|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
194-1437 |
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: 885.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 194 FSEKADFDNRVSQfAKAGLFSTLSFWWLNSLIKRGNVKDLEEEDIPELRKEERAETCYSLFEENLIEQKRR--------- 264
Cdd:TIGR00957 192 FSETNHDPNPCPE-SSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKtrkqpvsav 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 265 ------------------------LGSSCQ----PSILKVTVLCVWRELLTSGFFAFMKIVAVSAGPLLLNAFILVAEGN 316
Cdd:TIGR00957 271 ygkkdpskpkgssqldaneevealIVKSPHkprkPSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVNDP 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 317 ASFRYEGLVLAVLLFFSKMIESLSQRQWYFRCRIVGLRVRSLLTAAINKKQLRLNNSSRLIHSGSEIMNYATVDAYRIGE 396
Cdd:TIGR00957 351 MAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMD 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 397 FPYWFHQLWTTSFQLLIALGILFHSVGVATFSALAVIILTVLCNAPIAKLQNKFQSELMTSQDERLKACNESLVNMKVLK 476
Cdd:TIGR00957 431 LATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLK 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 477 LYAWESHFKKVIEKLRNIELKSLKAVQMRKAYNAVLFWSSPVFVSAATFATCYFLDIP--LRASNVFTFVATLRLVQDPV 554
Cdd:TIGR00957 511 LYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENniLDAEKAFVSLALFNILRFPL 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 555 RMIPDVIGVTIQAKVAFSRIATFLEAPELQGGERRRKQRSEGNQNAIIIKSASFSWEEkgSTKPNLRNVSLEVKFGEKVA 634
Cdd:TIGR00957 591 NILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGNSITVHNATFTWAR--DLPPTLNGITFSIPEGALVA 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 635 VCGEVGSGKSTLLAAILGETPCVSGTIDFYGTIAYVSQTAWIQTGTIRDNILFGGVMDEHRYRETIQKSSLDKDLELLPD 714
Cdd:TIGR00957 669 VVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPS 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 715 GDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQEYV--MDALAGKAVLLVTHQVDFLPAF 792
Cdd:TIGR00957 749 GDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQV 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 793 DSVLLMSDGEITEADTYQELLARSRDFQDLV--------NAHRETAGSERVVAVENPTKPV-----------KEINRVIS 853
Cdd:TIGR00957 829 DVIIVMSGGKISEMGSYQELLQRDGAFAEFLrtyapdeqQGHLEDSWTALVSGEGKEAKLIengmlvtdvvgKQLQRQLS 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 854 S-------QSKVLKPS-------------RLIKQEEREKGDTGLRPYIQYMnQNKGYIFFFIASLAQVTFAVGQILQNSW 913
Cdd:TIGR00957 909 AsssdsgdQSRHHGSSaelqkaeakeetwKLMEADKAQTGQVELSVYWDYM-KAIGLFITFLSIFLFVCNHVSALASNYW 987
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 914 MAANVDNP-----QVSTLKLILVYLLIGLCSVLCLMVRSVCVVIMCMKSSASLFSQLLNSLFRAPMSFYDSTPLGRILSR 988
Cdd:TIGR00957 988 LSLWTDDPmvngtQNNTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNR 1067
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 989 VSSDLSIVDLDVPFGLIFVVASSVNTGCSLGVLAIVTWQVLFVSVPMVYLAFRLQKYYFQTAKELMRINGTTRSYVANHL 1068
Cdd:TIGR00957 1068 FSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHF 1147
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1069 AESVAGAITIRAFDEEERFFKKSLTLIDTNASPFFHSFAANEWLIQRLETV-SAIVLASTAFCMIllPTGTFSSGFIGMA 1147
Cdd:TIGR00957 1148 NETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVgNCIVLFAALFAVI--SRHSLSAGLVGLS 1225
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1148 LSYGLSLNMGLVYSVQNQCYLANWIISVERLNQYTHLTPEAPEVIEETRPPVNWPVTGRVEISDLQIRYRRESPLVLKGI 1227
Cdd:TIGR00957 1226 VSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHI 1305
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1228 SCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQDPTLFNGTVRFNLDPLCQ 1307
Cdd:TIGR00957 1306 NVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQ 1385
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1308 HSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIR 1387
Cdd:TIGR00957 1386 YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR 1465
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|
gi 22331862 1388 REFADCTVITVAHRIPTVMDCTMVLSISDGRIVEYDEPMKLMKDENSLFG 1437
Cdd:TIGR00957 1466 TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYS 1515
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-1441 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 842.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 19 CTVRFLQICFGiTLSFLTLCI----CLFHKEPPKRihqfFCLRlvSALFNGIIGSL----------DLVLGIWV--LREN 82
Cdd:PLN03130 32 CATDSLVINIS-HLVLLGLCLyriwLIKKDHKVQR----FCLR--SKWYNYFLALLaayctaeplfRLVMGISVlnLDGQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 83 HSKPLILWLVILIQGFTWLFINLIICVRgTRIRKSSLRLLSIFSFFYGLVSSCLSVNNAVFGDELAVRTILDVLLLPGSV 162
Cdd:PLN03130 105 TSLPPFEIVSLIVEALTWCSMLVMIGVE-TKIYIREFRWYVRFAVIYVLVGDAVMLNLVLSVKEYYSSFVLYLYISEVAA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 163 LLL-----------LSAYKGYR--FDESGESSLYEPLnAGDSNGFSEKadfdnrvsqfaKAGLFSTLSFWWLNSLIKRGN 229
Cdd:PLN03130 184 QVLfgilllvyfpnLDPYPGYTpiGSESVDDYEYEEL-PGGEQICPER-----------HANIFSRIFFGWMTPLMQLGY 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 230 VKDLEEEDIPELRKEERAETCYSLFEENLIEQKRRlgssCQPSILKVTVLCVWRELLTSGFFAFMKIVAVSAGPLLLNaF 309
Cdd:PLN03130 252 KRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKK----PKPWLLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLLN-L 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 310 ILVAEGNASFRYEGLVLAVLLFFSKMIESLSQRQWYFRCRIVGLRVRSLLTAAINKKQLRLNNSSRLIHSGSEIMNYATV 389
Cdd:PLN03130 327 LLESMQNGEPAWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLVAAVFRKSLRLTHEGRKKFTSGKITNLMTT 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 390 DAYRIGEFPYWFHQLWTTSFQLLIALGILFHSVGVAT-FSALAVIILTVLCNAPIAKLQnKFQSELMTSQDERLKACNES 468
Cdd:PLN03130 407 DAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASlIGSLMLVLMFPIQTFIISKMQ-KLTKEGLQRTDKRIGLMNEV 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 469 LVNMKVLKLYAWESHFKKVIEKLRNIELKSLKAVQMRKAYNAVLFWSSPVFVSAATFATCYFLDIPLRASNVFTFVATLR 548
Cdd:PLN03130 486 LAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNSIPVLVTVVSFGVFTLLGGDLTPARAFTSLSLFA 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 549 LVQDPVRMIPDVIGVTIQAKVAFSRIATFLEA--------PELQGGerrrkqrsegnQNAIIIKSASFSWEEKGStKPNL 620
Cdd:PLN03130 566 VLRFPLFMLPNLITQAVNANVSLKRLEELLLAeervllpnPPLEPG-----------LPAISIKNGYFSWDSKAE-RPTL 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 621 RNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVS-GTIDFYGTIAYVSQTAWIQTGTIRDNILFGGVMDEHRYRET 699
Cdd:PLN03130 634 SNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERA 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 700 IQKSSLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQEYVMDALAGKAV 779
Cdd:PLN03130 714 IDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTR 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 780 LLVTHQVDFLPAFDSVLLMSDGEITEADTYQELLARSRDFQDLVnahrETAGS--------ERVVAVENPTKPVKEIN-- 849
Cdd:PLN03130 794 VLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLM----ENAGKmeeyveenGEEEDDQTSSKPVANGNan 869
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 850 ----RVISSQSKVLKPSRLIKQEEREKGDTGLRPYIQYMNQNKGYIFFFIASLAQVTFAVGQILQNSWMAANVDNpqvST 925
Cdd:PLN03130 870 nlkkDSSSKKKSKEGKSVLIKQEERETGVVSWKVLERYKNALGGAWVVMILFLCYVLTEVFRVSSSTWLSEWTDQ---GT 946
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 926 LK------LILVYLLIGLCSVLCLMVRSVCVVIMCMKSSASLFSQLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLD 999
Cdd:PLN03130 947 PKthgplfYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRN 1026
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1000 VP----------FGLI--FVVASSVNTgcsLGVLAIVTWQVLFVSVpmvYLafrlqkYYFQTAKELMRINGTTRSYVANH 1067
Cdd:PLN03130 1027 VAvfvnmflgqiFQLLstFVLIGIVST---ISLWAIMPLLVLFYGA---YL------YYQSTAREVKRLDSITRSPVYAQ 1094
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1068 LAESVAGAITIRAFDEEERFFKKSLTLIDTNASPFFHSFAANEWLIQRLETVSAIvlastafcMILLpTGTFS------- 1140
Cdd:PLN03130 1095 FGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGL--------MIWL-TASFAvmqngra 1165
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1141 ------SGFIGMALSYGLSLNmGLVYSVQNQCYLA-NWIISVERLNQYTHLTPEAPEVIEETRPPVNWPVTGRVEISDLQ 1213
Cdd:PLN03130 1166 enqaafASTMGLLLSYALNIT-SLLTAVLRLASLAeNSLNAVERVGTYIDLPSEAPLVIENNRPPPGWPSSGSIKFEDVV 1244
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1214 IRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQDPTL 1293
Cdd:PLN03130 1245 LRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVL 1324
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1294 FNGTVRFNLDPLCQHSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATAS 1373
Cdd:PLN03130 1325 FSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
1450 1460 1470 1480 1490 1500
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 1374 IDNATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGRIVEYDEPMKLMKDENSLFGKLVK 1441
Cdd:PLN03130 1405 VDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQ 1472
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-1440 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 801.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 19 CTVRFLQICFGiTLSFLTLCICLFHKEPPKRIHQFFCLRlvSALFNGIIGSL----------DLVLGIWV--LRENHSKP 86
Cdd:PLN03232 32 CAIDSLVMIVS-HSVLLGLCFYRIWIILDNAKAQIYVLR--KKYYNCVLGILacycvvepvlRLVMGISLfdMDEETDLP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 87 LILWLVILIQGFTWlFINLIICVRGTRIRKSSLRLLSIFSFFYGLVSSC------LSVNNAVfgDELAVRTILDVLLLPG 160
Cdd:PLN03232 109 PFEVASLMVEAFAW-FSMLVLIGLETKQYVKEFRWYVRFGVVYVLVADAvlldlvLPLKNSI--NRTALYLCISSRCCQA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 161 SVLLLLSAY-------KGYRF--DESGESSLYEPLNAGDsngfsekadfdnRVSQFAKAGLFSTLSFWWLNSLIKRGNVK 231
Cdd:PLN03232 186 LFGILLLVYipeldpyPGYHIlnNESLDNVEYDALRGGE------------NICPERYASIFSRIYFSWMTPLMQLGYRK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 232 DLEEEDIPELRKEERAETCYSLFEENLIEQKRRlgssCQPSILKVTVLCVWRELLTSGFFAFMKIVAVSAGPLLLNAFIL 311
Cdd:PLN03232 254 PITEKDVWQLDQWDQTETLIKRFQRCWTEESRR----PKPWLLRALNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLLQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 312 -VAEGNASfrYEGLVLAVLLFFSKMIESLSQRQWYFRCRIVGLRVRSLLTAAINKKQLRLNNSSRLIHSGSEIMNYATVD 390
Cdd:PLN03232 330 sMQEGDPA--WVGYVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 391 AYRIGEFPYWFHQLWTTSFQLLIALGILFHSVGVATFSALAVIILTVLCNAPIAKLQNKFQSELMTSQDERLKACNESLV 470
Cdd:PLN03232 408 ANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILA 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 471 NMKVLKLYAWESHFKKVIEKLRNIELKSLKAVQMRKAYNAVLFWSSPVFVSAATFATCYFLDIPLRASNVFTFVATLRLV 550
Cdd:PLN03232 488 SMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVL 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 551 QDPVRMIPDVIGVTIQAKVAFSRIATFLEA--------PELQGGerrrkqrsegnQNAIIIKSASFSWEEKgSTKPNLRN 622
Cdd:PLN03232 568 RSPLNMLPNLLSQVVNANVSLQRIEELLLSeerilaqnPPLQPG-----------APAISIKNGYFSWDSK-TSKPTLSD 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 623 VSLEVKFGEKVAVCGEVGSGKSTLLAAILGE-TPCVSGTIDFYGTIAYVSQTAWIQTGTIRDNILFGGVMDEHRYRETIQ 701
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGElSHAETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAID 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 702 KSSLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQEYVMDALAGKAVLL 781
Cdd:PLN03232 716 VTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVL 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 782 VTHQVDFLPAFDSVLLMSDGEITEADTYQELLARSRDFQDLV-NAHRETAGSERVVAVENPTK--PVKEIN----RVISS 854
Cdd:PLN03232 796 VTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMeNAGKMDATQEVNTNDENILKlgPTVTIDvserNLGST 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 855 QSKVLKPSRLIKQEEREKGDTGLRPYIQYMNQNKGYIFFFIASLAQVTFAVGQILQNSWMAANVDNpqvSTLK------L 928
Cdd:PLN03232 876 KQGKRGRSVLVKQEERETGIISWNVLMRYNKAVGGLWVVMILLVCYLTTEVLRVSSSTWLSIWTDQ---STPKsyspgfY 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 929 ILVYLLIGLCSVLCLMVRSVCVVIMCMKSSASLFSQLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLIFVV 1008
Cdd:PLN03232 953 IVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFM 1032
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1009 ASSVNTGCSLGVLAIVTWQVLFVSVPMVYLAFRLQKYYFQTAKELMRINGTTRSYVANHLAESVAGAITIRAFDEEERFF 1088
Cdd:PLN03232 1033 NQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMA 1112
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1089 KKSLTLIDTNASPFFHSFAANEWLIQRLETVSAIVLASTA-FCMILLPTGTFSSGF---IGMALSYGLSLNMGLVYSVQN 1164
Cdd:PLN03232 1113 KINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTAtFAVLRNGNAENQAGFastMGLLLSYTLNITTLLSGVLRQ 1192
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1165 QCYLANWIISVERLNQYTHLTPEAPEVIEETRPPVNWPVTGRVEISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTG 1244
Cdd:PLN03232 1193 ASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTG 1272
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1245 SGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQDPTLFNGTVRFNLDPLCQHSDAEIWEVLGKCQLKE 1324
Cdd:PLN03232 1273 AGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKD 1352
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1325 VVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIRREFADCTVITVAHRIPT 1404
Cdd:PLN03232 1353 VIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNT 1432
|
1450 1460 1470
....*....|....*....|....*....|....*.
