGLDTWLGE 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 635 QGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVIgpgGLLQGTTRILVTHALHILPQADWIIVLAN 714
Cdd:COG4987 468 GGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLL---EALAGRTVLLITHRLAGLERMDRILVLED 544
|
490
....*....|....*...
gi 1199277034 715 GAIAEMGSYQELLQRKGA 732
Cdd:COG4987 545 GRIVEQGTHEELLAQNGR 562
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
198-487 |
1.71e-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: 200.86 E-value: 1.71e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 198 LLGTLSLIiSDVFRFTVPKLLSLFLEFIGDPKPPAWKGYLLAVLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITGLVYR 277
Cdd:cd18598 1 PLGLLKLL-ADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 278 KVLALSSGSRKASAVGDVVNLVSVDVQRLTESVLYLNGLW-LPLVwIVVCFVYLWQLLGPSALTAIAVFLSLLPLNFFIS 356
Cdd:cd18598 80 KALRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWsLPLQ-IIVALYLLYQQVGVAFLAGLVFALVLIPINKWIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 357 KKRNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLLFSVsLVSFQVST-FLVALV 435
Cdd:cd18598 159 KRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDAL-CVYFWATTpVLISIL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 436 VFAVHTLVAeNAMNAEKAFVTLTVLNIL----NkaqAFlPFSIHSLVQARVSFDRL 487
Cdd:cd18598 238 TFATYVLMG-NTLTAAKVFTSLALFNMLigplN---AF-PWVLNGLVEAWVSLKRL 288
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
199-487 |
1.47e-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: 1.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 199 LGTLSLIISDVFRFTVPKLLSLFLEFI-----GDPKPPAWKGYLLAVLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITG 273
Cdd:cd18597 1 LAGLLKLLADVLQVLSPLLLKYLINFVedaylGGPPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 274 LVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTESVLYLNGLWLPLVWIVVCFVYLWQLLGPSALTAIAVFLSLLPLNF 353
Cdd:cd18597 81 AIYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 354 FISKKRNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLLFSVSLVSFQVSTFLVA 433
Cdd:cd18597 161 FLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLAS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 434 LVVFAVHTLVaENAMNAEKAFVTLTVLNILNKAQAFLPFSIHSLVQARVSFDRL 487
Cdd:cd18597 241 MLSFITYYAT-GHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
879-1382 |
2.06e-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: 206.49 E-value: 2.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 879 LLGCLQAIGLFAS---MAAVLLGGARASRL-LFQRLLwdvvRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLL- 953
Cdd:TIGR02203 62 GLAVLRGICSFVStylLSWVSNKVVRDIRVrMFEKLL----GLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVr 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 954 --MYAFGLLEVSLVVAVATPLATVAILPLfllyagfqsLYVVSSCQLRRLESASYSSVCSH------MAETFQGSTVVRA 1025
Cdd:TIGR02203 138 etLTVIGLFIVLLYYSWQLTLIVVVMLPV---------LSILMRRVSKRLRRISKEIQNSMgqvttvAEETLQGYRVVKL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1026 FRTQAP----FVAQNNARVDESQRISfprlVADRWLAANVELLGNgLVFAAATCAVLSKA---HLSAG-LVGFsVSAALQ 1097
Cdd:TIGR02203 209 FGGQAYetrrFDAVSNRNRRLAMKMT----SAGSISSPITQLIAS-LALAVVLFIALFQAqagSLTAGdFTAF-ITAMIA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1098 VTQTLQWVVRNWTDLENSIVSVERMQDYAWTPKEapwrlPTCAAQPPWPQGGQIEFRDFGLRYRPELPLAVQGVSFKIHA 1177
Cdd:TIGR02203 283 LIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPE-----KDTGTRAIERARGDVEFRNVTFRYPGRDRPALDSISLVIEP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1178 GEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLDL--LQEHSDE 1255
Cdd:TIGR02203 358 GETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYgrTEQADRA 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1256 AIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFA 1335
Cdd:TIGR02203 438 EIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ 517
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1199277034 1336 QCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFYRL 1382
Cdd:TIGR02203 518 GRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQL 564
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
836-1126 |
7.74e-56 |
|
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: 196.67 E-value: 7.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 836 ALFLFLCQQVASFCRGYWLSLWA----DDPAVGGQQTQAALRG-------GIFGLLGCLQAIGLFASMAAVLLGGARASR 904
Cdd:cd18602 4 VLALALLKQGLRVATDFWLADWTeanhDVASVVFNITSSSLEDdevsyyiSVYAGLSLGAVILSLVTNLAGELAGLRAAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 905 LLFQRLLWDVVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLLY 984
Cdd:cd18602 84 RLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIVY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 985 AGFQSLYVVSSCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQrISFPRL-VADRWLAANVEL 1063
Cdd:cd18602 164 YFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNN-TAFLFLnTANRWLGIRLDY 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 1064 LGNGLVFAAATCAVLSKAH--LSAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDYA 1126
Cdd:cd18602 243 LGAVIVFLAALSSLTAALAgyISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
175-731 |
2.68e-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: 203.07 E-value: 2.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 175 LRQEGSQWRPL-LKAIWQVFHSTFLLG---TLSLIISDVFRFTVPkLLSLFLEFIgdpkppawkgyLLAVLMFLSACLqT 250
Cdd:COG4988 9 KRLARGARRWLaLAVLLGLLSGLLIIAqawLLASLLAGLIIGGAP-LSALLPLLG-----------LLLAVLLLRALL-A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 251 LFEQQNMYRLkvlQMRLRSAITGLVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTEsvlYLnGLWLP--LVWIVVC-- 326
Cdd:COG4988 76 WLRERAAFRA---AARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDG---YF-ARYLPqlFLAALVPll 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 327 -FVYLWQLLGPSALTaIAVFLSLLPLnFFI-----SKKRNHHQEEQMrqkdsrARLTSSilrnsktikfhgwegaFLDRV 400
Cdd:COG4988 149 iLVAVFPLDWLSGLI-LLVTAPLIPL-FMIlvgkgAAKASRRQWRAL------ARLSGH----------------FLDRL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 401 --------LGIRGQELGALRTSGLLFSVS----L-VSFQVSTFL-------VALV-VFAVHTLVAENaMNAEKAFVTLtv 459
Cdd:COG4988 205 rglttlklFGRAKAEAERIAEASEDFRKRtmkvLrVAFLSSAVLeffaslsIALVaVYIGFRLLGGS-LTLFAALFVL-- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 460 lnILnKAQAFLPF-----SIHSLVQARVSFDRLVTFLclEEVDPGVVDSSSSGSAAGKDCITIHSATFAWSQEsPPCLHR 534
Cdd:COG4988 282 --LL-APEFFLPLrdlgsFYHARANGIAAAEKIFALL--DAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGG-RPALDG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-------------VAYVPQEAWVQNTSVVENVCFGQ 601
Cdd:COG4988 356 LSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpaswrrqIAWVPQNPYLFAGTIRENLRLGR 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 602 -ELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFnQ 680
Cdd:COG4988 436 pDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEIL-Q 514
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 681 VIGPggLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKG 731
Cdd:COG4988 515 ALRR--LAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1151-1385 |
7.06e-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: 7.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELPLaVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISI 1230
Cdd:cd03253 1 IEFENVTFAYDPGRPV-LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1231 IPQDPILFPGSLRMNLDLLQEH-SDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQIL 1309
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 1310 ILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFYRLAQE 1385
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKA 235
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
204-487 |
9.36e-55 |
|
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: 192.85 E-value: 9.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 204 LIISDVFRFTVPKLLSLFLE-FIGDPKPPAWKGYLLAVLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITGLVYRKVLAL 282
Cdd:cd18594 6 LFLEESLKIVQPLLLGRLVAyFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTLKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 283 SSGSRKASAVGDVVNLVSVDVQRLTESVLYLNGLWLPLVWIVVCFVYLWQLLGPSALTAIAVFLSLLPLNFFISKKRNHH 362
Cdd:cd18594 86 SSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 363 QEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLLFSVSLVSFQVSTFLVALVVFAVHTL 442
Cdd:cd18594 166 RRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVL 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1199277034 443 VAeNAMNAEKAFVTLTVLNILNKAQA-FLPFSIHSLVQARVSFDRL 487
Cdd:cd18594 246 TG-NTLTARKVFTVISLLNALRMTITrFFPESIQTLSESRVSLKRI 290
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1151-1382 |
1.18e-54 |
|
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: 190.52 E-value: 1.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISI 1230
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1231 IPQDPILFPGSLRMNLDL-LQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQIL 1309
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYgRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 1310 ILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFYRL 1382
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
837-1125 |
9.98e-53 |
|
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: 9.98e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 837 LFLFLCQ--QVASFcrgYWLSLWaddpaVGGQQTQAALRGGIFGL--LGCLQAIGLFASMAAVL------LGGARASRLL 906
Cdd:cd18605 6 LSLILMQasRNLID---FWLSYW-----VSHSNNSFFNFINDSFNffLTVYGFLAGLNSLFTLLraflfaYGGLRAARRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 907 FQRLLWDVVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLLYAG 986
Cdd:cd18605 78 HNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 987 FQSLYVVSSCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANVELLGN 1066
Cdd:cd18605 158 IQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 1067 GLVFAAATCAVLS---KAHLSAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDY 1125
Cdd:cd18605 238 LIVTFVALTAVVQhffGLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQY 299
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
515-716 |
2.38e-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: 2.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQESPpCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFV-----------------SIEG 577
Cdd:cd03290 1 VQVTNGYFSWGSGLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 578 AVAYVPQEAWVQNTSVVENVCFGQELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKA 657
Cdd:cd03290 80 SVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 658 AVYLLDDPLAALDAHVGQHVFNQviGPGGLLQGTTR--ILVTHALHILPQADWIIVLANGA 716
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQE--GILKFLQDDKRtlVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1151-1362 |
1.60e-51 |
|
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: 179.12 E-value: 1.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISI 1230
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1231 IPQDPILFPGSLRMNLdllqehsdeaiwaaletvqlkalvaslpgqlqykcadrgedLSVGQKQLLCLARALLRKTQILI 1310
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 1311 LDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQ 1362
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1151-1384 |
7.94e-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: 179.66 E-value: 7.94e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRY--RPELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRI 1228
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1229 SIIPQDPILFPGSLRMNLDL-LQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQ 1307
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIRYgKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1308 ILILDEATAAVDPGTELQMQ-----AMLGSwfaqcTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFYRL 1382
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQealdrAMKGR-----TTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKL 234
|
..
gi 1199277034 1383 AQ 1384
Cdd:cd03249 235 VK 236
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
901-1384 |
1.84e-50 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 189.54 E-value: 1.84e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 901 RASRLLFQRLLWDV----VRSPISFFERTPIGHLLNRFSKETDT-----VDVdIPDKLRSL-LMYAFGLLEVSLVVAVAt 970
Cdd:PRK10790 91 RAAVGVVQQLRTDVmdaaLRQPLSAFDTQPVGQLISRVTNDTEVirdlyVTV-VATVLRSAaLIGAMLVAMFSLDWRMA- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 971 pLATVAILPLFLLYAGFQSLYvvSSCQLRRLESasY-SSVCSHMAETFQGSTVVRAFRTQAPFvaqnNARVDESQRISF- 1048
Cdd:PRK10790 169 -LVAIMIFPAVLVVMVIYQRY--STPIVRRVRA--YlADINDGFNEVINGMSVIQQFRQQARF----GERMGEASRSHYm 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1049 PRLVA---DRWLAAnvELLGngLVFAAATCAVLSkahlsagLVGFSVSAALQV-------------TQTLQWVVRNWTDL 1112
Cdd:PRK10790 240 ARMQTlrlDGFLLR--PLLS--LFSALILCGLLM-------LFGFSASGTIEVgvlyafisylgrlNEPLIELTTQQSML 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1113 ENSIVSVER--------MQDYAwtPKEAPWrlptcaaqppwpQGGQIEFRDFGLRYRPELPLaVQGVSFKIHAGEKVGIV 1184
Cdd:PRK10790 309 QQAVVAGERvfelmdgpRQQYG--NDDRPL------------QSGRIDIDNVSFAYRDDNLV-LQNINLSVPSRGFVALV 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1185 GRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLDLLQEHSDEAIWAALETV 1264
Cdd:PRK10790 374 GHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETV 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1265 QLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAH 1344
Cdd:PRK10790 454 QLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAH 533
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1199277034 1345 RLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFYRLAQ 1384
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 ... |
199-487 |
2.14e-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: 180.89 E-value: 2.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 199 LGTLSLIISDVFRFTVPKLLSLFLEFIGD-------------PKPPAWK-----GYLLAVLMFLSACLQTLFEQQNMYRL 260
Cdd:cd18591 1 LGGILKLLGDLLGFVGPLCISGIVDYVEEntysssnstdklsVSYVTVEeffsnGYVLAVILFLALLLQATFSQASYHIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 261 KVLQMRLRSAITGLVYRKVLALSSGSRKASAV--GDVVNLVSVDVQRLTESVLYLNGLW-LPLVwIVVCFVYLWQLLGPS 337
Cdd:cd18591 81 IREGIRLKTALQAMIYEKALRLSSWNLSSGSMtiGQITNHMSEDANNIMFFFWLIHYLWaIPLK-IIVGLILLYLKLGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 338 ALTAIAVFLSLLPLNFFISKKRNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLL 417
Cdd:cd18591 160 ALIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVY 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 418 FSVSLVSFQVSTFLVALVVFAVHTLVAENAMNAEKAFVTLTVLNILNKAQAFLPFSIHSLVQARVSFDRL 487
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, ... |
202-487 |
3.37e-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: 179.68 E-value: 3.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 202 LSLIISDVFRFTVPK-LLSLFLEFIGDPKPPAWKGYLLAVLMFLSACLQTLFEQQN---MYRLKVlqmRLRSAITGLVYR 277
Cdd:cd18592 4 LLLLISLIFGFIGPTiLIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTwaiSYRTGI---RLRGAVLGLLYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 278 KVLALSSGSRKAsaVGDVVNLVSVDVQRLTESVLYLNGLWLPLVWIVVCFVYLWQLLGPSALTAIAVFLSLLPLNFFISK 357
Cdd:cd18592 81 KILRLRSLGDKS--VGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 358 KRNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLLFSVSLVSFQVSTFLVALVVF 437
Cdd:cd18592 159 LTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTF 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1199277034 438 AVHTLvAENAMNAEKAFVTLTVLNILNKAQAFLPFSIHSLVQARVSFDRL 487
Cdd:cd18592 239 LAHVA-LGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1141-1382 |
1.16e-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: 1.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1141 AQPPWPQGGQIEFRDFGLRYRPELPLaVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG 1220
Cdd:COG5265 348 APPLVVGGGEVRFENVSFGYDPERPI-LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1221 LHTLRSRISIIPQDPILFPGSLRMNLDLLQEH-SDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLA 1299
Cdd:COG5265 427 QASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIA 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1300 RALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLF 1379
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLY 586
|
...
gi 1199277034 1380 YRL 1382
Cdd:COG5265 587 AQM 589
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
829-1126 |
4.09e-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: 4.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 829 GTPLCLYALFLFLCQQVASFCRGYWLSLWADDP---AVGGQQTQAALR----------------GGIFGLLGCLQAIGLF 889
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGsgnTTNNVDNSTVDSgnisdnpdlnfyqlvyGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 890 ASMAAVLlggaRASRLLFQRLLWDVVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVA 969
Cdd:cd18599 81 VFVKVTL----RASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 970 TPLATVAILPLFLLYAGFQSLYVVSSCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFP 1049
Cdd:cd18599 157 FPWFLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199277034 1050 RLVADRWLAANVELLGNGLVFAAATCAVLSKAHLSAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDYA 1126
Cdd:cd18599 237 FNCAMRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1149-1363 |
4.28e-49 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 173.93 E-value: 4.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1149 GQIEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRI 1228
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1229 SIIPQDPILFPGSLRMNLDL-LQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQ 1307
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLgAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 1308 ILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQV 1363
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1149-1379 |
3.58e-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: 173.50 E-value: 3.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1149 GQIEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAaEGGIWIDGVPIAHVGLHTLRSRI 1228
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1229 SIIPQDPILFPGSLRMNLDLLQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQI 1308
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 1309 LILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLF 1379
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
834-1125 |
5.66e-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: 173.55 E-value: 5.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 834 LYALFLFLCQQVASFCRGYWLSLWADDPaVGGQQTQAALRGGIFGLLGCLQAIGLFASMAAVLLGGARASRLLFQRLLWD 913
Cdd:cd18559 2 FLLIKLVLCNHVFSGPSNLWLLLWFDDP-VNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 914 VVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPLAtVAILPLFLLYAGFQSLYVV 993
Cdd:cd18559 81 ALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMA-AVGIPLGLLYVPVNRVYAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 994 SSCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDEsQRISFPRLVADRWLAANVELLGNGLVFAAA 1073
Cdd:cd18559 160 SSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDN-ELAYLPSIVYLRALAVRLWCVGPCIVLFAS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 1074 TCAVLSKAHLsAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDY 1125
Cdd:cd18559 239 FFAYVSRHSL-AGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLER 289
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
862-1382 |
9.07e-48 |
|
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: 9.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 862 AVGGQQTQAALRGGIFgLLGCLQaigLFASMAAVLLGG------ARASRLLFQRLLWDVVRSPISFFERTPIGHLLNRFS 935
Cdd:TIGR00958 190 TLGGDKGPPALASAIF-FMCLLS---IASSVSAGLRGGsfnytmARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLS 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 936 KETDTVDVDIPDK----LRSLLMyAFGLLEVSLVVAVATPLATVAILPL-FLLYAGFQSLYVVSSCQLRrlESASYSSvc 1010
Cdd:TIGR00958 266 SDTQTMSRSLSLNvnvlLRNLVM-LLGLLGFMLWLSPRLTMVTLINLPLvFLAEKVFGKRYQLLSEELQ--EAVAKAN-- 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1011 sHMAETfqgstVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANV------ELLGNGLVFAAATCA---VLSKA 1081
Cdd:TIGR00958 341 -QVAEE-----ALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAgylwttSVLGMLIQVLVLYYGgqlVLTGK 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1082 HLSAGLVGFsVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDYAwtpkEAPWRLPTCAAQPPWPQGGQIEFRDFGLRY- 1160
Cdd:TIGR00958 415 VSSGNLVSF-LLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYL----DRKPNIPLTGTLAPLNLEGLIEFQDVSFSYp 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1161 -RPELPLaVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFP 1239
Cdd:TIGR00958 490 nRPDVPV-LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFS 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1240 GSLRMNLDL-LQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAV 1318
Cdd:TIGR00958 569 GSVRENIAYgLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 1319 DpgteLQMQAMLGSW--FAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFYRL 1382
Cdd:TIGR00958 649 D----AECEQLLQESrsRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
212-487 |
1.27e-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: 172.40 E-value: 1.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 212 FTVPKLLSLFLEFIGDPKPPAWKGYLLAVLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITGLVYRKVLALSSGSRKASA 291
Cdd:cd18559 14 FSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 292 VGDVVNLVSVDVQRLTESVLYLNGLWLPLVWIVVCFVYLWQLLGPSALTAIAVFLSLLPLNFFISKKRNHHQEEQMRQKD 371
Cdd:cd18559 94 SGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 372 SRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLLFSVSLVSFQVSTFLVALVVFAVHTLVAENA-MNA 450
Cdd:cd18559 174 PRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHSLAgLVA 253
|
250 260 270
....*....|....*....|....*....|....*..
gi 1199277034 451 EKAFVTLTVLNILNKAQAFLPFSIHSLVQARVSFDRL 487
Cdd:cd18559 254 LKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
199-487 |
1.54e-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: 166.24 E-value: 1.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 199 LGTLSLIISDVFRFTVPKLLSLFLEFIGDPKPPA--WKGYLLAVLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITGLVY 276
Cdd:cd18593 1 LLGIFLFLEEAIRVVQPIFLGKLIRYFEGNGSSIslTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 277 RKVLALSSGSRKASAVGDVVNLVSVDVQRLTESVLYLNGLWL-PLVWIVVCFVyLWQLLGPSALTAIAVFLSLLPLNFFI 355
Cdd:cd18593 81 RKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVaPLQLIAVIYI-LWFEIGWSCLAGLAVLLILIPLQSFF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 356 SKKRNHhqeeqMRQK-----DSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLLFSVSLVSFQVSTF 430
Cdd:cd18593 160 GKLFSK-----LRRKtaartDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSK 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 431 LVALVVFAVHTLVaENAMNAEKAFVTLTVLNILNKAQA-FLPFSIHSLVQARVSFDRL 487
Cdd:cd18593 235 LILFLTFLAYILL-GNILTAERVFVTMALYNAVRLTMTlFFPFAIQFGSELSVSIRRI 291
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
829-1126 |
1.54e-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: 1.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 829 GTPLCLYALFLFLCQQVASFCRGYWLSLWADDPAVGGQQTQAALRG----------------GIFGLLGCLQAIGLFASM 892
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEEKLNDTTDRVQGEnstnvdiedldrdfnlGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 893 AAVLLGGARASRLLFQRLLWDVVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPL 972
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 973 ATVAILPLFLLYAGFQSLYVVSSCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLV 1052
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 1053 ADRWLAANVELLGNGLVFAAATCAVLSKAHLSAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDYA 1126
Cdd:cd18601 241 TSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEYS 314
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1151-1384 |
6.18e-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: 162.66 E-value: 6.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISI 1230
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1231 IPQDPILFPGSLRMNLDLLQEHSD-EAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQIL 1309
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSmERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 1310 ILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFYRLAQ 1384
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
530-726 |
6.65e-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: 6.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 530 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQEAWVQNTSVVENVCFGQELDPPWLE 609
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 610 RVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVIGPggLLQ 689
Cdd:cd03291 131 SVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCK--LMA 208
|
170 180 190
....*....|....*....|....*....|....*..
gi 1199277034 690 GTTRILVTHALHILPQADWIIVLANGAIAEMGSYQEL 726
Cdd:cd03291 209 NKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
874-1389 |
3.15e-42 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 164.75 E-value: 3.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 874 GGIFGLLGCLQAIGLFASMAAVLLggAR-ASRLLFQR---LLWD----VVRSPISFFERTPIGHLLNRFSKETDTVdvdi 945
Cdd:PRK13657 53 GDIFPLLAAWAGFGLFNIIAGVLV--ARhADRLAHRRrlaVLTEyferIIQLPLAWHSQRGSGRALHTLLRGTDAL---- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 946 pdklrsllmyaFGL-LE---------VSLVVAVATPLAT---VAILpLFLLYAGFqslYVVSSCQLRRLES------ASY 1006
Cdd:PRK13657 127 -----------FGLwLEfmrehlatlVALVVLLPLALFMnwrLSLV-LVVLGIVY---TLITTLVMRKTKDgqaaveEHY 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1007 SSVCSHMAETFQGSTVVRAFrtqapfvaqnnARVDESQRISfpRLVADRWLAANVELLG-----NGLVFAAATCAVLS-- 1079
Cdd:PRK13657 192 HDLFAHVSDAIGNVSVVQSY-----------NRIEAETQAL--RDIADNLLAAQMPVLSwwalaSVLNRAASTITMLAil 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1080 --------KAHLSAGLVGFSVSAALQVTQTLQWVVrnwtDLENSIV-SVERMQDYAWTPKEAPWRLPTCAAQPPWPQGGQ 1150
Cdd:PRK13657 259 vlgaalvqKGQLRVGEVVAFVGFATLLIGRLDQVV----AFINQVFmAAPKLEEFFEVEDAVPDVRDPPGAIDLGRVKGA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYrPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISI 1230
Cdd:PRK13657 335 VEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAV 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1231 IPQDPILFPGSLRMNLDLLQEH-SDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQIL 1309
Cdd:PRK13657 414 VFQDAGLFNRSIEDNIRVGRPDaTDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPIL 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1310 ILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFYRLAQESGLV 1389
Cdd:PRK13657 494 ILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQGML 573
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
521-732 |
1.02e-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: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 521 TFAWSQESPpCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAYVPQEAW 587
Cdd:cd03253 7 TFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVVPQDTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 588 VQNTSVVENVCFGQELDPPwlERVLEAC---ALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDD 664
Cdd:cd03253 86 LFNDTIGYNIRYGRPDATD--EEVIEAAkaaQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 665 PLAALDAHVGQHVFNQVIgpgGLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGA 732
Cdd:cd03253 164 ATSALDTHTEREIQAALR---DVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGL 228
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
515-715 |
9.28e-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: 145.22 E-value: 9.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAY 581
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 582 VPQEAWVQNTSVVENVcfgqeldppwlervleacalqpdvdsfpegihtsigeqgmnLSGGQKQRLSLARAVYRKAAVYL 661
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 662 LDDPLAALDAHVGQHVFnQVIgpGGLLQGTTRILVTHALHILPQADWIIVLANG 715
Cdd:cd03228 120 LDEATSALDPETEALIL-EAL--RALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
530-731 |
2.07e-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: 2.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 530 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAYVPQEAWVQNTSVVEN 596
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGVVLQDTFLFSGTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 597 VCFGQELDPPwlERVLEAC-ALQPD--VDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHV 673
Cdd:cd03254 97 IRLGRPNATD--EEVIEAAkEAGAHdfIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTET 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 674 GQHVFNQVigpGGLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKG 731
Cdd:cd03254 175 EKLIQEAL---EKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
515-732 |
3.50e-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: 146.22 E-value: 3.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAY 581
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 582 VPQEAWVQNTSVVENVCFGQ-ELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVY 660
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRpGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 661 LLDDPLAALDA---HVGQHVFNQvigpggLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGA 732
Cdd:cd03251 161 ILDEATSALDTeseRLVQAALER------LMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGV 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
530-732 |
1.05e-37 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 141.91 E-value: 1.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 530 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-------------VAYVPQEAWVQNTSVVEN 596
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIGLVSQEPVLFDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 597 VCFGqeLDPPWLERVLEACAL---QPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAH- 672
Cdd:cd03249 97 IRYG--KPDATDEEVEEAAKKaniHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAEs 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 673 --VGQHVFNQVIgpggllQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGA 732
Cdd:cd03249 175 ekLVQEALDRAM------KGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGV 230
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
237-712 |
2.39e-37 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 148.59 E-value: 2.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 237 LLAVLMFLSACLQTLFEqqnmYRLKVLQMRLRSAITGLVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTESV-LYLNG 315
Cdd:TIGR02857 49 ALALVLLLRALLGWLQE----RAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFaRYLPQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 316 LWL----PLVWIVVCFVYLWqllgpsaLTAIAVFLSLLPLNFFISKKRNHHQEEQMRQKDSRARLTS---SILRNSKTIK 388
Cdd:TIGR02857 125 LVLavivPLAILAAVFPQDW-------ISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGhflDRLRGLPTLK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 389 FHGWEGAFLDRVLGI----RGQELGALRTSgllFSVSLVSFQVSTFLVALV-VFAVHTLVAENaMNAEKAFVTLtvlnIL 463
Cdd:TIGR02857 198 LFGRAKAQAAAIRRSseeyRERTMRVLRIA---FLSSAVLELFATLSVALVaVYIGFRLLAGD-LDLATGLFVL----LL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 464 nKAQAFLPF-----SIHSLVQARVSFDRLVTFLCLEE-VDPGVVDSSSSGSAAgkdcITIHSATFAWsQESPPCLHRINL 537
Cdd:TIGR02857 270 -APEFYLPLrqlgaQYHARADGVAAAEALFAVLDAAPrPLAGKAPVTAAPASS----LEFSGVSVAY-PGRRPALRPVSF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 538 TVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-------------VAYVPQEAWVQNTSVVENVCFGQ-EL 603
Cdd:TIGR02857 344 TVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVpladadadswrdqIAWVPQHPFLFAGTIAENIRLARpDA 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 604 DPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVIg 683
Cdd:TIGR02857 424 SDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALR- 502
|
490 500
....*....|....*....|....*....
gi 1199277034 684 pgGLLQGTTRILVTHALHILPQADWIIVL 712
Cdd:TIGR02857 503 --ALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1149-1363 |
2.49e-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: 140.30 E-value: 2.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1149 GQIEFRD--FGLRYRPELPLaVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRS 1226
Cdd:cd03248 10 GIVKFQNvtFAYPTRPDTLV-LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1227 RISIIPQDPILFPGSLRMNLDL-LQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRK 1305
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAYgLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 1306 TQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQV 1363
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
897-1346 |
1.07e-36 |
|
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: 146.74 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 897 LGGARASrlLFQRLlwdvVRSPISFFERTPIGHLLNRFSKETDTVD-----VDIPDKLRSLLMYAFGLLEVSLVVAVATP 971
Cdd:TIGR02868 85 LGALRVR--VYERL----ARQALAGRRRLRRGDLLGRLGADVDALQdlyvrVIVPAGVALVVGAAAVAAIAVLSVPAALI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 972 LATVAILPLFLLYAGFQSLYVVSSCQLRRLESASYSSVcshmAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRL 1051
Cdd:TIGR02868 159 LAAGLLLAGFVAPLVSLRAARAAEQALARLRGELAAQL----TDALDGAAELVASGALPAALAQVEEADRELTRAERRAA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1052 VADRWLAAnVELLGNGLV----FAAATCAVLSKAHLSAGL--VGFSVSAALQVTQTLQWVVRNWTdleNSIVSVERMqdY 1125
Cdd:TIGR02868 235 AATALGAA-LTLLAAGLAvlgaLWAGGPAVADGRLAPVTLavLVLLPLAAFEAFAALPAAAQQLT---RVRAAAERI--V 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1126 AWTPKEAPWRLPTCAAQPPWPQGG-QIEFRDFGLRYrPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEA 1204
Cdd:TIGR02868 309 EVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1205 AEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLDLLQ-EHSDEAIWAALETVQLKALVASLPGQLQYKCAD 1283
Cdd:TIGR02868 388 LQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARpDATDEELWAALERVGLADWLRALPDGLDTVLGE 467
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 1284 RGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRL 1346
Cdd:TIGR02868 468 GGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1171-1389 |
1.12e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 147.68 E-value: 1.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1171 VSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQeAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLDLLQ 1250
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1251 EH-SDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTE-LQMQA 1328
Cdd:PRK11174 448 PDaSDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEqLVMQA 527
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 1329 MLGSWFAQcTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFYR-LAQESGLV 1389
Cdd:PRK11174 528 LNAASRRQ-TTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATlLAHRQEEI 588
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1151-1376 |
1.20e-36 |
|
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: 138.62 E-value: 1.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLA---SGLLRLQEaaeGGIWIDGVPIAHVGLHTLRSR 1227
Cdd:COG1122 1 IELENLSFSYPGGTP-ALDDVSLSIEKGEFVAIIGPNGSGKSTLLrllNGLLKPTS---GEVLVDGKDITKKNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1228 ISIIPQDP------------ILFpgSLRmNLDLLQEHSDEAIWAALETVQLKALvaslpgqlqykcADRG-EDLSVGQKQ 1294
Cdd:COG1122 77 VGLVFQNPddqlfaptveedVAF--GPE-NLGLPREEIRERVEEALELVGLEHL------------ADRPpHELSGGQKQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1295 LLCLARALLRKTQILILDEATAAVDP-GTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQL 1372
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLDPrGRRELLELLKRLNKEGKTVIIVTHDLDLVAELAdRVIVLDDGRIVADGTPREV 221
|
....
gi 1199277034 1373 LAQK 1376
Cdd:COG1122 222 FSDY 225
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1140-1384 |
8.72e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 144.97 E-value: 8.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1140 AAQPPWPQGGQIEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHV 1219
Cdd:PRK11160 328 TTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADY 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1220 GLHTLRSRISIIPQDPILFPGSLRMNLDLLQEH-SDEAIWAALETVQLKALVASLPGqLQYKCADRGEDLSVGQKQLLCL 1298
Cdd:PRK11160 408 SEAALRQAISVVSQRVHLFSATLRDNLLLAAPNaSDEALIEVLQQVGLEKLLEDDKG-LNAWLGEGGRQLSGGEQRRLGI 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1299 ARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSV--MDcaRVLVMDKGQVAESGSPAQLLAQK 1376
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLeqFD--RICVMDNGQIIEQGTHQELLAQQ 564
|
....*...
gi 1199277034 1377 GLFYRLAQ 1384
Cdd:PRK11160 565 GRYYQLKQ 572
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
260-700 |
5.35e-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: 141.73 E-value: 5.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 260 LKVLQmRLRSAitglVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTEsvLYLNGLWLPLVWIVV-------CFVYLWQ 332
Cdd:TIGR02868 82 LRSLG-ALRVR----VYERLARQALAGRRRLRRGDLLGRLGADVDALQD--LYVRVIVPAGVALVVgaaavaaIAVLSVP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 333 LlGPSALTAIAVFLSLLPLnFFISKKRNHHQEEQmRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRV---------LGI 403
Cdd:TIGR02868 155 A-ALILAAGLLLAGFVAPL-VSLRAARAAEQALA-RLRGELAAQLTDALDGAAELVASGALPAALAQVeeadreltrAER 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 404 RGQELGALRTSGLLFSVSLVsfqvstflVALVVFAVHTLVAENAMNAekAFVTLTVLNILNKAQAFLPFS--IHSLVQAR 481
Cdd:TIGR02868 232 RAAAATALGAALTLLAAGLA--------VLGALWAGGPAVADGRLAP--VTLAVLVLLPLAAFEAFAALPaaAQQLTRVR 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 482 VSFDRLVTFLCLEEVDPGVVDSSSSGSAAGKDCITIHSATFAWSQeSPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSA 561
Cdd:TIGR02868 302 AAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYPG-APPVLDGVSLDLPPGERVAILGPSGSGKSTLLAT 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 562 LLGELSKVEGFVSIEGA-------------VAYVPQEAWVQNTSVVENVCFGQ-ELDPPWLERVLEACALQPDVDSFPEG 627
Cdd:TIGR02868 381 LAGLLDPLQGEVTLDGVpvssldqdevrrrVSVCAQDAHLFDTTVRENLRLARpDATDEELWAALERVGLADWLRALPDG 460
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 628 IHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVIGPgglLQGTTRILVTHAL 700
Cdd:TIGR02868 461 LDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA---LSGRTVVLITHHL 530
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
906-1382 |
6.36e-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: 143.73 E-value: 6.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 906 LFQRLLWDVVRS--------PISFFERTPIGHLLNRFSketdtvDVD-IPDKLRSLLMYAFglLEVSLVVAVATPLATVA 976
Cdd:TIGR01193 223 LGQRLSIDIILSyikhlfelPMSFFSTRRTGEIVSRFT------DASsIIDALASTILSLF--LDMWILVIVGLFLVRQN 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 977 ILpLFLLYAGFQSLYVVSSCQLRR---------LESASYSSvcSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRIS 1047
Cdd:TIGR01193 295 ML-LFLLSLLSIPVYAVIIILFKRtfnklnhdaMQANAVLN--SSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKS 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1048 FPRLVAD---RWLAANVELLGNGLVFAAATCAVLSKaHLSAG-LVGFSVSAALqVTQTLQWVVRNWTDLENSIVSVERMQ 1123
Cdd:TIGR01193 372 FKYQKADqgqQAIKAVTKLILNVVILWTGAYLVMRG-KLTLGqLITFNALLSY-FLTPLENIINLQPKLQAARVANNRLN 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1124 DYAWTPKE-APWRLPTCAAQPpwpqGGQIEFRDFGLRYRPELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQ 1202
Cdd:TIGR01193 450 EVYLVDSEfINKKKRTELNNL----NGDIVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFF 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1203 EAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLdLLQEH---SDEAIWAALETVQLKALVASLPGQLQY 1279
Cdd:TIGR01193 525 QARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENL-LLGAKenvSQDEIWAACEIAEIKDDIENMPLGYQT 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1280 KCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSwFAQCTVLLIAHRLRSVMDCARVLVMD 1359
Cdd:TIGR01193 604 ELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLD 682
|
490 500
....*....|....*....|...
gi 1199277034 1360 KGQVAESGSPAQLLAQKGLFYRL 1382
Cdd:TIGR01193 683 HGKIIEQGSHDELLDRNGFYASL 705
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1141-1358 |
1.88e-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: 1.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1141 AQPPWPQGGQIEFRDFGLRYRPELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG 1220
Cdd:TIGR02857 312 APVTAAPASSLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1221 LHTLRSRISIIPQDPILFPGSLRMNLDLLQ-EHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLA 1299
Cdd:TIGR02857 391 ADSWRDQIAWVPQHPFLFAGTIAENIRLARpDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALA 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 1300 RALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVM 1358
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
535-742 |
3.87e-34 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 139.98 E-value: 3.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELsKVEGFVSIEG-------AVAYVPQEAWV-QNT-----SVVENVCFGQ 601
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGielreldPESWRKHLSWVgQNPqlphgTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 602 -ELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHV--- 677
Cdd:PRK11174 448 pDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVmqa 527
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 678 FNQVIgpggllQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGALVCLLDQARQ 742
Cdd:PRK11174 528 LNAAS------RRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQE 586
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
219-731 |
4.87e-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: 141.03 E-value: 4.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 219 SLFLEFIGDPK-PPAWKGYL--LAVLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITGLVYRKVLALSSGSRKASAVGDV 295
Cdd:TIGR01193 176 SYYLQKIIDTYiPHKMMGTLgiISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEI 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 296 VNLVSvDVQRLTESV------LYLNgLWLpLVWIVVCFVYLWQLLGPSALTAIAVFLSLLPLNFFISKKRNHhqeEQMRq 369
Cdd:TIGR01193 256 VSRFT-DASSIIDALastilsLFLD-MWI-LVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNH---DAMQ- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 370 kdSRARLTSSILRN---SKTIKFHGWE-----------GAFLDR--VLGIRGQELGALRTsGLLFSVSLVSFQVSTFLVA 433
Cdd:TIGR01193 329 --ANAVLNSSIIEDlngIETIKSLTSEaeryskidsefGDYLNKsfKYQKADQGQQAIKA-VTKLILNVVILWTGAYLVM 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 434 LVVFAVHTLVAENAMnaeKAFVTLTVLNILN---KAQAflpfsihslvqARVSFDRL--VTFLCLEEVDPGVVDSSSSGS 508
Cdd:TIGR01193 406 RGKLTLGQLITFNAL---LSYFLTPLENIINlqpKLQA-----------ARVANNRLneVYLVDSEFINKKKRTELNNLN 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 509 AAgkdcITIHSATFAWSQESPpCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG----------- 577
Cdd:TIGR01193 472 GD----IVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslkdidrhtl 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 578 --AVAYVPQEAWVQNTSVVENVCFG--QELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAV 653
Cdd:TIGR01193 547 rqFINYLPQEPYIFSGSILENLLLGakENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARAL 626
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 654 YRKAAVYLLDDPLAALDAHVGQHVFNQVIGpgglLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKG 731
Cdd:TIGR01193 627 LTDSKVLILDESTSNLDTITEKKIVNNLLN----LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNG 700
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1151-1375 |
1.74e-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: 136.96 E-value: 1.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLA---SGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSR 1227
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLAlalMGLLPHGGRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1228 ISIIPQDPI--LFPGSLR-------MNLDLLQEHSDEAIWAALETVQLKALVASLPGQlqykcadrgedLSVGQKQLLCL 1298
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGdqiaealENLGLSRAEARARVLELLEAVGLERRLDRYPHQ-----------LSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1299 ARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQ 1375
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVVAEIAdRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
515-731 |
3.70e-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: 128.76 E-value: 3.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAY 581
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 582 VPQEAWVQNTSVVENVCFGQELDPpwLERVLEACALQpDVDSF----PEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKA 657
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMS--MERVIEAAKLA-GAHDFiselPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 658 AVYLLDDPLAALDaHVGQHVFNQVIgpGGLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKG 731
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 ... |
193-731 |
7.91e-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: 135.61 E-value: 7.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 193 FHSTFLLGTLSLIISDVFRFTVPKLLSLFLE--FIGDPKPPAWKGYLLAVLMFLsacLQTLFEQQNMYRLKVLQMRLRSA 270
Cdd:TIGR02203 12 YKAGLVLAGVAMILVAATESTLAALLKPLLDdgFGGRDRSVLWWVPLVVIGLAV---LRGICSFVSTYLLSWVSNKVVRD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 271 ITGLVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTES------VLYLNGLWLpLVWIVVCFVYLWQLLgpsalTAIAV 344
Cdd:TIGR02203 89 IRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAatdafiVLVRETLTV-IGLFIVLLYYSWQLT-----LIVVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 345 FLSLLPLNFFISKKR----NHHQEEQMRQKdsrARLTSSILRNSKTIKFHGWEGAFLDRvlgirgqeLGALRTSGLLFSV 420
Cdd:TIGR02203 163 MLPVLSILMRRVSKRlrriSKEIQNSMGQV---TTVAEETLQGYRVVKLFGGQAYETRR--------FDAVSNRNRRLAM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 421 SLVSFQ-----VSTFLVALVVFAVHTLVAENAMNAEKAFVTLTVLnILNKAQAFLPFSIHSLVQAR-----VSFDRLVTF 490
Cdd:TIGR02203 232 KMTSAGsisspITQLIASLALAVVLFIALFQAQAGSLTAGDFTAF-ITAMIALIRPLKSLTNVNAPmqrglAAAESLFTL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 491 LCLE-EVDPGVVdssssGSAAGKDCITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKV 569
Cdd:TIGR02203 311 LDSPpEKDTGTR-----AIERARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 570 EGFVSIEGA-------------VAYVPQEAWVQNTSVVENVCFGQ--ELDPPWLERVLEACALQPDVDSFPEGIHTSIGE 634
Cdd:TIGR02203 386 SGQILLDGHdladytlaslrrqVALVSQDVVLFNDTIANNIAYGRteQADRAEIERALAAAYAQDFVDKLPLGLDTPIGE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 635 QGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVigpGGLLQGTTRILVTHALHILPQADWIIVLAN 714
Cdd:TIGR02203 466 NGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAAL---ERLMQGRTTLVIAHRLSTIEKADRIVVMDD 542
|
570
....*....|....*..
gi 1199277034 715 GAIAEMGSYQELLQRKG 731
Cdd:TIGR02203 543 GRIVERGTHNELLARNG 559
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
317-729 |
1.25e-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: 134.88 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 317 WLPLvWIVVCFVyLWQLLGPSALTAIAVFLSLLPLNFFISKKrnhHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAF 396
Cdd:COG4618 142 WAPI-FLAVLFL-FHPLLGLLALVGALVLVALALLNERLTRK---PLKEANEAAIRANAFAEAALRNAEVIEAMGMLPAL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 397 LDRVLGIRGQELG----ALRTSGLLFSVSLV---SFQVST-----FLV------ALVVFAVHTLVA------ENAMNAEK 452
Cdd:COG4618 217 RRRWQRANARALAlqarASDRAGGFSALSKFlrlLLQSAVlglgaYLViqgeitPGAMIAASILMGralapiEQAIGGWK 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 453 AFVtltvlnilnkaqaflpfsihslvQARVSFDRLVTFLCLEEVDPGVVDSSSSGSAagkdcITIHSATFAWSQESPPCL 532
Cdd:COG4618 297 QFV-----------------------SARQAYRRLNELLAAVPAEPERMPLPRPKGR-----LSVENLTVVPPGSKRPIL 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 533 HRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-------------VAYVPQEawVQ--NTSVVENV 597
Cdd:COG4618 349 RGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAdlsqwdreelgrhIGYLPQD--VElfDGTIAENI 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 598 C-FGqELDPpwlERVLEACALQpDVD----SFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAh 672
Cdd:COG4618 427 ArFG-DADP---EKVVAAAKLA-GVHemilRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD- 500
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 673 VGQHVFNQVIgpGGL-LQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQR 729
Cdd:COG4618 501 EGEAALAAAI--RALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1131-1375 |
1.56e-32 |
|
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: 133.88 E-value: 1.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1131 EAPWRLPTCAAQPPWPQGGQ--IEFRD----FGLRYRPELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEA 1204
Cdd:COG1123 239 AVPRLGAARGRAAPAAAAAEplLEVRNlskrYPVRGKGGVR-AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRP 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1205 AEGGIWIDGVPIAHVG---LHTLRSRISIIPQDPI--LFPgslRMN--------LDLLQEHSDEAIWA----ALETVQLK 1267
Cdd:COG1123 318 TSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPYssLNP---RMTvgdiiaepLRLHGLLSRAERRErvaeLLERVGLP 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1268 ALVAS-LPGQlqykcadrgedLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQM-------QAMLGswfaqCTV 1339
Cdd:COG1123 395 PDLADrYPHE-----------LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQIlnllrdlQRELG-----LTY 458
|
250 260 270
....*....|....*....|....*....|....*...
gi 1199277034 1340 LLIAHRLrSVMD--CARVLVMDKGQVAESGSPAQLLAQ 1375
Cdd:COG1123 459 LFISHDL-AVVRyiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
225-742 |
1.64e-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: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 225 IGDPKPPAWKGYLLAVLMFLSACL--QTLFE--QQnmyrLKVLQM--RLRSAITGLVYRKVLALSSGSRKASAVGDVVNL 298
Cdd:TIGR03797 163 IGTAIPDADRSLLVQIALALLAAAvgAAAFQlaQS----LAVLRLetRMDASLQAAVWDRLLRLPVSFFRQYSTGDLASR 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 299 VSVDVQ---RLTESVL-YLNGLWLPLVWIVVCFVYLWQLlgpsALTAIAVFLSLLPLNFFISKKRNHHQEEQMRQKDSRA 374
Cdd:TIGR03797 239 AMGISQirrILSGSTLtTLLSGIFALLNLGLMFYYSWKL----ALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKIS 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 375 RLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQElgalrtSGLLFSVSLVSFQVSTFLVALVVFAVHTLVAenAMNAEKAF 454
Cdd:TIGR03797 315 GLTVQLINGISKLRVAGAENRAFARWAKLFSRQ------RKLELSAQRIENLLTVFNAVLPVLTSAALFA--AAISLLGG 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 455 VTLTVLNILNKAQAFLPF--SIHSLVQARVS-------FDRLVTFL-CLEEVDPGVVDSSSSGSAagkdcITIHSATFAW 524
Cdd:TIGR03797 387 AGLSLGSFLAFNTAFGSFsgAVTQLSNTLISilaviplWERAKPILeALPEVDEAKTDPGKLSGA-----IEVDRVTFRY 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 525 SQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG---------AV----AYVPQEAWVQNT 591
Cdd:TIGR03797 462 RPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGqdlagldvqAVrrqlGVVLQNGRLMSG 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 592 SVVENVCFGQELDPpwlERVLEA---CALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAA 668
Cdd:TIGR03797 542 SIFENIAGGAPLTL---DEAWEAarmAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSA 618
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 669 LD----AHVGQHVfnqvigpgGLLQGtTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGALVCLLdqARQ 742
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 ... |
1152-1362 |
2.61e-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: 125.27 E-value: 2.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1152 EFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISII 1231
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1232 PQDP------------ILFpgSLRmNLDLLQEHSDEAIWAALETVQLKALVASLPgqlqykcadrgEDLSVGQKQLLCLA 1299
Cdd:cd03225 81 FQNPddqffgptveeeVAF--GLE-NLGLPEEEIEERVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 1300 RALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQC-TVLLIAHRLRSVMDCA-RVLVMDKGQ 1362
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGkTIIIVTHDLDLLLELAdRVIVLEDGK 211
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
515-731 |
5.51e-32 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 133.30 E-value: 5.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQESPpCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAY 581
Cdd:PRK10790 341 IDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsslshsvlrqGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 582 VPQEAWVQNTSVVENVCFGQELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYL 661
Cdd:PRK10790 420 VQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILI 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 662 LDDPLAALDAHVGQHVfNQVIgpGGLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKG 731
Cdd:PRK10790 500 LDEATANIDSGTEQAI-QQAL--AAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQG 566
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
514-728 |
6.81e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 125.20 E-value: 6.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 514 CITIHSATFAWSQEspPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------VAYVPQE 585
Cdd:COG1121 6 AIELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKpprrarrrIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 586 AWVQNT---SVVENVCFGQELDPPWL--------ERVLEACAlQPDVDSFpegIHTSIGEqgmnLSGGQKQRLSLARAVY 654
Cdd:COG1121 84 AEVDWDfpiTVRDVVLMGRYGRRGLFrrpsradrEAVDEALE-RVGLEDL---ADRPIGE----LSGGQQQRVLLARALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 655 RKAAVYLLDDPLAALDAHvGQHVFNQVIgpGGLL-QGTTRILVTHALHILPQ-ADWIIVLANGAIAEmGSYQELLQ 728
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAA-TEEALYELL--RELRrEGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPEEVLT 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1151-1367 |
7.71e-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: 124.54 E-value: 7.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPEL--PLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTL---R 1225
Cdd:cd03257 2 LEVKNLSVSFPTGGgsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1226 SRISIIPQDPIlfpGSL--RMN-----LDLLQEHSDEAIWAALETVQLKALVA-SLPGQlqykCADR--GEdLSVGQKQL 1295
Cdd:cd03257 82 KEIQMVFQDPM---SSLnpRMTigeqiAEPLRIHGKLSKKEARKEAVLLLLVGvGLPEE----VLNRypHE-LSGGQRQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1296 LCLARALLRKTQILILDEATAAVDPGTELQ-------MQAMLGswfaqCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESG 1367
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQildllkkLQEELG-----LTLLFITHDLGVVAKIAdRVAVMYAGKIVEEG 228
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
515-717 |
3.97e-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: 122.31 E-value: 3.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-------------VAY 581
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdirqldpadlrrnIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 582 VPQEAWVQNTSVVENVCFG-QELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVY 660
Cdd:cd03245 83 VPQDVTLFYGTLRDNITLGaPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199277034 661 LLDDPLAALDAHVGQHVFNQVigpGGLLQGTTRILVTHALHILPQADWIIVLANGAI 717
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERL---RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1150-1384 |
6.10e-31 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 129.83 E-value: 6.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1150 QIEFRDFglRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRIS 1229
Cdd:PRK10789 315 DVNIRQF--TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1230 IIPQDPILFPGSLRMNL-----DLLQEHSDEAiwAALETVQLKALvaSLPGQLQYKCADRGEDLSVGQKQLLCLARALLR 1304
Cdd:PRK10789 393 VVSQTPFLFSDTVANNIalgrpDATQQEIEHV--ARLASVHDDIL--RLPQGYDTEVGERGVMLSGGQKQRISIARALLL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1305 KTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLF---YR 1381
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYrdmYR 548
|
...
gi 1199277034 1382 LAQ 1384
Cdd:PRK10789 549 YQQ 551
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
904-1382 |
1.13e-30 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 129.37 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 904 RLLFQRLLwdvvRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLL---MYAFGLL--------EVSLVVAVATPL 972
Cdd:PRK11176 102 RRLFGHMM----GMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVregASIIGLFimmfyyswQLSLILIVIAPI 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 973 ATVAIlplfllyagfqslYVVSScQLRRLE---SASYSSVCSHMAETFQGSTVVRAFRTQ----------APFVAQNNAR 1039
Cdd:PRK11176 178 VSIAI-------------RVVSK-RFRNISknmQNTMGQVTTSAEQMLKGHKEVLIFGGQevetkrfdkvSNRMRQQGMK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1040 VDESQRISFP--RLVADRWLAAnvellgngLVFAAATCAVlsKAHLSAG--LVGFS--------------VSAALQ---- 1097
Cdd:PRK11176 244 MVSASSISDPiiQLIASLALAF--------VLYAASFPSV--MDTLTAGtiTVVFSsmialmrplksltnVNAQFQrgma 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1098 VTQTLQWVVRNWTDLENSIVSVERMQdyawtpkeapwrlptcaaqppwpqgGQIEFRDFGLRYRPELPLAVQGVSFKIHA 1177
Cdd:PRK11176 314 ACQTLFAILDLEQEKDEGKRVIERAK-------------------------GDIEFRNVTFTYPGKEVPALRNINFKIPA 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1178 GEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLDLLQE--HSDE 1255
Cdd:PRK11176 369 GKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTeqYSRE 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1256 AIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFA 1335
Cdd:PRK11176 449 QIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK 528
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1199277034 1336 QCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFYRL 1382
Cdd:PRK11176 529 NRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
168-737 |
1.65e-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: 1.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 168 APETEPFLRQEGSQWRPLL-------KAIWQVFHSTFLLgtlsLIISDVFRFTVPKLLSLFLEFI-GDPKPPAWKG--YL 237
Cdd:TIGR00958 131 AGASEKEAEQGQSETADLLfrllglsGRDWPWLISAFVF----LTLSSLGEMFIPFYTGRVIDTLgGDKGPPALASaiFF 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 238 LAVLMFLSACLQTLFEQQNMYRLKVLQMRLRsaitGLVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTESV-LYLNGL 316
Cdd:TIGR00958 207 MCLLSIASSVSAGLRGGSFNYTMARINLRIR----EDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLsLNVNVL 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 317 WLPLVwIVVCFVYLWQLLGPSaLTAIAVFLslLPLNFFISKKRN-HHQEEQMRQKDSRARLTS---SILRNSKTIKFHGW 392
Cdd:TIGR00958 283 LRNLV-MLLGLLGFMLWLSPR-LTMVTLIN--LPLVFLAEKVFGkRYQLLSEELQEAVAKANQvaeEALSGMRTVRSFAA 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 393 EGAFLDRVLGIRGQELGALRTSGLLFSVSLVSFQVSTFLVALVVFA--VHtLVAENAMNAEK--AFVtLTVLNILNKAQA 468
Cdd:TIGR00958 359 EEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYygGQ-LVLTGKVSSGNlvSFL-LYQEQLGEAVRV 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 469 FLpfSIHSLVQARVSFDRLVtfLCLEEVDPGVVDSSSSGSAAGKDCITIHSATFAW-SQESPPCLHRINLTVPQGCLLAV 547
Cdd:TIGR00958 437 LS--YVYSGMMQAVGASEKV--FEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYpNRPDVPVLKGLTFTLHPGEVVAL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 548 VGPVGAGKSSLLSALLGELSKVEGFVSIEGA-------------VAYVPQEAWVQNTSVVENVCFGqeLDPPWLERVLEA 614
Cdd:TIGR00958 513 VGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplvqydhhylhrqVALVGQEPVLFSGSVRENIAYG--LTDTPDEEIMAA 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 615 cALQPDVDSF----PEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVgqhvfNQVIGPGGLLQG 690
Cdd:TIGR00958 591 -AKAANAHDFimefPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC-----EQLLQESRSRAS 664
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1199277034 691 TTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGALVCLL 737
Cdd:TIGR00958 665 RTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
515-722 |
1.92e-30 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 120.29 E-value: 1.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAY 581
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 582 VPQEAWVQNTSVVENVCFGQELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYL 661
Cdd:cd03244 83 IPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 662 LDDPLAALDAHVGQHVfNQVIgpGGLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGS 722
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 ... |
1151-1367 |
2.23e-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: 118.57 E-value: 2.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGlHTLRSRISI 1230
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1231 IPQDPILFPGSLRMNLdllqehsdeaiwaaletvqlkalvaslpgqlqykcadrGEDLSVGQKQLLCLARALLRKTQILI 1310
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199277034 1311 LDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESG 1367
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
320-732 |
4.66e-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: 124.55 E-value: 4.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 320 LVWIVVCFVYLWQLLGPS--ALTAIAVFLSLLpLNFFISKKRNHHQEEqMRQKDSRA--RLTSSILrNSKTIKFHG---W 392
Cdd:COG5265 163 LLEIALVAGILLVKYDWWfaLITLVTVVLYIA-FTVVVTEWRTKFRRE-MNEADSEAntRAVDSLL-NYETVKYFGneaR 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 393 EGAFLDRVLgiRGQELGALRTSGLLFSVSLV-SFQVSTFLVALVVFAVHTlVAENAMNAeKAFVTLTVLNIlnkaQAFLP 471
Cdd:COG5265 240 EARRYDEAL--ARYERAAVKSQTSLALLNFGqALIIALGLTAMMLMAAQG-VVAGTMTV-GDFVLVNAYLI----QLYIP 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 472 FSIHSLV-----QARVSFDRLVTFLcleEVDPGVVDSSSSGSAAGKDC-ITIHSATFAWSQESPpCLHRINLTVPQGCLL 545
Cdd:COG5265 312 LNFLGFVyreirQALADMERMFDLL---DQPPEVADAPDAPPLVVGGGeVRFENVSFGYDPERP-ILKGVSFEVPAGKTV 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 546 AVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAYVPQEAWVQNTSVVENVCFGQ-ELDPPWLERV 611
Cdd:COG5265 388 AIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdirdvtqaslraAIGIVPQDTVLFNDTIAYNIAYGRpDASEEEVEAA 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 612 LEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVG---QHVFNQVIgpggll 688
Cdd:COG5265 468 ARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTEraiQAALREVA------ 541
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1199277034 689 QGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGA 732
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 ... |
521-715 |
1.32e-28 |
|
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: 114.87 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 521 TFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-------------VAYVPQEAW 587
Cdd:cd03225 6 SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKdltklslkelrrkVGLVFQNPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 588 VQ--NTSVVENVCFGQE---LDPPWLER----VLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAA 658
Cdd:cd03225 86 DQffGPTVEEEVAFGLEnlgLPEEEIEErveeALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 659 VYLLDDPLAALDAHVGQHVFNQVIGpgglL--QGTTRILVTHALH-ILPQADWIIVLANG 715
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKK----LkaEGKTIIIVTHDLDlLLELADRVIVLEDG 210
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1151-1374 |
1.49e-28 |
|
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: 115.67 E-value: 1.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRP--ELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRI 1228
Cdd:COG1124 2 LEVRNLSVSYGQggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1229 SIIPQDPilfPGSL--RMNLD-----LLQEH----SDEAIWAALETVQLKALVAS-LPGQLqykcadrgedlSVGQKQLL 1296
Cdd:COG1124 82 QMVFQDP---YASLhpRHTVDrilaePLRIHglpdREERIAELLEQVGLPPSFLDrYPHQL-----------SGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1297 CLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRsVMD--CARVLVMDKGQVAESGSPAQL 1372
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErgLTYLFVSHDLA-VVAhlCDRVAVMQNGRIVEELTVADL 226
|
..
gi 1199277034 1373 LA 1374
Cdd:COG1124 227 LA 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
521-717 |
1.67e-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: 113.08 E-value: 1.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 521 TFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-------------VAYVPQEAW 587
Cdd:cd03246 7 SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGYLPQDDE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 588 VQNTSVVENVcfgqeldppwlervleacalqpdvdsfpegihtsigeqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLA 667
Cdd:cd03246 87 LFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNS 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 668 ALDaHVGQHVFNQVIgpGGL-LQGTTRILVTHALHILPQADWIIVLANGAI 717
Cdd:cd03246 126 HLD-VEGERALNQAI--AALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
521-731 |
2.03e-27 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 119.05 E-value: 2.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 521 TFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFV-------------SIEGAVAYVPQEAW 587
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdipltklqldSWRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 588 VQNTSVVENVCFGQ-ELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPL 666
Cdd:PRK10789 400 LFSDTVANNIALGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 667 AALDAHVGQHVFNQVIGPGgllQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKG 731
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWG---EGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
532-667 |
4.22e-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: 4.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-------------VAYVPQEAWVQN-TSVVENV 597
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrkeIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199277034 598 CFGQELDPP-------WLERVLEACALqpdvdsfPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLA 667
Cdd:pfam00005 81 RLGLLLKGLskrekdaRAEEALEKLGL-------GDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
517-718 |
4.27e-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: 110.32 E-value: 4.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 517 IHSATFAWSQEspPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------VAYVPQEA-- 586
Cdd:cd03235 2 VEDLTVSYGGH--PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerkrIGYVPQRRsi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 587 -WVQNTSVVENVCFGQELDPPWL--------ERVLEACALqpdVDSFpEGIHTSIGEqgmnLSGGQKQRLSLARAVYRKA 657
Cdd:cd03235 80 dRDFPISVRDVVLMGLYGHKGLFrrlskadkAKVDEALER---VGLS-ELADRQIGE----LSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199277034 658 AVYLLDDPLAALDAHVGQHVFnqvigpgGLL-----QGTTRILVTHALH-ILPQADWIIVLANGAIA 718
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIY-------ELLrelrrEGMTILVVTHDLGlVLEYFDRVLLLNRTVVA 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1168-1316 |
4.51e-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: 108.12 E-value: 4.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1168 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPG-SLRMNL 1246
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199277034 1247 -------DLLQEHSDEAIWAALETVQLKALVASLPGqlqykcaDRGEDLSVGQKQLLCLARALLRKTQILILDEATA 1316
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKLGLGDLADRPVG-------ERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
834-1102 |
4.65e-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: 4.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 834 LYALFLFLCQQVASFCRGYWLSLWADDPAVGGQQ--TQAALRGGIFGLLGCLQAIGLFASMAAVLLGGARASRLLFQRLL 911
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDPetQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 912 WDVVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLLYAGFQSLY 991
Cdd:pfam00664 82 KKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 992 VVSSCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANVELLGNGLVFA 1071
Cdd:pfam00664 162 AKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYAL 241
|
250 260 270
....*....|....*....|....*....|...
gi 1199277034 1072 AA-TCAVLSKAH-LSAGLVGFSVSAALQVTQTL 1102
Cdd:pfam00664 242 ALwFGAYLVISGeLSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1151-1363 |
4.78e-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: 108.84 E-value: 4.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISI 1230
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1231 IPQDPILFPGSLRMNLdllqehsdeaiwaaletvqlkalvaslpgqlqykcadrgedLSVGQKQLLCLARALLRKTQILI 1310
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 1311 LDEATAAVDPGTE-LQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQV 1363
Cdd:cd03246 120 LDEPNSHLDVEGErALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1151-1375 |
5.77e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 110.92 E-value: 5.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELplAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHvGLHTLRSRISI 1230
Cdd:COG1131 1 IEVRGLTKRYGDKT--ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1231 IPQDPILFPG-SLRMNLDLL-------QEHSDEAIWAALETVQLKAlvaslpgqlqyKCADRGEDLSVGQKQLLCLARAL 1302
Cdd:COG1131 78 VPQEPALYPDlTVRENLRFFarlyglpRKEARERIDELLELFGLTD-----------AADRKVGTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 1303 LRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ-CTVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQLLAQ 1375
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
532-729 |
2.97e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 108.61 E-value: 2.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA------------VAYVPQEAWV-QNTSVVENVC 598
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvardpaevrrrIGYVPQEPALyPDLTVRENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 599 F-------GQELDPPWLERVLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDA 671
Cdd:COG1131 96 FfarlyglPRKEARERIDELLELFGLTDAADRKVG-----------TLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 672 hVGQHVFNQVIgpGGLL-QGTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELLQR 729
Cdd:COG1131 165 -EARRELWELL--RELAaEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
532-729 |
6.80e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 110.62 E-value: 6.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYV---PQE---AWV-QN------TSVVENVC 598
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnlpPRErrvGFVfQHyalfphMTVAENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 599 FGQELDPP-----------WLERV-LEACAlqpdvDSFPegihtsigeqgMNLSGGQKQRLSLARAVYRKAAVYLLDDPL 666
Cdd:COG1118 98 FGLRVRPPskaeirarveeLLELVqLEGLA-----DRYP-----------SQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 667 AALDAHVGQ-------HVFNQvigpgglLQGTTrILVTH----ALHIlpqADWIIVLANGAIAEMGSYQELLQR 729
Cdd:COG1118 162 GALDAKVRKelrrwlrRLHDE-------LGGTT-VFVTHdqeeALEL---ADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1151-1378 |
2.55e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 106.33 E-value: 2.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELplAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVglhtlRSRISI 1230
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1231 IPQDPIL---FPGSLR----MNLD-------LLQEHSDEAIWAALETVQLKALvaslpgqlqykcADR--GEdLSVGQKQ 1294
Cdd:COG1121 80 VPQRAEVdwdFPITVRdvvlMGRYgrrglfrRPSRADREAVDEALERVGLEDL------------ADRpiGE-LSGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1295 llclarallrKT----------QILILDEATAAVDPGTELQMQAMLGSWFAQ-CTVLLIAHRLRSVMDCA-RVLVMDKGQ 1362
Cdd:COG1121 147 ----------RVllaralaqdpDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREYFdRVLLLNRGL 216
|
250
....*....|....*.
gi 1199277034 1363 VAeSGSPAQLLAQKGL 1378
Cdd:COG1121 217 VA-HGPPEEVLTPENL 231
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
521-715 |
3.23e-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: 106.33 E-value: 3.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 521 TFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------VAYVPQEA----Wv 588
Cdd:COG1116 16 RFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKpvtgpgpdRGVVFQEPallpW- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 589 qnTSVVENVCFGQEL-------DPPWLERVLEACALQPDVDSFPegiHTsigeqgmnLSGGQKQRLSLARAVYRKAAVYL 661
Cdd:COG1116 95 --LTVLDNVALGLELrgvpkaeRRERARELLELVGLAGFEDAYP---HQ--------LSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 662 LDDPLAALDAHVGQHVFNQVIgpgGLLQ--GTTRILVTH----ALHIlpqADWIIVLANG 715
Cdd:COG1116 162 MDEPFGALDALTRERLQDELL---RLWQetGKTVLFVTHdvdeAVFL---ADRVVVLSAR 215
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
528-737 |
6.30e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 111.59 E-value: 6.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 528 SPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAYVPQEAWVQNTSVV 594
Cdd:PRK13657 347 SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtvtraslrrNIAVVFQDAGLFNRSIE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 595 ENVCFGQE-LDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHV 673
Cdd:PRK13657 427 DNIRVGRPdATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVET 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 674 GQHVfNQVIGPggLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGALVCLL 737
Cdd:PRK13657 507 EAKV-KAALDE--LMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALL 567
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1157-1377 |
6.82e-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: 6.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1157 GLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHtLRSRISIIPQDPI 1236
Cdd:COG4555 6 NLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLPDERG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1237 LFPG-SLRMNLDL---LQEHSDEAIWAALEtvqlkALVASLpgQLQyKCADRG-EDLSVGQKQLLCLARALLRKTQILIL 1311
Cdd:COG4555 85 LYDRlTVRENIRYfaeLYGLFDEELKKRIE-----ELIELL--GLE-EFLDRRvGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 1312 DEATAAVDPGTELQMQAMLGSWFAQ-CTVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQLLAQKG 1377
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEgKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
515-753 |
8.57e-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: 110.38 E-value: 8.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGEL---SKVEGFVSIEG-------------A 578
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphgGRISGEVLLDGrdllelsealrgrR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 579 VAYVPQEAWVQ--NTSVVENVCFGQELD-------PPWLERVLEACALQPDVDSFPegiHTsigeqgmnLSGGQKQRLSL 649
Cdd:COG1123 85 IGMVFQDPMTQlnPVTVGDQIAEALENLglsraeaRARVLELLEAVGLERRLDRYP---HQ--------LSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 650 ARAVYRKAAVYLLDDPLAALDAHVGQHVFnQVIGPGGLLQGTTRILVTHALH-ILPQADWIIVLANGAIAEMGSYQELLQ 728
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEIL-DLLRELQRERGTTVLLITHDLGvVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
250 260
....*....|....*....|....*..
gi 1199277034 729 RKGAL--VCLLDQARQPGDRGEGETEP 753
Cdd:COG1123 233 APQALaaVPRLGAARGRAAPAAAAAEP 259
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
515-731 |
8.80e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 111.07 E-value: 8.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAY 581
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiadyseaalrqAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 582 VPQEAWVQNTSVVENVCFGQ-ELDPPWLERVLEACALQPDVDSfPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVY 660
Cdd:PRK11160 419 VSQRVHLFSATLRDNLLLAApNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLL 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 661 LLDDPLAALDAHVGQHVFNqvigpggLL----QGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKG 731
Cdd:PRK11160 498 LLDEPTEGLDAETERQILE-------LLaehaQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQG 565
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
532-719 |
8.82e-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: 8.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------VAYVPQEA----WvqnTSVVENVCF 599
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgpdRGYVFQQDallpW---LTVLDNVAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 600 GQEL----DPPWLERV---LEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAH 672
Cdd:cd03293 97 GLELqgvpKAEARERAeelLELVGLSGFENAYPH-----------QLSGGMRQRVALARALAVDPDVLLLDEPFSALDAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 673 VGQHVFNQVIgpgGLLQ--GTTRILVTH----ALHIlpqADWIIVLAN--GAIAE 719
Cdd:cd03293 166 TREQLQEELL---DIWRetGKTVLLVTHdideAVFL---ADRVVVLSArpGRIVA 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1152-1362 |
1.06e-24 |
|
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: 101.55 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1152 EFRDFGLRYRPelPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISII 1231
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1232 PQdpilfpgslrmnldllqehsdeaiwaaletvqlkalvaslpgqlqykcadrgedLSVGQKQLLCLARALLRKTQILIL 1311
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 1312 DEATAAVDPGTELQMQAMLGSWFAQ-CTVLLIAHRLRSVMD-CARVLVMDKGQ 1362
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
515-731 |
1.17e-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: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSqeSPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG------------AVAYV 582
Cdd:COG4555 2 IEVENLSKKYG--KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 583 PQE-AWVQNTSVVENVCFGQELDPPWLERVLEACALQPDVDSFPEGIHTSIGEqgmnLSGGQKQRLSLARAVYRKAAVYL 661
Cdd:COG4555 80 PDErGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGE----LSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 662 LDDPLAALDAhVGQHVFNQVIgpgGLL--QGTTRILVTHALH-ILPQADWIIVLANGAIAEMGSYQELLQRKG 731
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 ... |
532-715 |
1.33e-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: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGavayvpqeawvqnTSVVENVcfgqeldppwlERV 611
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG-------------KDIKKEP-----------EEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 612 LEACALQPDVDSFPEGIhTsiGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAhVGQHVFNQVIgpGGLL-QG 690
Cdd:cd03230 72 KRRIGYLPEEPSLYENL-T--VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREFWELL--RELKkEG 145
|
170 180
....*....|....*....|....*.
gi 1199277034 691 TTRILVTHALHILPQ-ADWIIVLANG 715
Cdd:cd03230 146 KTILLSSHILEEAERlCDRVAILNNG 171
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
512-732 |
1.91e-24 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 109.72 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 512 KDCITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSaLLGELSKV-EGFVSIEG------------- 577
Cdd:PRK11176 339 KGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIAN-LLTRFYDIdEGEILLDGhdlrdytlaslrn 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 578 AVAYVPQEAWVQNTSVVENVCFGQElDPPWLERVLEACALQPDVD---SFPEGIHTSIGEQGMNLSGGQKQRLSLARAVY 654
Cdd:PRK11176 418 QVALVSQNVHLFNDTIANNIAYART-EQYSREQIEEAARMAYAMDfinKMDNGLDTVIGENGVLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 655 RKAAVYLLDDPLAALDA---HVGQHVFNQvigpggLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKG 731
Cdd:PRK11176 497 RDSPILILDEATSALDTeseRAIQAALDE------LQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNG 570
|
.
gi 1199277034 732 A 732
Cdd:PRK11176 571 V 571
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
522-721 |
2.13e-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: 102.60 E-value: 2.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 522 FAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-----------VAYVPQE-AWVQ 589
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvpperrnIGMVFQDyALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 590 NTSVVENVCFGQEL----DPPWLERVLEACA---LQPDVDSFPEGihtsigeqgmnLSGGQKQRLSLARAVYRKAAVYLL 662
Cdd:cd03259 86 HLTVAENIAFGLKLrgvpKAEIRARVRELLElvgLEGLLNRYPHE-----------LSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 663 DDPLAALDAHVGQHVFNQVIgpgGLL--QGTTRILVTH----ALHIlpqADWIIVLANGAIAEMG 721
Cdd:cd03259 155 DEPLSALDAKLREELREELK---ELQreLGITTIYVTHdqeeALAL---ADRIAVMNEGRIVQVG 213
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
197-464 |
3.16e-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: 3.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 197 FLLGTLSLIISDVFRFTVPKLLSLFLEFI---GDPKPPAWKGYLLAVLMFLSACLQTLFEQQnmYRLKVLQMRLRSAITG 273
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLlpdGDPETQALNVYSLALLLLGLAQFILSFLQS--YLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 274 LVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTESVLYLNGLWLPLVWIVVC-----FVYLWQLlgpsALTAIAVFLSL 348
Cdd:pfam00664 79 KLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGgiivmFYYGWKL----TLVLLAVLPLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 349 LPLNFFISKKRNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLLFSVSLVSFQ-V 427
Cdd:pfam00664 155 ILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQfI 234
|
250 260 270
....*....|....*....|....*....|....*..
gi 1199277034 428 STFLVALVVFAVHTLVAENAMNAEKAFVTLTVLNILN 464
Cdd:pfam00664 235 GYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLF 271
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
532-727 |
3.40e-24 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 103.20 E-value: 3.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAYVPQEAWVQ-NTSVVENV 597
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAYVPQEPPAPfGLTVRELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 598 CFG--------QELDPPWLERVLEACALQpDVDSFpegIHTSIGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAAL 669
Cdd:COG1120 97 ALGryphlglfGRPSAEDREAVEEALERT-GLEHL---ADRPVDE----LSGGERQRVLIARALAQEPPLLLLDEPTSHL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 670 DAHVGQHVFNqvigpggLL------QGTTRILVTHAL-HILPQADWIIVLANGAIAEMGSYQELL 727
Cdd:COG1120 169 DLAHQLEVLE-------LLrrlareRGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
532-728 |
4.09e-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: 102.58 E-value: 4.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA----------------VAYVPQE-AWVQNTSVV 594
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrrMGMLFQSgALFDSLTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 595 ENVCFG----QELDPPWLERV----LEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPL 666
Cdd:cd03261 96 ENVAFPlrehTRLSEEEIREIvlekLEAVGLRGAEDLYPA-----------ELSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 667 AALDAhVGQHVFNQVIgpgGLLQ---GTTRILVTHALH-ILPQADWIIVLANGAIAEMGSYQELLQ 728
Cdd:cd03261 165 AGLDP-IASGVIDDLI---RSLKkelGLTSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
515-733 |
1.05e-23 |
|
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: 101.26 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQEsPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-------------VAY 581
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKditkknlrelrrkVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 582 VPQEAWVQ--NTSVVENVCFG---QELDPPWLER----VLEACALQPDVDSFPegiHTsigeqgmnLSGGQKQRLSLARA 652
Cdd:COG1122 80 VFQNPDDQlfAPTVEEDVAFGpenLGLPREEIRErveeALELVGLEHLADRPP---HE--------LSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 653 VYRKAAVYLLDDPLAALDAHVGQHVFNQVigpGGL-LQGTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELLQRK 730
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELL---KRLnKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
...
gi 1199277034 731 GAL 733
Cdd:COG1122 226 ELL 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
515-721 |
2.30e-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: 98.54 E-value: 2.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG------------AVAYV 582
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvsdlekalssLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 583 PQEAWVQNTSVVENVcfgqeldppwlervleacalqpdvdsfpegihtsigeqGMNLSGGQKQRLSLARAVYRKAAVYLL 662
Cdd:cd03247 81 NQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 663 DDPLAALDAHVGQHVFNQVIgpgGLLQGTTRILVTHALHILPQADWIIVLANGAIAEMG 721
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIF---EVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1151-1373 |
3.18e-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: 100.50 E-value: 3.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELplAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISI 1230
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1231 IPQDPIL-FPGSLR----M-------NLDLLQEHSDEAIWAALETVQLKALvaslpgqlqykcADRG-EDLSVGQKQLLC 1297
Cdd:COG1120 80 VPQEPPApFGLTVRelvaLgryphlgLFGRPSAEDREAVEEALERTGLEHL------------ADRPvDELSGGERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 1298 LARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLL 1373
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErgRTVVMVLHDLNLAARYAdRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
521-717 |
3.48e-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: 99.47 E-value: 3.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 521 TFAWSQESP-PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAYVPQEA 586
Cdd:cd03248 18 TFAYPTRPDtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyehkylhsKVSLVGQEP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 587 WVQNTSVVENVCFGQELDPpwLERVLEAcALQPDVDSF----PEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLL 662
Cdd:cd03248 98 VLFARSLQDNIAYGLQSCS--FECVKEA-AQKAHAHSFiselASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 663 DDPLAALDAHvGQHVFNQVIGPGglLQGTTRILVTHALHILPQADWIIVLANGAI 717
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 ... |
532-717 |
4.07e-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: 97.89 E-value: 4.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAYVPQeawvqntsvvenvc 598
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGkdlaslspkelarKIAYVPQ-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 599 fgqeldppWLERVleacalqpDVDSFpegIHTSIGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDahvgqhVF 678
Cdd:cd03214 81 --------ALELL--------GLAHL---ADRPFNE----LSGGERQRVLLARALAQEPPILLLDEPTSHLD------IA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1199277034 679 NQVIgpggLLQ---------GTTRILVTHAL-HILPQADWIIVLANGAI 717
Cdd:cd03214 132 HQIE----LLEllrrlarerGKTVVMVLHDLnLAARYADRVILLKDGRI 176
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
528-715 |
5.12e-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: 96.93 E-value: 5.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 528 SPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-AVAYVPQEAWVQNTSVVenvcfgqeldpp 606
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGkDIAKLPLEELRRRIGYV------------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 607 wlervleacaLQpdvdsfpegihtsigeqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVIGPgg 686
Cdd:cd00267 79 ----------PQ--------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLREL-- 126
|
170 180 190
....*....|....*....|....*....|
gi 1199277034 687 LLQGTTRILVTHAL-HILPQADWIIVLANG 715
Cdd:cd00267 127 AEEGRTVIIVTHDPeLAELAADRVIVLKDG 156
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
522-717 |
6.10e-23 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 98.35 E-value: 6.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 522 FAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-------------VAYVPQE-AW 587
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKplsampppewrrqVAYVPQEpAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 588 VQNTsVVENVCF-----GQELDPPWLERVLEACALQPDVdsfpegIHTSIGEqgmnLSGGQKQRLSLARAVYRKAAVYLL 662
Cdd:COG4619 86 WGGT-VRDNLPFpfqlrERKFDRERALELLERLGLPPDI------LDKPVER----LSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 663 DDPLAALDAHVGQHVFNqvigpggLLQ------GTTRILVTH-ALHILPQADWIIVLANGAI 717
Cdd:COG4619 155 DEPTSALDPENTRRVEE-------LLReylaeeGRAVLWVSHdPEQIERVADRVLTLEAGRL 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1167-1375 |
6.93e-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: 6.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEaAEGGIWIDGVPIAHVG---LHTLRSRISIIPQDPilFpGSL- 1242
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--F-GSLs 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1243 -RMN--------LDLLQEHSDEA-----IWAALETVQLKAlvaslpgqlqyKCADR--GEdLSVGQKQLLCLARALLRKT 1306
Cdd:COG4172 377 pRMTvgqiiaegLRVHGPGLSAAerrarVAEALEEVGLDP-----------AARHRypHE-FSGGQRQRIAIARALILEP 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 1307 QILILDEATAAVDPGTELQM-------QAMLGswfaqCTVLLIAHRLRSV--MdCARVLVMDKGQVAESGSPAQLLAQ 1375
Cdd:COG4172 445 KLLVLDEPTSALDVSVQAQIldllrdlQREHG-----LAYLFISHDLAVVraL-AHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
532-729 |
8.04e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 101.69 E-value: 8.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGeLSKV-EGFVSIEGA-----------VAYVPQE-AWVQNTSVVENVC 598
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG-LEDPtSGEILIGGRdvtdlppkdrnIAMVFQSyALYPHMTVYENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 599 FG--------QELDppwlERVLEACA---LQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLA 667
Cdd:COG3839 98 FPlklrkvpkAEID----RRVREAAEllgLEDLLDRKPK-----------QLSGGQRQRVALGRALVREPKVFLLDEPLS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 668 ALDAHvgqhvfnqvigpggL----------LQ---GTTRILVTH----ALHIlpqADWIIVLANGAIAEMGSYQELLQR 729
Cdd:COG3839 163 NLDAK--------------LrvemraeikrLHrrlGTTTIYVTHdqveAMTL---ADRIAVMNDGRIQQVGTPEELYDR 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
532-719 |
2.23e-22 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 97.42 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSaLLGELSKV-EGFVSIEG-----------------AVAYVPQEA-WVQNTS 592
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVLIDGqdisslserelarlrrrHIGFVFQFFnLLPELT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 593 VVENVCFGQEL-------DPPWLERVLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDP 665
Cdd:COG1136 103 ALENVALPLLLagvsrkeRRERARELLERVGLGDRLDHRPS-----------QLSGGQQQRVAIARALVNRPKLILADEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 666 LAALDAHVGQHVFNqvigpggLLQ------GTTRILVTHALHILPQADWIIVLANGAIAE 719
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 ... |
1151-1375 |
2.50e-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: 97.27 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRY--RPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHV---GLHTLR 1225
Cdd:cd03258 2 IELKNVSKVFgdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1226 SRISIIPQ-----------DPILFPgslrmnLDLL---QEHSDEAIWAALETVQLKALVASLPGQLqykcadrgedlSVG 1291
Cdd:cd03258 82 RRIGMIFQhfnllssrtvfENVALP------LEIAgvpKAEIEERVLELLELVGLEDKADAYPAQL-----------SGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1292 QKQLLCLARALLRKTQILILDEATAAVDPGT-----EL--QMQAMLGswfaqCTVLLIAHRLRSVMD-CARVLVMDKGQV 1363
Cdd:cd03258 145 QKQRVGIARALANNPKVLLCDEATSALDPETtqsilALlrDINRELG-----LTIVLITHEMEVVKRiCDRVAVMEKGEV 219
|
250
....*....|..
gi 1199277034 1364 AESGSPAQLLAQ 1375
Cdd:cd03258 220 VEEGTVEEVFAN 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1167-1362 |
3.65e-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: 94.95 E-value: 3.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHT--LRSRISIIPQDPILFPgslRM 1244
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIGMVFQDFALFP---HL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1245 NldllqehsdeaiwaALETVQLKalvaslpgqlqykcadrgedLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTEL 1324
Cdd:cd03229 92 T--------------VLENIALG--------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1199277034 1325 QMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQ 1362
Cdd:cd03229 138 EVRALLKSLQAQlgITVVLVTHDLDEAARLAdRVVVLRDGK 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1151-1372 |
9.74e-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: 95.33 E-value: 9.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELplAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEA-----AEGGIWIDGVPIAHVGLH--T 1223
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1224 LRSRISIIPQDPILFPGSLRMNLDL--------LQEHSDEAIWAALETVQLKALVAslpgqlqykcaDR--GEDLSVGQK 1293
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYglrlhgikLKEELDERVEEALRKAALWDEVK-----------DRlhALGLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1294 QLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQL 1372
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVAdRTAFLLNGRLVEFGPTEQI 227
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1091-1345 |
1.07e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 101.04 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1091 SVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDYAWTPKEAPwRLPTCAAQPPWPQGGQIEFRDFGLRYRPELPLaVQG 1170
Cdd:COG4178 304 AASAFGQVQGALSWFVDNYQSLAEWRATVDRLAGFEEALEAAD-ALPEAASRIETSEDGALALEDLTLRTPDGRPL-LED 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1171 VSFKIHAGEKVGIVGRTGAGKSSLasglLRlqeaAEGGIWidgvPIA--HVGLHTLrSRISIIPQDPILFPGSLRMNL-- 1246
Cdd:COG4178 382 LSLSLKPGERLLITGPSGSGKSTL----LR----AIAGLW----PYGsgRIARPAG-ARVLFLPQRPYLPLGTLREALly 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1247 -DLLQEHSDEAIWAALETVQLKALVASLpgqlqykcaDRGED----LSVGQKQLLCLARALLRKTQILILDEATAAVDPG 1321
Cdd:COG4178 449 pATAEAFSDAELREALEAVGLGHLAERL---------DEEADwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
250 260
....*....|....*....|....
gi 1199277034 1322 TELQMQAMLGSWFAQCTVLLIAHR 1345
Cdd:COG4178 520 NEAALYQLLREELPGTTVISVGHR 543
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
532-721 |
1.51e-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: 94.63 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYVPQE----AWV-QN------TSVVENVCF 599
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdVTDLPPKdrdiAMVfQNyalyphMTVYDNIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 600 G--------QELDppwlERVLEACALQpdvdsfpeGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDA 671
Cdd:cd03301 96 GlklrkvpkDEID----ERVREVAELL--------QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199277034 672 HVGQHVFNQVIGpgglLQ---GTTRILVTH----ALHIlpqADWIIVLANGAIAEMG 721
Cdd:cd03301 164 KLRVQMRAELKR----LQqrlGTTTIYVTHdqveAMTM---ADRIAVMNDGQIQQIG 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
532-698 |
1.81e-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: 94.08 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG------------AVAYV-PQEAWVQNTSVVENVC 598
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYLgHADGLKPELTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 599 F-----GQELDPPWLERVLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHv 673
Cdd:COG4133 98 FwaalyGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA- 165
|
170 180
....*....|....*....|....*....
gi 1199277034 674 GQHVFNQVI----GPGGLLqgttrILVTH 698
Cdd:COG4133 166 GVALLAELIaahlARGGAV-----LLTTH 189
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
532-729 |
2.59e-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: 97.09 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-----------VAYVPQE-AWVQNTSVVENVCF 599
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppekrnVGMVFQDyALFPHLTVAENVAF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 600 G--------QELDppwlERVLEACALqpdvdsfpegihTSIGEQG----MNLSGGQKQRLSLARAVYRKAAVYLLDDPLA 667
Cdd:COG3842 101 GlrmrgvpkAEIR----ARVAELLEL------------VGLEGLAdrypHQLSGGQQQRVALARALAPEPRVLLLDEPLS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 668 ALDAHVGQHVFNQVIgpgGLLQ--GTTRILVTH----ALHIlpqADWIIVLANGAIAEMGSYQELLQR 729
Cdd:COG3842 165 ALDAKLREEMREELR---RLQRelGITFIYVTHdqeeALAL---ADRIAVMNDGRIEQVGTPEEIYER 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1151-1362 |
2.97e-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: 2.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRP---ELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGvpiahvglhtlrsR 1227
Cdd:cd03250 1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1228 ISIIPQDPILFPGSLRMNLDLLQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQ 1307
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199277034 1308 ILILDEATAAVDPGTELQM--QAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQ 1362
Cdd:cd03250 148 IYLLDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1152-1367 |
3.20e-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: 92.50 E-value: 3.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1152 EFRDFGLRYRPelPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISII 1231
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1232 PQdpilfpgslrmnldllqehsdeaiwaALETVQLKALvaslpgqlqykcADRG-EDLSVGQKQLLCLARALLRKTQILI 1310
Cdd:cd03214 79 PQ--------------------------ALELLGLAHL------------ADRPfNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1311 LDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESG 1367
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARErgKTVVMVLHDLNLAARYAdRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1151-1375 |
6.57e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 94.31 E-value: 6.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLA---SGLLRLQEaaeGGIWIDGVPIAHVGLHTLRSR 1227
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAkllNGLLLPEA---GTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1228 ISIIPQDP------------ILFpgSLRmNLDLLQEHSDEAIWAALETVQLKALVASLPGQLqykcadrgedlSVGQKQL 1295
Cdd:PRK13635 83 VGMVFQNPdnqfvgatvqddVAF--GLE-NIGVPREEMVERVDQALRQVGMEDFLNREPHRL-----------SGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1296 LCLARALLRKTQILILDEATAAVDP-------GT--ELQMQAMLgswfaqcTVLLIAHRLRSVMDCARVLVMDKGQVAES 1366
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPrgrrevlETvrQLKEQKGI-------TVLSITHDLDEAAQADRVIVMNKGEILEE 221
|
....*....