gi 22331862 1405 VMDCTMVLSISDGRIVEYDEPMKLMKDENSLFGKLV 1440
Cdd:PLN03232 1433 IIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMV 1468
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
264-1440 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 624.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 264 RLGSSCQPSILKVTVLCVWRELLTSGFFAFMKIVAVSAGPLLLNAFI-LVAEGNASFRYeGLVLAVLLFFSKMIESLSQR 342
Cdd:PTZ00243 225 PPPTPKRLSLLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVkFLDADNATWGR-GLGLVLTLFLTQLIQSVCLH 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 343 QWY---FRCrivGLRVRSLLTAAINKKQLRLNNSSrLIH---SGSEIMNYATVDAYRIGEFPYWFHQLWTTSFQLLIALG 416
Cdd:PTZ00243 304 RFYyisIRC---GLQYRSALNALIFEKCFTISSKS-LAQpdmNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSIL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 417 ILFHSVGVATFSALAVIILTVLCNAPIAKLQNKFQSELMTSQDERLKACNESLVNMKVLKLYAWESHFKKVIEKLRNIEL 496
Cdd:PTZ00243 380 LLSRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRAREL 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 497 KSLKAVQMRKAYNAVLFWSSPVFVSAATFATCYFLDIPLRASNVFTFVATLRLVQDPVRMIPDVIGVTIQAKVAFSRIAT 576
Cdd:PTZ00243 460 RYLRDVQLARVATSFVNNATPTLMIAVVFTVYYLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRIST 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 577 FLEAP--------ELQGGERRRKQRSEGNQNAIIIKSAS--------------------------FSWE----------- 611
Cdd:PTZ00243 540 FLECDnatcstvqDMEEYWREQREHSTACQLAAVLENVDvtafvpvklprapkvktsllsralrmLCCEqcrptkrhpsp 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 612 ---------------------------------EKGSTKPN---------------LRNVSLEVKFGEKVAVCGEVGSGK 643
Cdd:PTZ00243 620 svvvedtdygspssasrhiveggtgggheatptSERSAKTPkmktddffelepkvlLRDVSVSVPRGKLTVVLGATGSGK 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 644 STLLAAILGETPCVSGTIDFYGTIAYVSQTAWIQTGTIRDNILFGGVMDEHRYRETIQKSSLDKDLELLPDGDQTEIGER 723
Cdd:PTZ00243 700 STLLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEK 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 724 GVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQEYVMDALAGKAVLLVTHQVDFLPAFDSVLLMSDGEI 803
Cdd:PTZ00243 780 GVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRV 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 804 ----TEAD-----TYQELLARSRDFQDLVN--AHRETAGSERV--VAVENPTKPVKEINRVISSQSKVLKPS--RLIKQE 868
Cdd:PTZ00243 860 efsgSSADfmrtsLYATLAAELKENKDSKEgdADAEVAEVDAApgGAVDHEPPVAKQEGNAEGGDGAALDAAagRLMTRE 939
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 869 EREKGDTGLRPYIQYMNQNKGYIfffIASLAQVTFAVGQILQNS-------WMAANVDNPQVSTLkliLVYLLIGLCSVL 941
Cdd:PTZ00243 940 EKASGSVPWSTYVAYLRFCGGLH---AAGFVLATFAVTELVTVSsgvwlsmWSTRSFKLSAATYL---YVYLGIVLLGTF 1013
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 942 CLMVR-SVCVVIMCMkSSASLFSQLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLIFVVASSVNTGCSLGV 1020
Cdd:PTZ00243 1014 SVPLRfFLSYEAMRR-GSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILV 1092
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1021 LAIVTWQVLFVSVPMVYLAFRLQKYYFQTAKELMRINGTTRSYVANHLAESVAGAITIRAFDEEERFFKKSLTLIDTNAS 1100
Cdd:PTZ00243 1093 TSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVYS 1172
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1101 PFFHSFAANEWLIQRLETVSAIVLASTAFCMILLPTGTFSSGFIGMAlsyGLSLNMGLVYSVQnqcylANWII------- 1173
Cdd:PTZ00243 1173 CSYLENVANRWLGVRVEFLSNIVVTVIALIGVIGTMLRATSQEIGLV---SLSLTMAMQTTAT-----LNWLVrqvatve 1244
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1174 ----SVERLNQYTHLTP--EAPE----------------------VIEETRPPVNWP---VTGRVEISDLQIRYRRESPL 1222
Cdd:PTZ00243 1245 admnSVERLLYYTDEVPheDMPEldeevdalerrtgmaadvtgtvVIEPASPTSAAPhpvQAGSLVFEGVQMRYREGLPL 1324
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1223 VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQDPTLFNGTVRFNL 1302
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV 1404
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1303 DPLCQHSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRR-SRVLVLDEATASIDNATDLI 1381
Cdd:PTZ00243 1405 DPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFILMDEATANIDPALDRQ 1484
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*....
gi 22331862 1382 LQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGRIVEYDEPMKLMKDENSLFGKLV 1440
Cdd:PTZ00243 1485 IQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMV 1543
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
205-1436 |
9.36e-153 |
|
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: 502.52 E-value: 9.36e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 205 SQFAKAGLFSTLSFWWLNSLIKRGNVKDLEEEDIPELRKEERAETCYSLFEEnliEQKRRLGSSCQ-PSILKVTVLCVWR 283
Cdd:TIGR01271 4 SPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLER---EWDRELASAKKnPKLLNALRRCFFW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 284 ELLTSGFFAFMKIVAVSAGPLLLNAFILVAEG-NASFRYEGLVLAVLLFFSKMIESLSQRQWYFRCRIVGLRVRSLLTAA 362
Cdd:TIGR01271 81 RFVFYGILLYFGEATKAVQPLLLGRIIASYDPfNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 363 INKKQLRLnnSSRLIH--SGSEIMNYATVDAYRIGEFPYWFHQLWTTSFQLLIALGILFHSVGVATFSALAVIILTVLCN 440
Cdd:TIGR01271 161 IYKKTLKL--SSRVLDkiSTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 441 APIAKLQNKFQSELMTSQDERLKACNESLVNMKVLKLYAWESHFKKVIEKLRNIELK-SLKAVQMRKAYNAVLFWSSPVF 519
Cdd:TIGR01271 239 ACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKlTRKIAYLRYFYSSAFFFSGFFV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 520 VSAATFATCYFLDIPLRasNVFT---FVATLRLVQdpVRMIPDVIGVTIQAKVAFSRIATFLEAPELQG----------- 585
Cdd:TIGR01271 319 VFLSVVPYALIKGIILR--RIFTtisYCIVLRMTV--TRQFPGAIQTWYDSLGAITKIQDFLCKEEYKTleynlttteve 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 586 ------------GERRRKQRSEGNQNAIIIKSAS-FSWEEKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILG 652
Cdd:TIGR01271 395 mvnvtaswdegiGELFEKIKQNNKARKQPNGDDGlFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 653 ETPCVSGTIDFYGTIAYVSQTAWIQTGTIRDNILFGGVMDEHRYRETIQKSSLDKDLELLPDGDQTEIGERGVNLSGGQK 732
Cdd:TIGR01271 475 ELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 733 QRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQEYVMDALAGKAVLLVTHQVDFLPAFDSVLLMSDGEITEADTYQEL 812
Cdd:TIGR01271 555 ARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 813 LARSRDFQ---------DLVNAHRE-----------------------------------TAGSERVVA-VENPTKPVKE 847
Cdd:TIGR01271 635 QAKRPDFSslllgleafDNFSAERRnsiltetlrrvsidgdstvfsgpetikqsfkqpppEFAEKRKQSiILNPIASARK 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 848 I-----------------------------------------------------------------------NRVISSQS 856
Cdd:TIGR01271 715 FsfvqmgpqkaqattiedavrepserkfslvpedeqgeeslprgnqyhhglqhqaqrrqsvlqlmthsnrgeNRREQLQT 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 857 KVLKPSRLIKQEE----------REKGDTGL----------------------------RPYIQYMNQNKGYIFFFI--- 895
Cdd:TIGR01271 795 SFRKKSSITQQNElaseldiysrRLSKDSVYeiseeineedlkecfaderenvfetttwNTYLRYITTNRNLVFVLIfcl 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 896 --------ASLAQV------TFAVGQILQNSWMAANVDNPQ----VSTLKLILVYLLIGLC-SVLCL-MVRSVCVVIMCM 955
Cdd:TIGR01271 875 viflaevaASLLGLwlitdnPSAPNYVDQQHANASSPDVQKpviiTPTSAYYIFYIYVGTAdSVLALgFFRGLPLVHTLL 954
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 956 KSSASLFSQLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLIFVVASSVNTGCSLGVLAIVTWQVLFVSVPM 1035
Cdd:TIGR01271 955 TVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPV 1034
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1036 VYLAFRLQKYYFQTAKELMRINGTTRSYVANHLAESVAGAITIRAFDEE---ERFFKKSLTLIDTNaspFFHSFAANEWL 1112
Cdd:TIGR01271 1035 AVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQsyfETLFHKALNLHTAN---WFLYLSTLRWF 1111
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1113 IQRLETVSAIVLASTAFCMILlpTGTFSSGFIGMALSYGLSLNMGLVYSVQNQCYLANWIISVERLNQYTHLTPEAPE-- 1190
Cdd:TIGR01271 1112 QMRIDIIFVFFFIAVTFIAIG--TNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRps 1189
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1191 ------------VIEETRPPVNWPVTGRVEISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLV 1258
Cdd:TIGR01271 1190 ggggkyqlstvlVIENPHAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL 1269
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1259 EpVGGKIVVDGVDISKIGVHDLRSRFGIIPQDPTLFNGTVRFNLDPLCQHSDAEIWEVLGKCQLKEVVQEKENGLDSLVV 1338
Cdd:TIGR01271 1270 S-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLV 1348
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1339 EDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGR 1418
Cdd:TIGR01271 1349 DGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSS 1428
|
1450
....*....|....*...