gi 1199277034 1367 GSPAQLLAQ 1375
Cdd:PRK13635 222 GTPEEIFKS 230
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1167-1375 |
6.58e-21 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 95.92 E-value: 6.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHV---GLHTLRSRISIIPQ---------- 1233
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALserELRAARRKIGMIFQhfnllssrtv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1234 -DPILFPgsLRmnldlLQEHSDEAIWAA----LETVQLKALVASLPGQLqykcadrgedlSVGQKQllclarallrktQI 1308
Cdd:COG1135 100 aENVALP--LE-----IAGVPKAEIRKRvaelLELVGLSDKADAYPSQL-----------SGGQKQrvgiaralannpKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 1309 LILDEATAAVDPGT-----EL--QMQAMLGSwfaqcTVLLIAHRlrsvMD-----CARVLVMDKGQVAESGSPAQLLAQ 1375
Cdd:COG1135 162 LLCDEATSALDPETtrsilDLlkDINRELGL-----TIVLITHE----MDvvrriCDRVAVLENGRIVEQGPVLDVFAN 231
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
532-726 |
7.52e-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: 93.01 E-value: 7.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSAL-----LGELSKVEGFVSIEGA---------------VAYVPQEAWVQNT 591
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKdiydldvdvlelrrrVGMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 592 SVVENVCFGqeldpPWL-------------ERVLEACALQPDVDSFPEGIHtsigeqgmnLSGGQKQRLSLARAVYRKAA 658
Cdd:cd03260 96 SIYDNVAYG-----LRLhgiklkeeldervEEALRKAALWDEVKDRLHALG---------LSGGQQQRLCLARALANEPE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 659 VYLLDDPLAALDAhVGQHVFNQVIgpGGLLQGTTRILVTHALHilpQA----DWIIVLANGAIAEMGSYQEL 726
Cdd:cd03260 162 VLLLDEPTSALDP-ISTAKIEELI--AELKKEYTIVIVTHNMQ---QAarvaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1151-1374 |
8.09e-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: 92.95 E-value: 8.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELPLavQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG---LHTLRSR 1227
Cdd:cd03261 1 IELRGLTKSFGGRTVL--KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1228 ISIIPQDPILF-----------PgsLRMNLDLLQEHSDEAIWAALETVQLKALVASLPGQlqykcadrgedLSVGQKQLL 1296
Cdd:cd03261 79 MGMLFQSGALFdsltvfenvafP--LREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAE-----------LSGGMKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1297 CLARALLRKTQILILDEATAAVDPGTE-------LQMQAMLGswfaqCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGS 1368
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDPIASgviddliRSLKKELG-----LTSIMVTHDLDTAFAIAdRIAVLYDGKIVAEGT 220
|
....*.
gi 1199277034 1369 PAQLLA 1374
Cdd:cd03261 221 PEELRA 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1151-1376 |
8.41e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 93.90 E-value: 8.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISI 1230
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1231 IPQDP------------ILFpgSLRmNLDLLQEHSDEAIWAALETVQLKALVASLPgqlqykcadrgEDLSVGQKQLLCL 1298
Cdd:PRK13632 88 IFQNPdnqfigatveddIAF--GLE-NKKVPPKKMKDIIDDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1299 ARALLRKTQILILDEATAAVDPG---------TELQMQamlgswfAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSP 1369
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKgkreikkimVDLRKT-------RKKTLISITHDMDEAILADKVIVFSEGKLIAQGKP 226
|
....*..
gi 1199277034 1370 AQLLAQK 1376
Cdd:PRK13632 227 KEILNNK 233
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
532-717 |
8.82e-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: 92.55 E-value: 8.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSaLLGELSKV-EGFVSIEGA-----------------VAYVPQE-AWVQNTS 592
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVRVDGTdisklsekelaafrrrhIGFVFQSfNLLPDLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 593 VVENVCFGQEL----DPPWLERVLEACALqpdVDsFPEGIHTSIGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAA 668
Cdd:cd03255 99 ALENVELPLLLagvpKKERRERAEELLER---VG-LGDRLNHYPSE----LSGGQQQRVAIARALANDPKIILADEPTGN 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 669 LDAHVGQHVFNqvigpggLLQ------GTTRILVTHALHILPQADWIIVLANGAI 717
Cdd:cd03255 171 LDSETGKEVME-------LLRelnkeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1152-1364 |
9.12e-21 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 92.21 E-value: 9.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1152 EFRDFGLRYRPELplAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVglhtlRSRISII 1231
Cdd:cd03235 1 EVEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1232 PQDPIL---FPGSLR----------MNLDLLQEHSD-EAIWAALETVQLKALvaslpgqlqykcADR--GEdLSVGQKQL 1295
Cdd:cd03235 74 PQRRSIdrdFPISVRdvvlmglyghKGLFRRLSKADkAKVDEALERVGLSEL------------ADRqiGE-LSGGQQQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 1296 LCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ-CTVLLIAHRLRSVMD-CARVLVMDKGQVA 1364
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEyFDRVLLLNRTVVA 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
519-729 |
1.14e-20 |
|
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: 92.94 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 519 SATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAYVPQE 585
Cdd:COG1124 8 SVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGrpvtrrrrkafrrRVQMVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 586 AWvqnTSV-----VENV------CFGQELDPPWLERVLEACALQPDV-DSFPegiHTsigeqgmnLSGGQKQRLSLARAV 653
Cdd:COG1124 88 PY---ASLhprhtVDRIlaeplrIHGLPDREERIAELLEQVGLPPSFlDRYP---HQ--------LSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 654 YRKAAVYLLDDPLAALDAHVGQHVFNqvigpggLLQ------GTTRILVTH----ALHIlpqADWIIVLANGAIAEMGSY 723
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILN-------LLKdlreerGLTYLFVSHdlavVAHL---CDRVAVMQNGRIVEELTV 223
|
....*.
gi 1199277034 724 QELLQR 729
Cdd:COG1124 224 ADLLAG 229
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1151-1365 |
1.44e-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: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELP--LAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGlhtlrSRI 1228
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1229 SIIPQDPILFP-GSLRMNLDL---LQEHSD----EAIWAALETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLAR 1300
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALgleLQGVPKaearERAEELLELVGLSGFENAYPHQL-----------SGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1301 ALLRKTQILILDEATAAVDPGTELQMQA-MLGSWFAQC-TVLLIAHRLR-SVMDCARVLVMDK--GQVAE 1365
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEeLLDIWRETGkTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
530-712 |
2.33e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.37 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 530 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--VAYVPQEAWVQNT---SVVENVCFGQELD 604
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGarVAYVPQRSEVPDSlplTVRDLVAMGRWAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 605 PPWLER-------VLEACALQPDVDSFPegiHTSIGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHV 677
Cdd:NF040873 86 RGLWRRltrddraAVDDALERVGLADLA---GRQLGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1199277034 678 FnqvigpgGLL-----QGTTRILVTHALHILPQADWIIVL 712
Cdd:NF040873 159 I-------ALLaeehaRGATVVVVTHDLELVRRADPCVLL 191
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1168-1375 |
2.59e-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: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1168 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLD 1247
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1248 LLQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQ 1327
Cdd:COG4618 428 RFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALA 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1199277034 1328 AMLGSWFAQ-CTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQ 1375
Cdd:COG4618 508 AAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1151-1369 |
3.04e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 92.12 E-value: 3.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISI 1230
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1231 IPQDPI-LFPGSLrMNLDL---LQEHS------DEAIWAALETVQLKALVASLPgqlqykcadrgEDLSVGQKQLLCLAR 1300
Cdd:PRK13648 88 VFQNPDnQFVGSI-VKYDVafgLENHAvpydemHRRVSEALKQVDMLERADYEP-----------NALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 1301 ALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCARVLVMDKGQVAESGSP 1369
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhnITIISITHDLSEAMEADHVIVMNKGTVYKEGTP 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1162-1363 |
3.91e-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: 3.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1162 PELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAhvgLHTLRSRISIIPQDP--ILFP 1239
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGYVMQDVdyQLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1240 GS----LRMNLDLLQEhSDEAIWAALETVQLKALVASLPgqlqykcadrgEDLSVGQKQLLCLARALLRKTQILILDEAT 1315
Cdd:cd03226 87 DSvreeLLLGLKELDA-GNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 1316 AAVDPGtelQMQAmLGSWFAQC-----TVLLIAHRLRSVMDCA-RVLVMDKGQV 1363
Cdd:cd03226 155 SGLDYK---NMER-VGELIRELaaqgkAVIVITHDYEFLAKVCdRVLLLANGAI 204
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1167-1372 |
4.23e-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: 4.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG---LHTLRSRISIIPQDPIlfpGSL- 1242
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDPY---ASLn 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1243 -RMNL-DLLQE----HS-------DEAIWAALETVQLKALVAS-LPGQlqykcadrgedLSVGQKQLLCLARALLRKTQI 1308
Cdd:COG4608 110 pRMTVgDIIAEplriHGlaskaerRERVAELLELVGLRPEHADrYPHE-----------FSGGQRQRIGIARALALNPKL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 1309 LILDEATAAVDPGTELQ-------MQAMLGswfaqCTVLLIAHRL---RSVMDcaRVLVMDKGQVAESGSPAQL 1372
Cdd:COG4608 179 IVCDEPVSALDVSIQAQvlnlledLQDELG-----LTYLFISHDLsvvRHISD--RVAVMYLGKIVEIAPRDEL 245
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1167-1375 |
4.24e-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: 92.81 E-value: 4.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEA---AEGGIWIDGVPIAHVGLHTLR----SRISIIPQDPIlfp 1239
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRkirgREIQMIFQDPM--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1240 GSL--RMNL-----DLLQEH---SDEAIWA----ALETVQL---KALVASLPGQlqykcadrgedLSVGQKQLLCLARAL 1302
Cdd:COG0444 97 TSLnpVMTVgdqiaEPLRIHgglSKAEAREraieLLERVGLpdpERRLDRYPHE-----------LSGGMRQRVMIARAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1303 LRKTQILILDEATAAVDPGTELQ-------MQAMLGswfaqCTVLLIAHRLRSV--MdCARVLVMDKGQVAESGSPAQLL 1373
Cdd:COG0444 166 ALEPKLLIADEPTTALDVTIQAQilnllkdLQRELG-----LAILFITHDLGVVaeI-ADRVAVMYAGRIVEEGPVEELF 239
|
..
gi 1199277034 1374 AQ 1375
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 ... |
1167-1374 |
8.47e-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: 89.80 E-value: 8.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTlRSR--ISIIPQDPILFPG-SLR 1243
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARagIGYVPEGRRIFPElTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1244 MNLDL-LQEHSDEAIWAALETVqlkalVASLPgQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGT 1322
Cdd:cd03224 94 ENLLLgAYARRRAKRKARLERV-----YELFP-RLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 1323 ELQMQAMLGSWFAQ-CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLA 1374
Cdd:cd03224 168 VEEIFEAIRELRDEgVTILLVEQNARFALEIAdRAYVLERGRVVLEGTAAELLA 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
534-729 |
1.63e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 89.04 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 534 RINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-----------VAYVPQEawvqNT-----SVVENV 597
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltalppaerpVSMLFQE----NNlfphlTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 598 CFGQE----LDPPWLERVLEACA---LQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 670
Cdd:COG3840 93 GLGLRpglkLTAEQRAQVEQALErvgLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 671 -----------AHVGQHvfnqvigpggllQGTTRILVTH----ALHIlpqADWIIVLANGAIAEMGSYQELLQR 729
Cdd:COG3840 162 palrqemldlvDELCRE------------RGLTVLMVTHdpedAARI---ADRVLLVADGRIAADGPTAALLDG 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1160-1371 |
1.72e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 90.49 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1160 YRPELPL---AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIA--HVGLHTLRSRISIIPQD 1234
Cdd:PRK13637 12 YMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1235 P------------ILFPGSlrmNLDLLQEHSDEAIWAALETVQLKALVaslpgqlqYKcaDRGE-DLSVGQKQLLCLARA 1301
Cdd:PRK13637 92 PeyqlfeetiekdIAFGPI---NLGLSEEEIENRVKRAMNIVGLDYED--------YK--DKSPfELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 1302 LLRKTQILILDEATAAVDPGT--EL--QMQAMLGSWfaQCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQ 1371
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGrdEIlnKIKELHKEY--NMTIILVSHSMEDVAKLAdRIIVMNKGKCELQGTPRE 231
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
530-726 |
1.77e-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: 89.32 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 530 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-----------AVAYVPQE-AWVQNTSVVENV 597
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatdvpvqerNVGFVFQHyALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 598 CFGQEL-----DPPWLE------RVLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPL 666
Cdd:cd03296 96 AFGLRVkprseRPPEAEirakvhELLKLVQLDWLADRYPA-----------QLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 667 AALDAHVGQH-------VFNQVigpggllqGTTRILVTH----ALHIlpqADWIIVLANGAIAEMGSYQEL 726
Cdd:cd03296 165 GALDAKVRKElrrwlrrLHDEL--------HVTTVFVTHdqeeALEV---ADRVVVMNKGRIEQVGTPDEV 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
529-719 |
3.44e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 87.80 E-value: 3.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 529 PPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG---------AVAY-------VPQEAW-VQNT 591
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlkrrEIPYlrrrigvVFQDFRlLPDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 592 SVVENVCFGQELD-----------PPWLERV-LEACAlqpdvDSFPegihtsigeqgMNLSGGQKQRLSLARAVYRKAAV 659
Cdd:COG2884 95 TVYENVALPLRVTgksrkeirrrvREVLDLVgLSDKA-----KALP-----------HELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199277034 660 YLLDDPLAALDAHVGQHV------FNQVigpggllqGTTRILVTHALHILPQADW-IIVLANGAIAE 719
Cdd:COG2884 159 LLADEPTGNLDPETSWEImelleeINRR--------GTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1167-1363 |
3.62e-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: 3.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGlHTLRSRISIIPQDPILFPG-SLRMN 1245
Cdd:cd03230 15 ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGYLPEEPSLYENlTVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1246 LDLlqehsdeaiwaaletvqlkalvaslpgqlqykcadrgedlSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQ 1325
Cdd:cd03230 94 LKL----------------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGLDPESRRE 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1199277034 1326 MQAMLGSWFAQ-CTVLLIAHRLRSVMD-CARVLVMDKGQV 1363
Cdd:cd03230 134 FWELLRELKKEgKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1167-1375 |
3.78e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 88.74 E-value: 3.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHvGLHTLRSR-ISIIPQDP---------- 1235
Cdd:COG4167 28 AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY-GDYKYRCKhIRMIFQDPntslnprlni 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1236 --IL-FPgsLRMNLDLLQEHSDEAIWAALETVQLkalvasLPGQLQYKCadrgEDLSVGQKQLLCLARALLRKTQILILD 1312
Cdd:COG4167 107 gqILeEP--LRLNTDLTAEEREERIFATLRLVGL------LPEHANFYP----HMLSSGQKQRVALARALILQPKIIIAD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 1313 EATAAVDPGTELQM-------QAMLGSWFaqctvLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQ 1375
Cdd:COG4167 175 EALAALDMSVRSQIinlmlelQEKLGISY-----IYVSQHLGIVKHISdKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
530-728 |
4.41e-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: 87.49 E-value: 4.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 530 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------------VAYVPQEAWV-QNTSVV 594
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEGRRIfPELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 595 ENV----CFGQELDPPW-LERVLEAcalqpdvdsFPEgIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAAL 669
Cdd:cd03224 94 ENLllgaYARRRAKRKArLERVYEL---------FPR-LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 670 DAHVGQHVFNQVIGpgglL--QGTTRILV----THALHIlpqADWIIVLANGAIAEMGSYQELLQ 728
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 ... |
1151-1367 |
4.56e-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: 87.19 E-value: 4.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELplAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHtlRSRISI 1230
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1231 IPQDPILFP----------GsLRMNLDLLQEHSDEAIWAaLETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLAR 1300
Cdd:cd03259 77 VFQDYALFPhltvaeniafG-LKLRGVPKAEIRARVREL-LELVGLEGLLNRYPHEL-----------SGGQQQRVALAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1301 ALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESG 1367
Cdd:cd03259 144 ALAREPSLLLLDEPLSALDAKLREELREELKELQRElgITTIYVTHDQEEALALAdRIAVMNEGRIVQVG 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1151-1374 |
5.05e-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: 88.13 E-value: 5.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYrPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISI 1230
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1231 IPQDPILFPG-SLRMNLDL---LQEHSDEAIWA-ALEtvqLKALVASLPGQLqykcADRGED-LSVGQKQLLCLARALLR 1304
Cdd:cd03295 80 VIQQIGLFPHmTVEENIALvpkLLKWPKEKIRErADE---LLALVGLDPAEF----ADRYPHeLSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1305 KTQILILDEATAAVDPGT--ELQ-----MQAMLGSwfaqcTVLLIAHRlrsvMDCA-----RVLVMDKGQVAESGSPAQL 1372
Cdd:cd03295 153 DPPLLLMDEPFGALDPITrdQLQeefkrLQQELGK-----TIVFVTHD----IDEAfrladRIAIMKNGEIVQVGTPDEI 223
|
..
gi 1199277034 1373 LA 1374
Cdd:cd03295 224 LR 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1150-1359 |
9.43e-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: 85.99 E-value: 9.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1150 QIEFRDFGLRYRPELPLAvqGVSFKIHAGEKVGIVGRTGAGKSSLasglLR----LQEAAEGGIWIDGVPIAHVGLHtLR 1225
Cdd:COG4133 2 MLEAENLSCRRGERLLFS--GLSFTLAAGEALALTGPNGSGKTTL----LRilagLLPPSAGEVLWNGEPIRDARED-YR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1226 SRISIIPQDPILFPG-SLRMNLDLLQ-----EHSDEAIWAALETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLA 1299
Cdd:COG4133 75 RRLAYLGHADGLKPElTVRENLRFWAalyglRADREAIDEALEAVGLAGLADLPVRQL-----------SAGQKRRVALA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 1300 RALLRKTQILILDEATAAVDPgtelQMQAMLGSWFAQ-----CTVLLIAHRLRSVmDCARVLVMD 1359
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDA----AGVALLAELIAAhlargGAVLLTTHQPLEL-AAARVLDLG 203
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
532-725 |
1.06e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 89.62 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYVPQEAWVQNT-----------SVVENVCF 599
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdITHVPAENRHVNTvfqsyalfphmTVFENVAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 600 G--------QELDPpwleRVLEACA---LQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLAA 668
Cdd:PRK09452 110 GlrmqktpaAEITP----RVMEALRmvqLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 669 LDAHVGQHVFNQVIGpgglLQ---GTTRILVTH----ALHIlpqADWIIVLANGAIAEMGSYQE 725
Cdd:PRK09452 175 LDYKLRKQMQNELKA----LQrklGITFVFVTHdqeeALTM---SDRIVVMRDGRIEQDGTPRE 231
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
527-745 |
1.08e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 92.73 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 527 ESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSAL--LGELSKVE-----------GFVSIEGAVAYVPQEAWVQNTSV 593
Cdd:PLN03232 1247 GLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALfrIVELEKGRimiddcdvakfGLTDLRRVLSIIPQSPVLFSGTV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 594 VENVCFGQELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHV 673
Cdd:PLN03232 1327 RFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT 1406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 674 GqhvfnqvigpgGLLQGTTR--------ILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGALVCLLDQARQPGD 745
Cdd:PLN03232 1407 D-----------SLIQRTIReefksctmLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPAN 1475
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
532-729 |
1.39e-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: 91.12 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG----------------AVAYVPQEAWVQ---NTS 592
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkdltklsrrslrelrrRVQMVFQDPYSSlnpRMT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 593 VVENVCFG----QELDPPWLER----VLEACALQPDV-DSFPegiHTsigeqgmnLSGGQKQRLSLARAVYRKAAVYLLD 663
Cdd:COG1123 361 VGDIIAEPlrlhGLLSRAERRErvaeLLERVGLPPDLaDRYP---HE--------LSGGQRQRVAIARALALEPKLLILD 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 664 DPLAALDAHVGQHVFNqvigpggLLQ------GTTRILVTH----ALHIlpqADWIIVLANGAIAEMGSYQELLQR 729
Cdd:COG1123 430 EPTSALDVSVQAQILN-------LLRdlqrelGLTYLFISHdlavVRYI---ADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1167-1374 |
1.64e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.92 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQeAAEGGIWIDGVPIAHVG---LHTLRSRISIIPQDPilfPGSLR 1243
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP---NSSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1244 MNLDLLQ---------------EHSDEAIWAALETVQLKAlvaslpgqlqykcADRGE---DLSVGQKQLLCLARALLRK 1305
Cdd:PRK15134 377 PRLNVLQiieeglrvhqptlsaAQREQQVIAVMEEVGLDP-------------ETRHRypaEFSGGQRQRIAIARALILK 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 1306 TQILILDEATAAVDPGTELQMQAMLGSWFA--QCTVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQLLA 1374
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQILALLKSLQQkhQLAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
532-728 |
1.67e-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: 86.19 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYVPQEAWV----------QN----TS--VV 594
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQdITGLSEKELYelrrrigmlfQGgalfDSltVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 595 ENVCFG----QELDPPWLER----VLEACALQPDVDSFPegihtsiGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPL 666
Cdd:COG1127 101 ENVAFPlrehTDLSEAEIRElvleKLELVGLPGAADKMP-------SE----LSGGMRKRVALARALALDPEILLYDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 667 AALDAhVGQHVFNQVIgpgglLQ-----GTTRILVTHALH-ILPQADWIIVLANGAIAEMGSYQELLQ 728
Cdd:COG1127 170 AGLDP-ITSAVIDELI-----RElrdelGLTSVVVTHDLDsAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
901-1122 |
2.84e-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: 87.55 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 901 RASRLLFQRLLWDVVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPL 980
Cdd:cd18600 100 TVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVVSILQPYIFLATVPV 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 981 FLLYAGFQSLYVVSSCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAAN 1060
Cdd:cd18600 180 IIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMR 259
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 1061 VELLGNGLVFAAATCAVLSKAHlSAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERM 1122
Cdd:cd18600 260 IEMIFVIFFTAVTFISIGTTGD-GEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRI 320
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
532-728 |
4.18e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 85.55 E-value: 4.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGavayVPQEAW----------V--QNTSV-----V 594
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNG----RPLAAWspwelarrraVlpQHSSLafpftV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 595 ENV--------CFGQELDPPWLERVLEACALQPDVD-SFPEgihtsigeqgmnLSGGQKQRLSLARA-------VYRKAA 658
Cdd:COG4559 93 EEVvalgraphGSSAAQDRQIVREALALVGLAHLAGrSYQT------------LSGGEQQRVQLARVlaqlwepVDGGPR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199277034 659 VYLLDDPLAALD-AHVgQHVFNqvigpggLL-----QGTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELLQ 728
Cdd:COG4559 161 WLFLDEPTSALDlAHQ-HAVLR-------LArqlarRGGGVVAVLHDLNLAAQyADRILLLHQGRLVAQGTPEEVLT 229
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
532-715 |
4.50e-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: 83.39 E-value: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGavayvpqeawvqntsvvENVCFGQELDPPWLERV 611
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDG-----------------EDLTDLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 612 leACALQpDVDSFPegiHTSIGEQ-GMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVfnqvigpGGLLQ- 689
Cdd:cd03229 79 --GMVFQ-DFALFP---HLTVLENiALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREV-------RALLKs 145
|
170 180 190
....*....|....*....|....*....|..
gi 1199277034 690 -----GTTRILVTHALH-ILPQADWIIVLANG 715
Cdd:cd03229 146 lqaqlGITVVLVTHDLDeAARLADRVVVLRDG 177
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
530-699 |
4.85e-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: 4.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 530 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG---------AVAYVPQEAWV--------QNTS 592
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgrAIPYLRRKIGVvfqdfrllPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 593 VVENVCFGQEL--DPP--WLERV---LEACALQPDVDSFPEGihtsigeqgmnLSGGQKQRLSLARAVYRKAAVYLLDDP 665
Cdd:cd03292 95 VYENVAFALEVtgVPPreIRKRVpaaLELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 1199277034 666 LAALDAHVGQHVFNqvigpggLLQ-----GTTRILVTHA 699
Cdd:cd03292 164 TGNLDPDTTWEIMN-------LLKkinkaGTTVVVATHA 195
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1172-1375 |
5.15e-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: 5.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1172 SFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTlrsR-ISIIPQDPILFPG-SLRMNLDL- 1248
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE---RpVSMLFQENNLFPHlTVAQNIGLg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1249 ------LQEHSDEAIWAALETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLARALLRKTQILILDEATAAVDPGT 1322
Cdd:COG3840 96 lrpglkLTAEQRAQVEQALERVGLAGLLDRLPGQL-----------SGGQRQRVALARCLVRKRPILLLDEPFSALDPAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 1323 ELQMQAMLGSWFA--QCTVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQLLAQ 1375
Cdd:COG3840 165 RQEMLDLVDELCRerGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1151-1375 |
6.80e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 85.55 E-value: 6.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELP-LAVQGVSFKIHAGEKVGIVGRTGAGKSS---LASGLLrlqEAAEGGIWIDGVPIAHVGLHTLRS 1226
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLL---EAESGQIIIDGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1227 RISIIPQDPI-LFPGSL------------RMNLDLLQEHSDEaiwaALETVQLKALVASLPGQlqykcadrgedLSVGQK 1293
Cdd:PRK13650 82 KIGMVFQNPDnQFVGATveddvafglenkGIPHEEMKERVNE----ALELVGMQDFKEREPAR-----------LSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1294 QLLCLARALLRKTQILILDEATAAVDPGTELQM----QAMLGSWfaQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSP 1369
Cdd:PRK13650 147 QRVAIAGAVAMRPKIIILDEATSMLDPEGRLELiktiKGIRDDY--QMTVISITHDLDEVALSDRVLVMKNGQVESTSTP 224
|
....*.
gi 1199277034 1370 AQLLAQ 1375
Cdd:PRK13650 225 RELFSR 230
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
532-719 |
8.53e-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: 84.02 E-value: 8.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-----------------VAYVPQ-EAWVQNTSV 593
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQdlfaldedararlrarhVGFVFQsFQLLPTLTA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 594 VENV-----------CFGQELDppWLERVleacALQPDVDSFPEGihtsigeqgmnLSGGQKQRLSLARAVYRKAAVYLL 662
Cdd:COG4181 108 LENVmlplelagrrdARARARA--LLERV----GLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 663 DDPLAALDAHVGQHVFnqvigpgGLL------QGTTRILVTHALHILPQADWIIVLANGAIAE 719
Cdd:COG4181 171 DEPTGNLDAATGEQII-------DLLfelnreRGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1151-1372 |
1.09e-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: 83.32 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIaHVGLHTLRSRISI 1230
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1231 IPQDPILFPGslrMN-LDLLQehsdeaIWAAL---ETVQLKALVASLPGQLQ-YKCADR-GEDLSVGQKQLLCLARALLR 1304
Cdd:cd03263 80 CPQFDALFDE---LTvREHLR------FYARLkglPKSEIKEEVELLLRVLGlTDKANKrARTLSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 1305 KTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRlrsvMD-----CARVLVMDKGQVAESGSPAQL 1372
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHS----MDeaealCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1167-1374 |
1.13e-17 |
|
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: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSL---ASGLLRlqeAAEGGIWIDGVPIAHVGLHtLRSRISIIP--QDPILFPG- 1240
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLfnlISGFLR---PTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFPEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1241 SLRMNLDL-LQEHSDEAIWAA----------------LETVQLKALVASLPGqlqykcadrgeDLSVGQKQLLCLARALL 1303
Cdd:cd03219 91 TVLENVMVaAQARTGSGLLLArarreereareraeelLERVGLADLADRPAG-----------ELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 1304 RKTQILILDEATAAVDPGTELQMQAMLGSWFAQ-CTVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQLLA 1374
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERgITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1149-1379 |
1.40e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 89.32 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1149 GQIEFRDFGLRY--RPELPLaVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLR-------------------------- 1200
Cdd:PTZ00265 1164 GKIEIMDVNFRYisRPNVPI-YKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfknehtndmtneqdy 1242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1201 ---------LQEAAE-------------------GGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLDLLQEH 1252
Cdd:PTZ00265 1243 qgdeeqnvgMKNVNEfsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKED 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1253 SD-EAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLG 1331
Cdd:PTZ00265 1323 ATrEDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1402
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 1332 SW--FAQCTVLLIAHRLRSVMDCARVLVMDKGQ-----VAESGSPAQLL-AQKGLF 1379
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 ... |
515-722 |
1.54e-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: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYVPQEAWVQNTSV 593
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 594 VENvcfgqelDPpwlerVLEACALQPDVDSFPE----GIHT--SIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLA 667
Cdd:cd03369 87 IPQ-------DP-----TLFSGTIRSNLDPFDEysdeEIYGalRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 668 ALDAHVgQHVFNQVIGPggLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGS 722
Cdd:cd03369 155 SIDYAT-DALIQKTIRE--EFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1151-1368 |
1.93e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 85.62 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYR---PELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHV---GLHTL 1224
Cdd:PRK11153 2 IELKNISKVFPqggRTIH-ALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1225 RSRISIIPQ-----------DPILFPgsLRmnldlLQEHSDEAIWAA----LETVQLKALVASLPGQLqykcadrgedlS 1289
Cdd:PRK11153 81 RRQIGMIFQhfnllssrtvfDNVALP--LE-----LAGTPKAEIKARvtelLELVGLSDKADRYPAQL-----------S 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1290 VGQKQLLCLARALLRKTQILILDEATAAVDPGT-----EL--QMQAMLGswfaqCTVLLIAHRlrsvMD-----CARVLV 1357
Cdd:PRK11153 143 GGQKQRVAIARALASNPKVLLCDEATSALDPATtrsilELlkDINRELG-----LTIVLITHE----MDvvkriCDRVAV 213
|
250
....*....|.
gi 1199277034 1358 MDKGQVAESGS 1368
Cdd:PRK11153 214 IDAGRLVEQGT 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1146-1365 |
2.00e-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: 83.60 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1146 PQGGQIEFRDFGLRYRPEL--PLAVQGVSFKIHAGEKVGIVGRTGAGKSSL---ASGLLRlqeAAEGGIWIDGVPIAHVG 1220
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGggVTALDDVSLTVAAGEFVALVGPSGCGKSTLlrlIAGLEK---PTSGEVLVDGKPVTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1221 lhtlrSRISIIPQDPILFP----------GsLRMNlDLLQEHSDEAIWAALETVQLKALVASLPGQLqykcadrgedlSV 1290
Cdd:COG1116 80 -----PDRGVVFQEPALLPwltvldnvalG-LELR-GVPKAERRERARELLELVGLAGFEDAYPHQL-----------SG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1291 GQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHrlrSVM------DcaRVLVMDK-- 1360
Cdd:COG1116 142 GMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQEtgKTVLFVTH---DVDeavflaD--RVVVLSArp 216
|
....*
gi 1199277034 1361 GQVAE 1365
Cdd:COG1116 217 GRIVE 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
519-721 |
2.10e-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: 82.94 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 519 SATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG----------------AVAYV 582
Cdd:cd03257 8 SVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirrkEIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 583 PQEAwvqNTS----------VVENVCFGQELDPPWLERV---LEACALQPD---VDSFPegiHTsigeqgmnLSGGQKQR 646
Cdd:cd03257 88 FQDP---MSSlnprmtigeqIAEPLRIHGKLSKKEARKEavlLLLVGVGLPeevLNRYP---HE--------LSGGQRQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 647 LSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNqvigpggLLQ------GTTRILVTHALHILPQ-ADWIIVLANGAIAE 719
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILD-------LLKklqeelGLTLLFITHDLGVVAKiADRVAVMYAGKIVE 226
|
..
gi 1199277034 720 MG 721
Cdd:cd03257 227 EG 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1151-1371 |
2.91e-17 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 82.41 E-value: 2.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPElPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHV---GLHTLRSR 1227
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1228 ISIIPQDPILFPG-SLRMNLDL---LQEHSDEAIW----AALETVQLKALVASLPGQlqykcadrgedLSVGQKQLLCLA 1299
Cdd:COG2884 81 IGVVFQDFRLLPDrTVYENVALplrVTGKSRKEIRrrvrEVLDLVGLSDKAKALPHE-----------LSGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 1300 RALLRKTQILILDEATAAVDPGTELQ-MQAM-----LGswfaqCTVLLIAHRLRSVMDC-ARVLVMDKGQVAESGSPAQ 1371
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEiMELLeeinrRG-----TTVLIATHDLELVDRMpKRVLELEDGRLVRDEARGV 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1167-1363 |
3.17e-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: 81.81 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPI--AHVGLHTLRSRISIIPQDPILFPgslrm 1244
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFP----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1245 NLDLLQ-----------EHSDEAIWAA---LETVQLKALVASLPGQlqykcadrgedLSVGQKQLLCLARALLRKTQILI 1310
Cdd:cd03262 90 HLTVLEnitlapikvkgMSKAEAEERAlelLEKVGLADKADAYPAQ-----------LSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 1311 LDEATAAVDP---GTELQ-MQAMlgswfAQ--CTVLLIAHRL---RSVMDcaRVLVMDKGQV 1363
Cdd:cd03262 159 FDEPTSALDPelvGEVLDvMKDL-----AEegMTMVVVTHEMgfaREVAD--RVIFMDDGRI 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1151-1372 |
3.98e-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: 82.23 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYrPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG---LHTLRSR 1227
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1228 ISIIPQDPILFP----------GSL-RMN-----LDLLQEHSDEAIWAALETVQLKALVaslpgqlqYKCADRgedLSVG 1291
Cdd:cd03256 80 IGMIFQQFNLIErlsvlenvlsGRLgRRStwrslFGLFPKEEKQRALAALERVGLLDKA--------YQRADQ---LSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1292 QKQLLCLARALLRKTQILILDEATAAVDPGTELQ-MQAMLGswFAQ---CTVLLIAHRLRSVMD-CARVLVMDKGQVAES 1366
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQvMDLLKR--INReegITVIVSLHQVDLAREyADRIVGLKDGRIVFD 226
|
....*.
gi 1199277034 1367 GSPAQL 1372
Cdd:cd03256 227 GPPAEL 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1167-1367 |
4.10e-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: 81.47 E-value: 4.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGeKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGlHTLRSRISIIPQDPILFPG-SLRMN 1245
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGYLPQEFGVYPNfTVREF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1246 LDLL-------QEHSDEAIWAALETVQLkalvaslpgqlqykcADRGED----LSVGQKQLLCLARALLRKTQILILDEA 1314
Cdd:cd03264 93 LDYIawlkgipSKEVKARVDEVLELVNL---------------GDRAKKkigsLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 1315 TAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMD-CARVLVMDKGQVAESG 1367
Cdd:cd03264 158 TAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1167-1364 |
5.56e-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: 79.78 E-value: 5.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG-LHTLRSRISIIPQdpilfpgslrmn 1245
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1246 ldllqehsdeaiwaaletvqlkalvaslpgqlqykcadrgedLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQ 1325
Cdd:cd03216 83 ------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1199277034 1326 MQAMLGSWFAQ-CTVLLIAHRLRSVMD-CARVLVMDKGQVA 1364
Cdd:cd03216 121 LFKVIRRLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1151-1363 |
6.38e-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: 80.91 E-value: 6.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYrPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHV---GLHTLRSR 1227
Cdd:cd03292 1 IEFINVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1228 ISIIPQDPILFPG-----SLRMNLDLLQEHSDEA---IWAALETVQLKALVASLPGQlqykcadrgedLSVGQKQLLCLA 1299
Cdd:cd03292 80 IGVVFQDFRLLPDrnvyeNVAFALEVTGVPPREIrkrVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 1300 RALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCA--RVLVMDKGQV 1363
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTrhRVIALERGKL 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1167-1363 |
6.38e-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: 6.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGlhtlRSRISIIPQDPILFP------- 1239
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYPkmkvidq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1240 ----GSLR-MNLDLLQEHSDEaiWaaLETVQLkalvaslpGQLQYKcadRGEDLSVGQKQLLCLARALLRKTQILILDEA 1314
Cdd:cd03269 91 lvylAQLKgLKKEEARRRIDE--W--LERLEL--------SEYANK---RVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 1315 TAAVDP-GTELQMQAMLGSWFAQCTVLLIAHRLRSVMD-CARVLVMDKGQV 1363
Cdd:cd03269 156 FSGLDPvNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
532-721 |
6.45e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 81.98 E-value: 6.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSAL-LGELSKvEGFVSIEGA-------------------VAYVPQE--AWVQ 589
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPR-SGTLNIAGNhfdfsktpsdkairelrrnVGMVFQQynLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 590 NTsVVENV----CFGQELDPPWL----ERVLEACALQPDVDSFPegihtsigeqgMNLSGGQKQRLSLARAVYRKAAVYL 661
Cdd:PRK11124 97 LT-VQQNLieapCRVLGLSKDQAlaraEKLLERLRLKPYADRFP-----------LHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 662 LDDPLAALDAHVGqhvfNQVIGPGGLLQGT--TRILVTHALHILPQ-ADWIIVLANGAIAEMG 721
Cdd:PRK11124 165 FDEPTAALDPEIT----AQIVSIIRELAETgiTQVIVTHEVEVARKtASRVVYMENGHIVEQG 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
532-729 |
7.74e-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: 7.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-----------VAYVPQE-AWVQNTSVVENVCF 599
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 600 G---QELDPPWLER-VLEACALQpdvdsfpeGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQ 675
Cdd:cd03299 95 GlkkRKVDKKEIERkVLEIAEML--------GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 676 HVFNQVIGPGGLLqGTTRILVTHAL-HILPQADWIIVLANGAIAEMGSYQELLQR 729
Cdd:cd03299 167 KLREELKKIRKEF-GVTVLHVTHDFeEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
532-726 |
8.03e-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: 81.13 E-value: 8.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYVPQEAWVQNT-----------SVVENVCF 599
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKdITNLPPHKRPVNTvfqnyalfphlTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 600 G--------QELDppwlERVLEACALQpDVDSFPegiHTSIGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDA 671
Cdd:cd03300 96 GlrlkklpkAEIK----ERVAEALDLV-QLEGYA---NRKPSQ----LSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 672 HVGQHvfnqvigpgglLQ----------GTTRILVTH----ALHIlpqADWIIVLANGAIAEMGSYQEL 726
Cdd:cd03300 164 KLRKD-----------MQlelkrlqkelGITFVFVTHdqeeALTM---SDRIAVMNKGKIQQIGTPEEI 218
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
525-714 |
8.47e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 80.60 E-value: 8.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 525 SQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELS---KVEGFVSIEG-----------AVAYVPQEAWV-Q 589
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGrrltalpaeqrRIGILFQDDLLfP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 590 NTSVVENVCFGQELDPPWLER------VLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLD 663
Cdd:COG4136 90 HLSVGENLAFALPPTIGRAQRrarveqALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRALLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 664 DPLAALDAH----VGQHVFNQVIgpgglLQGTTRILVTHALHILPQADWIIVLAN 714
Cdd:COG4136 159 EPFSKLDAAlraqFREFVFEQIR-----QRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1167-1374 |
9.81e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 81.76 E-value: 9.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIaHVGLHTLRS-RISIIPQDP---------- 1235
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSYRSqRIRMIFQDPstslnprqri 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1236 --IL-FPgsLRMNLDLLQEHSDEAIWAALETVQLkalvasLPGQLQYkcadRGEDLSVGQKQLLCLARALLRKTQILILD 1312
Cdd:PRK15112 107 sqILdFP--LRLNTDLEPEQREKQIIETLRQVGL------LPDHASY----YPHMLAPGQKQRLGLARALILRPKVIIAD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 1313 EATAAVDPGTE-------LQMQAMLGSWFAQCTVLLiaHRLRSVMDcaRVLVMDKGQVAESGSPAQLLA 1374
Cdd:PRK15112 175 EALASLDMSMRsqlinlmLELQEKQGISYIYVTQHL--GMMKHISD--QVLVMHQGEVVERGSTADVLA 239
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1166-1375 |
1.01e-16 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 81.92 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1166 LAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG---LHTLRS-RISIIPQDPILFPG- 1240
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRkKISMVFQSFALLPHr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1241 SLRMN----LDL----LQEHSDEAIwAALETVQLKALVASLPGQlqykcadrgedLSVGQKQLLCLARALLRKTQILILD 1312
Cdd:cd03294 118 TVLENvafgLEVqgvpRAEREERAA-EALELVGLEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 1313 EATAAVDPGTELQMQAMLGSWFA--QCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQ 1375
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRLQAelQKTIVFITHDLDEALRLGdRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
532-726 |
1.25e-16 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 81.08 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA----------------VAYVPQE-AWVQNTSVV 594
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrrqIGMIFQQfNLIERLSVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 595 ENVCFGQeLD--PPW--------LERVLEACALQPDVdsfpeGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDD 664
Cdd:cd03256 97 ENVLSGR-LGrrSTWrslfglfpKEEKQRALAALERV-----GLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 665 PLAALDAHVGQHVfnqvigpGGLL------QGTTRILVTHALHI-LPQADWIIVLANGAIAEMGSYQEL 726
Cdd:cd03256 171 PVASLDPASSRQV-------MDLLkrinreEGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
532-670 |
1.27e-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: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSAL--LGEL---SKVEGFVSIEGA---------------VAYVPQEAwvqN- 590
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLipgARVEGEILLDGEdiydpdvdvvelrrrVGMVFQKP---Np 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 591 --TSVVENVCFG---------QELDppwlERV---LEACALQPDV-DSfpegIHTSigeqGMNLSGGQKQRLSLARAVYR 655
Cdd:COG1117 104 fpKSIYDNVAYGlrlhgikskSELD----EIVeesLRKAALWDEVkDR----LKKS----ALGLSGGQQQRLCIARALAV 171
|
170
....*....|....*
gi 1199277034 656 KAAVYLLDDPLAALD 670
Cdd:COG1117 172 EPEVLLMDEPTSALD 186
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
530-727 |
1.33e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 83.74 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 530 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAYVPQEAWVQ-NTSVVE 595
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASVPQDTSLSfEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 596 NVCFGQ-----ELDP--PWLERVLEACALQPDVDSFPEGIHTSigeqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAA 668
Cdd:PRK09536 97 VVEMGRtphrsRFDTwtETDRAAVERAMERTGVAQFADRPVTS-------LSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 669 LDAHVGQHVFNQVigpgGLLQGTTRILVThALHILPQA----DWIIVLANGAIAEMGSYQELL 727
Cdd:PRK09536 170 LDINHQVRTLELV----RRLVDDGKTAVA-AIHDLDLAarycDELVLLADGRVRAAGPPADVL 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1151-1376 |
1.48e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 81.82 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYrPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHV--GLHTLRSRI 1228
Cdd:PRK13636 6 LKVEELNYNY-SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSrkGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1229 SIIPQDP--ILFPGSLR-------MNLDLLQEHSDEAIWAALEtvqlKALVASLPGQLQYKcadrgedLSVGQKQLLCLA 1299
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYqdvsfgaVNLKLPEDEVRKRVDNALK----RTGIEHLKDKPTHC-------LSFGQKKRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1300 RALLRKTQILILDEATAAVDP-GTE------LQMQAMLGswfaqCTVLLIAHRLRSV-MDCARVLVMDKGQVAESGSPAQ 1371
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPmGVSeimkllVEMQKELG-----LTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKE 228
|
....*
gi 1199277034 1372 LLAQK 1376
Cdd:PRK13636 229 VFAEK 233
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1168-1365 |
1.76e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 81.27 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1168 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHV---GLHTLRSRISIIPQDPI-------- 1236
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSIsavnprkt 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1237 ---LFPGSLRMNLDLLQEHSDEAIWAALETVQLKALVAS-LPGQlqykcadrgedLSVGQKQLLCLARALLRKTQILILD 1312
Cdd:PRK10419 108 vreIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDkRPPQ-----------LSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 1313 EATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMD-CARVLVMDKGQVAE 1365
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQQfgTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
532-728 |
2.02e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 80.59 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAvayvPQEAW----------V--QNTSV-----V 594
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGR----PLADWspaelarrraVlpQHSSLsfpftV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 595 ENV--------CFGQELDPPWLERVLEACALQPDVD-SFPEgihtsigeqgmnLSGGQKQRLSLARA------VYRKAAV 659
Cdd:PRK13548 94 EEVvamgraphGLSRAEDDALVAAALAQVDLAHLAGrDYPQ------------LSGGEQQRVQLARVlaqlwePDGPPRW 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 660 YLLDDPLAALDAHVGQHVFNqvigpggLL------QGTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELLQ 728
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLR-------LArqlaheRGLAVIVVLHDLNLAARyADRIVLLHQGRLVADGTPAEVLT 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
535-700 |
2.06e-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: 79.65 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGcLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-----------------AVAYVPQE-AWVQNTSVVEN 596
Cdd:cd03297 17 IDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrkkinlppqqrKIGLVFQQyALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 597 VCFGQELDPPWLER-----VLEACALQPDVDSFPEGihtsigeqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDA 671
Cdd:cd03297 96 LAFGLKRKRNREDRisvdeLLDLLGLDHLLNRYPAQ-----------LSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180
....*....|....*....|....*....
gi 1199277034 672 HVGQHVFNQVIGPGGLLQGTTrILVTHAL 700
Cdd:cd03297 165 ALRLQLLPELKQIKKNLNIPV-IFVTHDL 192
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1151-1363 |
2.49e-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: 79.46 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELP--LAVQGVSFKIHAGEKVGIVGRTGAGKSSL---ASGLLRLQeaaEGGIWIDGVPIAHVGLHTL- 1224
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLlniLGGLDRPT---SGEVRVDGTDISKLSEKELa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1225 ---RSRISIIPQDPILFPG-SLRMNLDLLQEHS-------DEAIWAALETVQLKALVASLPGQlqykcadrgedLSVGQK 1293
Cdd:cd03255 78 afrRRHIGFVFQSFNLLPDlTALENVELPLLLAgvpkkerRERAEELLERVGLGDRLNHYPSE-----------LSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 1294 QLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSwFAQ---CTVLLIAHRLRSVMDCARVLVMDKGQV 1363
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRE-LNKeagTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1175-1367 |
4.01e-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: 4.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1175 IHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHvgLHTLRSRISIIPQDPILFPG-SLRMNLDL----- 1248
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA--APPADRPVSMLFQENNLFAHlTVEQNVGLglspg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1249 --LQEHSDEAIWAALETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQM 1326
Cdd:cd03298 99 lkLTAEDRQAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1199277034 1327 QAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESG 1367
Cdd:cd03298 168 LDLVLDLHAEtkMTVLMVTHQPEDAKRLAqRVVFLDNGRIAAQG 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
534-721 |
6.10e-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: 78.30 E-value: 6.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 534 RINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-----------VAYVPQEAWV-QNTSVVENVCFGQ 601
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdvtaappadrpVSMLFQENNLfAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 602 EldpPWLErvleacaLQPDVDSFPEGIHTSIGEQGM------NLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQ 675
Cdd:cd03298 96 S---PGLK-------LTAEDRQAIEVALARVGLAGLekrlpgELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1199277034 676 HVFNQVIGPGGlLQGTTRILVTH----ALHIlpqADWIIVLANGAIAEMG 721
Cdd:cd03298 166 EMLDLVLDLHA-ETKMTVLMVTHqpedAKRL---AQRVVFLDNGRIAAQG 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
532-727 |
6.32e-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: 6.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------------VAYVPQEAWV-QNTSVVEN 596
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarlgIGYVPEGRRIfPSLTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 597 -----VCFGQELDPPW-LERVLEAcalqpdvdsFPEgIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 670
Cdd:COG0410 99 lllgaYARRDRAEVRAdLERVYEL---------FPR-LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 671 AHVGQHVFNQVigpgGLL--QGTTRILV----THALHIlpqADWIIVLANGAIAEMGSYQELL 727
Cdd:COG0410 169 PLIVEEIFEII----RRLnrEGVTILLVeqnaRFALEI---ADRAYVLERGRIVLEGTAAELL 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
519-727 |
6.78e-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: 78.39 E-value: 6.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 519 SATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA----------------VAYV 582
Cdd:cd03258 8 SKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltllsgkelrkarrrIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 583 PQE-AWVQNTSVVENVCFGQELD-------PPWLERVLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVY 654
Cdd:cd03258 88 FQHfNLLSSRTVFENVALPLEIAgvpkaeiEERVLELLELVGLEDKADAYPA-----------QLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 655 RKAAVYLLDDPLAALDAHVGQHVFNqvigpggLLQ------GTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELL 727
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILA-------LLRdinrelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
519-671 |
7.17e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 79.14 E-value: 7.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 519 SATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAV--------AYVPQE----A 586
Cdd:COG4525 10 SVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVFQKdallP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 587 WVqntSVVENVCFGQELDP-PWLERVLEACALQPDVdsfpeGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDP 665
Cdd:COG4525 90 WL---NVLDNVAFGLRLRGvPKAERRARAEELLALV-----GLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEP 161
|
....*.
gi 1199277034 666 LAALDA 671
Cdd:COG4525 162 FGALDA 167
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1151-1376 |
7.93e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 79.49 E-value: 7.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELPLAVQG---VSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPI----AHVGLHT 1223
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGldnISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1224 LRSRISIIPQDP--ILFPGSLRMNLDL----LQEHSDEAIWAALETVQLKALVASLPGQLQYkcadrgeDLSVGQKQLLC 1297
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTVLKDVEFgpknFGFSEDEAKEKALKWLKKVGLSEDLISKSPF-------ELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1298 LARALLRKTQILILDEATAAVDPGTELQM-QAMLGSWFAQCTVLLIAHRLRSVMDCAR-VLVMDKGQVAESGSPAQLLAQ 1375
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMmQLFKDYQKAGHTVILVTHNMDDVAEYADdVLVLEHGKLIKHASPKEIFSD 235
|
.
gi 1199277034 1376 K 1376
Cdd:PRK13641 236 K 236
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
515-733 |
9.95e-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: 78.80 E-value: 9.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYVPQEAWVQNTSV 593
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIdISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 594 V--ENVCFGQ----ELDPPW------LERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYL 661
Cdd:cd03288 100 IlqDPILFSGsirfNLDPECkctddrLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 662 LDDPLAALDAHVgQHVFNQVIGPGglLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGAL 733
Cdd:cd03288 180 MDEATASIDMAT-ENILQKVVMTA--FADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGV 248
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
535-717 |
1.21e-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: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG----------AVAYVPQEAWVQ--NTSVVENVCFGQE 602
Cdd:cd03226 19 LSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQDVDYQlfTDSVREELLLGLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 603 L---DPPWLERVLEACALQPDVDSFPegihtsigeqgMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHV-- 677
Cdd:cd03226 99 EldaGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVge 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1199277034 678 -FNQVIGpggllQGTTRILVTHALHILPQ-ADWIIVLANGAI 717
Cdd:cd03226 168 lIRELAA-----QGKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
515-746 |
1.23e-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: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLgELSKVEGFVSIEG-------------AVAY 581
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGvswnsvtlqtwrkAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 582 VPQEAWVQNTSvvenvcFGQELDP--PW----LERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYR 655
Cdd:TIGR01271 1297 IPQKVFIFSGT------FRKNLDPyeQWsdeeIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILS 1370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 656 KAAVYLLDDPLAALDAhVGQHVFNQVIGPGglLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGalvc 735
Cdd:TIGR01271 1371 KAKILLLDEPSAHLDP-VTLQIIRKTLKQS--FSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETS---- 1443
|
250
....*....|.
gi 1199277034 736 LLDQARQPGDR 746
Cdd:TIGR01271 1444 LFKQAMSAADR 1454
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
535-728 |
1.84e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 77.96 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSAL-----LGELSKVEGFVSIEGAVAYVPQEAWVQ----------------NTSV 593
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIEvrrevgmvfqypnpfpHLTI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 594 VENVCFG----------QELDppwlERV---LEACALQPDVDSfpegihtSIGEQGMNLSGGQKQRLSLARAVYRKAAVY 660
Cdd:PRK14267 103 YDNVAIGvklnglvkskKELD----ERVewaLKKAALWDEVKD-------RLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 661 LLDDPLAALDAhVGQHVFNQVIGPggLLQGTTRILVTHA-LHILPQADWIIVLANGAIAEMGSYQELLQ 728
Cdd:PRK14267 172 LMDEPTANIDP-VGTAKIEELLFE--LKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
532-721 |
2.03e-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: 76.05 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELS--KVEGFVSIEG----------AVAYVPQEAWVQNT-SVVENVC 598
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGrpldkrsfrkIIGYVPQDDILHPTlTVRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 599 FGQELdppwlervleacalqpdvdsfpegihtsigeQGmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVF 678
Cdd:cd03213 105 FAAKL-------------------------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1199277034 679 nqvigpgGLL-----QGTTRILVTHAL--HILPQADWIIVLANGAIAEMG 721
Cdd:cd03213 152 -------SLLrrladTGRTIICSIHQPssEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
532-718 |
2.23e-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: 75.16 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVayvpqeawVQNTSVVEnvcfgqeldppwlerv 611
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE--------VSFASPRD---------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 612 leacALQpdvdsfpEGIhtsigeqGM--NLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVigpgGLL- 688
Cdd:cd03216 72 ----ARR-------AGI-------AMvyQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVI----RRLr 129
|
170 180 190
....*....|....*....|....*....|..
gi 1199277034 689 -QGTTRILVTHAL-HILPQADWIIVLANGAIA 718
Cdd:cd03216 130 aQGVAVIFISHRLdEVFEIADRVTVLRDGRVV 161
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
515-746 |
2.23e-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: 77.97 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLgELSKVEGFVSIEGaVAY--VPQEAWVQNTS 592
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDG-VSWnsVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 593 VVENVCF------GQELDP--PW----LERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVY 660
Cdd:cd03289 81 VIPQKVFifsgtfRKNLDPygKWsdeeIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 661 LLDDPLAALDAhVGQHVFNQVIGPGglLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGalvcLLDQA 740
Cdd:cd03289 161 LLDEPSAHLDP-ITYQVIRKTLKQA--FADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKS----HFKQA 233
|
....*.
gi 1199277034 741 RQPGDR 746
Cdd:cd03289 234 ISPSDR 239
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
535-698 |
2.54e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.07 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG----------AVAYV-PQEAWVQNTSVVENVCFGQEL 603
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpdvaeACHYLgHRNAMKPALTVAENLEFWAAF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 604 ---DPPWLERVLEACALQPdVDSFPEGihtsigeqgmNLSGGQKQRLSLAR--AVYRkaAVYLLDDPLAALDAHvGQHVF 678
Cdd:PRK13539 101 lggEELDIAAALEAVGLAP-LAHLPFG----------YLSAGQKRRVALARllVSNR--PIWILDEPTAALDAA-AVALF 166
|
170 180
....*....|....*....|
gi 1199277034 679 NQVIGpGGLLQGTTRILVTH 698
Cdd:PRK13539 167 AELIR-AHLAQGGIVIAATH 185
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1151-1374 |
2.71e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 77.83 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELPL-AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRIS 1229
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1230 IIPQDP--ILFPGSLRMNLDLLQEHSDEAIWAALETVQLKALVASLpgqLQYKCADRGEdLSVGQKQLLCLARALLRKTQ 1307
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNM---LDFKTREPAR-LSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 1308 ILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLA 1374
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
535-729 |
2.84e-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: 78.99 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-----------------AVAYVPQEAwvq-ntSVVEN 596
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargiflpphrrRIGYVFQEArlfphlSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 597 VCFGQ-----ELDPPWLERVLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDA 671
Cdd:COG4148 98 LLYGRkraprAERRISFDEVVELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199277034 672 HVGQHVfnqvigpggL-----LQGTTRI---LVTHALH-ILPQADWIIVLANGAIAEMGSYQELLQR 729
Cdd:COG4148 167 ARKAEI---------LpylerLRDELDIpilYVSHSLDeVARLADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
517-701 |
3.63e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 77.00 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 517 IHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALlGELSKVEGFVSIEGAVAYVPQEAWVQNT----- 591
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEFFNQNIYERRVnlnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 592 ----------------SVVENVCFGQELdPPW-----LERVLEACALQPDV-DSFPEGIHTSigeqGMNLSGGQKQRLSL 649
Cdd:PRK14258 87 rrqvsmvhpkpnlfpmSVYDNVAYGVKI-VGWrpkleIDDIVESALKDADLwDEIKHKIHKS----ALDLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 650 ARAVYRKAAVYLLDDPLAALDAHVGQHVfNQVIGPGGLLQGTTRILVTHALH 701
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKV-ESLIQSLRLRSELTMVIVSHNLH 212
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
530-725 |
4.22e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 75.91 E-value: 4.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 530 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-AVAYVPQEAWVQNTS------------VVEN 596
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGeDISTLKPEIYRQQVSycaqtptlfgdtVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 597 VCFgqeldpPWLER--VLEACALQPDVDSFpeGIHTSIGEQGMN-LSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHV 673
Cdd:PRK10247 101 LIF------PWQIRnqQPDPAIFLDDLERF--ALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 674 GQHVfNQVIGPGGLLQGTTRILVTHALHILPQADWIIVLAngaiAEMGSYQE 725
Cdd:PRK10247 173 KHNV-NEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQ----PHAGEMQE 219
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
532-726 |
5.42e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 78.20 E-value: 5.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-----------VAYVPQE-AWVQNTSVVENVCF 599
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHyALFRHMTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 600 GQELDP-----------PWLERVLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLAA 668
Cdd:PRK10851 98 GLTVLPrrerpnaaaikAKVTQLLEMVQLAHLADRYPA-----------QLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 669 LDAHVGQHVFNQVIGPGGLLQGTTrILVTH----ALHIlpqADWIIVLANGAIAEMGSYQEL 726
Cdd:PRK10851 167 LDAQVRKELRRWLRQLHEELKFTS-VFVTHdqeeAMEV---ADRVVVMSQGNIEQAGTPDQV 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1151-1385 |
6.45e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 76.76 E-value: 6.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLA---SGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSR 1227
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISkliNGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1228 ISIIPQDPI-LFPGSlRMNLDLLQEHSDEAIwAALETVQLKALVASLPGQLQYKCADRgEDLSVGQKQLLCLARALLRKT 1306
Cdd:PRK13640 86 VGIVFQNPDnQFVGA-TVGDDVAFGLENRAV-PRPEMIKIVRDVLADVGMLDYIDSEP-ANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1307 QILILDEATAAVDPGTELQMQAMLGSWFA--QCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQ------LLAQKGL 1378
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEifskveMLKEIGL 242
|
250
....*....|.
gi 1199277034 1379 ----FYRLAQE 1385
Cdd:PRK13640 243 dipfVYKLKNK 253
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1151-1388 |
8.49e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 76.31 E-value: 8.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISI 1230
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1231 IPQDP--ILFPGSL-------RMNLDLLQEHSDEAIWAALETVQLKALVASLPGQLQYkcadrgedlsvGQKQLLCLARA 1301
Cdd:PRK13647 84 VFQDPddQVFSSTVwddvafgPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSY-----------GQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1302 LLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIA-HRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQKglf 1379
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEWAdQVIVLKEGRVLAEGDKSLLTDED--- 229
|
....*....
gi 1199277034 1380 yrLAQESGL 1388
Cdd:PRK13647 230 --IVEQAGL 236
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
515-733 |
8.75e-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: 8.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQEAW------- 587
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeirkkvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 588 -V-QN-------TSVVENVCFGQE---LDPPWLER----VLEACALQPDVDSFPegiHtsigeqgmNLSGGQKQRLSLAR 651
Cdd:TIGR04520 81 mVfQNpdnqfvgATVEDDVAFGLEnlgVPREEMRKrvdeALKLVGMEDFRDREP---H--------LLSGGQKQRVAIAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 652 AVYRKAAVYLLDDPLAALDahvgqhvfnqvigPGG---LL---------QGTTRILVTHALHILPQADWIIVLANGAIAE 719
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLD-------------PKGrkeVLetirklnkeEGITVISITHDMEEAVLADRVIVMNKGKIVA 216
|
250
....*....|....
gi 1199277034 720 MGSYQELLQRKGAL 733
Cdd:TIGR04520 217 EGTPREIFSQVELL 230
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1164-1373 |
9.52e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 78.15 E-value: 9.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1164 LPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRS----RISIIPQDPILFP 1239
Cdd:PRK10070 40 LSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1240 gslRMNLDLLQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVD 1319
Cdd:PRK10070 120 ---HMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199277034 1320 PGTELQMQAMLGSWFA--QCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLL 1373
Cdd:PRK10070 197 PLIRTEMQDELVKLQAkhQRTIVFISHDLDEAMRIGdRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1167-1367 |
1.02e-14 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 74.88 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHT-LRSRISIIpqDPILFPGSLR-M 1244
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGGgFNPELTGR--ENIYLNGRLLgL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1245 NLDLLQEHSDEAI-WAALETVQlkalvaslpgQLQYKcadrgeDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTE 1323
Cdd:cd03220 115 SRKEIDEKIDEIIeFSELGDFI----------DLPVK------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1199277034 1324 LQMQAMLGSWFAQC-TVLLIAHRLRSVMD-CARVLVMDKGQVAESG 1367
Cdd:cd03220 179 EKCQRRLRELLKQGkTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
535-733 |
1.46e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 76.68 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-----------VAYVPQE-AWVQNTSVVENVCFG-Q 601
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvthrsiqqrdICMVFQSyALFPHMSLGENVGYGlK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 602 ELDPPWLE---RVLEACALQpDVDSFPEGIHTSIgeqgmnlSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVF 678
Cdd:PRK11432 105 MLGVPKEErkqRVKEALELV-DLAGFEDRYVDQI-------SGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMR 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 679 NQVIGpgglLQ---GTTRILVTH----ALHIlpqADWIIVLANGAIAEMGSYQELLQRKGAL 733
Cdd:PRK11432 177 EKIRE----LQqqfNITSLYVTHdqseAFAV---SDTVIVMNKGKIMQIGSPQELYRQPASR 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1167-1375 |
1.49e-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: 78.19 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRL----QEAAEGGIWIDGVPIAHVGLHTLR----SRISIIPQDPI-- 1236
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLLGLSERELRrirgNRIAMIFQEPMts 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1237 LFP----G-----SLRMNLDLLQEHSDEAIWAALETVQL---KALVASLPGQlqykcadrgedLSVGQKQLLCLARALLR 1304
Cdd:COG4172 105 LNPlhtiGkqiaeVLRLHRGLSGAAARARALELLERVGIpdpERRLDAYPHQ-----------LSGGQRQRVMIAMALAN 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 1305 KTQILILDEATAAVDPGTELQM-------QAMLGSwfaqcTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQ 1375
Cdd:COG4172 174 EPDLLIADEPTTALDVTVQAQIldllkdlQRELGM-----ALLLITHDLGVVRRFAdRVAVMRQGEIVEQGPTAELFAA 247
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
547-730 |
1.64e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 79.05 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 547 VVGPVGAGKSSLLSALLGELSKVEGFVSIEG--AVAY-----------VPQEAWVQNTSVVENVCFGQELDPPWLERVLE 613
Cdd:PTZ00243 1341 IVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGreIGAYglrelrrqfsmIPQDPVLFDGTVRQNVDPFLEASSAEVWAALE 1420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 614 ACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVY-LLDDPLAALDAHVGQHVFNQVIGPgglLQGTT 692
Cdd:PTZ00243 1421 LVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFiLMDEATANIDPALDRQIQATVMSA---FSAYT 1497
|
170 180 190
....*....|....*....|....*....|....*...
gi 1199277034 693 RILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRK 730
Cdd:PTZ00243 1498 VITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1165-1375 |
1.79e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.51 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1165 PLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG-LHTLRSRISIIPQDP-------- 1235
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQNPdnqivati 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1236 ----ILF-PGSLRMNLDLLQEHSDEAiwaaletvqLKALvaslpGQLQYKcadRGED--LSVGQKQLLCLARALLRKTQI 1308
Cdd:PRK13633 103 veedVAFgPENLGIPPEEIRERVDES---------LKKV-----GMYEYR---RHAPhlLSGGQKQRVAIAGILAMRPEC 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1309 LILDEATAAVDP-GTELQMQAM--LGSWFAqCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQ 1375
Cdd:PRK13633 166 IIFDEPTAMLDPsGRREVVNTIkeLNKKYG-ITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1172-1376 |
1.88e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 74.23 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1172 SFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPiahvglHTL----RSRISIIPQDPILF--------- 1238
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD------HTTtppsRRPVSMLFQENNLFshltvaqni 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1239 -----PGsLRMNLDllQEHSDEAIwaaLETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLARALLRKTQILILDE 1313
Cdd:PRK10771 93 glglnPG-LKLNAA--QREKLHAI---ARQMGIEDLLARLPGQL-----------SGGQRQRVALARCLVREQPILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 1314 ATAAVDPGTELQMQAMLGSWFA--QCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQK 1376
Cdd:PRK10771 156 PFSALDPALRQEMLTLVSQVCQerQLTLLMVSHSLEDAARIApRSLVVADGRIAWDGPTDELLSGK 221
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1168-1376 |
2.64e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.02 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1168 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGlHTLRSRISIIPQ-DPILFPGSLRMNL 1246
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA-RLARARIGVVPQfDNLDLEFTVRENL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1247 DLLQEhsdeaiWAALETVQLKALVASLP--GQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTEL 1324
Cdd:PRK13536 136 LVFGR------YFGMSTREIEAVIPSLLefARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARH 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 1325 QMQAMLGSWFAQC-TVLLIAH------RLrsvmdCARVLVMDKGQVAESGSPAQLLAQK 1376
Cdd:PRK13536 210 LIWERLRSLLARGkTILLTTHfmeeaeRL-----CDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
534-726 |
3.45e-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: 3.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 534 RINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA------------VAYVPQE-AWVQNTSVVENVCF- 599
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsirtdrkaarqsLGYCPQFdALFDELTVREHLRFy 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 600 ----------GQELDppwlERVLEACALQPDvdsfpegIHTSIGeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLAAL 669
Cdd:cd03263 100 arlkglpkseIKEEV----ELLLRVLGLTDK-------ANKRAR----TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 670 DAHVGQHVFNQVIgpgGLLQGTTRILVTHALH---ILpqADWIIVLANGAIAEMGSYQEL 726
Cdd:cd03263 165 DPASRRAIWDLIL---EVRKGRSIILTTHSMDeaeAL--CDRIAIMSDGKLRCIGSPQEL 219
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
883-1365 |
4.10e-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: 76.76 E-value: 4.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 883 LQAIGLFASMAAVLLGGARASRLLF------------QRLLWDVVRSPISFFERTPIGHLLNRFSKETDTVdvdipdkLR 950
Cdd:COG4615 48 ARLLLLFAGLLVLLLLSRLASQLLLtrlgqhavarlrLRLSRRILAAPLERLERIGAARLLAALTEDVRTI-------SQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 951 SLLMYAFGLLEVSLVVAVATPLATVAiLPLFLLYAGFQSLYVVSSCQL-----RRLESASyssvcshMAET--FQG-STV 1022
Cdd:COG4615 121 AFVRLPELLQSVALVLGCLAYLAWLS-PPLFLLTLVLLGLGVAGYRLLvrrarRHLRRAR-------EAEDrlFKHfRAL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1023 VRAF--------RTQAPFVAQNNARVDESQRIsfpRLVADRWLAANVeLLGNGLVFAAATCAVLSKAHLSAG----LVGF 1090
Cdd:COG4615 193 LEGFkelklnrrRRRAFFDEDLQPTAERYRDL---RIRADTIFALAN-NWGNLLFFALIGLILFLLPALGWAdpavLSGF 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1091 sVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDYAWTPKEAPWRLPTCAAQPPWPQGGQIEFRDFGLRYRPEL---PLA 1167
Cdd:COG4615 269 -VLVLLFLRGPLSQLVGALPTLSRANVALRKIEELELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDgdeGFT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1168 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGslrmNLD 1247
Cdd:COG4615 348 LGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR----LLG 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1248 LLQEHSDEAIWAALETVQLKALVAslpgqlqykcADRGE----DLSVGQKQLLCLARALLRKTQILILDEATAAVDPG-- 1321
Cdd:COG4615 424 LDGEADPARARELLERLELDHKVS----------VEDGRfsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEfr 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 1322 ----TEL--QMQAMlGSwfaqcTVLLIAH--RLRSVMDcaRVLVMDKGQVAE 1365
Cdd:COG4615 494 rvfyTELlpELKAR-GK-----TVIAISHddRYFDLAD--RVLKMDYGKLVE 537
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1167-1365 |
4.23e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 73.15 E-value: 4.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSL---ASGLLRlqeAAEGGIWIDGVPIAHVG---LHTLRSR-ISIIPQDPILFP 1239
Cdd:COG1136 23 ALRGVSLSIEAGEFVAIVGPSGSGKSTLlniLGGLDR---PTSGEVLIDGQDISSLSereLARLRRRhIGFVFQFFNLLP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1240 gSL------RMNLDLLQEHSDEA---IWAALETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLARALLRKTQILI 1310
Cdd:COG1136 100 -ELtalenvALPLLLAGVSRKERrerARELLERVGLGDRLDHRPSQL-----------SGGQQQRVAIARALVNRPKLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 1311 LDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAH--RLRSVMDcaRVLVMDKGQVAE 1365
Cdd:COG1136 168 ADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHdpELAARAD--RVIRLRDGRIVS 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
535-729 |
4.42e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 73.79 E-value: 4.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSAL--LGEL---SKVEGFVSIEGA----------------VAYVPQEawVQNTSV 593
Cdd:PRK14247 22 VNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELypeARVSGEVYLDGQdifkmdvielrrrvqmVFQIPNP--IPNLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 594 VENVCFGQELD------PPWLERVLEACalqpDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLA 667
Cdd:PRK14247 100 FENVALGLKLNrlvkskKELQERVRWAL----EKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 668 ALDAHVGQHVFNQVIgpgGLLQGTTRILVThalHILPQA----DWIIVLANGAIAEMGSYQELLQR 729
Cdd:PRK14247 176 NLDPENTAKIESLFL---ELKKDMTIVLVT---HFPQQAarisDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1168-1374 |
4.43e-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: 73.35 E-value: 4.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1168 VQGVSFKIHAGEKVGIVGRTGAGKSSL---ASGLLRlqeAAEGGIWIDGVPIAHVGLHTlRSRISII--PQDPILFPG-S 1241
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTfymIVGLVK---PDSGKILLDGQDITKLPMHK-RARLGIGylPQEASIFRKlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1242 LRMNLDLLQE--HSDEAIWAALetvqLKALVASLpgQLQyKCADR-GEDLSVGQKQLLCLARALLRKTQILILDEATAAV 1318
Cdd:cd03218 92 VEENILAVLEirGLSKKEREEK----LEELLEEF--HIT-HLRKSkASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1319 DPGTELQMQAM---LGSWfaQCTVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQLLA 1374
Cdd:cd03218 165 DPIAVQDIQKIikiLKDR--GIGVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1167-1379 |
5.25e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 74.89 E-value: 5.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAH-------VGLHT---------LRSRISI 1230
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDkknnhelITNPYskkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1231 IPQDP--ILFPGSLRMNLDL----LQEHSDEAiwaaletVQLKALVASLPGqLQYKCADRGE-DLSVGQKQLLCLARALL 1303
Cdd:PRK13631 121 VFQFPeyQLFKDTIEKDIMFgpvaLGVKKSEA-------KKLAKFYLNKMG-LDDSYLERSPfGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 1304 RKTQILILDEATAAVDP-GTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQKGLF 1379
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPkGEHEMMQLILDAKANNKTVFVITHTMEHVLEVAdEVIVMDKGKILKTGTPYEIFTDQHII 270
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
532-717 |
5.52e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 73.56 E-value: 5.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGeLSKVEGFVSIEGAVAYVP---------QEA----WvqnTSVVENVC 598
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-LETPSAGELLAGTAPLAEaredtrlmfQDArllpW---KKVIDNVG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 599 FGqeLDPPWLERVLEACAlqpdvdsfPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAhVGQHVF 678
Cdd:PRK11247 104 LG--LKGQWRDAALQALA--------AVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA-LTRIEM 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1199277034 679 NQVIGPGGLLQGTTRILVTHAL-HILPQADWIIVLANGAI 717
Cdd:PRK11247 173 QDLIESLWQQHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1167-1374 |
5.73e-14 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 73.09 E-value: 5.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTL-RSRISIIPQDPILFPG-SLRM 1244
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1245 NLDL--LQEHSDEAIWAALETV-----QLKALVASlpgqlqykcadRGEDLSVGQKQLLCLARALLRKTQILILDEATAA 1317
Cdd:COG0410 98 NLLLgaYARRDRAEVRADLERVyelfpRLKERRRQ-----------RAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 1318 VDPgtelQMQAMLGSWFAQ-----CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLA 1374
Cdd:COG0410 167 LAP----LIVEEIFEIIRRlnregVTILLVEQNARFALEIAdRAYVLERGRIVLEGTAAELLA 225
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1167-1374 |
6.74e-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: 73.15 E-value: 6.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSL---ASGLLRlqeAAEGGIWIDGVPIAHVGLHtLRSRISI-----IPQdpiLF 1238
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLfnlITGFYR---PTSGRILFDGRDITGLPPH-RIARLGIartfqNPR---LF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1239 PG-SLRMNLDL-----------------------LQEHSDEAiWAALETVQLKALVASLPGqlqykcadrgeDLSVGQKQ 1294
Cdd:COG0411 92 PElTVLENVLVaaharlgrgllaallrlprarreEREARERA-EELLERVGLADRADEPAG-----------NLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1295 LLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQ 1371
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErgITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAE 239
|
...
gi 1199277034 1372 LLA 1374
Cdd:COG0411 240 VRA 242
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1151-1376 |
6.77e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 73.57 E-value: 6.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYrPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAH--VGLHTLRSRI 1228
Cdd:PRK13639 2 LETRDLKYSY-PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYdkKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1229 SIIPQDP--ILFPGSLR-------MNLDLLQEHSDEAIWAALETVQLKALVASLPgqlqykcadrgEDLSVGQKQLLCLA 1299
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEedvafgpLNLGLSKEEVEKRVKEALKAVGMEGFENKPP-----------HHLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 1300 RALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ-CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQK 1376
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEgITIIISTHDVDLVPVYAdKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1166-1371 |
8.38e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.83 E-value: 8.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1166 LAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAhvgLHT----LRSRISIIPQDPILFP-- 1239
Cdd:COG3845 19 VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR---IRSprdaIALGIGMVHQHFMLVPnl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1240 -----------GSLRMNLDL------LQEHSDEAiwaALEtVQLKALVaslpgqlqykcadrgEDLSVGQKQllclaral 1302
Cdd:COG3845 96 tvaenivlglePTKGGRLDRkaararIRELSERY---GLD-VDPDAKV---------------EDLSVGEQQ-------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1303 lrK----------TQILILDEATAAVDPG--TEL-----QMQAmlgswfAQCTVLLIAHRLRSVMDCA-RVLVMDKGQVA 1364
Cdd:COG3845 149 --RveilkalyrgARILILDEPTAVLTPQeaDELfeilrRLAA------EGKSIIFITHKLREVMAIAdRVTVLRRGKVV 220
|
....*..
gi 1199277034 1365 ESGSPAQ 1371
Cdd:COG3845 221 GTVDTAE 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1166-1372 |
8.47e-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: 8.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1166 LAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGlHTLRSRISIIPQDPILfpgslrmn 1245
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP-REVRRRIGIVFQDLSV-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1246 ldllqehsDEAIwAALETVQLKALVASLPGQLQYKCADRGEDL--------------SVGQKQLLCLARALLRKTQILIL 1311
Cdd:cd03265 85 --------DDEL-TGWENLYIHARLYGVPGAERRERIDELLDFvglleaadrlvktySGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 1312 DEATAAVDPGTELQM----QAMLGSWfaQCTVLLIAHRLRSV-MDCARVLVMDKGQVAESGSPAQL 1372
Cdd:cd03265 156 DEPTIGLDPQTRAHVweyiEKLKEEF--GMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1151-1378 |
8.73e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 73.52 E-value: 8.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELP---LAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWI-DGVPIAHV---GLHT 1223
Cdd:PRK13634 3 ITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVITAGKknkKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1224 LRSRISIIPQDP------------ILF-PgslrMNLDLLQEhsdEAIWAALETVQLKALVASLPGQLQYkcadrgeDLSV 1290
Cdd:PRK13634 83 LRKKVGIVFQFPehqlfeetvekdICFgP----MNFGVSEE---DAKQKAREMIELVGLPEELLARSPF-------ELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1291 GQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMlgswFAQC------TVLLIAHrlrSVMDCAR----VLVMDK 1360
Cdd:PRK13634 149 GQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEM----FYKLhkekglTTVLVTH---SMEDAARyadqIVVMHK 221
|
250 260
....*....|....*....|....
gi 1199277034 1361 GQVAESGSPAQL------LAQKGL 1378
Cdd:PRK13634 222 GTVFLQGTPREIfadpdeLEAIGL 245
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1155-1374 |
1.00e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.12 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1155 DFGLRYRPELPLAVQGVSFKIHAgeKVGIVGRTGAGKSSL---ASGLLRLQEAAEggIWiDGVPIAHV--GLHTLRSRIS 1229
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSP--VTGLVGANGCGKSTLfmnLSGLLRPQKGAV--LW-QGKPLDYSkrGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1230 IIPQDP------------ILFpgSLRmNLDLLQEHSDEAIWAALETVQLKALvaslpGQLQYKCadrgedLSVGQKQLLC 1297
Cdd:PRK13638 81 TVFQDPeqqifytdidsdIAF--SLR-NLGVPEAEITRRVDEALTLVDAQHF-----RHQPIQC------LSHGQKKRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 1298 LARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCT-VLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLA 1374
Cdd:PRK13638 147 IAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNhVIISSHDIDLIYEISdAVYVLRQGQILTHGAPGEVFA 225
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
532-729 |
1.07e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 72.43 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSAL--LGELSK----VEGFVSIEGAVA--YVPQEA---------WVQNTSVv 594
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITSgdliVDGLKVNDPKVDerLIRQEAgmvfqqfylFPHLTAL- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 595 ENVCFG------------QELDPPWLERVleacALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLL 662
Cdd:PRK09493 96 ENVMFGplrvrgaskeeaEKQARELLAKV----GLAERAHHYPS-----------ELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 663 DDPLAALDAHVGQHVFNqvigpggLLQ-----GTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELLQR 729
Cdd:PRK09493 161 DEPTSALDPELRHEVLK-------VMQdlaeeGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
512-670 |
1.09e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.99 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 512 KDCITIHSATFAWsQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA----------VAY 581
Cdd:PRK15056 4 QAGIVVNDVTVTW-RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 582 VPQEA---WVQNTSVVENVCFGQELDPPWLER-------VLEACALQPDVDSFPegiHTSIGEqgmnLSGGQKQRLSLAR 651
Cdd:PRK15056 83 VPQSEevdWSFPVLVEDVVMMGRYGHMGWLRRakkrdrqIVTAALARVDMVEFR---HRQIGE----LSGGQKKRVFLAR 155
|
170
....*....|....*....
gi 1199277034 652 AVYRKAAVYLLDDPLAALD 670
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVD 174
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
197-487 |
1.14e-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: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 197 FLLGTLSLIISDVFRFTVPKLLSLFLEFIGdPKPPAWKGYLLAVLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITGLVY 276
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVI-PAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 277 RKVLALSSGSRKASAVGDVVNLVSVDVQRLTESV-LYLNGLWLPLVWIVVCFVYL----WQLlgpsaltAIAVFLsLLPL 351
Cdd:cd07346 80 RHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVsSGLLQLLSDVLTLIGALVILfylnWKL-------TLVALL-LLPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 352 NFFISKK-RNHHQEEQMRQKDSRARLTSSI---LRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLLFSVSLVSFQV 427
Cdd:cd07346 152 YVLILRYfRRRIRKASREVRESLAELSAFLqesLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 428 STFLVALVVFAVHT-LVAENAMNAEKAFVTLTVLNILNKAQAFLPFSIHSLVQARVSFDRL 487
Cdd:cd07346 232 LTALGTALVLLYGGyLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1168-1367 |
1.15e-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: 71.04 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1168 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGL--LRLQEAAEGGIWIDGVPIahvGLHTLRSRISIIPQDPILFPgslrmN 1245
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKRSFRKIIGYVPQDDILHP-----T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1246 LdllqehsdeaiwAALETVQLKALVASLPGqlqykcadrgedlsvGQKQLLCLARALLRKTQILILDEATAAVDPGTELQ 1325
Cdd:cd03213 97 L------------TVRETLMFAAKLRGLSG---------------GERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1199277034 1326 -MQAMLGSWFAQCTVLLIAHRLRSVM--DCARVLVMDKGQVAESG 1367
Cdd:cd03213 150 vMSLLRRLADTGRTIICSIHQPSSEIfeLFDKLLLLSQGRVIYFG 194
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
532-717 |
1.27e-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: 71.41 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGeLSKV-EGFVSIEGAVAYVPQEAWVQ----------------NTSVV 594
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINL-LEEPdSGTIIIDGLKLTDDKKNINElrqkvgmvfqqfnlfpHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 595 ENVCFGqeldPPWL------------ERVLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLL 662
Cdd:cd03262 95 ENITLA----PIKVkgmskaeaeeraLELLEKVGLADKADAYPA-----------QLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 663 DDPLAALDAHVGQHVFNQVIgpgGLLQ-GTTRILVTH----ALHIlpqADWIIVLANGAI 717
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMK---DLAEeGMTMVVVTHemgfAREV---ADRVIFMDDGRI 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
532-727 |
1.34e-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: 71.95 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGeLSKV-EGFVSIEGAVAYVPQEAWVQ----------------NTSVV 594
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINL-LEEPdSGTITVDGEDLTDSKKDINKlrrkvgmvfqqfnlfpHLTVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 595 ENVCFGQ----------------ELdppwLERV-LEACAlqpdvDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKA 657
Cdd:COG1126 96 ENVTLAPikvkkmskaeaeeramEL----LERVgLADKA-----DAYPA-----------QLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 658 AVYLLDDPLAALDahvgqhvfnqvigP---GGLLQ--------GTTRILVTH----ALHIlpqADWIIVLANGAIAEMGS 722
Cdd:COG1126 156 KVMLFDEPTSALD-------------PelvGEVLDvmrdlakeGMTMVVVTHemgfAREV---ADRVVFMDGGRIVEEGP 219
|
....*
gi 1199277034 723 YQELL 727
Cdd:COG1126 220 PEEFF 224
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1151-1376 |
1.54e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 72.89 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELPL---AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG----LHT 1223
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1224 LRSRISIIPQDP------------ILF-PGSLRMNLDllqEHSDEAIWAALETVQLKALVASLPGQlqykcadrgedLSV 1290
Cdd:PRK13646 83 VRKRIGMVFQFPesqlfedtvereIIFgPKNFKMNLD---EVKNYAHRLLMDLGFSRDVMSQSPFQ-----------MSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1291 GQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESG 1367
Cdd:PRK13646 149 GQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARYAdEVIVMKEGSIVSQT 228
|
....*....
gi 1199277034 1368 SPAQLLAQK 1376
Cdd:PRK13646 229 SPKELFKDK 237
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
535-730 |
1.75e-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: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-----------------AVAYVPQEAWV-QNTSVVEN 596
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrkgiflppekrRIGYVFQEARLfPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 597 VCFG-QELDPPWL----ERVLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDa 671
Cdd:TIGR02142 96 LRYGmKRARPSERrisfERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD- 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 672 hvgQHVFNQVIGPGGLLQGTTRI---LVTHAL-HILPQADWIIVLANGAIAEMGSYQELLQRK 730
Cdd:TIGR02142 164 ---DPRKYEILPYLERLHAEFGIpilYVSHSLqEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
534-728 |
2.59e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 71.15 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 534 RINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-----------VAYVPQEawvqNT-----SVVENV 597
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsrrpVSMLFQE----NNlfshlTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 598 CFGqeLDPPW---------LERVLEACALQPDVDSFPegihtsiGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAA 668
Cdd:PRK10771 93 GLG--LNPGLklnaaqrekLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 669 LDAHVGQHVFNqvigpggLL------QGTTRILVTH----ALHILPQAdwiIVLANGAIAEMGSYQELLQ 728
Cdd:PRK10771 160 LDPALRQEMLT-------LVsqvcqeRQLTLLMVSHsledAARIAPRS---LVVADGRIAWDGPTDELLS 219
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1167-1368 |
2.93e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 72.82 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGI-WI--DGVPIAHVGLHTLRSRISIIPQDPIlfpGSL- 1242
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVaWLgkDLLGMKDDEWRAVRSDIQMIFQDPL---ASLn 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1243 -RMNL-DLLQEH--------SDEAIWAALETVQLKalVASLPGQL-QYKcadrgEDLSVGQKQLLCLARALLRKTQILIL 1311
Cdd:PRK15079 113 pRMTIgEIIAEPlrtyhpklSRQEVKDRVKAMMLK--VGLLPNLInRYP-----HEFSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 1312 DEATAAVDPGTELQ-------MQAMLGswfaqCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGS 1368
Cdd:PRK15079 186 DEPVSALDVSIQAQvvnllqqLQREMG-----LSLIFIAHDLAVVKHISdRVLVMYLGHAVELGT 245
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
582-727 |
3.11e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.07 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 582 VPQEAWVQNTSVVENVCFGQEldPPWLERVLEAC---ALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAA 658
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGKE--DATREDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPK 1378
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 659 VYLLDDPLAALDAHvGQHVFNQVIGPGGLLQGTTRILVTHALHILPQADWIIVLAN----GAIAEM-GSYQELL 727
Cdd:PTZ00265 1379 ILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAhGTHEELL 1451
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1166-1367 |
3.13e-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: 70.76 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1166 LAVQGVSFKIHAGEKVGIVGRTGAGKSSL---ASGLLRLQEAAEGGIWIDGVPIAHvglHTLRSRISIIPQDPILFPG-- 1240
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLldaISGRVEGGGTTSGQILFNGQPRKP---DQFQKCVAYVRQDDILLPGlt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1241 ---SLR-MNLDLLQEHSDEAIWAAL-ETVQLKALVASLPGQlqykcaDRGEDLSVGQKQLLCLARALLRKTQILILDEAT 1315
Cdd:cd03234 98 vreTLTyTAILRLPRKSSDAIRKKRvEDVLLRDLALTRIGG------NLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 1316 AAVDPGTELQMQAMLgSWFAQ--CTVLLIAHRLRS----VMDcaRVLVMDKGQVAESG 1367
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 ... |
535-721 |
3.24e-13 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 70.30 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGcLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG------------AVAYVPQE-AWVQNTSVVENV---C 598
Cdd:cd03264 19 VSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQEfGVYPNFTVREFLdyiA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 599 FGQELDPPWLERvlEACALQPDVDSFPEGiHTSIGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDahVGQ-HV 677
Cdd:cd03264 98 WLKGIPSKEVKA--RVDEVLELVNLGDRA-KKKIGS----LSGGMRRRVGIAQALVGDPSILIVDEPTAGLD--PEErIR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1199277034 678 FNQVIgpGGLLQGTTRILVTHALH-ILPQADWIIVLANGAIAEMG 721
Cdd:cd03264 169 FRNLL--SELGEDRIVILSTHIVEdVESLCNQVAVLNKGKLVFEG 211
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
530-671 |
3.26e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 71.27 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 530 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVP---------QEAWVQNTSVVENVCFG 600
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPgaergvvfqNEGLLPWRNVQDNVAFG 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 601 QEL-DPPWLERVLEACALQPDVDSfpEGIHTSIGEQgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDA 671
Cdd:PRK11248 95 LQLaGVEKMQRLEIAHQMLKKVGL--EGAEKRYIWQ---LSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1151-1374 |
3.69e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.15 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELplAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTlRSRISI 1230
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1231 IPQDPILFPG-SLRMNLDLLQEhsdeaiWAALETVQLKALVASLP--GQLQYKCADRGEDLSVGQKQLLCLARALLRKTQ 1307
Cdd:PRK13537 85 VPQFDNLDPDfTVRENLLVFGR------YFGLSAAAARALVPPLLefAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 1308 ILILDEATAAVDPGTELQMQAMLGSWFAQC-TVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQLLA 1374
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGkTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1169-1372 |
4.71e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.55 E-value: 4.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1169 QGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAH---VGLHTLRsrISIIPQDPILFPG-SLRM 1244
Cdd:PRK15439 28 KGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARltpAKAHQLG--IYLVPQEPLLFPNlSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1245 NLDL-LQEHSDEaiwaaleTVQLKALVASLPGQLqyKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPG-T 1322
Cdd:PRK15439 106 NILFgLPKRQAS-------MQKMKQLLAALGCQL--DLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAeT 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 1323 EL---QMQAMLGSWFAqctVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQL 1372
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 ... |
1166-1372 |
5.10e-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: 69.96 E-value: 5.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1166 LAVQGVSFKIHAGEKVGIVGRTGAGKSSLasglLRL----QEAAEGGIWIDGVPIAHVGLHtlRSRISIIPQDPILFPG- 1240
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLiagfETPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALFPHl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1241 --------SLRMnLDLLQEHSDEAIWAALETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLARALLRKTQILILD 1312
Cdd:cd03300 88 tvfeniafGLRL-KKLPKAEIKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 1313 EATAAVDPG--TELQ-----MQAMLGSwfaqcTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQL 1372
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 ... |
1151-1367 |
5.32e-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: 69.70 E-value: 5.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELP--LAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTlRSRI 1228
Cdd:cd03266 2 ITADALTKRFRDVKKtvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEA-RRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1229 SIIPQDPILFPG-SLRMNLDLLqehsdeAIWAALETVQLKALVASLPGQLQYK--CADRGEDLSVGQKQLLCLARALLRK 1305
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYF------AGLYGLKGDELTARLEELADRLGMEelLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 1306 TQILILDEATAAVD-PGTELQMQAMLGSWFAQCTVLLIAHRLRSVMD-CARVLVMDKGQVAESG 1367
Cdd:cd03266 155 PPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
532-728 |
6.06e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 70.43 E-value: 6.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAYVPQEAWV-QNTSVVENV 597
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTpEGITVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 598 CFGQEldpPWL-----------ERVLEACAlQPDVDSFPEGIHTSigeqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPL 666
Cdd:PRK11231 98 AYGRS---PWLslwgrlsaednARVNQAME-QTRINHLADRRLTD-------LSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 667 AALDahvgqhvFNQVIGPGGLL-----QGTTRILVthaLHILPQA----DWIIVLANGAIAEMGSYQELLQ 728
Cdd:PRK11231 167 TYLD-------INHQVELMRLMrelntQGKTVVTV---LHDLNQAsrycDHLVVLANGHVMAQGTPEEVMT 227
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
519-670 |
6.53e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.43 E-value: 6.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 519 SATFAWSQesppCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGEL-------SKVEGF---VSIEGAVA-------- 580
Cdd:PRK09984 11 AKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdksagSHIELLgrtVQREGRLArdirksra 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 581 ---YVPQE-AWVQNTSVVENVCFGQELDPP-------WLERVLEACALQPDVDSfpeGIHTSIGEQGMNLSGGQKQRLSL 649
Cdd:PRK09984 87 ntgYIFQQfNLVNRLSVLENVLIGALGSTPfwrtcfsWFTREQKQRALQALTRV---GMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180
....*....|....*....|.