gi 22331862 1419 IVEYDEPMKLMkDENSLF 1436
Cdd:TIGR01271 1429 VKQYDSIQKLL-NETSLF 1445
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1205-1425 |
1.45e-125 |
|
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: 388.78 E-value: 1.45e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1205 GRVEISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRF 1284
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1285 GIIPQDPTLFNGTVRFNLDPLCQHSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRV 1364
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331862 1365 LVLDEATASIDNATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGRIVEYDEP 1425
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
601-802 |
5.13e-104 |
|
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: 329.43 E-value: 5.13e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 601 IIIKSASFSWEEKG-STKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGTIAYVSQTAWIQTG 679
Cdd:cd03250 1 ISVEDASFTWDSGEqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 680 TIRDNILFGGVMDEHRYRETIQKSSLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDA 759
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 22331862 760 HTASSLFQEYVMDALA-GKAVLLVTHQVDFLPAFDSVLLMSDGE 802
Cdd:cd03250 161 HVGRHIFENCILGLLLnNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
877-1421 |
1.15e-98 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 329.05 E-value: 1.15e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 877 LRPYIQYMNQNKGYIFF-FIASLAQVTFAVGQILQNSWMA-ANVDNPQVSTL-KLILVYLLIGLCSVLCLMVRSVCVVIM 953
Cdd:COG1132 9 LRRLLRYLRPYRGLLILaLLLLLLSALLELLLPLLLGRIIdALLAGGDLSALlLLLLLLLGLALLRALLSYLQRYLLARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 954 CMKSSASLFSQLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLIFVVASSVNTGCSLGVLAIVTWQ---VLF 1030
Cdd:COG1132 89 AQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRlalIVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1031 VSVPMVYLAFRlqkYYFQTAKELMRINGTTRSYVANHLAESVAGAITIRAFDEEERFFKKSLTLIDTNASPFFHSFAANE 1110
Cdd:COG1132 169 LVLPLLLLVLR---LFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1111 WLIQRLETVSAIVLAST-AFCMILLPTGTFSSGFIGMALSYGLSLNMGL--VYSVQNQcyLANWIISVERLNQYTHLTPE 1187
Cdd:COG1132 246 LFFPLMELLGNLGLALVlLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLrqLANVLNQ--LQRALASAERIFELLDEPPE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1188 APEVIEETRPPvnwPVTGRVEISDLQIRYRRESPlVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVV 1267
Cdd:COG1132 324 IPDPPGAVPLP---PVRGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1268 DGVDISKIGVHDLRSRFGIIPQDPTLFNGTVRFNL---DPlcQHSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNW 1344
Cdd:COG1132 400 DGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNL 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 1345 SMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGRIVE 1421
Cdd:COG1132 478 SGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVE 554
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
288-574 |
2.41e-94 |
|
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: 305.95 E-value: 2.41e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 288 SGFFAFMKIVAVSAGPLLLNAFIL-VAEGNASFRYEGLVLAVLLFFSKMIESLSQRQWYFRCRIVGLRVRSLLTAAINKK 366
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISyLSSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 367 QLRLNNSSRLIHSGSEIMNYATVDAYRIGEFPYWFHQLWTTSFQLLIALGILFHSVGVATFSALAVIILTVLCNAPIAKL 446
Cdd:cd18579 82 ALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 447 QNKFQSELMTSQDERLKACNESLVNMKVLKLYAWESHFKKVIEKLRNIELKSLKAVQMRKAYNAVLFWSSPVFVSAATFA 526
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 22331862 527 TCYFLDIPLRASNVFTFVATLRLVQDPVRMIPDVIGVTIQAKVAFSRI 574
Cdd:cd18579 242 TYVLLGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
844-1442 |
1.51e-90 |
|
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: 310.23 E-value: 1.51e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 844 PVKEINRVISSQSKVLKPSRLIKQEEREKgdTGLRPYIQYMNQNKGYIFF-FIASLAQVTFAVGQILQNSWMaanVD--- 919
Cdd:COG2274 113 SLEEFAESWTGVALLLEPTPEFDKRGEKP--FGLRWFLRLLRRYRRLLLQvLLASLLINLLALATPLFTQVV---IDrvl 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 920 -NPQVSTLKLILVYLLIGLCSVLCL-MVRSVCVVIMCMKSSASLFSQLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVD 997
Cdd:COG2274 188 pNQDLSTLWVLAIGLLLALLFEGLLrLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRDVESIRE 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 998 ----------LDVPFGLIFvvassvntgcsLGVLAIVTWQ----VLFVSVPMVYLAFRLQKYYFQTAKELMRINGTtrsy 1063
Cdd:COG2274 268 fltgslltalLDLLFVLIF-----------LIVLFFYSPPlalvVLLLIPLYVLLGLLFQPRLRRLSREESEASAK---- 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1064 VANHLAESVAGAITIRAFDEEERFFKKSLTLIDTNASPFFHSFAANEW------LIQRLETVSAIVLASTafcMIL---L 1134
Cdd:COG2274 333 RQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLlstlsgLLQQLATVALLWLGAY---LVIdgqL 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1135 PTGTF--SSGFIGMALSYGLSLnMGLVYSVQNQcylanwIISVERLNQYTHLTPEAPEVIEETRPPvnwPVTGRVEISDL 1212
Cdd:COG2274 410 TLGQLiaFNILSGRFLAPVAQL-IGLLQRFQDA------KIALERLDDILDLPPEREEGRSKLSLP---RLKGDIELENV 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1213 QIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQDPT 1292
Cdd:COG2274 480 SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVF 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1293 LFNGTVRFNL---DPlcQHSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDE 1369
Cdd:COG2274 560 LFSGTIRENItlgDP--DATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDE 637
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22331862 1370 ATASIDNATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGRIVE---YDEPMKLmkdeNSLFGKLVKE 1442
Cdd:COG2274 638 ATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEdgtHEELLAR----KGLYAELVQQ 709
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1201-1425 |
1.36e-89 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 289.31 E-value: 1.36e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1201 WPVTGRVEISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDL 1280
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1281 RSRFGIIPQDPTLFNGTVRFNLDPLCQHSDAEIWEVLGkcqlkevvqekengldslVVEDGSNWSMGQRQLFCLGRAVLR 1360
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 1361 RSRVLVLDEATASIDNATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGRIVEYDEP 1425
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
889-1182 |
7.35e-84 |
|
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: 276.69 E-value: 7.35e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 889 GYIFFFIASLAQVTFAVGQILQNSWMAANVDNPQVSTLKLILVYLLIGL-CSVLCLMVRSVCVVIMCMKSSASLFSQLLN 967
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVlASVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 968 SLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLIFVVASSVNTGCSLGVLAIVTWQVLFVSVPMVYLAFRLQKYYF 1047
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1048 QTAKELMRINGTTRSYVANHLAESVAGAITIRAFDEEERFFKKSLTLIDTNASPFFHSFAANEWLIQRLETVSAIVLAST 1127
Cdd:cd18580 161 RTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALVV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 1128 AFCMILLPtGTFSSGFIGMALSYGLSLNMGLVYSVQNQCYLANWIISVERLNQYT 1182
Cdd:cd18580 241 ALLAVLLR-SSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1205-1441 |
2.58e-83 |
|
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: 273.71 E-value: 2.58e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1205 GRVEISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRF 1284
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1285 GIIPQDPTLFNGTVRFNLDPLCQHSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRV 1364
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 1365 LVLDEATASIDNATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGRIVEYDEPMKLMKDENSLFGKLVK 1441
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVR 254
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
282-830 |
3.11e-74 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 258.94 E-value: 3.11e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 282 WRELLTSGFFAFMKIVAVSAGPLLLNAFI--LVAEGNASFRYEGLVLAVLLFFSKMIESLSQRQWYFRcriVGLRVRSLL 359
Cdd:COG1132 20 RGLLILALLLLLLSALLELLLPLLLGRIIdaLLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLAR---LAQRVVADL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 360 TAAINKKQLRLNNSSRLIHSGSEIMNYATVDAYRIGEFPYW-FHQLWTTSFQLLIALGILFHSVGVATFSALAVIILTVL 438
Cdd:COG1132 97 RRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHgLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 439 CNAPIAKLQNKFQSELMTSQDERLKACNESLVNMKVLKLYAWESH----FKKVIEKLRNIELKSLKAvqMRKAYNAVLFW 514
Cdd:COG1132 177 VLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERelerFREANEELRRANLRAARL--SALFFPLMELL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 515 SSPVFVSAATFATCYFLDIPLRASNVFTFVATLRLVQDPVRMIPDVIGVTIQAKVAFSRIATFLEAP-ELQGGERRRKQR 593
Cdd:COG1132 255 GNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPpEIPDPPGAVPLP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 594 SEgnQNAIIIKSASFSWEEKgstKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTI------------ 661
Cdd:COG1132 335 PV--RGEIEFENVSFSYPGD---RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlidgvdirdltl 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 662 -DFYGTIAYVSQTAWIQTGTIRDNILFG--GVmDEHRYRETIQKSSLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLA 738
Cdd:COG1132 410 eSLRRQIGVVPQDTFLFSGTIRENIRYGrpDA-TDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIA 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 739 RALYQDADIYLLDDPFSAVDAHTASSLfQEYVMDALAGKAVLLVTHQVDFLPAFDSVLLMSDGEITEADTYQELLARSRD 818
Cdd:COG1132 489 RALLKDPPILILDEATSALDTETEALI-QEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGL 567
|
570
....*....|..
gi 22331862 819 FQDLVNAHRETA 830
Cdd:COG1132 568 YARLYRLQFGEE 579
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
288-574 |
1.65e-71 |
|
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: 241.22 E-value: 1.65e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 288 SGFFAFMKIVAVSAGPLLLNAFILVAEGNASFRYEGLVLAVLLFFSKMIESLSQRQWYFRCRIVGLRVRSLLTAAINKKQ 367
Cdd:cd18595 2 AALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 368 LRLNNSSRLIHSGSEIMNYATVDAYRIGEFPYWFHQLWTTSFQLLIALGILFHSVGVATFSALAVIILTVLCNAPIAKLQ 447
Cdd:cd18595 82 LRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 448 NKFQSELMTSQDERLKACNESLVNMKVLKLYAWESHFKKVIEKLRNIELKSLKAVQMRKAYNAVLFWSSPVFVSAATFAT 527
Cdd:cd18595 162 KKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFAT 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 22331862 528 cYFL---DIPLRASNVF---TFVATLRLvqdPVRMIPDVIGVTIQAKVAFSRI 574
Cdd:cd18595 242 -YVLsdpDNVLDAEKAFvslSLFNILRF---PLSMLPMVISNLVQASVSLKRL 290
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
891-1182 |
5.92e-65 |
|
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: 222.74 E-value: 5.92e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 891 IFFFIASLAQVTFavgQILQNSWMAA-------NVDNPQVSTLKLILVYLLIGLCSVLCLMVRSVCVVIMCMKSSASLFS 963
Cdd:cd18603 2 LLILLLYLLSQAF---SVGSNIWLSEwsddpalNGTQDTEQRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 964 QLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLIFVVASSVNTGCSLGVLAIVTWQVLFVSVPMVYLAFRLQ 1043
Cdd:cd18603 79 KLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1044 KYYFQTAKELMRINGTTRSYVANHLAESVAGAITIRAFDEEERFFKKSLTLIDTNASPFFHSFAANEWLIQRLETVSAIV 1123
Cdd:cd18603 159 RFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLI 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 22331862 1124 LASTAFCMILLPtGTFSSGFIGMALSYGLSLNMGLVYSVQNQCYLANWIISVERLNQYT 1182
Cdd:cd18603 239 VLFAALFAVLSR-DSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
891-1432 |
1.17e-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: 1.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 891 IFFFIASLAQVTFA--VGQILQNSWMAanvDNPQVSTLKLILVYLLIGLCSVLCLMVRSVCVVIMCMKSSASLFSQLLNS 968
Cdd:COG4988 24 LLGLLSGLLIIAQAwlLASLLAGLIIG---GAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAAARVKRRLRRRLLEK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 969 LFRAPMSFYDSTPLGRILSRVSSdlSIVDLDVPFGLIF--VVASSVNTgcsLGVLAIVTWQ------VLFVSVPMVYLAF 1040
Cdd:COG4988 101 LLALGPAWLRGKSTGELATLLTE--GVEALDGYFARYLpqLFLAALVP---LLILVAVFPLdwlsglILLVTAPLIPLFM 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1041 RL-QKYyfqtAKELMRINGTTRSYVANHLAESVAGAITIRAF----DEEERFFKKS----------LTLidtnAspFFHS 1105
Cdd:COG4988 176 ILvGKG----AAKASRRQWRALARLSGHFLDRLRGLTTLKLFgrakAEAERIAEASedfrkrtmkvLRV----A--FLSS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1106 FAanewliqrLETVSAIvlaSTAFCMIllptgtfssgFIGMALSYG-LSLNMGLVysVqnqcylanWIISVE------RL 1178
Cdd:COG4988 246 AV--------LEFFASL---SIALVAV----------YIGFRLLGGsLTLFAALF--V--------LLLAPEfflplrDL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1179 NQYTH---------------LTPEAPEVIEETRPpVNWPVTGRVEISDLQIRYRRESPlVLKGISCTFEGGHKIGIVGRT 1243
Cdd:COG4988 295 GSFYHarangiaaaekifalLDAPEPAAPAGTAP-LPAAGPPSIELEDVSFSYPGGRP-ALDGLSLTIPPGERVALVGPS 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1244 GSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQDPTLFNGTVRFNL---DPlcQHSDAEIWEVLGKC 1320
Cdd:COG4988 373 GAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLrlgRP--DASDEELEAALEAA 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1321 QLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIRREFADCTVITVAH 1400
Cdd:COG4988 451 GLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITH 530
|
570 580 590
....*....|....*....|....*....|..