gi 1199277034 650 ARAVYRKAAVYLLDDPLAALD 670
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLD 184
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1167-1372 |
7.32e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 72.74 E-value: 7.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLA---SGLLRlqeAAEGGIWIDGVPIAHVG-LHTLRSRISIIPQDPILFP--- 1239
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMkilSGVYQ---PDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPnls 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1240 -------GSLRMNLDLLQehsdeaiWAALETvQLKALVASLpgQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILD 1312
Cdd:COG1129 96 vaeniflGREPRRGGLID-------WRAMRR-RARELLARL--GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 1313 EATAAVDPG---------TELQmqamlgswfAQ-CTVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQL 1372
Cdd:COG1129 166 EPTASLTEReverlfriiRRLK---------AQgVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
532-734 |
7.72e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 70.82 E-value: 7.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIE--------------------GAVAYVPQEAWVQNT 591
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGervitagkknkklkplrkkvGIVFQFPEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 592 sVVENVCFG------QELDPpwLERVLEACALqpdVDSFPEGIHTSIGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDP 665
Cdd:PRK13634 103 -VEKDICFGpmnfgvSEEDA--KQKAREMIEL---VGLPEELLARSPFE----LSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 666 LAALDAHvGQH----VFNQVIGPGGLlqgtTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELLQRKGALV 734
Cdd:PRK13634 173 TAGLDPK-GRKemmeMFYKLHKEKGL----TTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADPDELE 241
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1151-1381 |
7.99e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 70.60 E-value: 7.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISI 1230
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1231 I---PQDPILFP--------GSLRMNLDllQEHSDEAIWAALETVQLKALVASLPgqlqykcadrgEDLSVGQKQLLCLA 1299
Cdd:PRK13652 83 VfqnPDDQIFSPtveqdiafGPINLGLD--EETVAHRVSSALHMLGLEELRDRVP-----------HHLSGGEKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1300 RALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCAR-VLVMDKGQVAESGSPAQLLAQK 1376
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMADyIYVMDKGRIVAYGTVEEIFLQP 229
|
....*
gi 1199277034 1377 GLFYR 1381
Cdd:PRK13652 230 DLLAR 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
532-726 |
8.63e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 72.36 E-value: 8.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------------VAYVPQE-AWVQNTSVVEN 596
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvrfrsprdaqaagIAIIHQElNLVPNLSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 597 VCFGQELDPPWL-------ERVLEACA-LQPDVDsfPegiHTSIGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAA 668
Cdd:COG1129 100 IFLGREPRRGGLidwramrRRARELLArLGLDID--P---DTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 669 LDAHVGQHVFNQVigpgGLL--QGTTRILVTHALH-ILPQADWIIVLANGAIAEMGSYQEL 726
Cdd:COG1129 171 LTEREVERLFRII----RRLkaQGVAIIYISHRLDeVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
515-734 |
1.09e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 70.04 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVaYVPQEAW------- 587
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV-LSEETVWdvrrqvg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 588 --VQN-------TSVVENVCFGQELD----PPWLERVLEACAlQPDVDSFPEgihtsigEQGMNLSGGQKQRLSLARAVY 654
Cdd:PRK13635 85 mvFQNpdnqfvgATVQDDVAFGLENIgvprEEMVERVDQALR-QVGMEDFLN-------REPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 655 RKAAVYLLDDPLAALDAHVGQHVFNQVigpgGLL---QGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKG 731
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETV----RQLkeqKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGH 232
|
...
gi 1199277034 732 ALV 734
Cdd:PRK13635 233 MLQ 235
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
534-670 |
1.12e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.83 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 534 RINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEgavayVPQEAWVQNTSVVEnvCFGQELDPPWLERVLE 613
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----VPDNQFGREASLID--AIGRKGDFKDAVELLN 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 614 ACALqpdVD------SFPEgihtsigeqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 670
Cdd:COG2401 121 AVGL---SDavlwlrRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1168-1363 |
1.12e-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: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1168 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAA-EGGIWIDGVPIA-HVGLHTLRSRISIIPQD-------PILF 1238
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDiRNPAQAIRAGIAMVPEDrkrhgivPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1239 PG-----------SLRMNLDLLQEhsDEAIWAALETVQLKALVASLPGQlqykcadrgeDLSVGQKQLLCLARALLRKTQ 1307
Cdd:TIGR02633 356 VGknitlsvlksfCFKMRIDAAAE--LQIIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNPR 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 1308 ILILDEATAAVDPGTELQMQAMLGSWFAQ-CTVLLIAHRLRSVMDCA-RVLVMDKGQV 1363
Cdd:TIGR02633 424 VLILDEPTRGVDVGAKYEIYKLINQLAQEgVAIIVVSSELAEVLGLSdRVLVIGEGKL 481
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1168-1376 |
1.40e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.15 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1168 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTlRSR--ISIIPQDPILFP------ 1239
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA-RARrgIGYLPQEASIFRrlsvyd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1240 ---GSLRMNLDLLQEHSDEAIWAALETVQLKALVASLpgqlqykcadrGEDLSVGQKQLLCLARALLRKTQILILDEATA 1316
Cdd:PRK10895 98 nlmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 1317 AVDPGTELQMQAMLGSWF-AQCTVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQLLAQK 1376
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
515-715 |
1.51e-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: 66.32 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWsqESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--VAYVPQeawvqnts 592
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTvkIGYFEQ-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 593 vvenvcfgqeldppwlervleacalqpdvdsfpegihtsigeqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAH 672
Cdd:cd03221 71 ----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1199277034 673 vGQHVFNQVIG--PGGLlqgttrILVTHALHILPQ-ADWIIVLANG 715
Cdd:cd03221 105 -SIEALEEALKeyPGTV------ILVSHDRYFLDQvATKIIELEDG 143
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1159-1363 |
2.13e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.94 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1159 RYRPELPLAVQGVS-------------FKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPiahvgLHTLR 1225
Cdd:PRK11247 6 RLNQGTPLLLNAVSkrygertvlnqldLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAP-----LAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1226 SRISIIPQDPILFP-GSLRMNLDL-LQEHSDEAIWAALETVQLkalvaslpgqlqykcADRGED----LSVGQKQLLCLA 1299
Cdd:PRK11247 81 EDTRLMFQDARLLPwKKVIDNVGLgLKGQWRDAALQALAAVGL---------------ADRANEwpaaLSGGQKQRVALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199277034 1300 RALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQV 1363
Cdd:PRK11247 146 RALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhgFTVLLVTHDVSEAVAMAdRVLLIEEGKI 212
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
532-717 |
2.23e-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: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGavayvpqEAWVQNTSVVENVcfGQELDPPWL--- 608
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG-------KSYQKNIEALRRI--GALIEAPGFypn 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 609 ---ERVLEACALQPDVDSfpEGIHTSIGEQGM---------NLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDahvgqh 676
Cdd:cd03268 87 ltaRENLRLLARLLGIRK--KRIDEVLDVVGLkdsakkkvkGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD------ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 677 vfnqvigPGGLL-----------QGTTRILVTHALHILPQ-ADWIIVLANGAI 717
Cdd:cd03268 159 -------PDGIKelrelilslrdQGITVLISSHLLSEIQKvADRIGIINKGKL 204
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
832-1121 |
2.34e-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: 69.13 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 832 LCLYALFLFLCQQVASFCRGYWLSLWaddpavgGQQTQAALRggifgllgclqaiglfasmaavllggarasRLLFQRLL 911
Cdd:cd18557 38 LALILLAIYLLQSVFTFVRYYLFNIA-------GERIVARLR------------------------------RDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 912 wdvvRSPISFFERTPIGHLLNRFSKET----DTVDVDIPDKLRSLLMYAFGLLeVSLVVAVATPLATVAILPLFLLYAGF 987
Cdd:cd18557 81 ----RQEIAFFDKHKTGELTSRLSSDTsvlqSAVTDNLSQLLRNILQVIGGLI-ILFILSWKLTLVLLLVIPLLLIASKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 988 QSLYVVsscQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANVELLGNG 1067
Cdd:cd18557 156 YGRYIR---KLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 1068 LVFAAATCA---VLSKaHLSAG-LVGFSVsAALQVTQTLQWVVRNWTDLENSIVSVER 1121
Cdd:cd18557 233 SLLLVLWYGgylVLSG-QLTVGeLTSFIL-YTIMVASSVGGLSSLLADIMKALGASER 288
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1167-1372 |
2.36e-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: 70.13 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLasglLR----LQEAAEGGIWIDGVPIAHVGLHtlRSRISIIPQDPILFP--- 1239
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTL----LRmiagFETPDSGRILLDGRDVTGLPPE--KRNVGMVFQDYALFPhlt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1240 -------GsLRMnldllQEHSDEAIWA----ALETVQLKALVASLPGQLqykcadrgedlSVGQKQllclarallrktQI 1308
Cdd:COG3842 94 vaenvafG-LRM-----RGVPKAEIRArvaeLLELVGLEGLADRYPHQL-----------SGGQQQrvalaralapepRV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 1309 LILDEATAAVDPGTELQMQAMLGSWFAQC--TVLLIAHRLR---SVMDcaRVLVMDKGQVAESGSPAQL 1372
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHDQEealALAD--RIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1167-1372 |
2.39e-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: 68.13 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVglhTLRSR-ISIIPQDPILF------- 1238
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV---PVQERnVGFVFQHYALFrhmtvfd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1239 ---------PGSLRMNLDLLQEHSDEaiwaALETVQLKALVASLPGQlqykcadrgedLSVGQKQLLCLARALLRKTQIL 1309
Cdd:cd03296 94 nvafglrvkPRSERPPEAEIRAKVHE----LLKLVQLDWLADRYPAQ-----------LSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1310 ILDEATAAVDPgtelQMQAMLGSWFAQ------CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQL 1372
Cdd:cd03296 159 LLDEPFGALDA----KVRKELRRWLRRlhdelhVTTVFVTHDQEEALEVAdRVVVMNKGRIEQVGTPDEV 224
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1167-1375 |
2.60e-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: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHT---------LRSRISIIPQdpIL 1237
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpeergLYPKMKVGEQ--LV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1238 FPGSLR-MNLDLLQEHSDEaiWaaLETVQLKAlvaslpgqlqYKcADRGEDLSVGQKQllclarallrKTQI-------- 1308
Cdd:COG4152 94 YLARLKgLSKAEAKRRADE--W--LERLGLGD----------RA-NKKVEELSKGNQQ----------KVQLiaallhdp 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 1309 --LILDEATAAVDP-GTELQMQAML-----GSwfaqcTVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQLLAQ 1375
Cdd:COG4152 149 elLILDEPFSGLDPvNVELLKDVIRelaakGT-----TVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1162-1380 |
2.71e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 68.86 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1162 PELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLA---SGLLRLQEaaeGGIWIDGVPIAHVG-LHTLRSRISIIPQDP-I 1236
Cdd:PRK13644 12 PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLAlhlNGLLRPQK---GKVLVSGIDTGDFSkLQGIRKLVGIVFQNPeT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1237 LFPGslRMNLDLLQEHSDEAIWAALETVQL--KALVASLPGQLQYKCAdrgEDLSVGQKQLLCLARALLRKTQILILDEA 1314
Cdd:PRK13644 89 QFVG--RTVEEDLAFGPENLCLPPIEIRKRvdRALAEIGLEKYRHRSP---KTLSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199277034 1315 TAAVDPGTELQMQAMLGSWFAQC-TVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFY 1380
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQT 230
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
530-729 |
2.84e-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: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 530 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVayV----PQE---AWV-QN------TSVVE 595
Cdd:PRK11650 18 QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRV--VnelePADrdiAMVfQNyalyphMSVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 596 NVCFG--------QELDppwlERVLEACA---LQPDVDSFPegihtsigeqgMNLSGGQKQRLSLARAVYRKAAVYLLDD 664
Cdd:PRK11650 96 NMAYGlkirgmpkAEIE----ERVAEAARileLEPLLDRKP-----------RELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 665 PLAALDAHvgqhvfnqvigpggL----------LQ---GTTRILVTH-ALHILPQADWIIVLANGAIAEMGSYQELLQR 729
Cdd:PRK11650 161 PLSNLDAK--------------LrvqmrleiqrLHrrlKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEVYEK 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
515-729 |
2.99e-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: 68.10 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSqESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------AVAY 581
Cdd:cd03295 1 IEFENVTKRYG-GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 582 VPQEAWV-QNTSVVENVcfgqELDPPWL--------ERVLEACALqpdVDSFPEGIHTSIGEQgmnLSGGQKQRLSLARA 652
Cdd:cd03295 80 VIQQIGLfPHMTVEENI----ALVPKLLkwpkekirERADELLAL---VGLDPAEFADRYPHE---LSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 653 VYRKAAVYLLDDPLAALDAHVGQHVFNQVIGpgglLQ---GTTRILVTH----ALHIlpqADWIIVLANGAIAEMGSYQE 725
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKR----LQqelGKTIVFVTHdideAFRL---ADRIAIMKNGEIVQVGTPDE 222
|
....
gi 1199277034 726 LLQR 729
Cdd:cd03295 223 ILRS 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1168-1349 |
3.32e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 68.52 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1168 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAaEGGIWIDG--------VPIAHVGLHTLRSRISIIPQDPILFP 1239
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGrveffnqnIYERRVNLNRLRRQVSMVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1240 GSLRMNL----DLLQEHSDEAIWAALETVqLKAlvASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEAT 1315
Cdd:PRK14258 102 MSVYDNVaygvKIVGWRPKLEIDDIVESA-LKD--ADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPC 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 1199277034 1316 AAVDPGTELQMQAMLGSWF--AQCTVLLIAHRLRSV 1349
Cdd:PRK14258 179 FGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQV 214
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
532-726 |
3.46e-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: 67.49 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVP---QEAWVQNTSVVenvcfgqeldpPWL 608
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpdRMVVFQNYSLL-----------PWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 609 ErVLEACALQPD--VDSFPEGIHTSIGEQGMNL--------------SGGQKQRLSLARAVYRKAAVYLLDDPLAALDAH 672
Cdd:TIGR01184 70 T-VRENIALAVDrvLPDLSKSERRAIVEEHIALvglteaadkrpgqlSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 673 VGQHVFNQvigpggLLQ-----GTTRILVTHAL-HILPQADWIIVLANGAIAEMGSYQEL 726
Cdd:TIGR01184 149 TRGNLQEE------LMQiweehRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1168-1373 |
3.63e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 68.26 E-value: 3.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1168 VQGVSFKIHAGEKVGIVGRTGAGKSSlasgLLRL----QEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPIL-FPGSL 1242
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKST----LLRAlsgeLSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1243 -------RMNLDLLQEHSDEAIWAALETVQLKALvaslpgqlqykcADRG-EDLSVGQKQ------LLCLARALLRKTQI 1308
Cdd:PRK13548 94 eevvamgRAPHGLSRAEDDALVAAALAQVDLAHL------------AGRDyPQLSGGEQQrvqlarVLAQLWEPDGPPRW 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 1309 LILDEATAAVDPGTELQMQAMLGSwFAQ---CTVLLIAHRLR-SVMDCARVLVMDKGQVAESGSPAQLL 1373
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQ-LAHergLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
532-730 |
4.71e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.22 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQEAWVQN---------------TSVVEN 596
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSkvglvfqdpddqvfsSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 597 VCFG---QELDPPWLERVLEACALQPDVDSFPEgihtsigEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHv 673
Cdd:PRK13647 101 VAFGpvnMGLDKDEVERRVEEALKAVRMWDFRD-------KPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR- 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 674 GQHVFNQVIgpGGL-LQGTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELLQRK 730
Cdd:PRK13647 173 GQETLMEIL--DRLhNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
532-727 |
5.48e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 67.76 E-value: 5.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQEAW--------------------VQNT 591
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFqidaiklrkevgmvfqqpnpFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 592 SVVENVCFGQEL----DPPWLERVLEACALQpdVDSFPEgIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLA 667
Cdd:PRK14246 106 SIYDNIAYPLKShgikEKREIKKIVEECLRK--VGLWKE-VYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 668 ALDAhVGQHVFNQVIGPggLLQGTTRILVTHAlhilPQ-----ADWIIVLANGAIAEMGSYQELL 727
Cdd:PRK14246 183 MIDI-VNSQAIEKLITE--LKNEIAIVIVSHN----PQqvarvADYVAFLYNGELVEWGSSNEIF 240
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1167-1375 |
6.75e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 68.45 E-value: 6.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIA---HVGLHTLRSRISIIPQDPI--LFP-- 1239
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNPYgsLNPrk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1240 --GS-----LRMNLDLLQEHSDEAIWAALETVQLKAlvaslpgqlqyKCADRGEDL-SVGQKQLLCLARALLRKTQILIL 1311
Cdd:PRK11308 110 kvGQileepLLINTSLSAAERREKALAMMAKVGLRP-----------EHYDRYPHMfSGGQRQRIAIARALMLDPDVVVA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 1312 DEATAAVDPGTELQ-------MQAMLGSWFaqctvLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQ 1375
Cdd:PRK11308 179 DEPVSALDVSVQAQvlnlmmdLQQELGLSY-----VFISHDLSVVEHIAdEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1150-1358 |
7.58e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.44 E-value: 7.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1150 QIEFRDFGLRYRPELPLAV-QGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWI-DGVPIAHVGLHTLRSR 1227
Cdd:PTZ00265 382 KIQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1228 ISIIPQDPILFPGSLRMN----------LDLLQEHSDEAIWAALE----------------------------------- 1262
Cdd:PTZ00265 462 IGVVSQDPLLFSNSIKNNikyslyslkdLEALSNYYNEDGNDSQEnknkrnscrakcagdlndmsnttdsneliemrkny 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1263 ---------TVQLKAL----VASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAM 1329
Cdd:PTZ00265 542 qtikdsevvDVSKKVLihdfVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
|
250 260 270
....*....|....*....|....*....|.
gi 1199277034 1330 LGSWFAQCT--VLLIAHRLRSVMDCARVLVM 1358
Cdd:PTZ00265 622 INNLKGNENriTIIIAHRLSTIRYANTIFVL 652
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1151-1373 |
8.24e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 66.65 E-value: 8.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELPLavQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPI--AHVGLHTLRSRI 1228
Cdd:PRK09493 2 IEFKNVSKHFGPTQVL--HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1229 SIIPQDPILFP----------GSLRMNLDLLQEHSDEAIwAALETVQLKALVASLPGQlqykcadrgedLSVGQKQLLCL 1298
Cdd:PRK09493 80 GMVFQQFYLFPhltalenvmfGPLRVRGASKEEAEKQAR-ELLAKVGLAERAHHYPSE-----------LSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1299 ARALLRKTQILILDEATAAVDPgtELQ------MQAMlgswfAQ--CTVLLIAHRL---RSVmdCARVLVMDKGQVAESG 1367
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDP--ELRhevlkvMQDL-----AEegMTMVIVTHEIgfaEKV--ASRLIFIDKGRIAEDG 218
|
....*.
gi 1199277034 1368 SPAQLL 1373
Cdd:PRK09493 219 DPQVLI 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1151-1375 |
1.15e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.07 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELPLAVQG---VSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG----LHT 1223
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRAlfdIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1224 LRSRISIIPQdpilFPGSLRMNLDLLQE----------HSDEAIWAALETVQLKALVASLPGQLQYkcadrgeDLSVGQK 1293
Cdd:PRK13643 82 VRKKVGVVFQ----FPESQLFEETVLKDvafgpqnfgiPKEKAEKIAAEKLEMVGLADEFWEKSPF-------ELSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1294 QLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQC-TVLLIAHRLRSVMDCAR-VLVMDKGQVAESGSPAQ 1371
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGqTVVLVTHLMDDVADYADyVYLLEKGHIISCGTPSD 230
|
....
gi 1199277034 1372 LLAQ 1375
Cdd:PRK13643 231 VFQE 234
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1167-1363 |
1.16e-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: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSL---ASGLLRLQEaaeGGIWIDGVPIAHVGLHTlRSR-ISIIPQDPIL--FPG 1240
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLlnaIAGSLPPDS---GSILIDGKDVTKLPEYK-RAKyIGRVFQDPMMgtAPS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1241 -------SL------RMNLDLLQEHSDEAiwaaletvQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQ 1307
Cdd:COG1101 97 mtieenlALayrrgkRRGLRRGLTKKRRE--------LFRELLATLGLGLENRLDTKVGLLSGGQRQALSLLMATLTKPK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 1308 ILILDEATAAVDPGT-----ELQMQAMLGSwfaQCTVLLIAHRLRSVMDCA-RVLVMDKGQV 1363
Cdd:COG1101 169 LLLLDEHTAALDPKTaalvlELTEKIVEEN---NLTTLMVTHNMEQALDYGnRLIMMHEGRI 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
535-726 |
1.21e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 68.32 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYVP-----------QEAWVQNTSVVENVCFGQE 602
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdLSHVPpyqrpinmmfqSYALFPHMTVEQNIAFGLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 603 LDP-PWLE---RVLEACALqpdvdsfpegIHTS--IGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQH 676
Cdd:PRK11607 118 QDKlPKAEiasRVNEMLGL----------VHMQefAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDR 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 677 VFNQVIgpgGLLQ--GTTRILVTH-ALHILPQADWIIVLANGAIAEMGSYQEL 726
Cdd:PRK11607 188 MQLEVV---DILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
512-665 |
1.39e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.55 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 512 KDCITIHSATFAWsqESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIeGA---VAYVPQEawv 588
Cdd:COG0488 313 KKVLELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GEtvkIGYFDQH--- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 589 qntsvvenvcfGQELDPPWleRVLEA-CALQPDVD---------SF---PEGIHTSIGeqgmNLSGGQKQRLSLARAVYR 655
Cdd:COG0488 387 -----------QEELDPDK--TVLDElRDGAPGGTeqevrgylgRFlfsGDDAFKPVG----VLSGGEKARLALAKLLLS 449
|
170
....*....|
gi 1199277034 656 KAAVYLLDDP 665
Cdd:COG0488 450 PPNVLLLDEP 459
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
532-727 |
1.89e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 66.01 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-AVAY------------VPQEAwvqNTSVVENVC 598
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhKLEYgdykyrckhirmIFQDP---NTSLNPRLN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 599 FGQELDPPWL-----------ERV---LEACALQPDVDSFPegIHTsigeqgmnLSGGQKQRLSLARAVYRKAAVYLLDD 664
Cdd:COG4167 106 IGQILEEPLRlntdltaeereERIfatLRLVGLLPEHANFY--PHM--------LSSGQKQRVALARALILQPKIIIADE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 665 PLAALDAHVGQHVFNqvigpggLL------QGTTRILVTHAL----HIlpqADWIIVLANGAIAEMGSYQELL 727
Cdd:COG4167 176 ALAALDMSVRSQIIN-------LMlelqekLGISYIYVSQHLgivkHI---SDKVLVMHQGEVVEYGKTAEVF 238
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
532-717 |
2.08e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 68.60 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSaLLGELSK-VEGFVSIEG---------AVAYVPQEAW---VQNTSVVENVC 598
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKpTSGTYRVAGqdvatldadALAQLRREHFgfiFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 599 FGQELDPPWL-------ERVLEACALQPDVdsfpeGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDA 671
Cdd:PRK10535 103 AAQNVEVPAVyaglerkQRLLRAQELLQRL-----GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 672 HVGQHVFNqvigpggLL-----QGTTRILVTHALHILPQADWIIVLANGAI 717
Cdd:PRK10535 178 HSGEEVMA-------ILhqlrdRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
515-730 |
2.16e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 66.17 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVayVPQEAW------- 587
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGIT--ISKENLkeirkki 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 588 ---VQN-------TSVVENVCFGQE---LDPPWLERVLEACALQPDVDSFpegihtsIGEQGMNLSGGQKQRLSLARAVY 654
Cdd:PRK13632 86 giiFQNpdnqfigATVEDDIAFGLEnkkVPPKKMKDIIDDLAKKVGMEDY-------LDKEPQNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 655 RKAAVYLLDDPLAALDAHvGQHVFNQVIGPgglLQGT---TRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRK 730
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPK-GKREIKKIMVD---LRKTrkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
532-728 |
2.24e-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: 66.13 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-AVAYVPQEAWVQ-----------------NTSV 593
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqDIAAMSRKELRElrrkkismvfqsfallpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 594 VENVCFGQELDP-PWLER------VLEACALQPDVDSFPegihtsiGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPL 666
Cdd:cd03294 120 LENVAFGLEVQGvPRAEReeraaeALELVGLEGWEHKYP-------DE----LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 667 AALDAHVGQHVFNQVIGPGGLLQGTTrILVTH----ALHIlpqADWIIVLANGAIAEMGSYQELLQ 728
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAELQKTI-VFITHdldeALRL---GDRIAIMKDGRLVQVGTPEEILT 250
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
515-716 |
2.56e-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: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAwSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSI--EGAVAYVPQEAWVQNTS 592
Cdd:cd03223 1 IELENLSLA-TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpeGEDLLFLPQRPYLPLGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 593 VVENVCFgqeldpPWlervleacalqpdvdsfpegihtsigeqGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAH 672
Cdd:cd03223 80 LREQLIY------PW----------------------------DDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1199277034 673 VGQHVFNQVigpggLLQGTTRILVTHALHILPQADWIIVLANGA 716
Cdd:cd03223 126 SEDRLYQLL-----KELGITVISVGHRPSLWKFHDRVLDLDGEG 164
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
527-717 |
3.01e-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: 65.05 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 527 ESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQEAWVQNTSVVenvcFGQELDPP 606
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVV----FGQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 607 WLERVLEACALQPDVDSFPEGIHTS----------IGE----QGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAh 672
Cdd:cd03267 108 WDLPVIDSFYLLAAIYDLPPARFKKrldelselldLEElldtPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV- 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1199277034 673 VGQHVFNQVIGPGGLLQGTTRILVTHALH-ILPQADWIIVLANGAI 717
Cdd:cd03267 187 VAQENIRNFLKEYNRERGTTVLLTSHYMKdIEALARRVLVIDKGRL 232
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1132-1365 |
3.94e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 67.30 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1132 APWR--LPTCAAQPPWPQggqIEFRDFGLRYrPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGI 1209
Cdd:PRK10522 305 APYKaeFPRPQAFPDWQT---LELRNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1210 WIDGVPIAHVGLHTLRSRISIIPQDPILFPgslRMNLDLLQEHSDEAIWAALETVQLKALVASLPGQLqykcadRGEDLS 1289
Cdd:PRK10522 381 LLDGKPVTAEQPEDYRKLFSAVFTDFHLFD---QLLGPEGKPANPALVEKWLERLKMAHKLELEDGRI------SNLKLS 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1290 VGQKQLLCLARALLRKTQILILDEATAAVDPG------TEL--QMQAMlGSwfaqcTVLLIAHRLRSVMDCARVLVMDKG 1361
Cdd:PRK10522 452 KGQKKRLALLLALAEERDILLLDEWAADQDPHfrrefyQVLlpLLQEM-GK-----TIFAISHDDHYFIHADRLLEMRNG 525
|
....
gi 1199277034 1362 QVAE 1365
Cdd:PRK10522 526 QLSE 529
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
532-665 |
5.23e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.01 E-value: 5.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--VAYVPQEA-WVQNTSVVENVCFG-QELDpPW 607
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGlrIGYLPQEPpLDDDLTVLDTVLDGdAELR-AL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 608 LERVLEACALQPDVDSFPE----------------------------GIHTSIGEQGM-NLSGGQKQRLSLARAVYRKAA 658
Cdd:COG0488 93 EAELEELEAKLAEPDEDLErlaelqeefealggweaearaeeilsglGFPEEDLDRPVsELSGGWRRRVALARALLSEPD 172
|
....*..
gi 1199277034 659 VYLLDDP 665
Cdd:COG0488 173 LLLLDEP 179
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
532-725 |
5.82e-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: 5.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYVPQEAWV--------QNT------SVVEN 596
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRdITGLPPHRIArlgiartfQNPrlfpelTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 597 V----------CFGQELDPPWL------------ERVLEACALQPDVDsfpegihtsigEQGMNLSGGQKQRLSLARAVY 654
Cdd:COG0411 100 VlvaaharlgrGLLAALLRLPRarreereareraEELLERVGLADRAD-----------EPAGNLSYGQQRRLEIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 655 RKAAVYLLDDPLAALDAHVGQHVfnqvigpGGLLQ------GTTRILVTHALHILPQ-ADWIIVLANGA-IAEmGSYQE 725
Cdd:COG0411 169 TEPKLLLLDEPAAGLNPEETEEL-------AELIRrlrderGITILLIEHDMDLVMGlADRIVVLDFGRvIAE-GTPAE 239
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1164-1363 |
7.13e-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: 62.45 E-value: 7.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1164 LPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHT-LRSRISIIPQDPI---LFP 1239
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDRKregLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1240 G-SLRMNLDLlqehsdeaiwaaleTVQL------KALVAslpgqlqyKCADRGedlsvgqkqllclarallrkTQILILD 1312
Cdd:cd03215 92 DlSVAENIAL--------------SSLLsggnqqKVVLA--------RWLARD--------------------PRVLILD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 1313 EATAAVDPGTELQMQAMLGSwFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQV 1363
Cdd:cd03215 130 EPTRGVDVGAKAEIYRLIRE-LADagKAVLLISSELDELLGLCdRILVMYEGRI 182
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
532-700 |
7.18e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 64.03 E-value: 7.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSAL--LGELS---KVEGFVSIEGAVAYVPQEAWVQ---------------NT 591
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNpevTITGSIVYNGHNIYSPRTDTVDlrkeigmvfqqpnpfPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 592 SVVENVCFGQEL----DPPWLERVLEACALQPDV-DSFPEGIHTSigeqGMNLSGGQKQRLSLARAVYRKAAVYLLDDPL 666
Cdd:PRK14239 101 SIYENVVYGLRLkgikDKQVLDEAVEKSLKGASIwDEVKDRLHDS----ALGLSGGQQQRVCIARVLATSPKIILLDEPT 176
|
170 180 190
....*....|....*....|....*....|....
gi 1199277034 667 AALDAHVGQHVFNQVIgpgGLLQGTTRILVTHAL 700
Cdd:PRK14239 177 SALDPISAGKIEETLL---GLKDDYTMLLVTRSM 207
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1167-1375 |
8.48e-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: 8.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSL---ASGLLrlqEAAEGGIWIDG---VPIAH-VGLH---TLRsrisiipqDPI 1236
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLlklIAGIL---EPTSGRVEVNGrvsALLELgAGFHpelTGR--------ENI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1237 LFPGS-LRMNLDLLQEHSDEAIW-AALE--------------TVQLK-ALVASLPgqlqykcADrgedlsvgqkqllcla 1299
Cdd:COG1134 110 YLNGRlLGLSRKEIDEKFDEIVEfAELGdfidqpvktyssgmRARLAfAVATAVD-------PD---------------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1300 rallrktqILILDEATAAVDPgtELQ------MQAMLGSwfaQCTVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQL 1372
Cdd:COG1134 167 --------ILLVDEVLAVGDA--AFQkkclarIRELRES---GRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEV 233
|
...
gi 1199277034 1373 LAQ 1375
Cdd:COG1134 234 IAA 236
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1168-1374 |
9.39e-11 |
|
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: 9.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1168 VQGVSFKIHAGEKVGIVGRTGAGKS---SLASGLLRlqeAAEGGIWIDGVPIAHVGLHtLRSR--ISIIPQDPILFPG-S 1241
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTttfYMIVGLVK---PDSGRIFLDGEDITHLPMH-KRARlgIGYLPQEASIFRKlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1242 LRMNldllqehsdeaIWAALETVQL-----KALVASLPGQLQ-YKCAD-RGEDLSVGQKQllclarallrKTQI------ 1308
Cdd:COG1137 95 VEDN-----------ILAVLELRKLskkerEERLEELLEEFGiTHLRKsKAYSLSGGERR----------RVEIaralat 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 1309 ----LILDEATAAVDPGTELQMQAM--------LGswfaqctVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQLLA 1374
Cdd:COG1137 154 npkfILLDEPFAGVDPIAVADIQKIirhlkergIG-------VLITDHNVRETLGiCDRAYIISEGKVLAEGTPEEILN 225
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
532-706 |
9.39e-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: 9.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQEAWVQNT-------------SVVENVC 598
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLlylghapgikttlSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 599 FgqeldppWlervleaCALQPDvdsfpEGIHTSIGEQGMN---------LSGGQKQRLSLARAVYRKAAVYLLDDPLAAL 669
Cdd:cd03231 96 F-------W-------HADHSD-----EQVEEALARVGLNgfedrpvaqLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 1199277034 670 DAHvGQHVFNQVIGpGGLLQGTTRILVTHalHILPQA 706
Cdd:cd03231 157 DKA-GVARFAEAMA-GHCARGGMVVLTTH--QDLGLS 189
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
532-727 |
9.84e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 63.62 E-value: 9.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSA--LLGELS----KVeGFVSIEGAVAYVPQEAWV-----------QN---- 590
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCinLLEQPEagtiRV-GDITIDTARSLSQQKGLIrqlrqhvgfvfQNfnlf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 591 --TSVVENVCFGQEL--DPPWLERVLEACALQPDV------DSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVY 660
Cdd:PRK11264 98 phRTVLENIIEGPVIvkGEPKEEATARARELLAKVglagkeTSYPR-----------RLSGGQQQRVAIARALAMRPEVI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 661 LLDDPLAALDAHVGQHVFNQVigpGGLLQ-GTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELL 727
Cdd:PRK11264 167 LFDEPTSALDPELVGEVLNTI---RQLAQeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALF 232
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1167-1367 |
1.11e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.13 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLrsrISIIPQD-------PILFP 1239
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSeevdwsfPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1240 GSLRMN-------LDLLQEHSDEAIWAALETVQLkalvaslpgqLQYKCADRGEdLSVGQKQLLCLARALLRKTQILILD 1312
Cdd:PRK15056 99 DVVMMGryghmgwLRRAKKRDRQIVTAALARVDM----------VEFRHRQIGE-LSGGQKKRVFLARAIAQQGQVILLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 1313 EATAAVDPGTELQMQAMLGSWFAQ-CTVLLIAHRLRSVMDCARVLVMDKGQVAESG 1367
Cdd:PRK15056 168 EPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
530-727 |
1.13e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 63.85 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 530 PCLHRINLTVPQGCLLAVVGPVGAGKSSL---LSALL--------------GELSKVEGFVSIEGAVAYVPQEAWVQNTs 592
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLalhLNGLLrpqkgkvlvsgidtGDFSKLQGIRKLVGIVFQNPETQFVGRT- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 593 VVENVCFGQE---LDPPWLERVLEACALQPDVDSFPegiHTSigeqGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAAL 669
Cdd:PRK13644 95 VEEDLAFGPEnlcLPPIEIRKRVDRALAEIGLEKYR---HRS----PKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 670 DAHVGQHVFNQVIGPGGllQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELL 727
Cdd:PRK13644 168 DPDSGIAVLERIKKLHE--KGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
535-670 |
1.22e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 63.65 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSAL-----LGELSKVEGFVSIEGAVAYVPQEAWVQ---------------NTSVV 594
Cdd:PRK14243 29 VWLDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYAPDVDPVEvrrrigmvfqkpnpfPKSIY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 595 ENVCFGQ-------ELDPpWLERVLEACALQPDVDSfpegihtSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLA 667
Cdd:PRK14243 109 DNIAYGAringykgDMDE-LVERSLRQAALWDEVKD-------KLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCS 180
|
...
gi 1199277034 668 ALD 670
Cdd:PRK14243 181 ALD 183
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1151-1345 |
1.30e-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: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLrYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLasglLRlqeaAEGGIWidgvPIA--HVGLHTlRSRI 1228
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSL----FR----ALAGLW----PWGsgRIGMPE-GEDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1229 SIIPQDPILFPGSLRmnldllqehsdeaiwaaletvqlkalvaslpGQLQYKCADRgedLSVGQKQLLCLARALLRKTQI 1308
Cdd:cd03223 67 LFLPQRPYLPLGTLR-------------------------------EQLIYPWDDV---LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*..
gi 1199277034 1309 LILDEATAAVDPGTELQMQAMLGSwfAQCTVLLIAHR 1345
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1161-1344 |
1.33e-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: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1161 RPELPLaVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPG 1240
Cdd:TIGR01189 10 RGERML-FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1241 SLRMNLDLLQE-HSDE--AIWAALETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLARALLRKTQILILDEATAA 1317
Cdd:TIGR01189 89 SALENLHFWAAiHGGAqrTIEDALAAVGLTGFEDLPAAQL-----------SAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*...
gi 1199277034 1318 VDP-GTELQMQAMLGSWFAQCTVLLIAH 1344
Cdd:TIGR01189 158 LDKaGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1178-1367 |
1.53e-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: 62.31 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1178 GEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPI----AHVGLHTLRSRISIIPQDPILFPG-SLRMNLDL-LQE 1251
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFPHlNVRENLAFgLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1252 HSDEAIwaaleTVQLKALVASLpgQLQyKCADRGED-LSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAML 1330
Cdd:cd03297 103 KRNRED-----RISVDELLDLL--GLD-HLLNRYPAqLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1199277034 1331 GSWFA--QCTVLLIAHRLRSV-MDCARVLVMDKGQVAESG 1367
Cdd:cd03297 175 KQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
535-725 |
1.65e-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: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYVPQEAWV--------QNT------SVVENV-- 597
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEdITGLPPHEIArlgigrtfQIPrlfpelTVLENVmv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 598 -CFGQELDPPWL--------------ERVLEACALQPDvdsfpegIHTSIGeqgmNLSGGQKQRLSLARAVYRKAAVYLL 662
Cdd:cd03219 99 aAQARTGSGLLLararreereareraEELLERVGLADL-------ADRPAG----ELSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 663 DDPLAALDAHVGQHVfnqvigpGGLL-----QGTTRILVTHALHILPQ-ADWIIVLANGA-IAEmGSYQE 725
Cdd:cd03219 168 DEPAAGLNPEETEEL-------AELIrelreRGITVLLVEHDMDVVMSlADRVTVLDQGRvIAE-GTPDE 229
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
530-726 |
1.69e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 530 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------------VAYVPQEAWV-QNTSVV 594
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLfPNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 595 ENVCFGQELDPPWLERVLE-----ACALQPDVdsfpegihtsigeQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAAL 669
Cdd:PRK15439 105 ENILFGLPKRQASMQKMKQllaalGCQLDLDS-------------SAGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 670 DAHVGQHVFNQVigpGGLL-QGTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQEL 726
Cdd:PRK15439 172 TPAETERLFSRI---RELLaQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
534-698 |
1.71e-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: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 534 RINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQEAWVQNT-------------SVVENVCFg 600
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENIlylghlpglkpelSALENLHF- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 601 qeldppwlervleacaLQPDVDSFPEGIHTSIGEQGMN---------LSGGQKQRLSLARAVYRKAAVYLLDDPLAALDA 671
Cdd:TIGR01189 97 ----------------WAAIHGGAQRTIEDALAAVGLTgfedlpaaqLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180
....*....|....*....|....*..
gi 1199277034 672 HvGQHVFNQVIGpGGLLQGTTRILVTH 698
Cdd:TIGR01189 161 A-GVALLAGLLR-AHLARGGIVLLTTH 185
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
532-721 |
1.91e-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: 62.16 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYV--PQEAWVQNTSVVENVCFG-------QE 602
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLlgLGGGFNPELTGRENIYLNgrllglsRK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 603 LDPPWLERVLEACALqpdvdsfPEGIHTSIGeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVG---QHVFN 679
Cdd:cd03220 118 EIDEKIDEIIEFSEL-------GDFIDLPVK----TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQekcQRRLR 186
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1199277034 680 QVIgpgglLQGTTRILVTHALHILPQ-ADWIIVLANGAIAEMG 721
Cdd:cd03220 187 ELL-----KQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1169-1358 |
2.31e-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: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1169 QGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLDL 1248
Cdd:cd03231 17 SGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1249 LQE-HSDEAIWAALETVQLKALVASLPGQlqykcadrgedLSVGQKQLLCLARALLRKTQILILDEATAAVD-PGTELQM 1326
Cdd:cd03231 97 WHAdHSDEQVEEALARVGLNGFEDRPVAQ-----------LSAGQQRRVALARLLLSGRPLWILDEPTTALDkAGVARFA 165
|
170 180 190
....*....|....*....|....*....|...
gi 1199277034 1327 QAMLGSWFAQCTVLLIAHR-LRSVMDCARVLVM 1358
Cdd:cd03231 166 EAMAGHCARGGMVVLTTHQdLGLSEAGARELDL 198
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
535-725 |
2.32e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 64.13 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAV-----------------AYVPQEAWV-QNTSVVEN 596
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgiclppekrriGYVFQDARLfPHYKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 597 VCFG-QELDPPWLERVLEACALQPDVDSFPegihtsigeqgMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQ 675
Cdd:PRK11144 97 LRYGmAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199277034 676 HVFNqvigpggLLQGTTR-----IL-VTHAL-HILPQADWIIVLANGAIAEMGSYQE 725
Cdd:PRK11144 166 ELLP-------YLERLAReinipILyVSHSLdEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1167-1375 |
2.35e-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: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWI----DGVPIAHVGLhTLRSR----ISIIPQDPILF 1238
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGP-DGRGRakryIGILHQEYDLY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1239 PGslRMNLDLLQehsdEAIWAAL--ETVQLKALVASLPGQLQYKCA----DRGED-LSVGQKQLLCLARALLRKTQILIL 1311
Cdd:TIGR03269 378 PH--RTVLDNLT----EAIGLELpdELARMKAVITLKMVGFDEEKAeeilDKYPDeLSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199277034 1312 DEATAAVDPGTELQM-QAMLGSWFA-QCTVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQLLAQ 1375
Cdd:TIGR03269 452 DEPTGTMDPITKVDVtHSILKAREEmEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1168-1378 |
2.47e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 62.72 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1168 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPG-SLR--- 1243
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRelv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1244 -------MNL-DLLQEHSDEAIWAALETVQLKALvaslpgqlqykcADRG-EDLSVGQKQLLCLARALLRKTQILILDEA 1314
Cdd:PRK11231 98 aygrspwLSLwGRLSAEDNARVNQAMEQTRINHL------------ADRRlTDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 1315 TAAVDPGTELQMQAMLGSWFAQC-TVLLIAHRL-RSVMDCARVLVMDKGQVAESGSPAQLLAQKGL 1378
Cdd:PRK11231 166 TTYLDINHQVELMRLMRELNTQGkTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVMTPGLL 231
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1167-1372 |
2.60e-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: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLasglLR----LQEAAEGGIWIDGVPIAHvgLHTLRSRISIIPQDPILFPG-- 1240
Cdd:COG3839 18 ALKDIDLDIEDGEFLVLLGPSGCGKSTL----LRmiagLEDPTSGEILIGGRDVTD--LPPKDRNIAMVFQSYALYPHmt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1241 -------SLRMNlDLLQEHSDEAIWAALETVQLKALVASLPGQLqykcadrgedlSVGQKQllclarallRKTQILILDE 1313
Cdd:COG3839 92 vyeniafPLKLR-KVPKAEIDRRVREAAELLGLEDLLDRKPKQL-----------SGGQRQrvalgralvREPKVFLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 1314 ATAAVDPG------TEL-QMQAMLGSwfaqcTVLLIAHRLRSVM---DcaRVLVMDKGQVAESGSPAQL 1372
Cdd:COG3839 160 PLSNLDAKlrvemrAEIkRLHRRLGT-----TTIYVTHDQVEAMtlaD--RIAVMNDGRIQQVGTPEEL 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
530-700 |
2.69e-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: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 530 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG------------AVAYVPQEAWV-QNTSVVEN 596
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldavrqSLGMCPQHNILfHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 597 VCFGQELD-PPWLERVLEACALQPDVdsfpeGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQ 675
Cdd:TIGR01257 1024 ILFYAQLKgRSWEEAQLEMEAMLEDT-----GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180
....*....|....*....|....*
gi 1199277034 676 HVFNQVIgpgGLLQGTTRILVTHAL 700
Cdd:TIGR01257 1099 SIWDLLL---KYRSGRTIIMSTHHM 1120
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
525-726 |
3.49e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 62.41 E-value: 3.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 525 SQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQEAW---------VQN----- 590
Cdd:PRK13633 19 ESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdirnkagmvFQNpdnqi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 591 --TSVVENVCFGQE---LDPPWL-ERV---LEACALQPDVDSFPegiHTsigeqgmnLSGGQKQRLSLARAVYRKAAVYL 661
Cdd:PRK13633 99 vaTIVEEDVAFGPEnlgIPPEEIrERVdesLKKVGMYEYRRHAP---HL--------LSGGQKQRVAIAGILAMRPECII 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 662 LDDPLAALDAHVGQHVFNqVIGPGGLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQEL 726
Cdd:PRK13633 168 FDEPTAMLDPSGRREVVN-TIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
532-727 |
4.21e-10 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 61.64 E-value: 4.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGF-----------VSIE------GAVAYVPQEAWVQNTSVV 594
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgerrggEDVWelrkriGLVSPALQLRFPRDETVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 595 ENVCFG--------QELDPP-------WLERV-LEACALQPdvdsfpegIHTsigeqgmnLSGGQKQRLSLARAVYRKAA 658
Cdd:COG1119 99 DVVLSGffdsiglyREPTDEqrerareLLELLgLAHLADRP--------FGT--------LSQGEQRRVLIARALVKDPE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 659 VYLLDDPLAALDAHvGQHVFNQVIgpGGLLQ--GTTRILVTHALHILPQA-DWIIVLANGAIAEMGSYQELL 727
Cdd:COG1119 163 LLILDEPTAGLDLG-ARELLLALL--DKLAAegAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVL 231
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
532-729 |
4.63e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 62.13 E-value: 4.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-------------VAYVPQEAWVQ--NTSVVEN 596
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfVGLVFQNPDDQifSPTVEQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 597 VCFGQ---ELDPPWLE-RVLEACALQpdvdsfpeGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAH 672
Cdd:PRK13652 100 IAFGPinlGLDEETVAhRVSSALHML--------GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQ 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 673 VGQHVFnQVIGPGGLLQGTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELLQR 729
Cdd:PRK13652 172 GVKELI-DFLNDLPETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
535-726 |
5.39e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.12 E-value: 5.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLS--ALLGELSKVEGFVS---------IEGAVAYVPQE-AWVQNTSVVENVCFGQE 602
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRmiAGLEDITSGDLFIGekrmndvppAERGVGMVFQSyALYPHLSVAENMSFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 603 L---DPPWLERVLEACA--LQPD--VDSFPEGihtsigeqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQ 675
Cdd:PRK11000 102 LagaKKEEINQRVNQVAevLQLAhlLDRKPKA-----------LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 676 HVFNQVigpgGLLQ---GTTRILVTH-ALHILPQADWIIVLANGAIAEMGSYQEL 726
Cdd:PRK11000 171 QMRIEI----SRLHkrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
532-742 |
6.85e-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: 63.28 E-value: 6.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGelskVEGFVSIEGA----VAYVPQEAWVQNTSVVENVC--FGQELDP 605
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRG----MDQYEPTSGRiiyhVALCEKCGYVERPSKVGEPCpvCGGTLEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 606 P----W------------------------------LERVLEAC---------ALQPDVDSFpEGIHTS--IGEQGMNLS 640
Cdd:TIGR03269 92 EevdfWnlsdklrrrirkriaimlqrtfalygddtvLDNVLEALeeigyegkeAVGRAVDLI-EMVQLShrITHIARDLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 641 GGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVIgPGGLLQGTTRILVTHALHILPQ-ADWIIVLANGAIAE 719
Cdd:TIGR03269 171 GGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALE-EAVKASGISMVLTSHWPEVIEDlSDKAIWLENGEIKE 249
|
250 260
....*....|....*....|...
gi 1199277034 720 MGSYQELLQRKGALVCLLDQARQ 742
Cdd:TIGR03269 250 EGTPDEVVAVFMEGVSEVEKECE 272
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
535-726 |
8.09e-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: 8.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG------------AVAYVPQEAWVQNT-SVVENV-CFG 600
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGWENLyIHA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 601 QELDPPWLER------VLEACALQPDVDsfpegihtsigEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVG 674
Cdd:cd03265 99 RLYGVPGAERrerideLLDFVGLLEAAD-----------RLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 675 QHVFnQVIGPGGLLQGTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQEL 726
Cdd:cd03265 168 AHVW-EYIEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
320-715 |
8.77e-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: 8.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 320 LVWIVVCFVylwqLLGpsalTAIAVFLS--LLPLNFfiskkrnhhqEEQMRQKDSRARLTSsILRNSKTIKFHGWEGA-- 395
Cdd:COG4178 184 MVWAALIYA----IIG----TLLTHLIGrpLIRLNF----------EQQRREADFRFALVR-VRENAESIALYRGEAAer 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 396 -----FLDRVLG-----IRGQelgaLRTSGLLFSVSLVSFQVSTFLVALVVFA-------VHTLVAenamnaekAFvtlt 458
Cdd:COG4178 245 rrlrrRFDAVIAnwrrlIRRQ----RNLTFFTTGYGQLAVIFPILVAAPRYFAgeitlggLMQAAS--------AF---- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 459 vlNILNKAQAFLPFSIHSLVQARVSFDRLVTFL-CLEEVDPgVVDSSSSGSAAGKDCITIHSATFAwSQESPPCLHRINL 537
Cdd:COG4178 309 --GQVQGALSWFVDNYQSLAEWRATVDRLAGFEeALEAADA-LPEAASRIETSEDGALALEDLTLR-TPDGRPLLEDLSL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 538 TVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSI--EGAVAYVPQEAWVQNTSVVENVCFGQ---ELDPPWLERVL 612
Cdd:COG4178 385 SLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQRPYLPLGTLREALLYPAtaeAFSDAELREAL 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 613 EACALQPDVDSFPEGIHTSigeqgMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVIgpgGLLQGTT 692
Cdd:COG4178 465 EAVGLGHLAERLDEEADWD-----QVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR---EELPGTT 536
|
410 420
....*....|....*....|...
gi 1199277034 693 RILVTHALHILPQADWIIVLANG 715
Cdd:COG4178 537 VISVGHRSTLAAFHDRVLELTGD 559
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
535-672 |
8.90e-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: 60.36 E-value: 8.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSALLG---ELSKVEGFVSIEGA----------VAYVPQ-EAWVQNTSVVENVCF- 599
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQprkpdqfqkcVAYVRQdDILLPGLTVRETLTYt 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 600 ----------GQELDPPWLERVLEACAlqpdvdsfpegiHTSIGEQGM-NLSGGQKQRLSLARAVYRKAAVYLLDDPLAA 668
Cdd:cd03234 106 ailrlprkssDAIRKKRVEDVLLRDLA------------LTRIGGNLVkGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
....
gi 1199277034 669 LDAH 672
Cdd:cd03234 174 LDSF 177
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1171-1386 |
9.59e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 63.64 E-value: 9.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1171 VSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDgvpiahvglhtlRSrISIIPQDPILFPGSLRMNLDLLQ 1250
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE------------RS-IAYVPQQAWIMNATVRGNILFFD 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1251 EHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGT-ELQMQAM 1329
Cdd:PTZ00243 746 EEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgERVVEEC 825
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199277034 1330 LGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQlLAQKGLFYRLAQES 1386
Cdd:PTZ00243 826 FLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSAD-FMRTSLYATLAAEL 881
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1157-1258 |
1.13e-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: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1157 GLRYRPELPL-AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSR-ISIIPQD 1234
Cdd:COG3845 262 NLSVRDDRGVpALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPED 341
|
90 100
....*....|....*....|....*...
gi 1199277034 1235 PI---LFPG-SLRMNLdLLQEHSDEAIW 1258
Cdd:COG3845 342 RLgrgLVPDmSVAENL-ILGRYRRPPFS 368
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
532-717 |
1.17e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 60.28 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG--------------AVAYVPQEAWV-QNTSVVEN 596
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditdwqtakimreAVAIVPEGRRVfSRMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 597 VCFG-----QELDPPWLERVLeacalqpdvDSFPEgIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDA 671
Cdd:PRK11614 101 LAMGgffaeRDQFQERIKWVY---------ELFPR-LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1199277034 672 HVGQHVFNQVigPGGLLQGTTRILV-THALHILPQADWIIVLANGAI 717
Cdd:PRK11614 171 IIIQQIFDTI--EQLREQGMTIFLVeQNANQALKLADRGYVLENGHV 215
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1166-1355 |
1.39e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 60.57 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1166 LAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQE-----AAEGGIWIDGVPI--AHVGLHTLRSRISIIPQDPILF 1238
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1239 PGSLRMNLDL------LQEHSDEAIWAALETvqlkalvASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILD 1312
Cdd:PRK14243 104 PKSIYDNIAYgaringYKGDMDELVERSLRQ-------AALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1199277034 1313 EATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVmdcARV 1355
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQA---ARV 216
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
512-739 |
1.55e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 60.52 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 512 KDCITIHSATFAWSQESP-PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAvAYVPQEAW--- 587
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-LLTEENVWdir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 588 ------VQN-------TSVVENVCFG--------QELdppwLERVLEACALQpDVDSFPEgihtsigEQGMNLSGGQKQR 646
Cdd:PRK13650 81 hkigmvFQNpdnqfvgATVEDDVAFGlenkgiphEEM----KERVNEALELV-GMQDFKE-------REPARLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 647 LSLARAVYRKAAVYLLDDPLAALDahvgqhvfnqvigPGGLLQ------------GTTRILVTHALHILPQADWIIVLAN 714
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLD-------------PEGRLEliktikgirddyQMTVISITHDLDEVALSDRVLVMKN 215
|
250 260
....*....|....*....|....*.
gi 1199277034 715 GAIAEMGSYQELLQRKGALVCL-LDQ 739
Cdd:PRK13650 216 GQVESTSTPRELFSRGNDLLQLgLDI 241
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
532-728 |
1.59e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 62.37 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSK---VEGFVSIEGAV----------AYVPQ-EAWVQNTSVVENV 597
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPidakemraisAYVQQdDLFIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 598 CFGQEL----DPPWLER------VLEACALQPdvdsfpeGIHTSIGEQGM--NLSGGQKQRLSLARAVYRKAAVYLLDDP 665
Cdd:TIGR00955 121 MFQAHLrmprRVTKKEKrervdeVLQALGLRK-------CANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 666 LAALDAHVGQHVFnQVIgpGGLLQ-GTTRILVTH--ALHILPQADWIIVLANGAIAEMGSYQELLQ 728
Cdd:TIGR00955 194 TSGLDSFMAYSVV-QVL--KGLAQkGKTIICTIHqpSSELFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
541-670 |
1.74e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.13 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 541 QGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQ----------EAWV-QNTSVVENVCFGQEL-DPPWL 608
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQyikpdydgtvEDLLrSITDDLGSSYYKSEIiKPLQL 443
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 609 ERVLEAcalqpDVDsfpegihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 670
Cdd:PRK13409 444 ERLLDK-----NVK---------------DLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
532-726 |
1.95e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 60.09 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYvpqeawvQNTSVVE-----NVCFGQELDP 605
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpIKY-------DKKSLLEvrktvGIVFQNPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 606 PWLERVLEACALQP-----DVDSFPEGIHTSIGEQGM---------NLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDA 671
Cdd:PRK13639 91 LFAPTVEEDVAFGPlnlglSKEEVEKRVKEALKAVGMegfenkpphHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 672 HVGQHVFNqvigpggLL-----QGTTRILVTHALHILP-QADWIIVLANGAIAEMGSYQEL 726
Cdd:PRK13639 171 MGASQIMK-------LLydlnkEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEV 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1152-1326 |
2.10e-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: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1152 EFRDFGLRYRPElPLaVQGVSFKIHAGEKVGIVGRTGAGKSSLAS---GLLRLQEAAEGGIWIDGVPIAHvgLHTLRSRI 1228
Cdd:COG4136 3 SLENLTITLGGR-PL-LAPLSLTVAPGEILTLMGPSGSGKSTLLAaiaGTLSPAFSASGEVLLNGRRLTA--LPAEQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1229 SIIPQDPILFP-----GSLRMNL--DLLQEHSDEAIWAALETVQLKALVASLPGQlqykcadrgedLSVGQKQLLCLARA 1301
Cdd:COG4136 79 GILFQDDLLFPhlsvgENLAFALppTIGRAQRRARVEQALEEAGLAGFADRDPAT-----------LSGGQRARVALLRA 147
|
170 180
....*....|....*....|....*
gi 1199277034 1302 LLRKTQILILDEATAAVDPGTELQM 1326
Cdd:COG4136 148 LLAEPRALLLDEPFSKLDAALRAQF 172
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
532-717 |
2.16e-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: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYVPQE---AWV----QNT--------SVVE 595
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdVTKLPEYkraKYIgrvfQDPmmgtapsmTIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 596 NVC----------FGQELDPPWLERVLEACAlqpdvdSFPEG----IHTSIGeqgmNLSGGQKQRLSLARAVYRKAAVYL 661
Cdd:COG1101 102 NLAlayrrgkrrgLRRGLTKKRRELFRELLA------TLGLGlenrLDTKVG----LLSGGQRQALSLLMATLTKPKLLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 662 LDDPLAALDAHVGQHVF---NQVIGPGGLlqgTTrILVTHALHilpQA----DWIIVLANGAI 717
Cdd:COG1101 172 LDEHTAALDPKTAALVLeltEKIVEENNL---TT-LMVTHNME---QAldygNRLIMMHEGRI 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1167-1375 |
2.40e-09 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 60.93 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLasglLR----LQEAAEGGIWIDGVpIAHVGLHTLRSRISIIPQDPILFP--- 1239
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTL----LRiiagLETPDSGRIVLNGR-DLFTNLPPRERRVGFVFQHYALFPhmt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1240 -------GsLRMnldllQEHSDEAI------WaaLETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLARALLRKT 1306
Cdd:COG1118 92 vaeniafG-LRV-----RPPSKAEIrarveeL--LELVQLEGLADRYPSQL-----------SGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 1307 QILILDEATAAVDPGTELQMQAMLGSWFA--QCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQ 1375
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRRLHDelGGTTVFVTHDQEEALELAdRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
535-715 |
2.84e-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: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA---------VAYVPQE-AWVQNTSVVEN-VCFGQ-- 601
Cdd:cd03269 19 ISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarnrIGYLPEErGLYPKMKVIDQlVYLAQlk 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 602 ---------ELDpPWLERV-LEACALQPDvdsfpegihtsigEQgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDA 671
Cdd:cd03269 99 glkkeearrRID-EWLERLeLSEYANKRV-------------EE---LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1199277034 672 hVGQHVFNQVIGPggLL-QGTTRILVTHAL-HILPQADWIIVLANG 715
Cdd:cd03269 162 -VNVELLKDVIRE--LArAGKTVILSTHQMeLVEELCDRVLLLNKG 204
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1167-1372 |
2.94e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 60.62 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHtlRSRISIIPQDPILFPG-SLRMN 1245
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPINMMFQSYALFPHmTVEQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1246 L--DLLQEHsdeaiwaaLETVQLKALVASLPG--QLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPG 1321
Cdd:PRK11607 112 IafGLKQDK--------LPKAEIASRVNEMLGlvHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 1322 TELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQL 1372
Cdd:PRK11607 184 LRDRMQLEVVDILERvgVTCVMVTHDQEEAMTMAgRIAIMNRGKFVQIGEPEEI 237
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1157-1375 |
3.70e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.87 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1157 GLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAA-----EGGIWIDGVPIAHVGLHTLR----SR 1227
Cdd:PRK15134 14 AFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRgvrgNK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1228 ISIIPQDPI--LFP---------GSLRMNLDLLQEHSDEAIWAALETVQLKalvaslpgQLQYKCADRGEDLSVGQKQLL 1296
Cdd:PRK15134 94 IAMIFQEPMvsLNPlhtlekqlyEVLSLHRGMRREAARGEILNCLDRVGIR--------QAAKRLTDYPHQLSGGERQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1297 CLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQC--TVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLL 1373
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELnmGLLFITHNLSIVRKLAdRVAVMQNGRCVEQNRAATLF 245
|
..
gi 1199277034 1374 AQ 1375
Cdd:PRK15134 246 SA 247
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1161-1372 |
3.72e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.02 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1161 RPELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVpiahvgLHTLRSR------------- 1227
Cdd:PRK10261 26 QQKIA-AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKM------LLRRRSRqvielseqsaaqm 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1228 -------ISIIPQDPI-----LFP------GSLRMNLDLLQEHSDEAIWAALETVQL---KALVASLPGQlqykcadrge 1286
Cdd:PRK10261 99 rhvrgadMAMIFQEPMtslnpVFTvgeqiaESIRLHQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQ---------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1287 dLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTE---LQMQAMLGSWFAQcTVLLIAHRLRSVMDCA-RVLVMDKGQ 1362
Cdd:PRK10261 169 -LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQaqiLQLIKVLQKEMSM-GVIFITHDMGVVAEIAdRVLVMYQGE 246
|
250
....*....|
gi 1199277034 1363 VAESGSPAQL 1372
Cdd:PRK10261 247 AVETGSVEQI 256
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1171-1366 |
4.18e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.83 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1171 VSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHT-LRSRISIIPQDP----ILFPGSLRMN 1245
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDRqssgLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1246 LDLLQeHSDEAIWaaLETVQLKALVASLPGQLQYKCADRGED---LSVGQKQLLCLARALLRKTQILILDEATAAVDPGT 1322
Cdd:PRK15439 362 VCALT-HNRRGFW--IKPARENAVLERYRRALNIKFNHAEQAartLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1199277034 1323 ELQMQAMLGSWFAQCT-VLLIAHRLRSVMDCA-RVLVMDKGQVAES 1366
Cdd:PRK15439 439 RNDIYQLIRSIAAQNVaVLFISSDLEEIEQMAdRVLVMHQGEISGA 484
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1168-1363 |
4.25e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.71 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1168 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLL-RLQEAAEGGIWIDGVPIA-HVGLHTLRSRISIIPQD-------PILF 1238
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFgAYPGRWEGEIFIDGKPVKiRNPQQAIAQGIAMVPEDrkrdgivPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1239 PGSlRMNLDLLQEHSD-EAIWAALEtvqLKALVASLpGQLQYKCAD---RGEDLSVGQKQLLCLARALLRKTQILILDEA 1314
Cdd:PRK13549 358 VGK-NITLAALDRFTGgSRIDDAAE---LKTILESI-QRLKVKTASpelAIARLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 1315 TAAVDPGTELQMQAMLGSWFAQ-CTVLLIAHRLRSVMD-CARVLVMDKGQV 1363
Cdd:PRK13549 433 TRGIDVGAKYEIYKLINQLVQQgVAIIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1169-1240 |
4.40e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 60.85 E-value: 4.40e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 1169 QGVSFKIHAGEKVGIVGRTGAGKSSlasgLLRL---QEAAEGG-IWIDGvpiahvglhtlRSRISIIPQDPILFPG 1240
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKST----LLKIlagELEPDSGeVSIPK-----------GLRIGYLPQEPPLDDD 75
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1168-1373 |
4.47e-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: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1168 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAhvGLHTLRSRISIIPQDPILFPG------- 1240
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFPHmtvykni 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1241 --SLRMNLDLLQEHSDEAIWAAlETVQLKALVASLPgqlqykcadrgEDLSVGQKQLLCLARALLRKTQILILDEATAAV 1318
Cdd:cd03299 93 ayGLKKRKVDKKEIERKVLEIA-EMLGIDHLLNRKP-----------ETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 1319 DPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLL 1373
Cdd:cd03299 161 DVRTKEKLREELKKIRKEfgVTVLHVTHDFEEAWALAdKVAIMLNGKLIQVGKPEEVF 218
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1167-1368 |
5.03e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 59.74 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQeAAEG---------GIWIDGVPIAHvgLHTLRS-RISIIPQDPI 1236
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGriggsatfnGREILNLPEKE--LNKLRAeQISMIFQDPM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1237 --LFP----GSLRMNLDLLQEHSDEAIwAALETVQLKALVaSLPgQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILI 1310
Cdd:PRK09473 108 tsLNPymrvGEQLMEVLMLHKGMSKAE-AFEESVRMLDAV-KMP-EARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 1311 LDEATAAVDpgTELQMQAM-----LGSWFaQCTVLLIAHRLRSVMD-CARVLVMDKGQVAESGS 1368
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 ... |
532-712 |
5.20e-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: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLL---------SALLGELSKVEGFVSIEGA-----VAYVPQEAWVQN------- 590
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalaRRLHLKKEQPGNHDRIEGLehidkVIVIDQSPIGRTprsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 591 -TSVVE-------NVCFGQELDPPWLE---------RVL-----EACALQPDVDSFPEGIHT---------SIGEQGMNL 639
Cdd:cd03271 91 yTGVFDeirelfcEVCKGKRYNRETLEvrykgksiaDVLdmtveEALEFFENIPKIARKLQTlcdvglgyiKLGQPATTL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 640 SGGQKQRLSLARAVYRKA---AVYLLDDPLAALDAHVGQH---VFNQVIGpggllQGTTRILVTHALHILPQADWIIVL 712
Cdd:cd03271 171 SGGEAQRIKLAKELSKRStgkTLYILDEPTTGLHFHDVKKlleVLQRLVD-----KGNTVVVIEHNLDVIKCADWIIDL 244
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
859-1121 |
5.47e-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: 5.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 859 DDPAVGGQQTQAALRGGIFGLLGCLQAI-GLFASMAAVLLGGARASRL---LFQRLLwdvvRSPISFFERTPIGHLLNRF 934
Cdd:cd07346 27 DDVIPAGDLSLLLWIALLLLLLALLRALlSYLRRYLAARLGQRVVFDLrrdLFRHLQ----RLSLSFFDRNRTGDLMSRL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 935 SKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLLYAGFQSLYVVSSCQLRRLESASYSSVCSHMA 1014
Cdd:cd07346 103 TSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1015 ETFQGSTVVRAFRTQ----APFVAQNNARVDESQRISfprlvadRWLAANVELLgnGLVFAAATCAVL-------SKAHL 1083
Cdd:cd07346 183 ESLSGIRVVKAFAAEereiERFREANRDLRDANLRAA-------RLSALFSPLI--GLLTALGTALVLlyggylvLQGSL 253
|
250 260 270
....*....|....*....|....*....|....*....
gi 1199277034 1084 SAG-LVGFsVSAALQVTQTLQWVVRNWTDLENSIVSVER 1121
Cdd:cd07346 254 TIGeLVAF-LAYLGMLFGPIQRLANLYNQLQQALASLER 291
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1167-1367 |
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 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG---LHTLRSRISIIPQDP-------- 1235
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPyasldprq 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1236 -----ILFPgsLRMNLDLLQEHSDEAIWAALETVQLKALVAslpgqLQYKcadrgEDLSVGQKQLLCLARALLRKTQILI 1310
Cdd:PRK10261 419 tvgdsIMEP--LRVHGLLPGKAAAARVAWLLERVGLLPEHA-----WRYP-----HEFSGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 1311 LDEATAAVDPGTE-------LQMQAMLGSWFaqctvLLIAHRLRSVMDCA-RVLVMDKGQVAESG 1367
Cdd:PRK10261 487 ADEAVSALDVSIRgqiinllLDLQRDFGIAY-----LFISHDMAVVERIShRVAVMYLGQIVEIG 546
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
532-717 |
6.25e-09 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 57.06 E-value: 6.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------------VAYVP----QEAWVQNTSV 593
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairagIAYVPedrkREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 594 VENVCFGQELdppwlervleacalqpdvdsfpegihtsigeqgmnlSGGQKQRLSLARAVYRKAAVYLLDDPLAALDahV 673
Cdd:cd03215 96 AENIALSSLL------------------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGVD--V 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1199277034 674 G--QHVFNQVIgpggLL--QGTTRILVTHALH-ILPQADWIIVLANGAI 717
Cdd:cd03215 138 GakAEIYRLIR----ELadAGKAVLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1151-1373 |
7.49e-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: 7.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELPLavQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGG-IWIDGVPIAHVGLHTLRSRIS 1229
Cdd:COG1119 4 LELRNVTVRRGGKTIL--DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1230 IIpqDPIL---FPGSLRM----------NLDLLQEHSDEAI---WAALETVQLKALvaslpgqlqykcADRG-EDLSVGQ 1292
Cdd:COG1119 82 LV--SPALqlrFPRDETVldvvlsgffdSIGLYREPTDEQReraRELLELLGLAHL------------ADRPfGTLSQGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1293 KQllclarallrKTQI----------LILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDC-ARVLVMD 1359
Cdd:COG1119 148 QR----------RVLIaralvkdpelLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEIPPGiTHVLLLK 217
|
250
....*....|....
gi 1199277034 1360 KGQVAESGSPAQLL 1373
Cdd:COG1119 218 DGRVVAAGPKEEVL 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1169-1348 |
8.14e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 57.19 E-value: 8.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1169 QGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIahvGLHTLRSRISII-PQD---PILfpgSLRM 1244
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHYLgHRNamkPAL---TVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1245 NLDLLQE---HSDEAIWAALETVQLkALVASLPGQlqykcadrgeDLSVGQKQLLCLARALLRKTQILILDEATAAVDPG 1321
Cdd:PRK13539 93 NLEFWAAflgGEELDIAAALEAVGL-APLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
170 180
....*....|....*....|....*..
gi 1199277034 1322 TelqmQAMLGSwfaqctvlLIAHRLRS 1348
Cdd:PRK13539 162 A----VALFAE--------LIRAHLAQ 176
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
532-670 |
8.57e-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: 57.55 E-value: 8.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------------VAYVPQEAWV-QNTSVVEN 596
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarlgIGYLPQEASIfRKLTVEEN 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 597 V-CFGQELDPPWLERVLEACALqpdVDSFpeGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 670
Cdd:cd03218 96 IlAVLEIRGLSKKEREEKLEEL---LEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
533-737 |
8.68e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 58.07 E-value: 8.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 533 HRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--VAYVPQEA------WVQNTS------VVENVC 598
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiQHYASKEVarriglLAQNATtpgditVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 599 FGQELDPPWLERvleacALQPDVDSFPEGIH----TSIGEQGMN-LSGGQKQRLSLARAVYRKAAVYLLDDPLAALD-AH 672
Cdd:PRK10253 104 RGRYPHQPLFTR-----WRKEDEEAVTKAMQatgiTHLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDiSH 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 673 vgQHVFNQVIGPGGLLQGTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQE-----LLQRKGALVCLL 737
Cdd:PRK10253 179 --QIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEivtaeLIERIYGLRCMI 247
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
532-671 |
9.15e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.56 E-value: 9.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGelskV------EGFVSIEGA--------------VAYVPQE-AWVQN 590
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG----VyphgtyEGEIIFEGEelqasnirdteragIAIIHQElALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 591 TSVVENVCFGQELDP----PWLERVLEACALQPDVdsfpeGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPL 666
Cdd:PRK13549 97 LSVLENIFLGNEITPggimDYDAMYLRAQKLLAQL-----KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
....*
gi 1199277034 667 AALDA 671
Cdd:PRK13549 172 ASLTE 176
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
515-730 |
9.91e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 58.25 E-value: 9.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQESP---PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIE--------------- 576
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDditithktkdkyirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 577 -----GAVAYVPqEAWVQNTSVVENVCFGQELDPPWLERVLE-ACALQPDVdSFPEGIHTSIGEQgmnLSGGQKQRLSLA 650
Cdd:PRK13646 83 vrkriGMVFQFP-ESQLFEDTVEREIIFGPKNFKMNLDEVKNyAHRLLMDL-GFSRDVMSQSPFQ---MSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 651 RAVYRKAAVYLLDDPLAALDAHVGQHVFnQVIGPGGLLQGTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELLQR 729
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVM-RLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKD 236
|
.
gi 1199277034 730 K 730
Cdd:PRK13646 237 K 237
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1153-1379 |
1.13e-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: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1153 FRDFGLRYRPELplavQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGgiwidgvPIAHVGlhtlrsRISIIP 1232
Cdd:cd03291 42 FSNLCLVGAPVL----KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG-------KIKHSG------RISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1233 QDPILFPGSLRMNLDLLQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILD 1312
Cdd:cd03291 105 QFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 1313 EATAAVDPGTELQM-QAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLF 1379
Cdd:cd03291 185 SPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDF 252
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
545-670 |
1.25e-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: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 545 LAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQ------EAWVQntSVVENVCfGQELDPPWLE-RVLEACAL 617
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQyispdyDGTVE--EFLRSAN-TDDFGSSYYKtEIIKPLGL 445
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 618 QPDVDSfpegihtSIGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 670
Cdd:COG1245 446 EKLLDK-------NVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1151-1365 |
1.31e-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: 57.06 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRY-RPELPLAV-QGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHV---GLHTLR 1225
Cdd:COG4181 9 IELRGLTKTVgTGAGELTIlKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedARARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1226 SR-ISIIPQDPILFPgSLRM--NLDL---LQEHSD--EAIWAALETVQLKALVASLPGQlqykcadrgedLSVGQKQLLC 1297
Cdd:COG4181 89 ARhVGFVFQSFQLLP-TLTAleNVMLpleLAGRRDarARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 1298 LARALLRKTQILILDEATAAVDPGTELQMQAMLgswFA-----QCTVLLIAHRLRSVMDCARVLVMDKGQVAE 1365
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATGEQIIDLL---FElnrerGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
544-670 |
1.35e-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: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 544 LLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYVPQEAWVQNTSVVENVCFGQeldppwLERVLEACALQPDVD 622
Cdd:cd03237 27 VIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDtVSYKPQYIKADYEGTVRDLLSSI------TKDFYTHPYFKTEIA 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1199277034 623 SfPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 670
Cdd:cd03237 101 K-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
532-728 |
1.46e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 57.49 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-------------VAYVPQE-AWVQNTSVVENV 597
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafarkVAYLPQQlPAAEGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 598 CFGQEldpPW-----------LERVLEACAL-------QPDVDSfpegihtsigeqgmnLSGGQKQRLSLARAVYRKAAV 659
Cdd:PRK10575 107 AIGRY---PWhgalgrfgaadREKVEEAISLvglkplaHRLVDS---------------LSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 660 YLLDDPLAALD-AHvgQHVFNQVIGPGGLLQGTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELLQ 728
Cdd:PRK10575 169 LLLDEPTSALDiAH--QVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMR 237
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
532-729 |
1.71e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 58.17 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLS--ALLGELSkvEGFVSIEGA----------------VAYVPQEAwvqN--- 590
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRciNLLERPT--SGSVLVDGVdltalserelraarrkIGMIFQHF---Nlls 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 591 --TsVVENVCF-----G----------QELdppwLERV-LEACAlqpdvDSFPEgihtsigeqgmNLSGGQKQRLSLARA 652
Cdd:COG1135 96 srT-VAENVALpleiaGvpkaeirkrvAEL----LELVgLSDKA-----DAYPS-----------QLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 653 VYRKAAVYLLDDPLAALDAHVGQHVFNqvigpggLLQ------GTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQE 725
Cdd:COG1135 155 LANNPKVLLCDEATSALDPETTRSILD-------LLKdinrelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVLD 227
|
....
gi 1199277034 726 LLQR 729
Cdd:COG1135 228 VFAN 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
515-728 |
1.79e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.44 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQESP---PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIE--------------- 576
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGdivvsstskqkeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 577 -----GAVAYVPQEAWVQNTsVVENVCFGQELDPPWLERVLEACALQPDVdsfpEGIHTSIGEQG-MNLSGGQKQRLSLA 650
Cdd:PRK13643 82 vrkkvGVVFQFPESQLFEET-VLKDVAFGPQNFGIPKEKAEKIAAEKLEM----VGLADEFWEKSpFELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 651 RAVYRKAAVYLLDDPLAALD--AHVGQHVFNQVIGPggllQGTTRILVTHAL-HILPQADWIIVLANGAIAEMGSYQELL 727
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDpkARIEMMQLFESIHQ----SGQTVVLVTHLMdDVADYADYVYLLEKGHIISCGTPSDVF 232
|
.
gi 1199277034 728 Q 728
Cdd:PRK13643 233 Q 233
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1162-1361 |
1.90e-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: 56.57 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1162 PELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSR----ISIIPQDPIL 1237
Cdd:cd03290 12 SGLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1238 FPGSLRMNLDLLQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAA 1317
Cdd:cd03290 91 LNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1199277034 1318 VDPG-TELQMQAMLGSWFA--QCTVLLIAHRLRSVMDCARVLVMDKG 1361
Cdd:cd03290 171 LDIHlSDHLMQEGILKFLQddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1154-1363 |
2.26e-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: 56.57 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1154 RDFGLRYRPELPlAVQGVSFKIHAGEKVGIVGRTGAGKSS---LASGLLRlqeAAEGGIWIDG-VP----IAHVglhtlr 1225
Cdd:cd03267 24 KSLFKRKYREVE-ALKGISFTIEKGEIVGFIGPNGAGKTTtlkILSGLLQ---PTSGEVRVAGlVPwkrrKKFL------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1226 SRISII------------PQDpilfpgSLRMNLDLLQEHSDEAiwaaleTVQLKALVASLP-GQLQYKCADRgedLSVGQ 1292
Cdd:cd03267 94 RRIGVVfgqktqlwwdlpVID------SFYLLAAIYDLPPARF------KKRLDELSELLDlEELLDTPVRQ---LSLGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 1293 KQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFA--QCTVLLIAHRLRSVMDCA-RVLVMDKGQV 1363
Cdd:cd03267 159 RMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRerGTTVLLTSHYMKDIEALArRVLVIDKGRL 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
515-725 |
2.50e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 56.98 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQESP---PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-------------- 577
Cdd:PRK13637 3 IKIENLTHIYMEGTPfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 578 -AVAYVPQ--EAWVQNTSVVENVCFG-QEL---DPPWLERVLEACAL-QPDVDSFPEgihtsigEQGMNLSGGQKQRLSL 649
Cdd:PRK13637 83 kKVGLVFQypEYQLFEETIEKDIAFGpINLglsEEEIENRVKRAMNIvGLDYEDYKD-------KSPFELSGGQKRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 650 ARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVigpgGLLQ---GTTRILVTHALH-ILPQADWIIVLANGAIAEMGSYQE 725
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKI----KELHkeyNMTIILVSHSMEdVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
532-703 |
2.93e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 56.28 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--VAYVPQEAWVQNTSVVENVCFGQeLDP---- 605
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlrIGYVPQKLYLDTTLPLTVNRFLR-LRPgtkk 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 606 ----PWLERVLEACALQpdvdsfpegihtsigeQGMN-LSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHvGQHVFNQ 680
Cdd:PRK09544 99 edilPALKRVQAGHLID----------------APMQkLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN-GQVALYD 161
|
170 180
....*....|....*....|...
gi 1199277034 681 VIGPGGLLQGTTRILVTHALHIL 703
Cdd:PRK09544 162 LIDQLRRELDCAVLMVSHDLHLV 184
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1168-1373 |
3.14e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 57.54 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1168 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPilfpgSLRMNLD 1247
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDT-----SLSFEFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1248 LLQ-------------EHSDEAIWAALETVQLKALVASLpgqlqykcADRGED-LSVGQKQLLCLARALLRKTQILILDE 1313
Cdd:PRK09536 94 VRQvvemgrtphrsrfDTWTETDRAAVERAMERTGVAQF--------ADRPVTsLSGGERQRVLLARALAQATPVLLLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 1314 ATAAVDPGTELQMQAMLGSWFAQC-TVLLIAHRLR-SVMDCARVLVMDKGQVAESGSPAQLL 1373
Cdd:PRK09536 166 PTASLDINHQVRTLELVRRLVDDGkTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
515-733 |
3.16e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 56.68 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIE----------------GA 578
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNnqaitddnfeklrkhiGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 579 VAYVPQEAWVQNTsVVENVCFGQELDP-PWLERVLEACALQPDVDSFPEGIHtsigeQGMNLSGGQKQRLSLARAVYRKA 657
Cdd:PRK13648 88 VFQNPDNQFVGSI-VKYDVAFGLENHAvPYDEMHRRVSEALKQVDMLERADY-----EPNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 658 AVYLLDDPLAALDAHVGQHVFNQVigpgGLLQGT---TRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGAL 733
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLV----RKVKSEhniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1167-1364 |
3.92e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 57.72 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDG--VPIAHVGlHTLRSRISIIPQDpilfpgslRM 1244
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPR-DAIRAGIAYVPED--------RK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1245 NLDLLQEHS--DEAIWAALETV---------QLKALVASLPGQLQYKCADRGE---DLSVGQKQllclarallrK----- 1305
Cdd:COG1129 338 GEGLVLDLSirENITLASLDRLsrgglldrrRERALAEEYIKRLRIKTPSPEQpvgNLSGGNQQ----------Kvvlak 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 1306 -----TQILILDEATAAVDPGTELQMQAMLGSwFAQ--CTVLLIAhrlrSVMD-----CARVLVMDKGQVA 1364
Cdd:COG1129 408 wlatdPKVLILDEPTRGIDVGAKAEIYRLIRE-LAAegKAVIVIS----SELPellglSDRILVMREGRIV 473
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1166-1372 |
4.56e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 55.77 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1166 LAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLrSRISIIP--QDPILFPgslR 1243
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVRtfQHVRLFR---E 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1244 M----NLdLLQEH--------------------SDEAI-WAA--LETVQLKALVASLPGQLQYkcadrgedlsvGQKQLL 1296
Cdd:PRK11300 95 MtvieNL-LVAQHqqlktglfsgllktpafrraESEALdRAAtwLERVGLLEHANRQAGNLAY-----------GQQRRL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 1297 CLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQL 1372
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhnVTVLLIEHDMKLVMGISdRIYVVNQGTPLANGTPEEI 241
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1168-1375 |
4.73e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 55.75 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1168 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHV-------------GLHTLRSRISIIPQD 1234
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1235 PILFpgSLRMNLDLLQEHSDEAIWAALETVQLKALV----ASLPGQLQYKCAdrgEDLSVGQKQLLCLARALLRKTQILI 1310
Cdd:PRK10619 101 FNLW--SHMTVLENVMEAPIQVLGLSKQEARERAVKylakVGIDERAQGKYP---VHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 1311 LDEATAAVDP---GTELQMQAMLGSwfAQCTVLLIAHRlrsvMDCAR-----VLVMDKGQVAESGSPAQLLAQ 1375
Cdd:PRK10619 176 FDEPTSALDPelvGEVLRIMQQLAE--EGKTMVVVTHE----MGFARhvsshVIFLHQGKIEEEGAPEQLFGN 242
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1171-1372 |
5.39e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 56.63 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1171 VSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVglHTLRSRISIIPQDPILFP-----GSLRMN 1245
Cdd:PRK10851 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL--HARDRKVGFVFQHYALFRhmtvfDNIAFG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1246 LDLLQEHS-------DEAIWAALETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLARALLRKTQILILDEATAAV 1318
Cdd:PRK10851 99 LTVLPRRErpnaaaiKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 1319 DPgtelQMQAMLGSWFAQC------TVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQL 1372
Cdd:PRK10851 168 DA----QVRKELRRWLRQLheelkfTSVFVTHDQEEAMEVAdRVVVMSQGNIEQAGTPDQV 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1151-1320 |
5.54e-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: 5.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELplAVQGVSFKIHAGEKVGIVGRTGAGKSSLasglLR-------LQEAA--EGGIWIDGVPI--AHV 1219
Cdd:COG1117 12 IEVRNLNVYYGDKQ--ALKDINLDIPENKVTALIGPSGCGKSTL----LRclnrmndLIPGArvEGEILLDGEDIydPDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1220 GLHTLRSRISIIPQDPILFPGS--------LRMNLDLLQEHSDEAIWAALETVQL----KAlvaslpgQLQykcaDRGED 1287
Cdd:COG1117 86 DVVELRRRVGMVFQKPNPFPKSiydnvaygLRLHGIKSKSELDEIVEESLRKAALwdevKD-------RLK----KSALG 154
|
170 180 190
....*....|....*....|....*....|...
gi 1199277034 1288 LSVGQKQLLCLARALLRKTQILILDEATAAVDP 1320
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDP 187
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1146-1326 |
5.56e-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: 57.45 E-value: 5.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1146 PQGGQIEFRDFGLRYRpELPLA-------VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLlrlqeaaeGGIWidgvPIaH 1218
Cdd:TIGR00954 440 PGRGIVEYQDNGIKFE-NIPLVtpngdvlIESLSFEVPSGNNLLICGPNGCGKSSLFRIL--------GELW----PV-Y 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1219 VGLHTL--RSRISIIPQDPILFPGSLR------MNLDLLQEH--SDEAIWAALETVQLKALVASLPGQlqYKCADRGEDL 1288
Cdd:TIGR00954 506 GGRLTKpaKGKLFYVPQRPYMTLGTLRdqiiypDSSEDMKRRglSDKDLEQILDNVQLTHILEREGGW--SAVQDWMDVL 583
|
170 180 190
....*....|....*....|....*....|....*...
gi 1199277034 1289 SVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQM 1326
Cdd:TIGR00954 584 SGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYM 621
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1168-1319 |
6.05e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 55.11 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1168 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNL- 1246
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNLi 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 1247 ---DLLQEHSDEAIWAAlETVQLkalvaSLPGQLQYKcadRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVD 1319
Cdd:PRK10247 103 fpwQIRNQQPDPAIFLD-DLERF-----ALPDTILTK---NIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
535-729 |
6.17e-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: 57.00 E-value: 6.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSALLGeLSKVEGFVSIEG-AVAYVPQEAW------VQntsVVenvcFgQE----L 603
Cdd:COG4172 305 VSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGqDLDGLSRRALrplrrrMQ---VV----F-QDpfgsL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 604 DP----------------PWL------ERVLEACA---LQPDV-DSFPegiHtsigEqgmnLSGGQKQRLSLARAVYRKA 657
Cdd:COG4172 376 SPrmtvgqiiaeglrvhgPGLsaaerrARVAEALEevgLDPAArHRYP---H----E----FSGGQRQRIAIARALILEP 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 658 AVYLLDDPLAALDAHVgQHvfnQVIgpgGLLQ------GTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELLQR 729
Cdd:COG4172 445 KLLVLDEPTSALDVSV-QA---QIL---DLLRdlqrehGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
530-670 |
6.27e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.57 E-value: 6.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 530 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA------VAYVPQEAWV-------QNTSVVEN 596
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlCTYQKQLCFVghrsginPYLTLREN 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199277034 597 VCFGQELDPPWLErVLEAC---ALQPDVDsFPEGIhtsigeqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 670
Cdd:PRK13540 95 CLYDIHFSPGAVG-ITELCrlfSLEHLID-YPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
515-721 |
6.32e-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: 54.68 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQESPPC--LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-AVAYVPQEAwVQNT 591
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEA-RRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 592 SVVenvcFGQELDPPWL---ERV--------LEACALQPDVDSFPE--GIHTSIGEQGMNLSGGQKQRLSLARAVYRKAA 658
Cdd:cd03266 81 GFV----SDSTGLYDRLtarENLeyfaglygLKGDELTARLEELADrlGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 659 VYLLDDPLAALDAhVGQHVFNQVIGPgglL--QGTTRILVTHALH-ILPQADWIIVLANGAIAEMG 721
Cdd:cd03266 157 VLLLDEPTTGLDV-MATRALREFIRQ---LraLGKCILFSTHIMQeVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1168-1367 |
6.34e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 55.30 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1168 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQE-----AAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPG-- 1240
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPNls 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1241 -----SLRMNLDLL---QEHSDEAIWAALETVQLKALVASLPGqlqykcADRGEdLSVGQKQLLCLARALLRKTQILILD 1312
Cdd:PRK14247 99 ifenvALGLKLNRLvksKKELQERVRWALEKAQLWDEVKDRLD------APAGK-LSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 1313 EATAAVDPGTELQMQAMLGSWFAQCTVLLIAH---RLRSVMDcaRVLVMDKGQVAESG 1367
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqQAARISD--YVAFLYKGQIVEWG 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
532-702 |
6.80e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 54.82 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-----------------VAYVPQ-EAWVQNTSV 593
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsklssaakaelrnqkLGFIYQfHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 594 VENVCF----GQELDPPWLERVLEACAlqpdvdsfPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAAL 669
Cdd:PRK11629 105 LENVAMplliGKKKPAEINSRALEMLA--------AVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190
....*....|....*....|....*....|...