gi 22331862 1401 RIPTVMDCTMVLSISDGRIVEYDEPMKLMKDE 1432
Cdd:COG4988 531 RLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
891-1182 |
4.32e-60 |
|
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: 208.48 E-value: 4.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 891 IFFFIASLAQVTfavgQILQNSWM---------AANVDNPQVSTLKLILVYLLIGLCSVLCLMVRSVCVVIMCMKSSASL 961
Cdd:cd18604 3 LLLLLFVLSQLL----SVGQSWWLgiwasayetSSALPPSEVSVLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 962 FSQLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLIFVVASSVNTGCSLGVLAIVTWQVLFVSVPMVYLAFR 1041
Cdd:cd18604 79 HERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1042 LQKYYFQTAKELMRINGTTRSYVANHLAESVAGAITIRAFDEEERFFKKSLTLIDTNASPFFHSFAANEWLIQRLETVSA 1121
Cdd:cd18604 159 IGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGA 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22331862 1122 IVLASTAFCMILlpTGTFSSGFIGMALSYGLSLNMGLVYSVQ--NQCYL-ANwiiSVERLNQYT 1182
Cdd:cd18604 239 LFSFATAALLVY--GPGIDAGLAGFSLSFALGFSSAILWLVRsyNELELdMN---SVERIQEYL 297
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1205-1430 |
2.03e-59 |
|
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: 204.00 E-value: 2.03e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1205 GRVEISDLQIRYRRESPlVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRF 1284
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1285 GIIPQDPTLFNGTVRFNLDPLCQHSDAEIWEVLGK-CQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSR 1363
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKeAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 1364 VLVLDEATASIDNATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGRIVEYDEPMKLMK 1430
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
566-815 |
2.44e-59 |
|
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: 215.01 E-value: 2.44e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 566 QAKVAFSRIATFLEAPELQGGERRRKQRSEGNqNAIIIKSASFSWEEkgsTKPNLRNVSLEVKFGEKVAVCGEVGSGKST 645
Cdd:COG4988 303 NGIAAAEKIFALLDAPEPAAPAGTAPLPAAGP-PSIELEDVSFSYPG---GRPALDGLSLTIPPGERVALVGPSGAGKST 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 646 LLAAILGETPCVSGTIDFYGT-------------IAYVSQTAWIQTGTIRDNILFGG-VMDEHRYRETIQKSSLDKDLEL 711
Cdd:COG4988 379 LLNLLLGFLPPYSGSILINGVdlsdldpaswrrqIAWVPQNPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDEFVAA 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 712 LPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQeyVMDALA-GKAVLLVTHQVDFLP 790
Cdd:COG4988 459 LPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQ--ALRRLAkGRTVILITHRLALLA 536
|
250 260
....*....|....*....|....*
gi 22331862 791 AFDSVLLMSDGEITEADTYQELLAR 815
Cdd:COG4988 537 QADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
289-574 |
4.34e-58 |
|
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: 202.40 E-value: 4.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 289 GFFAFMKIVAVSAGPLLLNAFILVAEGNASFRYEGLVLAVLLFFSKMIESLSQRQWYFRCRIVGLRVRSLLTAAINKKQL 368
Cdd:cd18598 3 GLLKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 369 RLNNSSRLIHSGSEIMNYATVDAYRIGEFPYWFHQLWTTSFQLLIALGILFHSVGVATFSALAVIILTVLCNAPIAKLQN 448
Cdd:cd18598 83 RVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 449 KFQSELMTSQDERLKACNESLVNMKVLKLYAWESHFKKVIEKLRNIELKSLKAVQMRKAYnAVLFWSS-PVFVSAATFAT 527
Cdd:cd18598 163 ALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDAL-CVYFWATtPVLISILTFAT 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 22331862 528 CYFLDIPLRASNVFTFVATLRLVQDPVRMIPDVIGVTIQAKVAFSRI 574
Cdd:cd18598 242 YVLMGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
323-824 |
1.32e-57 |
|
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: 213.54 E-value: 1.32e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 323 GLVLAVLLFFSKMIESLsqRQWYFRcrIVGLRVRSLLTAAINKKQLRLNNSSRLIHSGSEIMNYATvDAYRIGEF-PYWF 401
Cdd:COG2274 199 AIGLLLALLFEGLLRLL--RSYLLL--RLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFlTGSL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 402 HQLWTTSFQLLIALGILF--HS--VGVATFSALAVIILTVLCNAPIAKLQNkfqsELMTSQDERLKACNESLVNMKVLKL 477
Cdd:COG2274 274 LTALLDLLFVLIFLIVLFfySPplALVVLLLIPLYVLLGLLFQPRLRRLSR----EESEASAKRQSLLVETLRGIETIKA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 478 YAWESHFkkvIEKLRNIELKSLKAVQMRKAYNAVLFwSSPVFVSAATFATCYFLDIPLRASNVFT---FVA----TLRLV 550
Cdd:COG2274 350 LGAESRF---RRRWENLLAKYLNARFKLRRLSNLLS-TLSGLLQQLATVALLWLGAYLVIDGQLTlgqLIAfnilSGRFL 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 551 QdPVRMIPDVIGVTIQAKVAFSRIATFLEAPELQGGERRRKQRSEGnQNAIIIKSASFSWEekGSTKPNLRNVSLEVKFG 630
Cdd:COG2274 426 A-PVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRL-KGDIELENVSFRYP--GDSPPVLDNISLTIKPG 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 631 EKVAVCGEVGSGKSTLLAAILG-ETPcVSGTI-------------DFYGTIAYVSQTAWIQTGTIRDNILFGGV-MDEHR 695
Cdd:COG2274 502 ERVAIVGRSGSGKSTLLKLLLGlYEP-TSGRIlidgidlrqidpaSLRRQIGVVLQDVFLFSGTIRENITLGDPdATDEE 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 696 YRETIQKSSLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTAsSLFQEYVMDALA 775
Cdd:COG2274 581 IIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETE-AIILENLRRLLK 659
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 22331862 776 GKAVLLVTHQVDFLPAFDSVLLMSDGEITEADTYQELLARSRDFQDLVN 824
Cdd:COG2274 660 GRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
411-822 |
1.82e-57 |
|
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: 209.62 E-value: 1.82e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 411 LLIALGILFHSVGVATFSALAVIILTVLcnAPI--AKLQNKFQSELMTSQDERLKACNESLVNMKVLKLY-AWESHfkkv 487
Cdd:COG4987 144 LAAVAFLAFFSPALALVLALGLLLAGLL--LPLlaARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYgALDRA---- 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 488 IEKLRNIELKSLKAVQMRKAYNA----------------VLFWSSPVFVSAAtfatcyfLDIPLRASNVFTFVATLrlvq 551
Cdd:COG4987 218 LARLDAAEARLAAAQRRLARLSAlaqallqlaaglavvaVLWLAAPLVAAGA-------LSGPLLALLVLAALALF---- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 552 DPVRMIPDVIGVTIQAKVAFSRIATFLEAPELQGGERRRKQRSEGNqnAIIIKSASFSWEekGSTKPNLRNVSLEVKFGE 631
Cdd:COG4987 287 EALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGP--SLELEDVSFRYP--GAGRPVLDGLSLTLPPGE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 632 KVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-------------IAYVSQTAWIQTGTIRDNILFG--GVMDEhRY 696
Cdd:COG4987 363 RVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVdlrdldeddlrrrIAVVPQRPHLFDTTLRENLRLArpDATDE-EL 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 697 RETIQKSSLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQEyVMDALAG 776
Cdd:COG4987 442 WAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAG 520
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 22331862 777 KAVLLVTHQVDFLPAFDSVLLMSDGEITEADTYQELLARSRDFQDL 822
Cdd:COG4987 521 RTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
289-574 |
2.31e-57 |
|
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: 201.18 E-value: 2.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 289 GFFAFMKIVAVSAGPLLLNAFI-LVAEGNASFRYEGLVLAVLLFFSKMIESLSQRQWYFRCRIVGLRVRSLLTAAINKKQ 367
Cdd:cd18596 3 ALLAVLSSVLSFAPPFFLNRLLrYLEDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 368 LRLNNSSRLIHSGSE-------------------IMNYATVDAYRIGEFPYWFHQLWTTSFQLLIALGILFHSVGVATFS 428
Cdd:cd18596 83 LRRRDKSGSSKSSESkkkdkeededekssasvgkINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 429 ALAVIILTVLCNAPIAKLQNKFQSELMTSQDERLKACNESLVNMKVLKLYAWESHFKKVIEKLRNIELKSLKAVQMRKAY 508
Cdd:cd18596 163 GLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 509 NAVLFWSSPVFVSAATFAT-CYFLDIPLRASNVFTFVATLRLVQDPVRMIPDVIGVTIQAKVAFSRI 574
Cdd:cd18596 243 LSLLWFLIPILVTVVTFATyTLVMGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1205-1436 |
2.50e-56 |
|
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: 197.00 E-value: 2.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1205 GRVEISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEpVGGKIVVDGVDISKIGVHDLRSRF 1284
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1285 GIIPQDPTLFNGTVRFNLDPLCQHSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRV 1364
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331862 1365 LVLDEATASIDNATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGRIVEYDEPMKLMkDENSLF 1436
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL-NEKSHF 230
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1207-1418 |
5.50e-56 |
|
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: 191.83 E-value: 5.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGI 1286
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDPTLFNGTVRFNLdplcqhsdaeiwevlgkcqlkevvqekengldslvvedgsnWSMGQRQLFCLGRAVLRRSRVLV 1366
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 22331862 1367 LDEATASIDNATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGR 1418
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
926-1439 |
6.87e-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: 204.95 E-value: 6.87e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 926 LKLILVYLLIGLCSVLC--LMVRSVCVVIMCMKSsaslfsQLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFG 1003
Cdd:TIGR02203 58 LVVIGLAVLRGICSFVStyLLSWVSNKVVRDIRV------RMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1004 LIFVVASSVNTGCSLGVLAIVTWQVLFVSVPM----VYLAFRLQKYYFQTAKELMRINGTtrsyVANHLAESVAGAITIR 1079
Cdd:TIGR02203 132 FIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMlpvlSILMRRVSKRLRRISKEIQNSMGQ----VTTVAEETLQGYRVVK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1080 AFD----EEERFFKKSLTLIDtnaspffhsfaanewLIQRLETVSAI------VLASTAFCMIL-----------LPTGT 1138
Cdd:TIGR02203 208 LFGgqayETRRFDAVSNRNRR---------------LAMKMTSAGSIsspitqLIASLALAVVLfialfqaqagsLTAGD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1139 FSSGFIGMALSYG--LSLNmglvySVQNQcyLANWIISVERLnqYTHLTpEAPEVIEETRPPVNwpVTGRVEISDLQIRY 1216
Cdd:TIGR02203 273 FTAFITAMIALIRplKSLT-----NVNAP--MQRGLAAAESL--FTLLD-SPPEKDTGTRAIER--ARGDVEFRNVTFRY 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1217 RRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQDPTLFNG 1296
Cdd:TIGR02203 341 PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFND 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1297 TVRFNL--DPLCQHSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASI 1374
Cdd:TIGR02203 421 TIANNIayGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSAL 500
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 1375 DNATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGRIVEYDEPMKLMkDENSLFGKL 1439
Cdd:TIGR02203 501 DNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELL-ARNGLYAQL 564
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
287-574 |
3.71e-55 |
|
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: 194.21 E-value: 3.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 287 TSGFFAFMKIVAVSAGPLLLNAFILVAEGNASFR-----YEGLVLAVLLFFSKMIESLSQRQWYFRCRIVGLRVRSLLTA 361
Cdd:cd18597 1 LAGLLKLLADVLQVLSPLLLKYLINFVEDAYLGGpppsiGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 362 AINKKQLRLNNSSRLIHSGSEIMNYATVDAYRIGEFPYWFHQLWTTSFQLLIALGILFHSVGVATFSALAVIILTVLCNA 441
Cdd:cd18597 81 AIYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 442 PIAKLQNKFQSELMTSQDERLKACNESLVNMKVLKLYAWESHFKKVIEKLRNIELKSLKAVQMRKAYNAVLFWSSPVFVS 521
Cdd:cd18597 161 FLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLAS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 22331862 522 AATFATCYFLDIPLRASNVFTFVATLRLVQDPVRMIPDVIGVTIQAKVAFSRI 574
Cdd:cd18597 241 MLSFITYYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
601-801 |
1.19e-54 |
|
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: 189.85 E-value: 1.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 601 IIIKSASFSWeekGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDF----------------- 663
Cdd:cd03290 1 VQVTNGYFSW---GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWsnknesepsfeatrsrn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 664 YGTIAYVSQTAWIQTGTIRDNILFGGVMDEHRYRETIQKSSLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQ 743
Cdd:cd03290 78 RYSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 744 DADIYLLDDPFSAVDAHTASSLFQEYVMDALAG--KAVLLVTHQVDFLPAFDSVLLMSDG 801
Cdd:cd03290 158 NTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
891-1182 |
2.05e-54 |
|
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: 192.36 E-value: 2.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 891 IFFFIAS-LAQVTFAVGQILQNSWMAANVDNPQV----STLKLILVYLLIGLCSVLCLMVRSVCVVIMCMKSSASLFSQL 965
Cdd:cd18605 2 ILILLSLiLMQASRNLIDFWLSYWVSHSNNSFFNfindSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 966 LNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLIFVVASSVNTGCSLGVLAIVTWQVLFVSVPMVYLAFRLQKY 1045
Cdd:cd18605 82 LSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQRY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1046 YFQTAKELMRINGTTRSYVANHLAESVAGAITIRAFDEEERFFKKSLTLIDTNASPFFHSFAANEWLIQRLETVSAIVLA 1125
Cdd:cd18605 162 YRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVLIVT 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331862 1126 STAF--CMILLPTGTFSSGFIGMALSYGLS----LNmGLVYSvqnQCYLANWIISVERLNQYT 1182
Cdd:cd18605 242 FVALtaVVQHFFGLSIDAGLIGLALSYALPitglLS-GLLNS---FTETEKEMVSVERVRQYF 300
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
618-823 |
5.15e-54 |
|
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: 190.45 E-value: 5.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 618 PNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGTIAYVSQTAWIQTGTIRDNILFGGVMDEHRYR 697
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 698 ETIQKSSLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQEYVMDALAGK 777
Cdd:cd03291 131 SVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANK 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 22331862 778 AVLLVTHQVDFLPAFDSVLLMSDGEITEADTYQELLARSRDFQDLV 823
Cdd:cd03291 211 TRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
862-1432 |
8.45e-52 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 195.71 E-value: 8.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 862 SRLIKQEEREKGDTGLRPYIQYMNQNK-----GYIFFFIASLAQVT--FAVGQILqnSWMAANVDNPQVStlKLILVYLL 934
Cdd:TIGR00958 134 SEKEAEQGQSETADLLFRLLGLSGRDWpwlisAFVFLTLSSLGEMFipFYTGRVI--DTLGGDKGPPALA--SAIFFMCL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 935 IGLCSVLCLMVRSVCVVIMCMKSSASLFSQLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLIFVVASSVNT 1014
Cdd:TIGR00958 210 LSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVML 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1015 GCSLGVLAIVTWQ---VLFVSVPMVYLAFR-LQKYYFQTAKELMriNGTTRSyvaNHLAESVAGAI-TIRAFDEEE---- 1085
Cdd:TIGR00958 290 LGLLGFMLWLSPRltmVTLINLPLVFLAEKvFGKRYQLLSEELQ--EAVAKA---NQVAEEALSGMrTVRSFAAEEgeas 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1086 RFFKKSLTLIDTNASPFFhSFAANEWlIQRLeTVSAIVLASTAFCMILLPTGTFSSGFIGMALSYGLSL-----NMGLVY 1160
Cdd:TIGR00958 365 RFKEALEETLQLNKRKAL-AYAGYLW-TTSV-LGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLgeavrVLSYVY 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1161 SVQNQCYLANwiisvERLNQYTHLTPEAPEVIEEtRPPvnwPVTGRVEISDLQIRY-RRESPLVLKGISCTFEGGHKIGI 1239
Cdd:TIGR00958 442 SGMMQAVGAS-----EKVFEYLDRKPNIPLTGTL-APL---NLEGLIEFQDVSFSYpNRPDVPVLKGLTFTLHPGEVVAL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1240 VGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQDPTLFNGTVRFNLD-PLCQHSDAEIWEVLG 1318
Cdd:TIGR00958 513 VGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPDEEIMAAAK 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1319 KCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTirREFADCTVITV 1398
Cdd:TIGR00958 593 AANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLI 670
|
570 580 590
....*....|....*....|....*....|....