gi 1199277034 670 DAHVGQHVFnQVIGPGGLLQGTTRILVTHALHI 702
Cdd:PRK11629 177 DARNADSIF-QLLGELNRLQGTAFLVVTHDLQL 208
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
530-730 |
1.00e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 55.61 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 530 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA------------VAYVPQ-EAWVQNTSVVEN 596
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVpvpararlararIGVVPQfDNLDLEFTVREN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 597 -VCFGQ--ELDPPWLERV----LEACALQPDVDsfpegihTSIGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAAL 669
Cdd:PRK13536 135 lLVFGRyfGMSTREIEAVipslLEFARLESKAD-------ARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 670 DAHVGQHVFNQVigPGGLLQGTTRILVThalHILPQA----DWIIVLANG-AIAEmGSYQELLQRK 730
Cdd:PRK13536 204 DPHARHLIWERL--RSLLARGKTILLTT---HFMEEAerlcDRLCVLEAGrKIAE-GRPHALIDEH 263
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
535-727 |
1.59e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.41 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIE------GAVAYVPQEAWV----QNTSVVENVCFGQELD 604
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDdhplhfGDYSYRSQRIRMifqdPSTSLNPRQRISQILD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 605 PPW-LERVLEACALQpdvdsfpEGIHTSIGEQGM----------NLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHV 673
Cdd:PRK15112 112 FPLrLNTDLEPEQRE-------KQIIETLRQVGLlpdhasyyphMLAPGQKQRLGLARALILRPKVIIADEALASLDMSM 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 674 GQHVFNQVIGpgglLQ---GTTRILVTHAL----HIlpqADWIIVLANGAIAEMGSYQELL 727
Cdd:PRK15112 185 RSQLINLMLE----LQekqGISYIYVTQHLgmmkHI---SDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
518-704 |
1.70e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.31 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 518 HSATFawSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA----------VAYVPQ-EA 586
Cdd:PRK13543 15 HALAF--SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsrfMAYLGHlPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 587 WVQNTSVVENVCFgqeldppwlervleACALQP-DVDSFPEGIHTSIGEQGM------NLSGGQKQRLSLARAVYRKAAV 659
Cdd:PRK13543 93 LKADLSTLENLHF--------------LCGLHGrRAKQMPGSALAIVGLAGYedtlvrQLSAGQKKRLALARLWLSPAPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1199277034 660 YLLDDPLAALDAHvGQHVFNQVIGPGGLLQGTTrILVTHALHILP 704
Cdd:PRK13543 159 WLLDEPYANLDLE-GITLVNRMISAHLRGGGAA-LVTTHGAYAAP 201
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
515-731 |
1.78e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 54.42 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSS---LLSALLGELSKVEGFVSIEGA------------- 578
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGItltaktvwdirek 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 579 VAYV---PQEAWVQNTsVVENVCFGQE---LDPPWL----ERVLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLS 648
Cdd:PRK13640 86 VGIVfqnPDNQFVGAT-VGDDVAFGLEnraVPRPEMikivRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 649 LARAVYRKAAVYLLDDPLAALDAHvGQHVFNQVIGPGGLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGS------ 722
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPA-GKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSpveifs 232
|
....*....
gi 1199277034 723 YQELLQRKG 731
Cdd:PRK13640 233 KVEMLKEIG 241
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1169-1373 |
2.08e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.84 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1169 QGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILfPGSLRMN--- 1245
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATT-PGDITVQelv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1246 ----------LDLLQEHSDEAIWAALETVQLKALvaslpgqlqykcADRGED-LSVGQKQLLCLARALLRKTQILILDEA 1314
Cdd:PRK10253 103 argryphqplFTRWRKEDEEAVTKAMQATGITHL------------ADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 1315 TAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCARVLV-MDKGQVAESGSPAQLL 1373
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREkgYTLAAVLHDLNQACRYASHLIaLREGKIVAQGAPKEIV 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
532-715 |
2.27e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.03 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG----------AVAY----VPQE-AWVQNTSVVEN 596
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpvrirsprdAIALgigmVHQHfMLVPNLTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 597 VCFGQELDPPWL-------ERVLEACA---LQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPL 666
Cdd:COG3845 101 IVLGLEPTKGGRldrkaarARIRELSErygLDVDPDAKVE-----------DLSVGEQQRVEILKALYRGARILILDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 667 AALDAHVGQHVFnqvigpgGLL-----QGTTRILVTHALH-ILPQADWIIVLANG 715
Cdd:COG3845 170 AVLTPQEADELF-------EILrrlaaEGKSIIFITHKLReVMAIADRVTVLRRG 217
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
532-729 |
2.29e-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: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGelskVEGFVSIEGAVAYvpqeawvQNTSVvenvcfgqeLDPPWLERV 611
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG----HPKYEVTEGEILF-------KGEDI---------TDLPPEERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 612 LEAC--ALQ--PDVdsfpEGIHTS--IGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVigpG 685
Cdd:cd03217 76 RLGIflAFQypPEI----PGVKNAdfLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVI---N 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1199277034 686 GLL-QGTTRILVTHALHIL--PQADWIIVLANGAIAEMGSyQELLQR 729
Cdd:cd03217 149 KLReEGKSVLIITHYQRLLdyIKPDRVHVLYDGRIVKSGD-KELALE 194
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
534-679 |
2.39e-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: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 534 RINLTVPQGCLLAVVGPVGAGKSSLLSaLLGELSKVEG---FVSIEGAVAYVPQEAWVQNTSVVENVCFgqeldPPWLER 610
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIY-----PDSSED 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 611 VLEACALQPDVDSFPEGIH-TSIGEQGMN----------LSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFN 679
Cdd:TIGR00954 544 MKRRGLSDKDLEQILDNVQlTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYR 623
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
536-727 |
2.44e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 54.65 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 536 NLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-----------------VAYVPQE-AWVQNTSVVENV 597
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVdiakisdaelrevrrkkIAMVFQSfALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 598 CFGQEL-DPPWLER------VLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 670
Cdd:PRK10070 128 AFGMELaGINAEERrekaldALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 671 AHVGQHVFNQVIGPGGLLQGTTrILVTHAL-HILPQADWIIVLANGAIAEMGSYQELL 727
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKHQRTI-VFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
535-729 |
3.00e-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: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSALLG---ELSKVEGFVSIEGA-----------------VAYVPQEAWvqnTSvv 594
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEdllklsekelrkirgreIQMIFQDPM---TS-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 595 envcfgqeLDP---------------------PWLERVLEACAL----QPD--VDSFPegiHtsigeqgmNLSGGQKQRL 647
Cdd:COG0444 99 --------LNPvmtvgdqiaeplrihgglskaEARERAIELLERvglpDPErrLDRYP---H--------ELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 648 SLARAVYRKAAVYLLDDPLAALDAHVgQHvfnQVIgpgGLLQ------GTTRILVTH----ALHIlpqADWIIVLANGAI 717
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTI-QA---QIL---NLLKdlqrelGLAILFITHdlgvVAEI---ADRVAVMYAGRI 229
|
250
....*....|..
gi 1199277034 718 AEMGSYQELLQR 729
Cdd:COG0444 230 VEEGPVEELFEN 241
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1167-1377 |
3.23e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.13 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSS---LASGLLrlqEAAEGGIWIDGVPIAHVGLHTlRSRISIIPQDpilFpgSL- 1242
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTtmkMLTGLL---PASEGEAWLFGQPVDAGDIAT-RRRVGYMSQA---F--SLy 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1243 -----RMNLDL---L----QEHSDEAIWAALETVQLKALVASLPgqlqykcadrgEDLSVGQKQLLCLARALLRKTQILI 1310
Cdd:NF033858 352 geltvRQNLELharLfhlpAAEIAARVAEMLERFDLADVADALP-----------DSLPLGIRQRLSLAVAVIHKPELLI 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 1311 LDEATAAVDPGTELQMQAMLG--SWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKG 1377
Cdd:NF033858 421 LDEPTSGVDPVARDMFWRLLIelSREDGVTIFISTHFMNEAERCDRISLMHAGRVLASDTPAALVAARG 489
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1151-1372 |
3.27e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.59 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELPL---AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG----LHT 1223
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1224 LRSRISIIPQdpilFPGSLRMNLDLLQE----------HSDEAIWAALETVQLKALVASLPGQLQYkcadrgeDLSVGQK 1293
Cdd:PRK13649 83 IRKKVGLVFQ----FPESQLFEETVLKDvafgpqnfgvSQEEAEALAREKLALVGISESLFEKNPF-------ELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1294 QLLCLARALLRKTQILILDEATAAVDP-GTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCAR-VLVMDKGQVAESGSPAQ 1371
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPkGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADfVYVLEKGKLVLSGKPKD 231
|
.
gi 1199277034 1372 L 1372
Cdd:PRK13649 232 I 232
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
530-715 |
3.81e-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: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 530 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGelsKVEGFVSIEGAVAY---VPQEAWVQNTSvveNVCFGQELD-- 604
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSVEGDIHYngiPYKEFAEKYPG---EIIYVSEEDvh 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 605 PPWL--ERVLEAcALQPDVDSFPEGIhtsigeqgmnlSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQvi 682
Cdd:cd03233 95 FPTLtvRETLDF-ALRCKGNEFVRGI-----------SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKC-- 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1199277034 683 gpgglLQGTTRILVTHALHILPQA--------DWIIVLANG 715
Cdd:cd03233 161 -----IRTMADVLKTTTFVSLYQAsdeiydlfDKVLVLYEG 196
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
526-729 |
3.84e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 53.16 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 526 QESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGEL----SKVEGFVSIEGaVAYVPQE------AWV-QN---- 590
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDG-KPVAPCAlrgrkiATImQNprsa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 591 --------TSVVENV-CFGQELDPPWLERVLEACALQPD---VDSFPegihtsigeqgMNLSGGQKQRLSLARAVYRKAA 658
Cdd:PRK10418 92 fnplhtmhTHARETClALGKPADDATLTAALEAVGLENAarvLKLYP-----------FEMSGGMLQRMMIALALLCEAP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 659 VYLLDDPLAALDAHVGQHVFN------QVIGPGGLlqgttriLVTHALHILPQ-ADWIIVLANGAIAEMGSYQELLQR 729
Cdd:PRK10418 161 FIIADEPTTDLDVVAQARILDllesivQKRALGML-------LVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
535-728 |
3.87e-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: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKvEGFVSIEGA--VAYVPQE-----AWvqntsvvenvcFGQELDPPW 607
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRplSDWSAAElarhrAY-----------LSQQQSPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 608 LERVLEACAL-QPDVDSFPEGIHT------------SIGEQGMNLSGGQKQRLSLARAVYR-------KAAVYLLDDPLA 667
Cdd:COG4138 83 AMPVFQYLALhQPAGASSEAVEQLlaqlaealgledKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 668 ALD-AHvgQHVFNQVIgpGGL-LQGTTRILVTHAL-HILPQADWIIVLANGAIAEMGSYQELLQ 728
Cdd:COG4138 163 SLDvAQ--QAALDRLL--RELcQQGITVVMSSHDLnHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
515-729 |
4.34e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.09 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQESP---PCLHRINLTVPQGCLLAVVGPVGAGKSSLLS------------ALLGELSKVEGFVSIE--- 576
Cdd:PRK13645 7 IILDNVSYTYAKKTPfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqTIVGDYAIPANLKKIKevk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 577 ------GAVAYVPQEAWVQNTsVVENVCFGqeldPPWL----ERVLEACALQPDVDSFPEgihTSIGEQGMNLSGGQKQR 646
Cdd:PRK13645 87 rlrkeiGLVFQFPEYQLFQET-IEKDIAFG----PVNLgenkQEAYKKVPELLKLVQLPE---DYVKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 647 LSLARAVYRKAAVYLLDDPLAALDAHvGQHVFNQVIGPGGLLQGTTRILVTHAL-HILPQADWIIVLANGAIAEMG---- 721
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPK-GEEDFINLFERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGspfe 237
|
250
....*....|
gi 1199277034 722 --SYQELLQR 729
Cdd:PRK13645 238 ifSNQELLTK 247
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1171-1374 |
4.84e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 53.18 E-value: 4.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1171 VSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEG-----GIWIDGVPI-AHVGLHTLRSRISIIPQDPILFPGSLRM 1244
Cdd:PRK14271 40 VSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFPMSIMD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1245 N-LDLLQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTE 1323
Cdd:PRK14271 120 NvLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTT 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 1324 LQMQAMLGSWFAQCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLA 1374
Cdd:PRK14271 200 EKIEEFIRSLADRLTVIIVTHNLAQAARISdRAALFFDGRLVEEGPTEQLFS 251
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
515-729 |
5.73e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 52.82 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQESP---PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA------------- 578
Cdd:PRK13649 3 INLQNVSYTYQAGTPfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitstsknkdikq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 579 ----VAYVPQ--EAWVQNTSVVENVCFGQE---LDPPWLERV-LEACALQpdvdsfpeGIHTSIGEQG-MNLSGGQKQRL 647
Cdd:PRK13649 83 irkkVGLVFQfpESQLFEETVLKDVAFGPQnfgVSQEEAEALaREKLALV--------GISESLFEKNpFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 648 SLARAVYRKAAVYLLDDPLAALDAHVGQH---VFNQVigpggLLQGTTRILVTHAL-HILPQADWIIVLANGAIAEMGSY 723
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKElmtLFKKL-----HQSGMTIVLVTHLMdDVANYADFVYVLEKGKLVLSGKP 229
|
....*.
gi 1199277034 724 QELLQR 729
Cdd:PRK13649 230 KDIFQD 235
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1151-1219 |
6.98e-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: 6.98e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYrPELPLaVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGI-WIDGVPIAHV 1219
Cdd:cd03221 1 IELENLSKTY-GGKLL-LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVtWGSTVKIGYF 68
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1167-1367 |
8.20e-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: 51.49 E-value: 8.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDG-----VPIAHVGLHTLRSRISIIPQ----DPIL 1237
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdLPPKDRDIAMVFQNYALYPHmtvyDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1238 FPGSLRmnlDLLQEHSDEAIWAALETVQLKALVASLPGQlqykcadrgedLSVGQKQLLCLARALLRKTQILILDEATAA 1317
Cdd:cd03301 95 FGLKLR---KVPKDEIDERVREVAELLQIEHLLDRKPKQ-----------LSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 1318 VDPGTELQM-------QAMLGSwfaqcTVLLIAHRLRSVMDCA-RVLVMDKGQVAESG 1367
Cdd:cd03301 161 LDAKLRVQMraelkrlQQRLGT-----TTIYVTHDQVEAMTMAdRIAVMNDGQIQQIG 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1155-1387 |
8.76e-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: 52.80 E-value: 8.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1155 DFGLRyRPELPLAVQgvsFKIHAGEKVGIVGRTGAGKSSLA---SGLLRLQE---AAEGGIWIDGVPIAHVGLHtlRSRI 1228
Cdd:COG4148 6 DFRLR-RGGFTLDVD---FTLPGRGVTALFGPSGSGKTTLLraiAGLERPDSgriRLGGEVLQDSARGIFLPPH--RRRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1229 SIIPQDPILFPG-SLRMNLD-----LLQEHSDEAIWAALETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLARAL 1302
Cdd:COG4148 80 GYVFQEARLFPHlSVRGNLLygrkrAPRAERRISFDEVVELLGIGHLLDRRPATL-----------SGGERQRVAIGRAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1303 LRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQKGLF 1379
Cdd:COG4148 149 LSSPRLLLMDEPLAALDLARKAEILPYLERLRDEldIPILYVSHSLDEVARLAdHVVLLEQGRVVASGPLAEVLSRPDLL 228
|
....*...
gi 1199277034 1380 yRLAQESG 1387
Cdd:COG4148 229 -PLAGGEE 235
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1168-1373 |
8.95e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.97 E-value: 8.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1168 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGV------PIAHVGLHTLRSRISIIPQDPILFPG- 1240
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPHl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1241 SLRMNLDL-LQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVD 1319
Cdd:PRK14246 106 SIYDNIAYpLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 1320 PGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCAR-VLVMDKGQVAESGSPAQLL 1373
Cdd:PRK14246 186 IVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADyVAFLYNGELVEWGSSNEIF 240
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
535-722 |
9.05e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 52.66 E-value: 9.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-AVAYVPQEAWVQNTSVVENVcF-------------G 600
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqDLLKADPEAQKLLRQKIQIV-FqnpygslnprkkvG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 601 QELDPPWL-----------ERVLEACA---LQPD-VDSFPegiHtsigeqgMnLSGGQKQRLSLARAVYRKAAVYLLDDP 665
Cdd:PRK11308 113 QILEEPLLintslsaaerrEKALAMMAkvgLRPEhYDRYP---H-------M-FSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 666 LAALDAHVGQHVFNQVIGpgglLQ---GTTRILVTHAL----HIlpqADWIIVLANGAIAEMGS 722
Cdd:PRK11308 182 VSALDVSVQAQVLNLMMD----LQqelGLSYVFISHDLsvveHI---ADEVMVMYLGRCVEKGT 238
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
535-670 |
9.16e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 51.82 E-value: 9.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG--------------AVAYVPQEAWV-QNTSVVENVCF 599
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllplhararrGIGYLPQEASIfRRLSVYDNLMA 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 600 GQELdppwlERVLEACALQPDVDSFPEGIHTS--IGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 670
Cdd:PRK10895 102 VLQI-----RDDLSAEQREDRANELMEEFHIEhlRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1150-1374 |
9.69e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.40 E-value: 9.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1150 QIEFRDFGLRYRPELPL---AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGI-WI--DGVPIAHVGLHT 1223
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIfkDEKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1224 ---------------------LRSRISIIPQ------------DPILFpGSLRMNLDllqehSDEAIWAALETVQLKALV 1270
Cdd:PRK13651 82 kvleklviqktrfkkikkikeIRRRVGVVFQfaeyqlfeqtieKDIIF-GPVSMGVS-----KEEAKKRAAKYIELVGLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1271 ASLpgqLQykcadRGE-DLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQC-TVLLIAHRLRS 1348
Cdd:PRK13651 156 ESY---LQ-----RSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGkTIILVTHDLDN 227
|
250 260
....*....|....*....|....*..
gi 1199277034 1349 VMDCA-RVLVMDKGQVAESGSPAQLLA 1374
Cdd:PRK13651 228 VLEWTkRTIFFKDGKIIKDGDTYDILS 254
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
532-722 |
1.16e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 52.50 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSA--LLGELSkvEGFVSIEGA--VAYVPQE--AWVQNT-------------S 592
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCinLLERPT--SGRVLVDGQdlTALSEKElrKARRQIgmifqhfnllssrT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 593 VVENVCFGQELD-----------PPWLERV-LEACAlqpdvDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVY 660
Cdd:PRK11153 99 VFDNVALPLELAgtpkaeikarvTELLELVgLSDKA-----DRYPA-----------QLSGGQKQRVAIARALASNPKVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 661 LLDDPLAALDAHVGQHVFNqvigpggLLQ------GTTRILVTHALHILPQ-ADWIIVLANGAIAEMGS 722
Cdd:PRK11153 163 LCDEATSALDPATTRSILE-------LLKdinrelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
532-665 |
1.40e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 52.71 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------------VAYVP----QEAWVQNTSV 593
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVPedrkGEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 594 VENVCFgqeldpPWLERVLEACALQPD---------VDSF---PEGIHTSIGeqgmNLSGGQKQRLSLARAVYRKAAVYL 661
Cdd:COG1129 348 RENITL------ASLDRLSRGGLLDRRreralaeeyIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLI 417
|
....
gi 1199277034 662 LDDP 665
Cdd:COG1129 418 LDEP 421
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
632-712 |
1.42e-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: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 632 IGEQGMNLSGGQKQRLSLARAVYRKA---AVYLLDDPLAALDAH-VGQ--HVFNQVIGpggllQGTTRILVTHALHILPQ 705
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLHFDdIKKllEVLQRLVD-----KGNTVVVIEHNLDVIKT 897
|
....*..
gi 1199277034 706 ADWIIVL 712
Cdd:TIGR00630 898 ADYIIDL 904
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1167-1317 |
1.43e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.62 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAA--EGGIWIDGVPIAHVGLH-TLRSRISIIPQDPILFPG-SL 1242
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRdTERAGIAIIHQELALVKElSV 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199277034 1243 RMNLDLLQEHSDEAI--WAALeTVQLKALVASLpgQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAA 1317
Cdd:PRK13549 100 LENIFLGNEITPGGImdYDAM-YLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1167-1378 |
1.43e-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: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAH-VGLHTLRSRISIIPQDPILFPgslRMN 1245
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMREAVAIVPEGRRVFS---RMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1246 LDllQEHSDEAIWAALETVQLK-ALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTEL 1324
Cdd:PRK11614 97 VE--ENLAMGGFFAERDQFQERiKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 1325 QMQAMLGSWFAQ-CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQKGL 1378
Cdd:PRK11614 175 QIFDTIEQLREQgMTIFLVEQNANQALKLAdRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
633-727 |
1.48e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 51.12 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 633 GEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAH-VGQ--HVFNQVIGpggllQGTTRILVTH----ALHIlpq 705
Cdd:PRK10619 147 GKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElVGEvlRIMQQLAE-----EGKTMVVVTHemgfARHV--- 218
|
90 100
....*....|....*....|..
gi 1199277034 706 ADWIIVLANGAIAEMGSYQELL 727
Cdd:PRK10619 219 SSHVIFLHQGKIEEEGAPEQLF 240
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
876-1048 |
1.60e-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: 51.71 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 876 IFGLLGCLQAIGLFASMAAVLLGGARASRLLFQRLLWDVVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMY 955
Cdd:cd18577 52 YFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 956 AFGLLeVSLVVA------VAtpLATVAILPLFLLYAGFQSLYVVSSCQlrrLESASYSSVCSHMAETFQGSTVVRAFRTQ 1029
Cdd:cd18577 132 LSTFI-AGFIIAfiyswkLT--LVLLATLPLIAIVGGIMGKLLSKYTK---KEQEAYAKAGSIAEEALSSIRTVKAFGGE 205
|
170
....*....|....*....
gi 1199277034 1030 APFVAQNNARVDESQRISF 1048
Cdd:cd18577 206 EKEIKRYSKALEKARKAGI 224
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1168-1355 |
1.69e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.00 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1168 VQGVSFKIHAGEKVGIVGRTGAGKSSLASG---LLRLQEAA--EGGIWIDGVPI--AHVGLHTLRSRISIIPQDPILFPG 1240
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEArvEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1241 ---------SLRMN-LDLLQEHSDEAIWAALETvqlkalvASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILI 1310
Cdd:PRK14267 100 ltiydnvaiGVKLNgLVKSKKELDERVEWALKK-------AALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1199277034 1311 LDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHrlrSVMDCARV 1355
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH---SPAQAARV 214
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1167-1347 |
1.80e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 50.93 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQE-----AAEGGIWIDGVPIAHVGLHT--LRSRISIIPQDPILFP 1239
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1240 GSLRMN----LDLLQEHSDEAIWAALETvQLKAlvASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEAT 1315
Cdd:PRK14239 100 MSIYENvvygLRLKGIKDKQVLDEAVEK-SLKG--ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPT 176
|
170 180 190
....*....|....*....|....*....|..
gi 1199277034 1316 AAVDPGTELQMQAMLGSWFAQCTVLLIAHRLR 1347
Cdd:PRK14239 177 SALDPISAGKIEETLLGLKDDYTMLLVTRSMQ 208
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1163-1212 |
1.83e-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: 50.51 E-value: 1.83e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1163 ELPlAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWID 1212
Cdd:COG4778 23 RLP-VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR 71
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1167-1330 |
1.85e-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: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAA--EGGIWIDGVPIAHVGLH-TLRSRISIIPQDPILFPG-SL 1242
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRdTERAGIVIIHQELTLVPElSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1243 RMNLDLLQE--------HSDEAIWAA---LETVQLKALVASLPGQlqykcadrgeDLSVGQKQLLCLARALLRKTQILIL 1311
Cdd:TIGR02633 96 AENIFLGNEitlpggrmAYNAMYLRAknlLRELQLDADNVTRPVG----------DYGGGQQQLVEIAKALNKQARLLIL 165
|
170
....*....|....*....
gi 1199277034 1312 DEATAAVdpgTELQMQAML 1330
Cdd:TIGR02633 166 DEPSSSL---TEKETEILL 181
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
639-726 |
2.04e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 51.39 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 639 LSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHvGQHVFNQVIGPGGlLQGTTRILVTHAL-HILPQADWIIVLANGAI 717
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK-GEHEMMQLILDAK-ANNKTVFVITHTMeHVLEVADEVIVMDKGKI 254
|
....*....
gi 1199277034 718 AEMGSYQEL 726
Cdd:PRK13631 255 LKTGTPYEI 263
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1146-1374 |
2.08e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.85 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1146 PQGGQIEfrdfGLRYRPELPLaVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAA----EGGIWIDGVPIAhvgL 1221
Cdd:PRK10418 2 PQQIELR----NIALQAAQPL-VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVA---P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1222 HTLRSR-ISIIPQDPILFPGSLR-MN-------LDLLQEHSDEAIWAALETVQL---KALVASLPGQlqykcadrgedLS 1289
Cdd:PRK10418 74 CALRGRkIATIMQNPRSAFNPLHtMHtharetcLALGKPADDATLTAALEAVGLenaARVLKLYPFE-----------MS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1290 VGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQVAES 1366
Cdd:PRK10418 143 GGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKraLGMLLVTHDMGVVARLAdDVAVMSHGRIVEQ 222
|
....*...
gi 1199277034 1367 GSPAQLLA 1374
Cdd:PRK10418 223 GDVETLFN 230
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1134-1373 |
2.35e-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: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1134 WR---LPTCAAQP-PWPQGGQIEFRDFGlRYRPELPLaVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAA---E 1206
Cdd:TIGR00955 5 WRnsdVFGRVAQDgSWKQLVSRLRGCFC-RERPRKHL-LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1207 GGIWIDGVPIahvGLHTLRSRISIIPQDPILFP-----------GSLRMNLDLLQEHSDEAIWAALETVQLKalvaslpg 1275
Cdd:TIGR00955 83 GSVLLNGMPI---DAKEMRAISAYVQQDDLFIPtltvrehlmfqAHLRMPRRVTKKEKRERVDEVLQALGLR-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1276 qlqyKCAD-------RGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQ-MQAMLGswFAQ--CTVLLIAH- 1344
Cdd:TIGR00955 152 ----KCANtrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSvVQVLKG--LAQkgKTIICTIHq 225
|
250 260 270
....*....|....*....|....*....|..
gi 1199277034 1345 ---RLRSVMDcaRVLVMDKGQVAESGSPAQLL 1373
Cdd:TIGR00955 226 pssELFELFD--KIILMAEGRVAYLGSPDQAV 255
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
532-671 |
2.36e-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: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLG--ELSKVEGFVSIEGA--------------VAYVPQE-AWVQNTSVV 594
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSplkasnirdteragIVIIHQElTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 595 ENVCFGQELDPP-----WLERVLEACAL--QPDVDSFPEGIHTsigeqgMNLSGGQKQRLSLARAVYRKAAVYLLDDPLA 667
Cdd:TIGR02633 97 ENIFLGNEITLPggrmaYNAMYLRAKNLlrELQLDADNVTRPV------GDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
....
gi 1199277034 668 ALDA 671
Cdd:TIGR02633 171 SLTE 174
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
532-765 |
2.76e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 50.88 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA---------VAYVPQE-AWVQNTSVVEN-VCFG 600
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEpldpedrrrIGYLPEErGLYPKMKVGEQlVYLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 601 Q--ELDPP--------WLERVleacalqpdvdsfpeGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 670
Cdd:COG4152 97 RlkGLSKAeakrradeWLERL---------------GLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 671 AhVGQHVFNQVIgpgglL----QGTTRILVThalHILPQA----DWIIVLANGAIAEMGSYQELLQRKGALVCLLdqaRQ 742
Cdd:COG4152 162 P-VNVELLKDVI-----RelaaKGTTVIFSS---HQMELVeelcDRIVIINKGRKVLSGSVDEIRRQFGRNTLRL---EA 229
|
250 260
....*....|....*....|...
gi 1199277034 743 PGDRGEGETEPGTSTKDPRGTSA 765
Cdd:COG4152 230 DGDAGWLRALPGVTVVEEDGDGA 252
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1168-1374 |
3.08e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 50.13 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1168 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLlRLQEAAEGG------IWIDG-VPIAHVG--LHTLRSRISIIPQDPILF 1238
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLEQPEAGtirvgdITIDTaRSLSQQKglIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1239 PGslRMNLD--------LLQEHSDEAIWAALEtvqLKALVAsLPGQlqykcadrgED-----LSVGQKQLLCLARALLRK 1305
Cdd:PRK11264 98 PH--RTVLEniiegpviVKGEPKEEATARARE---LLAKVG-LAGK---------ETsyprrLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 1306 TQILILDEATAAVDP---GTELQMQAMLGSwfAQCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLA 1374
Cdd:PRK11264 163 PEVILFDEPTSALDPelvGEVLNTIRQLAQ--EKRTMVIVTHEMSFARDVAdRAIFMDQGRIVEQGPAKALFA 233
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
532-716 |
3.28e-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: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEgfvSIEGAVAYVPQEAwvqntsvvenVCFGQeldppwLERV 611
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKAR---LISFLPKFSRNKL----------IFIDQ------LQFL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 612 LEAcalqpdvdsfpeGI-HTSIGEQGMNLSGGQKQRLSLARAVYR--KAAVYLLDDPLAALDAHVGQHVFNQVigpGGLL 688
Cdd:cd03238 72 IDV------------GLgYLTLGQKLSTLSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQDINQLLEVI---KGLI 136
|
170 180
....*....|....*....|....*....
gi 1199277034 689 -QGTTRILVTHALHILPQADWIIVLANGA 716
Cdd:cd03238 137 dLGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1167-1369 |
3.28e-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: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIaHVGLHTLRSRISIIPQDPILFPGSLRMNL 1246
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1247 DLLQEHSDEAIWaalETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQM 1326
Cdd:TIGR01257 1024 ILFYAQLKGRSW---EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1199277034 1327 QAMLGSWFAQCTVLLIAHRlrsvMDCA-----RVLVMDKGQVAESGSP 1369
Cdd:TIGR01257 1101 WDLLLKYRSGRTIIMSTHH----MDEAdllgdRIAIISQGRLYCSGTP 1144
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
515-727 |
3.31e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 50.48 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 515 ITIHSATFAWSQESP-PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAvAYVPQEAW------ 587
Cdd:PRK13642 5 LEVENLVFKYEKESDvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVWnlrrki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 588 ---VQN-------TSVVENVCFGQELD----PPWLERVLEACaLQPDVDSFPEgihtsigEQGMNLSGGQKQRLSLARAV 653
Cdd:PRK13642 84 gmvFQNpdnqfvgATVEDDVAFGMENQgiprEEMIKRVDEAL-LAVNMLDFKT-------REPARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 654 YRKAAVYLLDDPLAALDAhVGQHVFNQVIGPGGLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELL 727
Cdd:PRK13642 156 ALRPEIIILDESTSMLDP-TGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
533-706 |
3.53e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.42 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 533 HRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQEAWVQNT-------------SVVENVCF 599
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLlylghqpgiktelTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 600 gqeldppwlervleACALQPDVDsfPEGIHTSIGEQGM---------NLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 670
Cdd:PRK13538 98 --------------YQRLHGPGD--DEALWEALAQVGLagfedvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1199277034 671 --------AHVGQHvfnqvigpggLLQGTTRILVTHA-LHILPQA 706
Cdd:PRK13538 162 kqgvarleALLAQH----------AEQGGMVILTTHQdLPVASDK 196
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
532-730 |
4.78e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 49.83 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-----------------AVAYVPQ--EAWVQNTS 592
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkKVSLVFQfpEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 593 VVENVCFG-----------QELDPPWLERVleacalqpdvdsfpeGIHTSIGEQG-MNLSGGQKQRLSLARAVYRKAAVY 660
Cdd:PRK13641 103 VLKDVEFGpknfgfsedeaKEKALKWLKKV---------------GLSEDLISKSpFELSGGQMRRVAIAGVMAYEPEIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 661 LLDDPLAALDAHvGQHVFNQVIgPGGLLQGTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELLQRK 730
Cdd:PRK13641 168 CLDEPAAGLDPE-GRKEMMQLF-KDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1150-1344 |
6.61e-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: 6.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1150 QIEFRDFGLRY--RPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGlhtlrSR 1227
Cdd:COG4525 3 MLTVRHVSVRYpgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG-----AD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1228 ISIIPQDPILFPG---------SLRM--------------NLDL--LQEHSDEAIWAaletvqlkalvaslpgqlqykca 1282
Cdd:COG4525 78 RGVVFQKDALLPWlnvldnvafGLRLrgvpkaerraraeeLLALvgLADFARRRIWQ----------------------- 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 1283 drgedLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQC--TVLLIAH 1344
Cdd:COG4525 135 -----LSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTgkGVFLITH 193
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1169-1371 |
6.65e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 50.49 E-value: 6.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1169 QGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTL----RSRISIIPQDPILFPgslrm 1244
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLS----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1245 nlDLLQEHSDE--AIWAALETVQLKALVASLPGQLqyKCADRGE----DLSVGQKQLLCLARALLRKTQILILDEATAAV 1318
Cdd:PRK10535 100 --HLTAAQNVEvpAVYAGLERKQRLLRAQELLQRL--GLEDRVEyqpsQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 1319 DPGTELQMQAMLGSWFAQC-TVLLIAHRLRSVMDCARVLVMDKGQVAeSGSPAQ 1371
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 ... |
1167-1374 |
6.71e-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: 6.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASgLLRLQEAAEGgiwIDGVPIAHVGL------------------------- 1221
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMH-VLRGMDQYEP---TSGRIIYHVALcekcgyverpskvgepcpvcggtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1222 --------------HTLRSRISIIPQDPILFPGSLRMnLDLLQEHSDEAIWAALETVQlKALVASLPGQLQYKCADRGED 1287
Cdd:TIGR03269 91 peevdfwnlsdklrRRIRKRIAIMLQRTFALYGDDTV-LDNVLEALEEIGYEGKEAVG-RAVDLIEMVQLSHRITHIARD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1288 LSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAML--GSWFAQCTVLLIAHRLRSVMDCA-RVLVMDKGQVA 1364
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeeAVKASGISMVLTSHWPEVIEDLSdKAIWLENGEIK 248
|
250
....*....|
gi 1199277034 1365 ESGSPAQLLA 1374
Cdd:TIGR03269 249 EEGTPDEVVA 258
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1167-1382 |
7.57e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 49.24 E-value: 7.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSS---LASGLLrlqeAAEGGIWIDGVPIAHVGLHT------LRSRISIIPQDP-- 1235
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTmiqLTNGLI----ISETGQTIVGDYAIPANLKKikevkrLRKEIGLVFQFPey 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1236 ILFPGSLRMNLDL----LQEHSDEAIWAALETVQLkalvASLPGQLqykcADRGE-DLSVGQKQLLCLARALLRKTQILI 1310
Cdd:PRK13645 102 QLFQETIEKDIAFgpvnLGENKQEAYKKVPELLKL----VQLPEDY----VKRSPfELSGGQKRRVALAGIIAMDGNTLV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 1311 LDEATAAVDPGTE---LQMQAMLGSWFAQcTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQKGLFYRL 1382
Cdd:PRK13645 174 LDEPTGGLDPKGEedfINLFERLNKEYKK-RIIMVTHNMDQVLRIAdEVIVMHEGKVISIGSPFEIFSNQELLTKI 248
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
530-730 |
7.80e-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: 7.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 530 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEG-FVSIEGA-VAYVPQEAWVQNT-SVVENVCFG-QEL-- 603
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGeARPQPGIkVGYLPQEPQLDPTkTVRENVEEGvAEIkd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 604 -------------DPPWLERVL--EACALQPDVDSfpEGIHT--SIGEQGM-------------NLSGGQKQRLSLARAV 653
Cdd:TIGR03719 99 aldrfneisakyaEPDADFDKLaaEQAELQEIIDA--ADAWDldSQLEIAMdalrcppwdadvtKLSGGERRRVALCRLL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 654 YRKAAVYLLDDPLAALDAH----VGQHVFNQvigPGgllqgtTRILVTHALHILPQ-ADWIIVLANG-AIAEMGSYQELL 727
Cdd:TIGR03719 177 LSKPDMLLLDEPTNHLDAEsvawLERHLQEY---PG------TVVAVTHDRYFLDNvAGWILELDRGrGIPWEGNYSSWL 247
|
...
gi 1199277034 728 QRK 730
Cdd:TIGR03719 248 EQK 250
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1169-1266 |
8.16e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 48.26 E-value: 8.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1169 QGVSFKIHAGEKVGIVGRTGAGKSSL---ASGLLRlqeAAEGGIWIDGVPIAHVGLHTLRSrisiipqdpILFPG----- 1240
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLlriLAGLAR---PDAGEVLWQGEPIRRQRDEYHQD---------LLYLGhqpgi 85
|
90 100 110
....*....|....*....|....*....|....
gi 1199277034 1241 --------SLRMNLDLLQEHSDEAIWAALETVQL 1266
Cdd:PRK13538 86 kteltaleNLRFYQRLHGPGDDEALWEALAQVGL 119
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1168-1365 |
8.83e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.17 E-value: 8.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1168 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIA-HVGLHTLRSRISIIPQ---DPILFPG-SL 1242
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITEsrrDNGFFPNfSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1243 RMNLDLLQEHSD---EAIWAALETVQLKALVASLPGQLQYKCADRGE---DLSVGQKQLLCLARALLRKTQILILDEATA 1316
Cdd:PRK09700 359 AQNMAISRSLKDggyKGAMGLFHEVDEQRTAENQRELLALKCHSVNQnitELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 1317 AVDPGTELQMQAMLGSWFAQC-TVLLIAHRLRSVMD-CARVLVMDKGQVAE 1365
Cdd:PRK09700 439 GIDVGAKAEIYKVMRQLADDGkVILMVSSELPEIITvCDRIAVFCEGRLTQ 489
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1167-1200 |
1.05e-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: 1.05e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSS---LASGLLR 1200
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTtikMLTGILV 73
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
532-678 |
1.34e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFV--------------SIEGAVAYVPQEA-WVQNTSVVEN 596
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSIlfqgkeidfksskeALENGISMVHQELnLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 597 VCFGQE------LDPPWLERVLEACALQPDVDSFPEgihtsigEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 670
Cdd:PRK10982 94 MWLGRYptkgmfVDQDKMYRDTKAIFDELDIDIDPR-------AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
....*...
gi 1199277034 671 AHVGQHVF 678
Cdd:PRK10982 167 EKEVNHLF 174
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
535-729 |
1.34e-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: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYVPQEAWV----------QN--TS--------- 592
Cdd:COG4608 37 VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQdITGLSGRELRplrrrmqmvfQDpyASlnprmtvgd 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 593 ------VVENVCFGQELDppwlERV---LEACALQPD-VDSFPegiHTsigeqgmnLSGGQKQRLSLARAVYRKAAVYLL 662
Cdd:COG4608 117 iiaeplRIHGLASKAERR----ERVaelLELVGLRPEhADRYP---HE--------FSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199277034 663 DDPLAALDAHVGQHVFNqvigpggLLQ------GTTRILVTHAL----HIlpqADWIIVLANGAIAEMGSYQELLQR 729
Cdd:COG4608 182 DEPVSALDVSIQAQVLN-------LLEdlqdelGLTYLFISHDLsvvrHI---SDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
532-712 |
1.35e-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: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRinLTVPQ-GCLLAVVGPVGAGKSSLLSALLGELSKVEGfvsiegavAYVPQEAWvqnTSVVENvcF-GQELDPpWLE 609
Cdd:cd03236 17 LHR--LPVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLG--------KFDDPPDW---DEILDE--FrGSELQN-YFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 610 RVLEA---CALQPD-VDSFPEGIHTSIG-------EQGM-------------------NLSGGQKQRLSLARAVYRKAAV 659
Cdd:cd03236 81 KLLEGdvkVIVKPQyVDLIPKAVKGKVGellkkkdERGKldelvdqlelrhvldrnidQLSGGELQRVAIAAALARDADF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 660 YLLDDPLAALDahVGQHvFNQVIGPGGLLQGTTRILVT-HALHILPQ-ADWIIVL 712
Cdd:cd03236 161 YFFDEPSSYLD--IKQR-LNAARLIRELAEDDNYVLVVeHDLAVLDYlSDYIHCL 212
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
535-727 |
1.36e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 48.39 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKvEGFVSIEGAvayvPQEAWVQNTSVVENVCFGQELDPPWLERVLEA 614
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQ----PLEAWSAAELARHRAYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 615 CALqpdvdSFPEGIHTSIGEQGMN------------------LSGGQKQRLSLARA---VYRKAAVY----LLDDPLAAL 669
Cdd:PRK03695 90 LTL-----HQPDKTRTEAVASALNevaealglddklgrsvnqLSGGEWQRVRLAAVvlqVWPDINPAgqllLLDEPMNSL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 670 DahVGQHV-----FNQVIGpggllQGTTRILVTHAL-HILPQADWIIVLANGAIAEMGSYQELL 727
Cdd:PRK03695 165 D--VAQQAaldrlLSELCQ-----QGIAVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
532-719 |
1.49e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 47.85 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-----------------VAYVPQE-AWVQNTSV 593
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQplhqmdeearaklrakhVGFVFQSfMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 594 VENVcfgqELdpPWLER-------------VLEACALQPDVDSFPEgihtsigeqgmNLSGGQKQRLSLARAVYRKAAVY 660
Cdd:PRK10584 106 LENV----EL--PALLRgessrqsrngakaLLEQLGLGKRLDHLPA-----------QLSGGEQQRVALARAFNGRPDVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 661 LLDDPLAALDAHVGQHVFNqvigpggLL------QGTTRILVTHALHILPQADWIIVLANGAIAE 719
Cdd:PRK10584 169 FADEPTGNLDRQTGDKIAD-------LLfslnreHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
532-793 |
1.50e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.40 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAV--AYVPQ---------EAWVQNTSVVENvcfg 600
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIklGYFAQhqleflradESPLQHLARLAP---- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 601 QELDPPwLERVLEACALQPDvdsfpegihtSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQ 680
Cdd:PRK10636 404 QELEQK-LRDYLGGFGFQGD----------KVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEA 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 681 VIGPGGLLqgttrILVTHALHIL-PQADWIIVLANGAIA----EMGSYQELlqrkgalvcLLDQARQpgdrgegETEPGT 755
Cdd:PRK10636 473 LIDFEGAL-----VVVSHDRHLLrSTTDDLYLVHDGKVEpfdgDLEDYQQW---------LSDVQKQ-------ENQTDE 531
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1199277034 756 STKDPRGTSA-GRRPELRRERSIKSVPE---KDRTTSEAQTE 793
Cdd:PRK10636 532 APKENNANSAqARKDQKRREAELRTQTQplrKEIARLEKEME 573
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1168-1377 |
2.41e-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: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1168 VQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQ--EAAEGGIWIDGVPIAHVGLHtLRSR--ISIIPQDPILFPGslr 1243
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPE-ERARlgIFLAFQYPPEIPG--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1244 mnldllqehsdeaiwaaletVQLKALVASLpgqlqykcadrGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPgTE 1323
Cdd:cd03217 92 --------------------VKNADFLRYV-----------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI-DA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1324 LQMQAMLGSWFAQ--CTVLLIAH--RLRSVMDCARVLVMDKGQVAESGSP--AQLLAQKG 1377
Cdd:cd03217 140 LRLVAEVINKLREegKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKelALEIEKKG 199
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
640-726 |
2.52e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 48.16 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 640 SGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNqvigpggLLQ------GTTRILVTHAL----HIlpqADWI 709
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVN-------LLQqlqremGLSLIFIAHDLavvkHI---SDRV 232
|
90
....*....|....*..
gi 1199277034 710 IVLANGAIAEMGSYQEL 726
Cdd:PRK15079 233 LVMYLGHAVELGTYDEV 249
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1156-1373 |
2.64e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.37 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1156 FGLRYRP--ELPLAVQG---------VSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIA-HVGLHT 1223
Cdd:PRK11288 246 YGYRPRPlgEVRLRLDGlkgpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1224 LRSRISIIPQD----PILFPGSLRMNLDL-LQEHSDEAIWaALETVQLKALVASLPGQLQYKCADRGED---LSVGQKQL 1295
Cdd:PRK11288 326 IRAGIMLCPEDrkaeGIIPVHSVADNINIsARRHHLRAGC-LINNRWEAENADRFIRSLNIKTPSREQLimnLSGGNQQK 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1296 LCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ-CTVLLIAHRLRSVMDCA-RVLVMDKGQVA-----ESGS 1368
Cdd:PRK11288 405 AILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQgVAVLFVSSDLPEVLGVAdRIVVMREGRIAgelarEQAT 484
|
....*
gi 1199277034 1369 PAQLL 1373
Cdd:PRK11288 485 ERQAL 489
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
530-672 |
2.80e-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: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 530 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGelskveGFVSIEGAVAYVPQEAWV--------------------- 588
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG------NYLPDSGSILVRHDGGWVdlaqaspreilalrrrtigyv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 589 -QNTSVVENVcfgqeldpPWLERVLEAcALQPDVDSfpegiHTSIGEQG-----MNL------------SGGQKQRLSLA 650
Cdd:COG4778 99 sQFLRVIPRV--------SALDVVAEP-LLERGVDR-----EEARARARellarLNLperlwdlppatfSGGEQQRVNIA 164
|
170 180
....*....|....*....|..
gi 1199277034 651 RAVYRKAAVYLLDDPLAALDAH 672
Cdd:COG4778 165 RGFIADPPLLLLDEPTASLDAA 186
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1167-1319 |
2.86e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 46.79 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG---LHTLRSRISIIPQD-PILFPGSL 1242
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRRQIGMIFQDhHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1243 RMNLDL---LQEHSDEAIW----AALETVQLKALVASLPGQlqykcadrgedLSVGQKQLLCLARALLRKTQILILDEAT 1315
Cdd:PRK10908 97 YDNVAIpliIAGASGDDIRrrvsAALDKVGLLDKAKNFPIQ-----------LSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
....
gi 1199277034 1316 AAVD 1319
Cdd:PRK10908 166 GNLD 169
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
532-649 |
2.99e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.58 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------------VAYVPQ---EAWVQNTSVV 594
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGdmadarhrravcprIAYMPQglgKNLYPTLSVF 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 595 ENV-----CFGQelDPPW----LERVLEACALQPDVDSfPEGihtsigeqgmNLSGGQKQRLSL 649
Cdd:NF033858 97 ENLdffgrLFGQ--DAAErrrrIDELLRATGLAPFADR-PAG----------KLSGGMKQKLGL 147
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
532-670 |
3.28e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.10 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------------VAYVPQE----AWVQNTSV 593
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsprerrrlgVAYIPEDrlgrGLVPDMSV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 594 VENVCFGQELDPPWLERVLeacaLQPD---------VDSF---PEGIHTSIGeqgmNLSGGQKQRLSLARAVYRKAAVYL 661
Cdd:COG3845 354 AENLILGRYRRPPFSRGGF----LDRKairafaeelIEEFdvrTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLI 425
|
....*....
gi 1199277034 662 LDDPLAALD 670
Cdd:COG3845 426 AAQPTRGLD 434
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
638-727 |
3.39e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.39 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 638 NLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNqvIGPGGLLQGTTRILVTHAL-HILPQADWIIVLANGA 716
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLdNVLEWTKRTIFFKDGK 242
|
90
....*....|.
gi 1199277034 717 IAEMGSYQELL 727
Cdd:PRK13651 243 IIKDGDTYDIL 253
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1151-1365 |
3.99e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 47.75 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYrPELPLaVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIwidgvpiaHVGlHTLrsRISI 1230
Cdd:COG0488 316 LELEGLSKSY-GDKTL-LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV--------KLG-ETV--KIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1231 IPQDPILFPGSLRMnLDLLQEHSDEAiwaalETVQLKALVASL--PGQLQYKcadRGEDLSVGQKQLLCLARALLRKTQI 1308
Cdd:COG0488 383 FDQHQEELDPDKTV-LDELRDGAPGG-----TEQEVRGYLGRFlfSGDDAFK---PVGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1309 LILDEATAAVDPGTELQMQAMLGSWfaQCTVLLIAH-R--LRSVmdCARVLVMDKGQVAE 1365
Cdd:COG0488 454 LLLDEPTNHLDIETLEALEEALDDF--PGTVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1172-1383 |
4.12e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1172 SFKIHAGEKVGIVGRTGAGKSSLA---SGLLRLqeaAEGGIWIDGVPIAHVGLHTLRSRISIIPQdpilfpgslRMNLDL 1248
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALAralAGELPL---LSGERQSQFSHITRLSFEQLQKLVSDEWQ---------RNNTDM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1249 LQEHSDEAIWAALETVQLK----ALVASLPGQLQYK--CADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGT 1322
Cdd:PRK10938 91 LSPGEDDTGRTTAEIIQDEvkdpARCEQLAQQFGITalLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 1323 ELQMQAMLGSWFAQ-CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQkGLFYRLA 1383
Cdd:PRK10938 171 RQQLAELLASLHQSgITLVLVLNRFDEIPDFVqFAGVLADCTLAETGEREEILQQ-ALVAQLA 232
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
534-670 |
4.50e-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: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 534 RINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAV--AYVPQ--EAWVQNTSVVENVCFGQEldppwle 609
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVklAYVDQsrDALDPNKTVWEEISGGLD------- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 610 rvleacalqpdvdsfpegiHTSIGEQGMN---------------------LSGGQKQRLSLARAVYRKAAVYLLDDPLAA 668
Cdd:TIGR03719 413 -------------------IIKLGKREIPsrayvgrfnfkgsdqqkkvgqLSGGERNRVHLAKTLKSGGNVLLLDEPTND 473
|
..
gi 1199277034 669 LD 670
Cdd:TIGR03719 474 LD 475
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
535-729 |
4.80e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 47.66 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA-VAYVPQEAWVQNTSVVenvcF-------------G 600
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKpVTAEQPEDYRKLFSAV----FtdfhlfdqllgpeG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 601 QELDPPWLERVLEACALQPDVdSFPEGIHTSIgeqgmNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQhVFNQ 680
Cdd:PRK10522 418 KPANPALVEKWLERLKMAHKL-ELEDGRISNL-----KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRR-EFYQ 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 681 VIGPggLLQ--GTTRILVTHALHILPQADWIIVLANGAIAEM-GSYQELLQR 729
Cdd:PRK10522 491 VLLP--LLQemGKTIFAISHDDHYFIHADRLLEMRNGQLSELtGEERDAASR 540
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1167-1217 |
4.81e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.60 E-value: 4.81e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIA 1217
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR 69
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
532-716 |
5.27e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.48 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSAllgeLSKVEGFVSIEGAVAY--------------------VPQE-AWVQN 590
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKV----LSGVYPHGSYEGEILFdgevcrfkdirdsealgiviIHQElALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 591 TSVVENVCFGQE------LDppWLERVLEACALQPDVdsfpeGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDD 664
Cdd:NF040905 93 LSIAENIFLGNErakrgvID--WNETNRRARELLAKV-----GLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 665 PLAALDAHVGQHVFNqvigpggLL-----QGTTRILVTHALH-ILPQADWIIVLANGA 716
Cdd:NF040905 166 PTAALNEEDSAALLD-------LLlelkaQGITSIIISHKLNeIRRVADSITVLRDGR 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
535-718 |
5.52e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.60 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA--------------VAYVP----QEAWVQNTSVVEN 596
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpidirsprdairagIMLCPedrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 597 V---C------FGQELDPPWlERVLeacalqpdVDSFPE--GIHTSIGEQG-MNLSGGQKQRLSLARAVYRKAAVYLLDD 664
Cdd:PRK11288 352 InisArrhhlrAGCLINNRW-EAEN--------ADRFIRslNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199277034 665 PLAALDahVG-QHVFNQVIgpGGLL-QGTTRILVTHAL-HILPQADWIIVLANGAIA 718
Cdd:PRK11288 423 PTRGID--VGaKHEIYNVI--YELAaQGVAVLFVSSDLpEVLGVADRIVVMREGRIA 475
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1171-1350 |
5.65e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 46.26 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1171 VSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIwidgvpiahvgLHTLRSRISIIPQ----DPILfPGSLRMNL 1246
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVPQklylDTTL-PLTVNRFL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1247 DLLQEHSDEAIWAALETVQLKALVASlPGQlqykcadrgeDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTEL-- 1324
Cdd:PRK09544 91 RLRPGTKKEDILPALKRVQAGHLIDA-PMQ----------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVal 159
|
170 180 190
....*....|....*....|....*....|.
gi 1199277034 1325 -----QMQAMLGswfaqCTVLLIAHRLRSVM 1350
Cdd:PRK09544 160 ydlidQLRRELD-----CAVLMVSHDLHLVM 185
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
871-1077 |
6.35e-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: 46.47 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 871 ALRGGIFGLLGCLQAIGLFASMAAVL--LGG----ARASRLLFQRLlwdvVRSPISFFERTPIGHLLNRFSKET----DT 940
Cdd:cd18780 40 ALNQAVLILLGVVLIGSIATFLRSWLftLAGervvARLRKRLFSAI----IAQEIAFFDVTRTGELLNRLSSDTqvlqNA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 941 VDVDIPDKLRSLLMyAFGLLEVSLVVAVATPLATVAILPLFLLYAGFQSLYVVsscQLRRL---ESASYSSVCShmaETF 1017
Cdd:cd18780 116 VTVNLSMLLRYLVQ-IIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVR---KLSKKfqdALAAASTVAE---ESI 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1018 QGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLaanvellgNGLVFAAATCAV 1077
Cdd:cd18780 189 SNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGF--------NGFMGAAAQLAI 240
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1171-1367 |
6.45e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 46.16 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1171 VSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDG------VPIAHVGLHTLRSRISIIPQDPILFPG-SLR 1243
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQYNLWPHlTVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1244 MNL-----DLLQEHSDEAIWAA---LETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLARALLRKTQILILDEAT 1315
Cdd:PRK11124 101 QNLieapcRVLGLSKDQALARAeklLERLRLKPYADRFPLHL-----------SGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 1316 AAVDPGTELQMQAMLGSwFAQC--TVLLIAHRLRSVMDCA-RVLVMDKGQVAESG 1367
Cdd:PRK11124 170 AALDPEITAQIVSIIRE-LAETgiTQVIVTHEVEVARKTAsRVVYMENGHIVEQG 223
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
532-729 |
6.58e-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: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGavaYVPQE---AWVQNTSVVenvcFGQ------- 601
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG---YVPFKrrkEFARRIGVV----FGQrsqlwwd 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 602 --------------ELDPPWLERVLEACALQPDVDSFpegIHTSIgeqgMNLSGGQKQRLSLARAVYRKAAVYLLDDPLA 667
Cdd:COG4586 111 lpaidsfrllkaiyRIPDAEYKKRLDELVELLDLGEL---LDTPV----RQLSLGQRMRCELAAALLHRPKILFLDEPTI 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199277034 668 ALDAHVGQHV------FNQVigpggllQGTTRILVTH------ALhilpqADWIIVLANGAIAEMGSYQELLQR 729
Cdd:COG4586 184 GLDVVSKEAIreflkeYNRE-------RGTTILLTSHdmddieAL-----CDRVIVIDHGRIIYDGSLEELKER 245
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
535-730 |
6.79e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 46.72 E-value: 6.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGA------------VAYVPQ-EAWVQNTSVVENV-CFG 600
Cdd:PRK13537 26 LSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharqrVGVVPQfDNLDPDFTVRENLlVFG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 601 Q----------ELDPPwlerVLEACALQPDVDSfpegihtSIGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 670
Cdd:PRK13537 106 RyfglsaaaarALVPP----LLEFAKLENKADA-------KVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 671 AHVGQHVFNQVigPGGLLQGTTRILVTHALHILPQ-ADWIIVLANG-AIAEmGSYQELLQRK 730
Cdd:PRK13537 171 PQARHLMWERL--RSLLARGKTILLTTHFMEEAERlCDRLCVIEEGrKIAE-GAPHALIESE 229
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
876-1026 |
7.92e-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: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 876 IFGLLGCLQAIGLFASMAAVLL---GGARASRLLFQRLLWDVVRSPISFFERTPIGHLLNRFSKET----DTVDVDIPDK 948
Cdd:cd18573 43 FALALLGVFVVGAAANFGRVYLlriAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTsvvgKSLTQNLSDG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 949 LRSLLMYAFGlleVSLVVAVATPLATV--AILPLFLLYAGFQSLYvVSSCQLRRLESASYSSVCShmAETFQGSTVVRAF 1026
Cdd:cd18573 123 LRSLVSGVGG---IGMMLYISPKLTLVmlLVVPPIAVGAVFYGRY-VRKLSKQVQDALADATKVA--EERLSNIRTVRAF 196
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
637-715 |
7.99e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 45.64 E-value: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 637 MNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHV------FNQVigpggllqGTTRILVTHALHILPQADW-I 709
Cdd:PRK10908 136 IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIlrlfeeFNRV--------GVTVLMATHDIGLISRRSYrM 207
|
....*.
gi 1199277034 710 IVLANG 715
Cdd:PRK10908 208 LTLSDG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1167-1369 |
9.28e-05 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 46.48 E-value: 9.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLasglLRL----QEAAEGGIWIDGVPIAHV-----GLHTlrsrisiIPQDPIL 1237
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTV----LRLiagfETPDSGRIMLDGQDITHVpaenrHVNT-------VFQSYAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1238 FPG---------SLRMnldllQEHSDEAIWA----ALETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLARALLR 1304
Cdd:PRK09452 98 FPHmtvfenvafGLRM-----QKTPAAEITPrvmeALRMVQLEEFAQRKPHQL-----------SGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1305 KTQILILDEATAAVDPGTELQMQAMLGSWFAQC--TVLLIAHRLR---SVMDcaRVLVMDKGQVAESGSP 1369
Cdd:PRK09452 162 KPKVLLLDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEealTMSD--RIVVMRDGRIEQDGTP 229
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
906-1122 |
1.02e-04 |
|
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: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 906 LFQRLLwdvvRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLL---MYAFGLLEV--------SLVVAVATPLAT 974
Cdd:cd18552 78 LFDKLL----RLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVrdpLTVIGLLGVlfyldwklTLIALVVLPLAA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 975 VAIlplflLYAGfqslyvvsscqlRRLESASYSS------VCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISF 1048
Cdd:cd18552 154 LPI-----RRIG------------KRLRKISRRSqesmgdLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSM 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 1049 PRLVADRWLAANVELLGnGLVFAA----ATCAVLSkAHLSAG-LVGFsVSAALQVTQTLQWVVRNWTDLENSIVSVERM 1122
Cdd:cd18552 217 KIARARALSSPLMELLG-AIAIALvlwyGGYQVIS-GELTPGeFISF-ITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
512-729 |
1.27e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.39 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 512 KDCITIHSATFAWSQESP--PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVS--------------- 574
Cdd:PRK10261 10 RDVLAVENLNIAFMQEQQkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrrrsrqvie 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 575 -----------IEGA-VAYVPQE-------AWVQNTSVVENVCFGQELDPpwlERVLEACALQPDVDSFPEGiHTSIGEQ 635
Cdd:PRK10261 90 lseqsaaqmrhVRGAdMAMIFQEpmtslnpVFTVGEQIAESIRLHQGASR---EEAMVEAKRMLDQVRIPEA-QTILSRY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 636 GMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFnQVIgpgGLLQGTTR---ILVTHALHILPQ-ADWIIV 711
Cdd:PRK10261 166 PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQIL-QLI---KVLQKEMSmgvIFITHDMGVVAEiADRVLV 241
|
250
....*....|....*...
gi 1199277034 712 LANGAIAEMGSYQELLQR 729
Cdd:PRK10261 242 MYQGEAVETGSVEQIFHA 259
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
532-716 |
1.34e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.32 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG--------------AVAYVPQEAWVQNT-SVVEN 596
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhklaaqlGIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 597 VCFGQELDPP--------WLERVLEACALQPDVdsfpeGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAA 668
Cdd:PRK09700 101 LYIGRHLTKKvcgvniidWREMRVRAAMMLLRV-----GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 669 L-DAHVGQ--HVFNQVIGpggllQGTTRILVTHAL-HILPQADWIIVLANGA 716
Cdd:PRK09700 176 LtNKEVDYlfLIMNQLRK-----EGTAIVYISHKLaEIRRICDRYTVMKDGS 222
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
603-712 |
1.71e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 603 LDPPWLERVLEA-CALQPDvdsfpegiHTSIGEQGMNLSGGQKQRLSLAR---AVYRKAAVYLLDDPLAAL---DAHVGQ 675
Cdd:PRK00635 781 LDEPSIHEKIHAlCSLGLD--------YLPLGRPLSSLSGGEIQRLKLAYellAPSKKPTLYVLDEPTTGLhthDIKALI 852
|
90 100 110
....*....|....*....|....*....|....*..
gi 1199277034 676 HVFNQVIgpgglLQGTTRILVTHALHILPQADWIIVL 712
Cdd:PRK00635 853 YVLQSLT-----HQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1167-1366 |
2.06e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVG-LHTLRSRISIIPQDPILFPG-SLRM 1244
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGpKSSQEAGIGIIHQELNLIPQlTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1245 NLDLLQEHSDeaIWAALETVQLKA----LVASLpgQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAV-D 1319
Cdd:PRK10762 99 NIFLGREFVN--RFGRIDWKKMYAeadkLLARL--NLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199277034 1320 PGT--------ELQMQAmlgswfaqCTVLLIAHRLRSVMD-CARVLVMDKGQ-VAES 1366
Cdd:PRK10762 175 TETeslfrvirELKSQG--------RGIVYISHRLKEIFEiCDDVTVFRDGQfIAER 223
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
197-369 |
2.23e-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: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 197 FLLGTLSLIISDVFRFTVPKLLSLFLEFIGDPKPPAWKGYLLAVLMFLSACLQTLFeqQNMYRLKV------LQMRLRSA 270
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTASQLLRYALLILLLALLIGIF--RFLWRYLIfgasrrIEYDLRND 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 271 ItglvYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTES----VLYL-NGLWLPLVWIVVCFVYLWQLlgpsALTAIAVF 345
Cdd:cd18541 79 L----FAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMAlgpgILYLvDALFLGVLVLVMMFTISPKL----TLIALLPL 150
|
170 180
....*....|....*....|....
gi 1199277034 346 LSLLPLNFFISKKRNHHQEEQMRQ 369
Cdd:cd18541 151 PLLALLVYRLGKKIHKRFRKVQEA 174
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
614-670 |
2.27e-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: 2.27e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 614 ACALQP--DVDSFPeGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 670
Cdd:cd03222 46 AGQLIPngDNDEWD-GITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLD 103
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
865-1096 |
2.35e-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: 44.78 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 865 GQQTQAALRGGIFGLLG--CLQAIGLFASMAAVLLGGARAS----RLLFQRLLwdvvRSPISFFERTPIGHLLNRFSkeT 938
Cdd:cd18575 28 AAGNTALLNRAFLLLLAvaLVLALASALRFYLVSWLGERVVadlrKAVFAHLL----RLSPSFFETTRTGEVLSRLT--T 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 939 DT------VDVDIPDKLRSLLMYAFGL-------LEVSLVVAVATPLatvAILPLFLLyagfqslyvvsSCQLRRLESAS 1005
Cdd:cd18575 102 DTtliqtvVGSSLSIALRNLLLLIGGLvmlfitsPKLTLLVLLVIPL---VVLPIILF-----------GRRVRRLSRAS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1006 ---YSSVCSHMAETFQGSTVVRAFrTQAPFVAQN-NARVDESQRISFPRLVADRWLAANVELlgngLVFAAATC------ 1075
Cdd:cd18575 168 qdrLADLSAFAEETLSAIKTVQAF-TREDAERQRfATAVEAAFAAALRRIRARALLTALVIF----LVFGAIVFvlwlga 242
|
250 260
....*....|....*....|...
gi 1199277034 1076 -AVLSKAhLSAG-LVGFSVSAAL 1096
Cdd:cd18575 243 hDVLAGR-MSAGeLSQFVFYAVL 264
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1171-1375 |
2.51e-04 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 45.10 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1171 VSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHvglHTLRSR-ISIIPQDPILFPG--------- 1240
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH---RSIQQRdICMVFQSYALFPHmslgenvgy 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1241 SLRMnLDLLQEHSDEAIWAALETVQLKALvaslpgqlqykcADRGED-LSVGQKQLLCLARALLRKTQILILDEATAAVD 1319
Cdd:PRK11432 102 GLKM-LGVPKEERKQRVKEALELVDLAGF------------EDRYVDqISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 1320 PG---------TELQMQAMLgswfaqcTVLLIAH---RLRSVMDcaRVLVMDKGQVAESGSPAQLLAQ 1375
Cdd:PRK11432 169 ANlrrsmrekiRELQQQFNI-------TSLYVTHdqsEAFAVSD--TVIVMNKGKIMQIGSPQELYRQ 227
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
876-1078 |
2.81e-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: 44.40 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 876 IFGLLGCLQAIGLFASMAAVLLGGARASRLLF----------QRLlwdvvrsPISFFERTPIGHLLNRFsketdTVDVDi 945
Cdd:cd18546 41 AAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYdlrlrvfahlQRL-------SLDFHERETSGRIMTRM-----TSDID- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 946 pdKLRSLLMYafGLleVSLVVAVATPLATVAIL-----PLFLLYAGFQSLYVVSSCQLRRLESASY-------SSVCSHM 1013
Cdd:cd18546 108 --ALSELLQT--GL--VQLVVSLLTLVGIAVVLlvldpRLALVALAALPPLALATRWFRRRSSRAYrrareriAAVNADL 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199277034 1014 AETFQGSTVVRAFR----TQAPFVAQNNARVDESQRISfpRLVAdrWLAANVELLGNglvfaAATCAVL 1078
Cdd:cd18546 182 QETLAGIRVVQAFRrerrNAERFAELSDDYRDARLRAQ--RLVA--IYFPGVELLGN-----LATAAVL 241
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
532-727 |
2.98e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 44.32 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGF-------------------VSIEGAVAYVPQEAWVQNTS 592
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdvllggrsifnyrdvLEFRRRVGMLFQRPNPFPMS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 593 VVENVCFGQELDP--PWLERVLEACALQPDVDSFpEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALD 670
Cdd:PRK14271 117 IMDNVLAGVRAHKlvPRKEFRGVAQARLTEVGLW-DAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199277034 671 AHVGQHVFNQVigpGGLLQGTTRILVTHALHILPQ-ADWIIVLANGAIAEMGSYQELL 727
Cdd:PRK14271 196 PTTTEKIEEFI---RSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLF 250
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1167-1365 |
3.59e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 43.92 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGlhtlrSRISIIPQDPILFP-----GS 1241
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVVFQNEGLLPwrnvqDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1242 LRMNLDLL---QEHSDEAIWAALETVQLKALVASLPGQLqykcadrgedlSVGQKQLLCLARALLRKTQILILDEATAAV 1318
Cdd:PRK11248 91 VAFGLQLAgveKMQRLEIAHQMLKKVGLEGAEKRYIWQL-----------SGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 1319 DPGTELQMQAMLGSWFAQC--TVLLIAHRLRSVMDCARVLVM---DKGQVAE 1365
Cdd:PRK11248 160 DAFTREQMQTLLLKLWQETgkQVLLITHDIEEAVFMATELVLlspGPGRVVE 211
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
863-1122 |
4.89e-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: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 863 VGGQQTQAALRGGIFGLLGCLQAIGLFASMA----AVLLGGARASRL---LFQRLLwdvvRSPISFFERTPIGHLLNRFS 935
Cdd:cd18563 32 QLGPGGNTSLLLLLVLGLAGAYVLSALLGILrgrlLARLGERITADLrrdLYEHLQ----RLSLSFFDKRQTGSLMSRVT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 936 KETDTVD---VD-IPDKLRSLLMyafgLLEVSLVVAVATP-LATVAILPLFLLYAGFQSLYVVSSCQLRRLeSASYSSVC 1010
Cdd:cd18563 108 SDTDRLQdflSDgLPDFLTNILM----IIGIGVVLFSLNWkLALLVLIPVPLVVWGSYFFWKKIRRLFHRQ-WRRWSRLN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1011 SHMAETFQGSTVVRAFrtqapfvAQNNarvDESQRisFpRLVADRWLAANVEL----------------LGNGLVFAAAT 1074
Cdd:cd18563 183 SVLNDTLPGIRVVKAF-------GQEK---REIKR--F-DEANQELLDANIRAeklwatffplltfltsLGTLIVWYFGG 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1199277034 1075 CAVLSkAHLSAG-LVGFsVSAALQVTQTLQWVVRNWTDLENSIVSVERM 1122
Cdd:cd18563 250 RQVLS-GTMTLGtLVAF-LSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
532-728 |
5.74e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 43.28 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 532 LHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELS--------KVEGFVSIEGAV-------------AYVPQEAWVQN 590
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPlaaidaprlarlrAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 591 T-SVVENVCFGQEldpPWLERVLEACALQPDVDSFP---EGIHTSIGEQGMNLSGGQKQRLSLARAV---------YRKA 657
Cdd:PRK13547 97 AfSAREIVLLGRY---PHARRAGALTHRDGEIAWQAlalAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 658 AVYLLDDPLAALD-AHvgQHvfnqvigpggLLQGTTRIL----------VTHALHILPQ-ADWIIVLANGAIAEMGSYQE 725
Cdd:PRK13547 174 RYLLLDEPTAALDlAH--QH----------RLLDTVRRLardwnlgvlaIVHDPNLAARhADRIAMLADGAIVAHGAPAD 241
|
...
gi 1199277034 726 LLQ 728
Cdd:PRK13547 242 VLT 244
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
640-726 |
7.14e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.93 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 640 SGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVIGpgglLQGTTR---ILVTHALHILPQ-ADWIIVLANG 715
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKS----LQQKHQlayLFISHDLHVVRAlCHQVIVLRQG 502
|
90
....*....|.
gi 1199277034 716 AIAEMGSYQEL 726
Cdd:PRK15134 503 EVVEQGDCERV 513
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1167-1213 |
8.15e-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: 8.15e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSlasgLLR----LQEAAEGGIWIDG 1213
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKST----LLRmvagLERITSGEIWIGG 65
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
854-1078 |
8.50e-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: 8.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 854 LSLWADDPAVGGQQTQAALRGGIFGLLGCLQAIGLFASMAAVLLGGARASRL---LFQRLLwdvvRSPISFFERTPIGHL 930
Cdd:cd18564 38 LLGLAPLLGPDPLALLLLAAAALVGIALLRGLASYAGTYLTALVGQRVVLDLrrdLFAHLQ----RLSLSFHDRRRTGDL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 931 LNRFsketdTVDVDipdKLRSLLMYAFGLLEVSLVVAVAT-----------PLATVAILPLFLLYA-GFQSLYVVSSCQL 998
Cdd:cd18564 114 LSRL-----TGDVG---AIQDLLVSGVLPLLTNLLTLVGMlgvmfwldwqlALIALAVAPLLLLAArRFSRRIKEASREQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 999 RRLESASYSSVcshmAETFQGSTVVRAF----RTQAPFVAQNNARVDESQRISfpRLVAdrWLAANVELLGnglvfAAAT 1074
Cdd:cd18564 186 RRREGALASVA----QESLSAIRVVQAFgreeHEERRFARENRKSLRAGLRAA--RLQA--LLSPVVDVLV-----AVGT 252
|
....
gi 1199277034 1075 CAVL 1078
Cdd:cd18564 253 ALVL 256
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1171-1372 |
8.78e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 43.48 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1171 VSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDG-----VPIAHVGlhtlrsrISIIPQDPILFPgslrmN 1245
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmndVPPAERG-------VGMVFQSYALYP-----H 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1246 LDLLQEHS-------------DEAIWAALETVQLKALVASLPgqlqykcadrgEDLSVGQKQLLCLARALLRKTQILILD 1312
Cdd:PRK11000 90 LSVAENMSfglklagakkeeiNQRVNQVAEVLQLAHLLDRKP-----------KALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 1313 EATAAVDPGTELQMQAMLGSWFA--QCTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQL 1372
Cdd:PRK11000 159 EPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHDQVEAMTLAdKIVVLDAGRVAQVGKPLEL 221
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
861-1071 |
8.80e-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: 42.86 E-value: 8.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 861 PAVGGQQTQAALRGGIFG--------LLGCLQAIGLFASMAAVLLG--GARASRLLFQRLLWDVVRSPISFFERTPIGHL 930
Cdd:cd18576 16 PLLAGQLIDAALGGGDTAslnqiallLLGLFLLQAVFSFFRIYLFArvGERVVADLRKDLYRHLQRLPLSFFHERRVGEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 931 LNRFSKET----DTVDVDIPDKLRSLLMYAFGlleVSLVVAVATPLATV--AILPLFLLYAgfqslyVVSSCQLRRLESA 1004
Cdd:cd18576 96 TSRLSNDVtqiqDTLTTTLAEFLRQILTLIGG---VVLLFFISWKLTLLmlATVPVVVLVA------VLFGRRIRKLSKK 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 1005 ---SYSSVCSHMAETFQGSTVVRAFrTQAPF-VAQNNARVDESQRISFPRLVADRWLAANVELLGNGLVFA 1071
Cdd:cd18576 167 vqdELAEANTIVEETLQGIRVVKAF-TREDYeIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVA 236
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
533-710 |
1.00e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.19 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 533 HRINLTV-----PQGCLLAVVGPVGAGKSSLLSAL---LGELSKVEGFVSIEGAVAYVPQEawvqntsvvenvcfgqeld 604
Cdd:cd03227 7 FPSYFVPndvtfGEGSLTIITGPNGSGKSTILDAIglaLGGAQSATRRRSGVKAGCIVAAV------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 605 ppwlervlEACalqpdvdsfpegIHTSIgeqgMNLSGGQKQRLSLARAV----YRKAAVYLLDDPLAALDAHVGQHVFNQ 680
Cdd:cd03227 68 --------SAE------------LIFTR----LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEA 123
|
170 180 190
....*....|....*....|....*....|
gi 1199277034 681 VIGPggLLQGTTRILVTHALHILPQADWII 710
Cdd:cd03227 124 ILEH--LVKGAQVIVITHLPELAELADKLI 151
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
876-1025 |
1.26e-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: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 876 IFGLLGCLQAIGLFASMAAVL---LGGAR-------ASRL-------LFQRLLwdvvRSPISFFERTPIGHLLNRFSkET 938
Cdd:cd18782 34 VQQDLATLYVIGVVMLVAALLeavLTALRtylftdtANRIdlelggtIIDHLL----RLPLGFFDKRPVGELSTRIS-EL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 939 DTVDVDIPDK-LRSLLMYAFGLLEVSLVVAVATPL--ATVAILPLFLLyagfqsLYVVSSCQLRRL---ESASYSSVCSH 1012
Cdd:cd18782 109 DTIRGFLTGTaLTTLLDVLFSVIYIAVLFSYSPLLtlVVLATVPLQLL------LTFLFGPILRRQirrRAEASAKTQSY 182
|
170
....*....|...
gi 1199277034 1013 MAETFQGSTVVRA 1025
Cdd:cd18782 183 LVESLTGIQTVKA 195
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1167-1374 |
1.69e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.10 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAaEGGIWIDGVPIAHVGLHTLRSR---------ISIIPQDP-- 1235
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKD-NWRVTADRMRFDDIDLLRLSPRerrklvghnVSMIFQEPqs 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1236 ILFPgSLRMNLDLLQehsdeAI--------------WAALETVQL---------KALVASLPGQLqykcadrgedlSVGQ 1292
Cdd:PRK15093 101 CLDP-SERVGRQLMQ-----NIpgwtykgrwwqrfgWRKRRAIELlhrvgikdhKDAMRSFPYEL-----------TEGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1293 KQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSP 1369
Cdd:PRK15093 164 CQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnnTTILLISHDLQMLSQWAdKINVLYCGQTVETAPS 243
|
....*
gi 1199277034 1370 AQLLA 1374
Cdd:PRK15093 244 KELVT 248
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1151-1372 |
1.84e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.04 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRpelplAVQGVSFKIHAGEKVGIVGRTGAGKS--SLA-SGLLRLqeaaEGGIWIDGVPIAHVGLHTLRSR 1227
Cdd:PRK11022 11 VHFGDESAPFR-----AVDRISYSVKQGEVVGIVGESGSGKSvsSLAiMGLIDY----PGRVMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1228 ---------ISIIPQDPI--LFP----GSLRMnlDLLQEHSD-EAIWAALETVQLKALVAsLPGQlqykcADRGE----D 1287
Cdd:PRK11022 82 errnlvgaeVAMIFQDPMtsLNPcytvGFQIM--EAIKVHQGgNKKTRRQRAIDLLNQVG-IPDP-----ASRLDvyphQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1288 LSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQ--CTVLLIAHRLRSVMDCA-RVLVMDKGQVA 1364
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKenMALVLITHDLALVAEAAhKIIVMYAGQVV 233
|
....*...
gi 1199277034 1365 ESGSPAQL 1372
Cdd:PRK11022 234 ETGKAHDI 241
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
546-569 |
1.91e-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: 1.91e-03
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1178-1351 |
3.07e-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: 39.66 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1178 GEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIwidgvpiahvglhtlrsrisiipqdpilfpgsLRMNLDLLQEHSDEAI 1257
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------------IYIDGEDILEEVLDQL 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1258 WAALETVqlkalvaslpgqlqykcadRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWF--- 1334
Cdd:smart00382 50 LLIIVGG-------------------KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLlll 110
|
170 180
....*....|....*....|.
gi 1199277034 1335 ----AQCTVLLIAHRLRSVMD 1351
Cdd:smart00382 111 lkseKNLTVILTTNDEKDLGP 131
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1154-1208 |
3.32e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 41.06 E-value: 3.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1199277034 1154 RDFGLRYRPELplAVQGVSFKIHAGEKVGIVGRTGAGKSSLASgLLRLQEAAEGG 1208
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 ... |
546-565 |
3.44e-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: 3.44e-03
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1151-1377 |
4.36e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.65 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1151 IEFRDFGLRYRPELplAVQGVSFKIHAGEKVGIVGRTGAGKSSL---ASGLLRLQEaaeGGIWIDGVPIAHVGlH--TLR 1225
Cdd:NF033858 2 ARLEGVSHRYGKTV--ALDDVSLDIPAGCMVGLIGPDGVGKSSLlslIAGARKIQQ---GRVEVLGGDMADAR-HrrAVC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1226 SRISIIPQD------PILfpgSLRMNLD-------LLQEHSDEAIWAALETVQLKALvaslpgqlqykcADR--GEdLSV 1290
Cdd:NF033858 76 PRIAYMPQGlgknlyPTL---SVFENLDffgrlfgQDAAERRRRIDELLRATGLAPF------------ADRpaGK-LSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1291 GQKQllclarallrKT----------QILILDEATAAVDPGTELQmqamlgswFAQctvlLIAhRLR------SV----- 1349
Cdd:NF033858 140 GMKQ----------KLglccalihdpDLLILDEPTTGVDPLSRRQ--------FWE----LID-RIRaerpgmSVlvata 196
|
250 260 270
....*....|....*....|....*....|...
gi 1199277034 1350 -MDCA----RVLVMDKGQVAESGSPAQLLAQKG 1377
Cdd:NF033858 197 yMEEAerfdWLVAMDAGRVLATGTPAELLARTG 229
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1171-1378 |
4.51e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 40.30 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1171 VSFKIHAGEKVGIVGRTGAGKSSL---ASGLLrlqeAAEGGIWIDGVPIAHVGLHTL-RSRISIIPQDPILFPGSLRMNL 1246
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLlarMAGLL----PGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1247 DLLQehSDEAIWAALETVqLKALVASLpgQLQYKCADRGEDLSVGQKQLLCLAR-------ALLRKTQILILDEATAAVD 1319
Cdd:PRK03695 91 TLHQ--PDKTRTEAVASA-LNEVAEAL--GLDDKLGRSVNQLSGGEWQRVRLAAvvlqvwpDINPAGQLLLLDEPMNSLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199277034 1320 PGTELQMQAMLgSWFAQC--TVLLIAHRLRSVMDCA-RVLVMDKGQVAESGSPAQLLAQKGL 1378
Cdd:PRK03695 166 VAQQAALDRLL-SELCQQgiAVVMSSHDLNHTLRHAdRVWLLKQGKLLASGRRDEVLTPENL 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
537-669 |
5.03e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.14 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 537 LTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEG-AVAY----VPQEA----------WVQNTSVVENVCFGQ 601
Cdd:PRK10762 25 LNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkEVTFngpkSSQEAgigiihqelnLIPQLTIAENIFLGR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 602 ELDPP-----WLERVLEACALQPDVdSFPEGIHTSIGEqgmnLSGGQKQRLSLARAVYRKAAVYLLDDPLAAL 669
Cdd:PRK10762 105 EFVNRfgridWKKMYAEADKLLARL-NLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1183-1368 |
5.78e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 40.63 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1183 IVGRTGAGKSSLA---SGLLRLQEA-----------AEGGIWidgvpiahvgLHTLRSRISIIPQDPILFPG-SLRMNLD 1247
Cdd:PRK11144 29 IFGRSGAGKTSLInaiSGLTRPQKGrivlngrvlfdAEKGIC----------LPPEKRRIGYVFQDARLFPHyKVRGNLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1248 LLQEHSDEAIWAALetVQL---KALVASLPGqlqykcadrgeDLSVGQKQLLCLARALLRKTQILILDEATAAVDpgteL 1324
Cdd:PRK11144 99 YGMAKSMVAQFDKI--VALlgiEPLLDRYPG-----------SLSGGEKQRVAIGRALLTAPELLLMDEPLASLD----L 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 1325 QMQAMLGSWFAQCT------VLLIAHRLRSVMDCA-RVLVMDKGQVAESGS 1368
Cdd:PRK11144 162 PRKRELLPYLERLAreinipILYVSHSLDEILRLAdRVVVLEQGKVKAFGP 212
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
238-399 |
6.27e-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: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 238 LAVLMFLSACLQTLFEQqnmYRLKVLQ---MRLRSAITGLVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTESVLYL- 313
Cdd:cd18586 44 LTLGMVVLLAFDGLLRQ---VRSRILQrvgLRLDVELGRRVFRAVLELPLESRPSGYWQQLLRDLDTLRNFLTGPSLFAf 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 314 -NGLWLPLVWIVVCFVYLWqlLGPSALTAIAVFLSLLPLNFFISKKRnhhQEEQMRQKDSRARLTSSILRNSKTIKFHGW 392
Cdd:cd18586 121 fDLPWAPLFLAVIFLIHPP--LGWVALVGAPVLVGLAWLNHRATRKP---LGEANEAQAARDALAAETLRNAETIKALGM 195
|
....*..
gi 1199277034 393 EGAFLDR 399
Cdd:cd18586 196 LGNLRRR 202
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
863-1047 |
6.41e-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: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 863 VGGQQTQAALRGGIFGLLGCLQAIGLFASMAAVLLG--GARASRLLfQRLLWD-VVRSPISFFERTPIGHLLNRFSKET- 938
Cdd:cd18551 26 IDALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGrtGERVVLDL-RRRLWRrLLRLPVSFFDRRRSGDLVSRVTNDTt 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 939 ---DTVDVDIPDKLRSLLMY--AFGLLEV-----SLVVAVATPLATVAILPLfllyagfqslyvvsscqLRRLESASY-- 1006
Cdd:cd18551 105 llrELITSGLPQLVTGVLTVvgAVVLMFLldwvlTLVTLAVVPLAFLIILPL-----------------GRRIRKASKra 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1199277034 1007 ----SSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRIS 1047
Cdd:cd18551 168 qdalGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAG 212
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
530-584 |
6.54e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.65 E-value: 6.54e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199277034 530 PCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFV--SIEGAVAYVPQ 584
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 ... |
918-1121 |
7.39e-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: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 918 PISFFERTPIGHLLNRFsKETDTVDVDI-PDKLRSLLMYAFGLLEVSLVVAVATPLATVAILpLFLLYAGfqsLYVVSSC 996
Cdd:cd18568 89 PLSFFASRKVGDIITRF-QENQKIRRFLtRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLA-FIPLYVL---LTLLSSP 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 997 QLRRLESASYSS---VCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVadrwLAANVELLGNgLVFAAA 1073
Cdd:cd18568 164 KLKRNSREIFQAnaeQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQK----LSIVLQLISS-LINHLG 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1199277034 1074 TCAVLS-------KAHLSAG-LVGFSVSAALqVTQTLQWVVRNWTDLENSIVSVER 1121
Cdd:cd18568 239 TIAVLWygaylviSGQLTIGqLVAFNMLFGS-VINPLLALVGLWDELQETRISVER 293
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1167-1366 |
7.66e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 7.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAA--EGGIWIDGVPiahVGLHTLRSR----ISIIPQDPILFPG 1240
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEV---CRFKDIRDSealgIVIIHQELALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1241 -SLRMNLDLLQEHSDEAI--WAA--LETVQLKALVAslpgqLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEAT 1315
Cdd:NF040905 93 lSIAENIFLGNERAKRGVidWNEtnRRARELLAKVG-----LDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199277034 1316 AA---------VDPGTELQMQAMlgswfaqcTVLLIAHRLRSVMDCA-RVLVMDKGQVAES 1366
Cdd:NF040905 168 AAlneedsaalLDLLLELKAQGI--------TSIIISHKLNEIRRVAdSITVLRDGRTIET 220
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1167-1372 |
9.03e-03 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 39.61 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1167 AVQGVSFKIHAGEKVGIVGRTGAGKSSLA---SGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLR 1243
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlSGLITGDKSAGSHIELLGRTVQREGRLARDIRKSRANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 1244 MNLDLLQEHSDEAI-----------WAALETVQlKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILD 1312
Cdd:PRK09984 99 NRLSVLENVLIGALgstpfwrtcfsWFTREQKQ-RALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199277034 1313 EATAAVDP-GTELQMQAMLG-SWFAQCTVLLIAHRLRSVMD-CARVLVMDKGQVAESGSPAQL 1372
Cdd:PRK09984 178 EPIASLDPeSARIVMDTLRDiNQNDGITVVVTLHQVDYALRyCERIVALRQGHVFYDGSSQQF 240
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
535-715 |
9.08e-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: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 535 INLTVPQGCLLAVVGPVGAGKSSLLSALLGEL-SKVEGFV--------------SIEGAVAYVPQEAwvQNTSVVENVCF 599
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNVfingkpvdirnpaqAIRAGIAMVPEDR--KRHGIVPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199277034 600 GQELDPPWLER-----VLEACALQPDVDSFPEGIHTSIGEQGM---NLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDA 671
Cdd:TIGR02633 357 GKNITLSVLKSfcfkmRIDAAAELQIIGSAIQRLKVKTASPFLpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1199277034 672 HVGQHVFNQVigpGGLLQ-GTTRILVTHAL-HILPQADWIIVLANG 715
Cdd:TIGR02633 437 GAKYEIYKLI---NQLAQeGVAIIVVSSELaEVLGLSDRVLVIGEG 479
|
|
| |