gi 22331862 1399 AHRIPTVMDCTMVLSISDGRIVEYDEPMKLMKDE 1432
Cdd:TIGR00958 671 AHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1207-1421 |
1.27e-51 |
|
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: 182.05 E-value: 1.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGI 1286
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDPTLFNGTVRFNL---DPlcQHSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSR 1363
Cdd:cd03251 81 VSQDVFLFNDTVAENIaygRP--GATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 1364 VLVLDEATASIDNATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGRIVE 1421
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVE 216
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1207-1439 |
2.25e-51 |
|
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: 181.27 E-value: 2.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESPlVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGI 1286
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDPTLFNGTVRFNL---DPlcQHSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSR 1363
Cdd:cd03253 80 VPQDTVLFNDTIGYNIrygRP--DATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22331862 1364 VLVLDEATASIDNATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGRIVEYDEPMKLMkDENSLFGKL 1439
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL-AKGGLYAEM 232
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
891-1182 |
6.14e-51 |
|
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: 182.42 E-value: 6.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 891 IFFFIASLAQVTFAVG-QILQNSWMAANVDNPQVSTLKL------------ILVYLLIGLCSVLCLMVRSVCVVIMCMKS 957
Cdd:cd18602 2 ALVLALALLKQGLRVAtDFWLADWTEANHDVASVVFNITsssleddevsyyISVYAGLSLGAVILSLVTNLAGELAGLRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 958 SASLFSQLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLIFVVASSVNTGCSLGVLAIVTWQVLFVSVPMVY 1037
Cdd:cd18602 82 ARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIII 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1038 LAFRLQKYYFQTAKELMRINGTTRSYVANHLAESVAGAITIRAFDEEERFFKKSLTLIDTNASPFFHSFAANEWLIQRLE 1117
Cdd:cd18602 162 VYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLD 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22331862 1118 TVSA-IVLASTAFCMILLPTGTFSSGFIGMALSYGLSLNMGLVYSVQNQCYLANWIISVERLNQYT 1182
Cdd:cd18602 242 YLGAvIVFLAALSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
891-1182 |
6.62e-51 |
|
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: 181.90 E-value: 6.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 891 IFFFIASLAQVTFAvgQILQNSWMAANVDN-PQVSTLKLILVYLLIGLCSVLCLMVRSVCVVIMCMKSSASLFSQLLNSL 969
Cdd:cd18606 1 LPLLLLLLILSQFA--QVFTNLWLSFWTEDfFGLSQGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 970 FRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLIFVVASSVNTGCSLGVLAIVTWQVLFVSVPMVYLAFRLQKYYFQT 1049
Cdd:cd18606 79 LRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1050 AKELMRINGTTRSYVANHLAESVAGAITIRAFDEEERFFKKSLTLIDTNASPFFHSFAANEWLIQRLETVSAI-VLASTA 1128
Cdd:cd18606 159 SRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLlVLIVAL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 22331862 1129 FCMILlpTGTFSSGFIGMALSYGLSLNMGLVYSVQNQCYLANWIISVERLNQYT 1182
Cdd:cd18606 239 LCVTR--RFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1207-1441 |
8.11e-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: 8.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRY--RRESPlVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRF 1284
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1285 GIIPQDPTLFNGTVRFNL-----DPlcqhSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVL 1359
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIrygkpDA----TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1360 RRSRVLVLDEATASIDNATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGRIVEYDEPMKLMKdENSLFGKL 1439
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMA-QKGVYAKL 234
|
..
gi 22331862 1440 VK 1441
Cdd:cd03249 235 VK 236
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1205-1420 |
1.52e-48 |
|
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: 172.39 E-value: 1.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1205 GRVEISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRF 1284
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1285 GIIPQDPTLFNGTVRFNL---DPLcqHSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRR 1361
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAPL--ADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 22331862 1362 SRVLVLDEATASIDNATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGRIV 1420
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
919-1182 |
3.16e-47 |
|
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: 171.98 E-value: 3.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 919 DNPQVSTLKLIlvYLLIGLCSVLCLMVRSVCVVIMCMKSSASLFSQLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDL 998
Cdd:cd18599 53 DNPDLNFYQLV--YGGSILVILLLSLIRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 999 DVPFGLIFVVASSVNTGCSLGVLAIVTWQVLFVSVPMVYLAFRLQKYYFQTAKELMRINGTTRSYVANHLAESVAGAITI 1078
Cdd:cd18599 131 RLPFTLENFLQNVLLVVFSLIIIAIVFPWFLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1079 RAFDEEERFFKKSLTLIDTNASPFFHSFAANEWLIQRLETVSAIVLASTAFCMILLPtGTFSSGFIGMALSYGLSLNMGL 1158
Cdd:cd18599 211 HAFNKEKEFLSKFKKLLDQNSSAFFLFNCAMRWLAVRLDILAVLITLITALLVVLLK-GSISPAFAGLALSYALQLSGLF 289
|
250 260
....*....|....*....|....
gi 22331862 1159 VYSVQNQCYLANWIISVERLNQYT 1182
Cdd:cd18599 290 QFTVRLASETEARFTSVERILEYI 313
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
961-1421 |
1.60e-46 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 177.60 E-value: 1.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 961 LFSQLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIV-DLDVpfgliFVVASSVNTGCSLGVLAI----VTWQVLFVSV-- 1033
Cdd:PRK10790 100 LRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIrDLYV-----TVVATVLRSAALIGAMLVamfsLDWRMALVAImi 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1034 -PMVYLAFRLQKYYfqtAKELMRingTTRSYVA---NHLAESVAGAITIRAFDEEERFFKKsltLIDTNASpffHSFAAN 1109
Cdd:PRK10790 175 fPAVLVVMVIYQRY---STPIVR---RVRAYLAdinDGFNEVINGMSVIQQFRQQARFGER---MGEASRS---HYMARM 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1110 EWLiqRLETV---------SAIVLastafCMILLPTGTFSSGFIGMALSYGL-----SLNMGLVYSVQNQCYLANWIISV 1175
Cdd:PRK10790 243 QTL--RLDGFllrpllslfSALIL-----CGLLMLFGFSASGTIEVGVLYAFisylgRLNEPLIELTTQQSMLQQAVVAG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1176 ERL--------NQYThltpeapeviEETRPPVnwpvTGRVEISDLQIRYRRESPlVLKGISCTFEGGHKIGIVGRTGSGK 1247
Cdd:PRK10790 316 ERVfelmdgprQQYG----------NDDRPLQ----SGRIDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGK 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1248 TTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQDPTLFNGTVRFNLDPLCQHSDAEIWEVLGKCQLKEVVQ 1327
Cdd:PRK10790 381 STLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELAR 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1328 EKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIRREFADCTVITVAHRIPTVMD 1407
Cdd:PRK10790 461 SLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVE 540
|
490
....*....|....
gi 22331862 1408 CTMVLSISDGRIVE 1421
Cdd:PRK10790 541 ADTILVLHRGQAVE 554
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
926-1426 |
5.31e-45 |
|
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: 174.76 E-value: 5.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 926 LKLILVYLLIGLCSVLCLMVRSVCVVIMCMKSSASLFSQLLNSLFRAPMSFYDSTPLGRILSRVSS------DLSIVDLD 999
Cdd:TIGR03797 176 VQIALALLAAAVGAAAFQLAQSLAVLRLETRMDASLQAAVWDRLLRLPVSFFRQYSTGDLASRAMGisqirrILSGSTLT 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1000 VPFGLIFVVASsvntgcsLGVLAIVTWQVLFVSVPM--VYLAFRLQKYYFQTAKE--LMRINGTtrsyVANHLAESVAGA 1075
Cdd:TIGR03797 256 TLLSGIFALLN-------LGLMFYYSWKLALVAVALalVAIAVTLVLGLLQVRKErrLLELSGK----ISGLTVQLINGI 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1076 ITIRAFDEEERFFKKSLTLidtnaspffhsFAANEWL---IQRLETVSAI------VLAST---AFCMILLPTGTFSSG- 1142
Cdd:TIGR03797 325 SKLRVAGAENRAFARWAKL-----------FSRQRKLelsAQRIENLLTVfnavlpVLTSAalfAAAISLLGGAGLSLGs 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1143 FigMALSYGLSLNMGLVYSvqnqcyLANWIISV-ERLNQYTHLTP---EAPEVIEETRPPvnWPVTGRVEISDLQIRYRR 1218
Cdd:TIGR03797 394 F--LAFNTAFGSFSGAVTQ------LSNTLISIlAVIPLWERAKPileALPEVDEAKTDP--GKLSGAIEVDRVTFRYRP 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1219 ESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQDPTLFNGTV 1298
Cdd:TIGR03797 464 DGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSI 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1299 RFNLDPLCQHSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNAT 1378
Cdd:TIGR03797 544 FENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRT 623
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 22331862 1379 DLILQKTIRREFAdcTVITVAHRIPTVMDCTMVLSISDGRIVE---YDEPM 1426
Cdd:TIGR03797 624 QAIVSESLERLKV--TRIVIAHRLSTIRNADRIYVLDAGRVVQqgtYDELM 672
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1207-1440 |
1.45e-43 |
|
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: 158.80 E-value: 1.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGI 1286
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDPTLFNGTVRFNL---DPlcQHSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSR 1363
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 1364 VLVLDEATASIDNATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGRIVEYDEPMKLMkDENSLFGKLV 1440
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL-AENGLYAYLY 234
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1205-1421 |
1.47e-43 |
|
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: 168.85 E-value: 1.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1205 GRVEISDLQIRYRRESPlVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRF 1284
Cdd:COG5265 356 GEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1285 GIIPQDPTLFNGTVRFNL---DPlcQHSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRR 1361
Cdd:COG5265 435 GIVPQDTVLFNDTIAYNIaygRP--DASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKN 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1362 SRVLVLDEATASIDNATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGRIVE 1421
Cdd:COG5265 513 PPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
566-798 |
3.79e-43 |
|
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: 166.31 E-value: 3.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 566 QAKVAFSRIATFLEAPELQGGERRrkQRSEGNQNAIIIKSASFSWEekgSTKPNLRNVSLEVKFGEKVAVCGEVGSGKST 645
Cdd:TIGR02857 289 DGVAAAEALFAVLDAAPRPLAGKA--PVTAAPASSLEFSGVSVAYP---GRRPALRPVSFTVPPGERVALVGPSGAGKST 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 646 LLAAILGETPCVSGTI-------------DFYGTIAYVSQTAWIQTGTIRDNILFG-GVMDEHRYRETIQKSSLDKDLEL 711
Cdd:TIGR02857 364 LLNLLLGFVDPTEGSIavngvpladadadSWRDQIAWVPQHPFLFAGTIAENIRLArPDASDAEIREALERAGLDEFVAA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 712 LPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLfqEYVMDALA-GKAVLLVTHQVDFLP 790
Cdd:TIGR02857 444 LPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEV--LEALRALAqGRTVLLVTHRLALAA 521
|
....*...
gi 22331862 791 AFDSVLLM 798
Cdd:TIGR02857 522 LADRIVVL 529
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
288-574 |
8.66e-42 |
|
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: 156.24 E-value: 8.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 288 SGFFAFMKIVAVSAGPLLLNAFIL----------VAEGNASFRY--------EGLVLAVLLFFSKMIES-LSQRQWYFRC 348
Cdd:cd18591 2 GGILKLLGDLLGFVGPLCISGIVDyveentysssNSTDKLSVSYvtveeffsNGYVLAVILFLALLLQAtFSQASYHIVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 349 RiVGLRVRSLLTAAINKKQLRLN--NSSRLIHSGSEIMNYATVDAYRIGEFPYWFHQLWTTSFQLLIALGILFHSVGV-A 425
Cdd:cd18591 82 R-EGIRLKTALQAMIYEKALRLSswNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVsA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 426 TFSALAVIILTVLcNAPIAKLQNKFQSELMTSQDERLKACNESLVNMKVLKLYAWESHFKKVIEKLRNIELKSLKAVQMR 505
Cdd:cd18591 161 LIGAALILVMTPL-QYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVY 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 506 KAYNAVLFWSSPVFVSAATFATCYFL-DIPLRASNVFTFVATLRLVQDPVRMIPDVIGVTIQAKVAFSRI 574
Cdd:cd18591 240 WSLMTFLTQASPILVTLVTFGLYPYLeGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
601-802 |
1.79e-41 |
|
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: 150.23 E-value: 1.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 601 IIIKSASFSWEEKGstKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-------------I 667
Cdd:cd03228 1 IEFKNVSFSYPGRP--KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdlrdldleslrknI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 668 AYVSQTAWIQTGTIRDNILfggvmdehryretiqkssldkdlellpdgdqteigergvnlSGGQKQRIQLARALYQDADI 747
Cdd:cd03228 79 AYVPQDPFLFSGTIRENIL-----------------------------------------SGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 748 YLLDDPFSAVDAHTAsSLFQEYVMDALAGKAVLLVTHQVDFLPAFDSVLLMSDGE 802
Cdd:cd03228 118 LILDEATSALDPETE-ALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
604-803 |
7.28e-41 |
|
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: 150.43 E-value: 7.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 604 KSASFSWeeKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-------------IAYV 670
Cdd:cd03245 6 RNVSFSY--PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdirqldpadlrrnIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 671 SQTAWIQTGTIRDNILFGG-VMDEHRYRETIQKSSLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYL 749
Cdd:cd03245 84 PQDVTLFYGTLRDNITLGApLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 750 LDDPFSAVDAHTASSLFQEyvMDA-LAGKAVLLVTHQVDFLPAFDSVLLMSDGEI 803
Cdd:cd03245 164 LDEPTSAMDMNSEERLKER--LRQlLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1020-1412 |
1.07e-40 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 158.99 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1020 VLAIVTWQ------VLFVSVPMVYLAFRLQKYYfqtAKELMRINGTTRSYVANHLAESVAGAITIRAFDEEERFFKKSLT 1093
Cdd:TIGR02857 135 ILAAVFPQdwisglILLLTAPLIPIFMILIGWA---AQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRR 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1094 LIDTNAS--------PFFHSFAanewliqrLETVSAIVLASTAFcmillptgtfssgFIGMALSYG-LSLNMGL-VYSVQ 1163
Cdd:TIGR02857 212 SSEEYRErtmrvlriAFLSSAV--------LELFATLSVALVAV-------------YIGFRLLAGdLDLATGLfVLLLA 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1164 NQCYL------------ANWIISVERLnqYTHLtpEAPEVIEETRPPVNWPVTGRVEISDLQIRYRRESPlVLKGISCTF 1231
Cdd:TIGR02857 271 PEFYLplrqlgaqyharADGVAAAEAL--FAVL--DAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGRRP-ALRPVSFTV 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1232 EGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQDPTLFNGTVRFNL---DPlcQH 1308
Cdd:TIGR02857 346 PPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRP--DA 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1309 SDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIRR 1388
Cdd:TIGR02857 424 SDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRA 503
|
410 420
....*....|....*....|....*.
gi 22331862 1389 EFADCTVITVAHRIPTV--MDCTMVL 1412
Cdd:TIGR02857 504 LAQGRTVLLVTHRLALAalADRIVVL 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
566-830 |
1.69e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 159.63 E-value: 1.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 566 QAKVAFSRIATFLEAPELQGGERRRKQRSEGNqNAIIIKSAS-FSWEEKGSTKPnlrnVSLEVKFGEKVAVCGEVGSGKS 644
Cdd:PRK11174 316 QAVGAAESLVTFLETPLAHPQQGEKELASNDP-VTIEAEDLEiLSPDGKTLAGP----LNFTLPAGQRIALVGPSGAGKT 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 645 TLLAAILGETPC-----VSGT-------IDFYGTIAYVSQTAWIQTGTIRDNILFGGV-MDEHRYRETIQKSSLDKDLEL 711
Cdd:PRK11174 391 SLLNALLGFLPYqgslkINGIelreldpESWRKHLSWVGQNPQLPHGTLRDNVLLGNPdASDEQLQQALENAWVSEFLPL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 712 LPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTasslfQEYVMDAL----AGKAVLLVTHQVD 787
Cdd:PRK11174 471 LPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS-----EQLVMQALnaasRRQTTLMVTHQLE 545
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 22331862 788 FLPAFDSVLLMSDGEITEADTYQELLARSRDFQDLvNAHRETA 830
Cdd:PRK11174 546 DLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL-LAHRQEE 587
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
983-1401 |
1.53e-39 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 155.60 E-value: 1.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 983 GRILSRVSSDLS-----IVDLDVPFGLIFVVASSVNTGCSL-----GVLAIVTWQVLFVSVPMVylAFRLQKYYFQTAKE 1052
Cdd:TIGR02868 110 GDLLGRLGADVDalqdlYVRVIVPAGVALVVGAAAVAAIAVlsvpaALILAAGLLLAGFVAPLV--SLRAARAAEQALAR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1053 LmringttRSYVANHLAESVAGAITIRAFDEEERFFKK------SLTLIDTNASPFFHSFAANEWLIQRLETVSAIVLAS 1126
Cdd:TIGR02868 188 L-------RGELAAQLTDALDGAAELVASGALPAALAQveeadrELTRAERRAAAATALGAALTLLAAGLAVLGALWAGG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1127 TAFCMILLPtGTFSSGFIGMALSYGLSLNmGLVYSVQnqcYLANWIISVERLNQYTHLTPEAPEVIEETRPPVnwPVTG- 1205
Cdd:TIGR02868 261 PAVADGRLA-PVTLAVLVLLPLAAFEAFA-ALPAAAQ---QLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAV--GLGKp 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1206 RVEISDLQIRYRrESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFG 1285
Cdd:TIGR02868 334 TLELRDLSAGYP-GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVS 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1286 IIPQDPTLFNGTVRFNL---DPLCqhSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRS 1362
Cdd:TIGR02868 413 VCAQDAHLFDTTVRENLrlaRPDA--TDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADA 490
|
410 420 430
....*....|....*....|....*....|....*....
gi 22331862 1363 RVLVLDEATASIDNATDLILQKTIRREFADCTVITVAHR 1401
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
889-1182 |
2.26e-39 |
|
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: 149.39 E-value: 2.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 889 GYIFFFIASLAQVTFAVGQILQNSWMA---------------------ANVDNPQVSTLKLILVY-LLIGLCSVLCLMvR 946
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSywanleeklndttdrvqgensTNVDIEDLDRDFNLGIYaGLTAATFVFGFL-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 947 SVCVVIMCMKSSASLFSQLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLI-FVVASSVNTGCSLGVLAIVT 1025
Cdd:cd18601 80 SLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLdFLQLLLQVVGVVLLAVVVNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1026 WqVLFVSVPMVYLAFRLQKYYFQTAKELMRINGTTRSYVANHLAESVAGAITIRAFDEEERFFKKSLTLIDTNASPFFHS 1105
Cdd:cd18601 160 W-VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLF 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 1106 FAANEWLIQRLETVSAIVLASTAFCMILLPTgTFSSGFIGMALSYGLSLNMGLVYSVQNQCYLANWIISVERLNQYT 1182
Cdd:cd18601 239 LATSRWLAVRLDALCALFVTVVAFGSLFLAE-SLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEYS 314
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
601-822 |
4.64e-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: 145.84 E-value: 4.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 601 IIIKSASFSWEEKGstKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-------------I 667
Cdd:cd03251 1 VEFKNVTFRYPGDG--PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 668 AYVSQTAWIQTGTIRDNILFG--GVMDEhRYRETIQKSSLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDA 745
Cdd:cd03251 79 GLVSQDVFLFNDTVAENIAYGrpGATRE-EVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 746 DIYLLDDPFSAVDAHTaSSLFQEYVMDALAGKAVLLVTHQVDFLPAFDSVLLMSDGEITEADTYQELLARSRDFQDL 822
Cdd:cd03251 158 PILILDEATSALDTES-ERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
917-1422 |
2.39e-38 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 152.87 E-value: 2.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 917 NVDNPQVSTLKLILVYLLI-----GLCSVLCLMVRSVCVViMCMKSSasLFSQLLNslfrAPMSFYDSTPLGRILSRVSS 991
Cdd:PRK11176 58 KADRSVLKWMPLVVIGLMIlrgitSFISSYCISWVSGKVV-MTMRRR--LFGHMMG----MPVSFFDKQSTGTLLSRITY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 992 DLSIVDLDVPFGLIFVVassvNTGCSLGVLAIV----TWQ---VLFVSVPMVYLAFRLQKYYFQTAKELMRingTTRSYV 1064
Cdd:PRK11176 131 DSEQVASSSSGALITVV----REGASIIGLFIMmfyySWQlslILIVIAPIVSIAIRVVSKRFRNISKNMQ---NTMGQV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1065 ANHLAESVAGAITIRAFD----EEERFFK-------KSLTLIDTNA--SPFFHsfaanewLIQRLETVSAIVLASTAFCM 1131
Cdd:PRK11176 204 TTSAEQMLKGHKEVLIFGgqevETKRFDKvsnrmrqQGMKMVSASSisDPIIQ-------LIASLALAFVLYAASFPSVM 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1132 ILLPTGTFSSGFIGM-ALSYGL-SL-NMglvySVQNQCYLAnwiiSVERLNQYTHLTPEAPE---VIEetrppvnwPVTG 1205
Cdd:PRK11176 277 DTLTAGTITVVFSSMiALMRPLkSLtNV----NAQFQRGMA----ACQTLFAILDLEQEKDEgkrVIE--------RAKG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1206 RVEISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFG 1285
Cdd:PRK11176 341 DIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVA 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1286 IIPQDPTLFNGTVRFNLDPLC--QHSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSR 1363
Cdd:PRK11176 421 LVSQNVHLFNDTIANNIAYARteQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSP 500
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 22331862 1364 VLVLDEATASIDNATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGRIVEY 1422
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVER 559
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
289-574 |
5.13e-38 |
|
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: 144.70 E-value: 5.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 289 GFFAFMKIVAVSAGPLLLNAFI-LVAEGNASFRYEGLVLAVLLFFSKMIESLSQRQWYFRCRIVGLRVRSLLTAAINKKQ 367
Cdd:cd18594 3 GILLFLEESLKIVQPLLLGRLVaYFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 368 LRLNNSSRLIHSGSEIMNYATVDAYRIGEFPYWFHQLWTTSFQLLIALGILFHSVGVATFSALAVIILTVLCNAPIAKLQ 447
Cdd:cd18594 83 LKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 448 NKFQSELMTSQDERLKACNESLVNMKVLKLYAWESHFKKVIEKLRNIELKS-LKAVQMRkAYNAVLFWSSPVFVSAATFA 526
Cdd:cd18594 163 AKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLiRKAAYIR-AFNMAFFFFSPTLVSFATFV 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 22331862 527 TCYFLDIPLRASNVFTFVATLRLVQDPV-RMIPDVIGVTIQAKVAFSRI 574
Cdd:cd18594 242 PYVLTGNTLTARKVFTVISLLNALRMTItRFFPESIQTLSESRVSLKRI 290
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
601-825 |
8.27e-38 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 142.29 E-value: 8.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 601 IIIKSASFSWeekgSTKPN---LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT----------- 666
Cdd:cd03249 1 IEFKNVSFRY----PSRPDvpiLKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 667 --IAYVSQTAWIQTGTIRDNILFG--GVMDEHRyRETIQKSSLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALY 742
Cdd:cd03249 77 sqIGLVSQEPVLFDGTIAENIRYGkpDATDEEV-EEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 743 QDADIYLLDDPFSAVDAHTaSSLFQEYVMDALAGKAVLLVTHQVDFLPAFDSVLLMSDGEITEADTYQELLARSRDFQDL 822
Cdd:cd03249 156 RNPKILLLDEATSALDAES-EKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKL 234
|
...
gi 22331862 823 VNA 825
Cdd:cd03249 235 VKA 237
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
597-808 |
8.73e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 142.54 E-value: 8.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 597 NQNAIIIKSASFSWEEKgstkPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT--------IA 668
Cdd:COG1121 3 MMPAIELENLTVSYGGR----PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKpprrarrrIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 669 YVSQ----------TAW--IQTGTIRDNILFGGVMDEHryRETIQKsSLDKdLELLPDGDQTeIGErgvnLSGGQKQRIQ 736
Cdd:COG1121 79 YVPQraevdwdfpiTVRdvVLMGRYGRRGLFRRPSRAD--REAVDE-ALER-VGLEDLADRP-IGE----LSGGQQQRVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 737 LARALYQDADIYLLDDPFSAVDAHTASSLFQeyVMDALA--GKAVLLVTHQVDFLPA-FDSVLLMSDGEITEADT 808
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYE--LLRELRreGKTILVVTHDLGAVREyFDRVLLLNRGLVAHGPP 222
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
601-808 |
1.19e-37 |
|
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: 141.09 E-value: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 601 IIIKSASFSWEEKGstKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTI-------------DFYGTI 667
Cdd:cd03244 3 IEFKNVSLRYRPNL--PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIlidgvdiskiglhDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 668 AYVSQTAWIQTGTIRDNILFGGVMDEHRYRETIQKSSLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADI 747
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331862 748 YLLDDPFSAVDAHTASSLfQEYVMDALAGKAVLLVTHQVDFLPAFDSVLLMSDGEITEADT 808
Cdd:cd03244 161 LVLDEATASVDPETDALI-QKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1168-1442 |
1.93e-37 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 150.11 E-value: 1.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1168 LANWIISveRLNQ----YTHLTPEAPEV-----IEETRPPVNWP--------VTGRVEISDLQIRYRRESPLVlKGISCT 1230
Cdd:PRK13657 281 FATLLIG--RLDQvvafINQVFMAAPKLeeffeVEDAVPDVRDPpgaidlgrVKGAVEFDDVSFSYDNSRQGV-EDVSFE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1231 FEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQDPTLFNGTVRFNL-----DPl 1305
Cdd:PRK13657 358 AKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIrvgrpDA- 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1306 cqhSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKT 1385
Cdd:PRK13657 437 ---TDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAA 513
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1386 IRREFADCTVITVAHRIPTVMDCTMVLSISDGRIVE---YDEpmklMKDENSLFGKLVKE 1442
Cdd:PRK13657 514 LDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVEsgsFDE----LVARGGRFAALLRA 569
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
601-815 |
4.70e-37 |
|
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: 139.67 E-value: 4.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 601 IIIKSASFSWEEKgstKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-------------I 667
Cdd:cd03254 3 IEFENVNFSYDEK---KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisrkslrsmI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 668 AYVSQTAWIQTGTIRDNILFGG-VMDEHRYRETIQKSSLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDAD 746
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRpNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22331862 747 IYLLDDPFSAVDAHTaSSLFQEYVMDALAGKAVLLVTHQVDFLPAFDSVLLMSDGEITEADTYQELLAR 815
Cdd:cd03254 160 ILILDEATSNIDTET-EKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
542-785 |
6.02e-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: 144.81 E-value: 6.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 542 TFVATLRLVQ----DPVRMIPDVIGVTIQAKVAFSRIATFLEAPELQG-GERRRKQRSEGNQNAIIIKSASFSWEekgST 616
Cdd:TIGR02868 271 VTLAVLVLLPlaafEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVAeGSAPAAGAVGLGKPTLELRDLSAGYP---GA 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 617 KPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG-------------TIAYVSQTAWIQTGTIRD 683
Cdd:TIGR02868 348 PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssldqdevrrRVSVCAQDAHLFDTTVRE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 684 NILFG--GVMDEHRYReTIQKSSLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHT 761
Cdd:TIGR02868 428 NLRLArpDATDEELWA-ALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAET 506
|
250 260
....*....|....*....|....
gi 22331862 762 ASSLFqEYVMDALAGKAVLLVTHQ 785
Cdd:TIGR02868 507 ADELL-EDLLAALSGRTVVLITHH 529
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
601-815 |
7.09e-36 |
|
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: 136.59 E-value: 7.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 601 IIIKSASFSWEekgSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG-------------TI 667
Cdd:cd03253 1 IEFENVTFAYD---PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 668 AYVSQTAWIQTGTIRDNILFG--GVMDEHRYrETIQKSSLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDA 745
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGrpDATDEEVI-EAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 746 DIYLLDDPFSAVDAHTASSLfQEYVMDALAGKAVLLVTHQVDFLPAFDSVLLMSDGEITEADTYQELLAR 815
Cdd:cd03253 157 PILLLDEATSALDTHTEREI-QAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1208-1419 |
1.49e-34 |
|
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: 130.41 E-value: 1.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1208 EISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGII 1287
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1288 PQDPTLFNGTVRfnldplcqhsdaeiwevlgkcqlkevvqekENGLdslvvedgsnwSMGQRQLFCLGRAVLRRSRVLVL 1367
Cdd:cd03246 82 PQDDELFSGSIA------------------------------ENIL-----------SGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22331862 1368 DEATASIDNATDLILQKTIRR-EFADCTVITVAHRIPTVMDCTMVLSISDGRI 1419
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1203-1419 |
5.16e-34 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 131.05 E-value: 5.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1203 VTGRVEISDLQIRYR-RESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLR 1281
Cdd:cd03248 8 LKGIVKFQNVTFAYPtRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1282 SRFGIIPQDPTLFNGTVRFNLD-PLCQHSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLR 1360
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 22331862 1361 RSRVLVLDEATASIDNATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGRI 1419
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
570-822 |
6.32e-34 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 139.08 E-value: 6.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 570 AFSRIATFL-EAPELQGGErrrKQRSEGnQNAIIIKSASFSWeeKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLA 648
Cdd:PRK10789 286 AYSRIRAMLaEAPVVKDGS---EPVPEG-RGELDVNIRQFTY--PQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLS 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 649 AILGETPCVSGTIDFY-------------GTIAYVSQTAWIQTGTIRDNILFGGV-MDEHRYRETIQKSSLDKDLELLPD 714
Cdd:PRK10789 360 LIQRHFDVSEGDIRFHdipltklqldswrSRLAVVSQTPFLFSDTVANNIALGRPdATQQEIEHVARLASVHDDILRLPQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 715 GDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQEyVMDALAGKAVLLVTHQVDFLPAFDS 794
Cdd:PRK10789 440 GYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHN-LRQWGEGRTVIISAHRLSALTEASE 518
|
250 260
....*....|....*....|....*...
gi 22331862 795 VLLMSDGEITEADTYQELLARSRDFQDL 822
Cdd:PRK10789 519 ILVMQHGHIAQRGNHDQLAQQSGWYRDM 546
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
601-799 |
4.69e-33 |
|
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: 127.97 E-value: 4.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 601 IIIKSASFSWEEKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT--------IAYVSQ 672
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgpdRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 673 TA----WIqtgTIRDNILFG----GVMDEHRY---RETIQKSSLDKDLELLPDgdqteigergvNLSGGQKQRIQLARAL 741
Cdd:cd03293 81 QDallpWL---TVLDNVALGlelqGVPKAEAReraEELLELVGLSGFENAYPH-----------QLSGGMRQRVALARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331862 742 YQDADIYLLDDPFSAVDAHTASSLfQEYVMDALA--GKAVLLVTHQVD---FLPafDSVLLMS 799
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQL-QEELLDIWRetGKTVLLVTHDIDeavFLA--DRVVVLS 206
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
591-815 |
1.27e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 135.34 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 591 KQRSEGNQNAIIIKSASFSWEEkgSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT---- 666
Cdd:PRK11160 329 TSTAAADQVSLTLNNVSFTYPD--QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiad 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 667 ---------IAYVSQTAWIQTGTIRDNILFGG-VMDEHRYRETIQKSSLDKDLELlPDGDQTEIGERGVNLSGGQKQRIQ 736
Cdd:PRK11160 407 yseaalrqaISVVSQRVHLFSATLRDNLLLAApNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLG 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 737 LARALYQDADIYLLDDPFSAVDAHTAS---SLFQEYVmdalAGKAVLLVTHQVDFLPAFDSVLLMSDGEITEADTYQELL 813
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERqilELLAEHA----QNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
..
gi 22331862 814 AR 815
Cdd:PRK11160 562 AQ 563
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
600-824 |
1.47e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 127.90 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 600 AIIIKSASFSWEEKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILG-ETPcVSGTIDFYGT--------IAYV 670
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGlEKP-TSGEVLVDGKpvtgpgpdRGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 671 SQTA----WIqtgTIRDNILFGGVM-------DEHRYRETIQKSSLDKDLELLPDgdqteigergvNLSGGQKQRIQLAR 739
Cdd:COG1116 86 FQEPallpWL---TVLDNVALGLELrgvpkaeRRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 740 ALYQDADIYLLDDPFSAVDAHTASSLfQEYVMDALA--GKAVLLVTHQVD---FLpAfDSVLLMSD--GEITEadtyqEL 812
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERL-QDELLRLWQetGKTVLFVTHDVDeavFL-A-DRVVVLSArpGRIVE-----EI 223
|
250 260
....*....|....*....|...
gi 22331862 813 ---LARSRD--------FQDLVN 824
Cdd:COG1116 224 dvdLPRPRDrelrtspeFAALRA 246
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
923-1430 |
1.72e-32 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 134.40 E-value: 1.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 923 VSTLkLILVYLLIGLCSVLCLM--VRSVCVVIMCMKSSASLFSQLLNSLFRAP---MSFYDSTPLgRILSRVSSDLS--- 994
Cdd:TIGR01842 42 VPTL-LMLTVLALGLYLFLGLLdaLRSFVLVRIGEKLDGALNQPIFAASFSATlrrGSGDGLQAL-RDLDQLRQFLTgpg 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 995 -IVDLDVP-----FGLIFVVASSvntgcsLGVLAIVTWQVLFVsvpMVYLAFRLQKYYFQTAKELmRINGTTRSYVANHL 1068
Cdd:TIGR01842 120 lFAFFDAPwmpiyLLVCFLLHPW------IGILALGGAVVLVG---LALLNNRATKKPLKEATEA-SIRANNLADSALRN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1069 AESVA-----GAITIRAFDEEERFFKKSLTLIDTNAspFFHSFAAnewlIQRLETVSAiVLASTAFCMIllpTGTFSSGF 1143
Cdd:TIGR01842 190 AEVIEamgmmGNLTKRWGRFHSKYLSAQSAASDRAG--MLSNLSK----YFRIVLQSL-VLGLGAYLAI---DGEITPGM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1144 IGMAlsyglSLNMGLVYSVQNQCyLANW------IISVERLNQYTHLTPEAPEVIEETRPpvnwpvTGRVEISDLQIRYR 1217
Cdd:TIGR01842 260 MIAG-----SILVGRALAPIDGA-IGGWkqfsgaRQAYKRLNELLANYPSRDPAMPLPEP------EGHLSVENVTIVPP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1218 RESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQDPTLFNGT 1297
Cdd:TIGR01842 328 GGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGT 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1298 VRFNLDPLCQHSDAE-IWEVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDN 1376
Cdd:TIGR01842 408 VAENIARFGENADPEkIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDE 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 22331862 1377 ATDLILQKTIRR-EFADCTVITVAHRiPTVMDCT-MVLSISDGRIVEYDEPMKLMK 1430
Cdd:TIGR01842 488 EGEQALANAIKAlKARGITVVVITHR-PSLLGCVdKILVLQDGRIARFGERDEVLA 542
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
617-798 |
1.98e-32 |
|
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: 125.72 E-value: 1.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 617 KPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT--------IAYVSQTAWIQTG---TIRDNI 685
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerkrIGYVPQRRSIDRDfpiSVRDVV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 686 LFGgvmdehRYRET-----IQKSSLDKDLELLPDGDQTEIGERGV-NLSGGQKQRIQLARALYQDADIYLLDDPFSAVDA 759
Cdd:cd03235 92 LMG------LYGHKglfrrLSKADKAKVDEALERVGLSELADRQIgELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 22331862 760 HTasslfQEYVMDALA-----GKAVLLVTH---QVdfLPAFDSVLLM 798
Cdd:cd03235 166 KT-----QEDIYELLRelrreGMTILVVTHdlgLV--LEYFDRVLLL 205
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
620-815 |
4.42e-32 |
|
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: 125.68 E-value: 4.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG-------------TIAYVSQTAWIQTGTIRDNIL 686
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 687 FGG-VMDEHRYRETIQKSSLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSL 765
Cdd:cd03252 98 LADpGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAI 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22331862 766 FQEyVMDALAGKAVLLVTHQVDFLPAFDSVLLMSDGEITEADTYQELLAR 815
Cdd:cd03252 178 MRN-MHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1207-1435 |
4.70e-32 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 125.52 E-value: 4.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESPlVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGI 1286
Cdd:COG1122 1 IELENLSFSYPGGTP-ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDPT--LFNGTVR----F---NLdplcQHSDAEIWEVLGKCqLKEVvqekenGLDSLvvEDGS--NWSMGQRQLFCLG 1355
Cdd:COG1122 80 VFQNPDdqLFAPTVEedvaFgpeNL----GLPREEIRERVEEA-LELV------GLEHL--ADRPphELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1356 RAVLRRSRVLVLDEATASID-NATDLILQ--KTIRREfaDCTVITVAHRIPTVMD-CTMVLSISDGRIVEYDEPMKLMKD 1431
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDpRGRRELLEllKRLNKE--GKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSD 224
|
....
gi 22331862 1432 ENSL 1435
Cdd:COG1122 225 YELL 228
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1176-1422 |
7.73e-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: 132.56 E-value: 7.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1176 ERLNQYTHLTPEAPEVIEETRPpvnwpvTGRVEISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALF 1255
Cdd:COG4618 306 RRLNELLAAVPAEPERMPLPRP------KGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLV 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1256 RLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQDPTLFNGTVRFNLDPLCQHSDAEIWEVLGKCQLKEVVQEKENGLDS 1335
Cdd:COG4618 380 GVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDT 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1336 LVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIR--REfADCTVITVAHRIPTVMDCTMVLS 1413
Cdd:COG4618 460 RIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRalKA-RGATVVVITHRPSLLAAVDKLLV 538
|
....*....
gi 22331862 1414 ISDGRIVEY 1422
Cdd:COG4618 539 LRDGRVQAF 547
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
565-815 |
1.65e-31 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 131.79 E-value: 1.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 565 IQAKVAFSRIATFLEAPELQGgERRRKQRSEGN---QNAIIIKSasfsweekGSTKPNLRNVSLEVKFGEKVAVCGEVGS 641
Cdd:COG4618 299 VSARQAYRRLNELLAAVPAEP-ERMPLPRPKGRlsvENLTVVPP--------GSKRPILRGVSFSLEPGEVLGVIGPSGS 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 642 GKSTLLAAILGETPCVSGTI-----DFY-------GT-IAYVSQTAWIQTGTIRDNI-LFGGVMDE-----------Hry 696
Cdd:COG4618 370 GKSTLARLLVGVWPPTAGSVrldgaDLSqwdreelGRhIGYLPQDVELFDGTIAENIaRFGDADPEkvvaaaklagvH-- 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 697 rETIQKssldkdlelLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQeyVMDAL-- 774
Cdd:COG4618 448 -EMILR---------LPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAA--AIRALka 515
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 22331862 775 AGKAVLLVTHQVDFLPAFDSVLLMSDGEITEADTYQELLAR 815
Cdd:COG4618 516 RGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1224-1372 |
2.04e-31 |
|
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: 120.83 E-value: 2.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1224 LKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQDPTLFNG-TVRFNL 1302
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 1303 D--PLCQ-----HSDAEIWEVLGKCQLKEVvqekengLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATA 1372
Cdd:pfam00005 81 RlgLLLKglskrEKDARAEEALEKLGLGDL-------ADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
601-803 |
2.06e-31 |
|
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: 122.98 E-value: 2.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 601 IIIKSASFSWEEKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILG-ETPcVSGTIDFYGT------------- 666
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGlDRP-TSGEVRVDGTdisklsekelaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 667 ----IAYVSQT-AWIQTGTIRDNILFGGVMDEHRYRETIQKSsldkdLELLpdgDQTEIGERG----VNLSGGQKQRIQL 737
Cdd:cd03255 80 rrrhIGFVFQSfNLLPDLTALENVELPLLLAGVPKKERRERA-----EELL---ERVGLGDRLnhypSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22331862 738 ARALYQDADIYLLDDPFSAVDAHTAS---SLFQEyvMDALAGKAVLLVTHQVDFLPAFDSVLLMSDGEI 803
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKevmELLRE--LNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
414-814 |
2.32e-31 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 131.36 E-value: 2.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 414 ALGILFH-SVGVATFSALAV-IILtvlcnAPIAKLQNKFQSELMTSQDeRLKACN----ESLVNMKVLKLYAWESH---- 483
Cdd:TIGR02204 149 GLIMMFItSPKLTSLVLLAVpLVL-----LPILLFGRRVRKLSRESQD-RIADAGsyagETLGAIRTVQAFGHEDAersr 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 484 FKKVIEKlrnielkSLKAVQMRKAYNAVLFWSSPVFVSAATFATCYF-----LDIPLRASNVFTFVATLRLVQDPVRMIP 558
Cdd:TIGR02204 223 FGGAVEK-------AYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVgahdvIAGKMSAGTLGQFVFYAVMVAGSIGTLS 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 559 DVIGVTIQAKVAFSRIATFLEA-PELQGGERRRKQRSEGnQNAIIIKSASFSWEEKGSTkPNLRNVSLEVKFGEKVAVCG 637
Cdd:TIGR02204 296 EVWGELQRAAGAAERLIELLQAePDIKAPAHPKTLPVPL-RGEIEFEQVNFAYPARPDQ-PALDGLNLTVRPGETVALVG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 638 EVGSGKSTLLAAILGETPCVSGTI-------------DFYGTIAYVSQTAWIQTGTIRDNILFGGV-MDEHRYRETIQKS 703
Cdd:TIGR02204 374 PSGAGKSTLFQLLLRFYDPQSGRIlldgvdlrqldpaELRARMALVPQDPVLFAASVMENIRYGRPdATDEEVEAAARAA 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 704 SLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTaSSLFQEYVMDALAGKAVLLVT 783
Cdd:TIGR02204 454 HAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAES-EQLVQQALETLMKGRTTLIIA 532
|
410 420 430
....*....|....*....|....*....|.
gi 22331862 784 HQVDFLPAFDSVLLMSDGEITEADTYQELLA 814
Cdd:TIGR02204 533 HRLATVLKADRIVVMDQGRIVAQGTHAELIA 563
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
299-574 |
2.86e-31 |
|
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: 125.02 E-value: 2.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 299 VSAGPLLLNAFI-LVAEGNASfRYEGLVLAVLLFFSKMIESLSQRQWYFRCRIVGLRVRSLLTAAINKKQLRLNNSSRLI 377
Cdd:cd18559 13 VFSGPSNLWLLLwFDDPVNGP-QEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 378 HSGSEIMNYATVDAYRIGEFPYWFHQLWTTSFQLLIALGILFHSVGVATFSALAVIILTVLCNAPIAKLQNKFQSELMTS 457
Cdd:cd18559 92 TPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 458 QDERLKACNESLVNMKVLKLYAWESHFKKVIEKLRNIELKSLKAVQMRKAYNAVLFWSSPVFVSAATFATCYFLD--IPL 535
Cdd:cd18559 172 KDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHslAGL 251
|
250 260 270
....*....|....*....|....*....|....*....
gi 22331862 536 RASNVFTFVATLRLVQDPVRMIPDVIGVTIQAKVAFSRI 574
Cdd:cd18559 252 VALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
620-755 |
3.62e-31 |
|
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: 120.06 E-value: 3.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-------------IAYVSQTAWIQTG-TIRDNI 685
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrkeIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331862 686 LFGGVMDEHRYREtiQKSSLDKDLELLPDGDQ--TEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFS 755
Cdd:pfam00005 81 RLGLLLKGLSKRE--KDARAEEALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
614-814 |
6.74e-31 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 129.39 E-value: 6.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 614 GSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG-------------TIAYVSQTAWIQTGT 680
Cdd:TIGR01842 328 GGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGadlkqwdretfgkHIGYLPQDVELFPGT 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 681 IRDNIL-FGGVMDEhryRETIQKSSLDKDLEL---LPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSA 756
Cdd:TIGR01842 408 VAENIArFGENADP---EKIIEAAKLAGVHELilrLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSN 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 757 VDAHTASSLFQEYVMDALAGKAVLLVTHQVDFLPAFDSVLLMSDGEITEADTYQELLA 814
Cdd:TIGR01842 485 LDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
601-805 |
2.19e-30 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 118.95 E-value: 2.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 601 IIIKSASFSWEEkgSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT------------IA 668
Cdd:cd03247 1 LSINNVSFSYPE--QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 669 YVSQTAWIQTGTIRDNIlfggvmdehryretiqkssldkdlellpdgdqteiGERgvnLSGGQKQRIQLARALYQDADIY 748
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL-----------------------------------GRR---FSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 749 LLDDPFSAVDAHTASSLFqEYVMDALAGKAVLLVTHQVDFLPAFDSVLLMSDGEITE 805
Cdd:cd03247 121 LLDEPTVGLDPITERQLL-SLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1185-1424 |
2.25e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 128.42 E-value: 2.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1185 TPEAPEVIEETRPPVNWPVTgrVEISDLQIRYRRESPLvLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVePVGGK 1264
Cdd:PRK11174 330 TPLAHPQQGEKELASNDPVT--IEAEDLEILSPDGKTL-AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGS 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1265 IVVDGVDISKIGVHDLRSRFGIIPQDPTLFNGTVRFNL---DPlcQHSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDG 1341
Cdd:PRK11174 406 LKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllgNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1342 SNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGRIVE 1421
Cdd:PRK11174 484 AGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQ 563
|
....*.
gi 22331862 1422 ---YDE 1424
Cdd:PRK11174 564 qgdYAE 569
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
616-802 |
6.17e-30 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 116.58 E-value: 6.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 616 TKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGTiayvsQTAWIQTGTIRDNILFggvmdehr 695
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK-----DIAKLPLEELRRRIGY-------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 696 yretiqkssldkdlelLPDgdqteigergvnLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLfqEYVMDALA 775
Cdd:cd00267 78 ----------------VPQ------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERL--LELLRELA 127
|
170 180 190
....*....|....*....|....*....|
gi 22331862 776 --GKAVLLVTHQVDFL-PAFDSVLLMSDGE 802
Cdd:cd00267 128 eeGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
286-574 |
6.41e-30 |
|
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: 121.13 E-value: 6.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 286 LTSGFFAFMKIVAVSAGPLLLNAFILVAEGNASFRYEGLVLAVLLFFSKMIESLSQRQWYFRCRIVGLRVRSLLTAAINK 365
Cdd:cd18592 1 FSILLLLISLIFGFIGPTILIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 366 KQLRLNNSSRliHSGSEIMNYATVDAYRIGE----FPYwfhqLWTTSFQLLIALGILFHSVGVATFSALAVIILTVLCNA 441
Cdd:cd18592 81 KILRLRSLGD--KSVGELINIFSNDGQRLFDaavfGPL----VIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 442 PIAKLQNKFQSELMTSQDERLKACNESLVNMKVLKLYAWESHFKKVIEKLRNIELKSLKAVQMRKAYNAVLFWSSPVFVS 521
Cdd:cd18592 155 FIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIAS 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 22331862 522 AATFATCYFLDIPLRASNVFTFVATLRLVQDPVRMIPDVIGVTIQAKVAFSRI 574
Cdd:cd18592 235 VVTFLAHVALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
617-803 |
6.91e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 118.38 E-value: 6.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 617 KPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-------------IAYVSQTAWIQTGTIRD 683
Cdd:COG4619 13 KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKplsampppewrrqVAYVPQEPALWGGTVRD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 684 NILF-----GGVMDEHRYRETIQKssLDKDLELLpdgdQTEIGErgvnLSGGQKQRIQLARALYQDADIYLLDDPFSAVD 758
Cdd:COG4619 93 NLPFpfqlrERKFDRERALELLER--LGLPPDIL----DKPVER----LSGGERQRLALIRALLLQPDVLLLDEPTSALD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 22331862 759 AHTAS---SLFQEYVMDalAGKAVLLVTHQVDFLPAF-DSVLLMSDGEI 803
Cdd:COG4619 163 PENTRrveELLREYLAE--EGRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1167-1433 |
8.94e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 126.48 E-value: 8.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1167 YLANWIISVERLNQYTHLTPEAPEVIEETRPPVNwpvtGRVEISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSG 1246
Cdd:PRK11160 303 HLGQVIASARRINEITEQKPEVTFPTTSTAAADQ----VSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCG 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1247 KTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQDPTLFNGTVRFNL---DPlcQHSDAEIWEVLGKCQLK 1323
Cdd:PRK11160 379 KSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1324 EVVQEKEnGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATD-LILQkTIRREFADCTVITVAHRI 1402
Cdd:PRK11160 457 KLLEDDK-GLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETErQILE-LLAEHAQNKTVLMITHRL 534
|
250 260 270
....*....|....*....|....*....|...
gi 22331862 1403 P--TVMDCTMVLsiSDGRIVEYDEPMKLMKDEN 1433
Cdd:PRK11160 535 TglEQFDRICVM--DNGQIIEQGTHQELLAQQG 565
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1207-1422 |
5.79e-29 |
|
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: 116.45 E-value: 5.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRE--SPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDL---R 1281
Cdd:cd03257 2 LEVKNLSVSFPTGggSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1282 SRFGIIPQDPTLfngtvrfNLDPLcqHSDAE-IWEVL-------GKCQLKEVVQEKENGldslvVEDGSNW--------S 1345
Cdd:cd03257 82 KEIQMVFQDPMS-------SLNPR--MTIGEqIAEPLrihgklsKKEARKEAVLLLLVG-----VGLPEEVlnryphelS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1346 MGQRQLFCLGRAVLRRSRVLVLDEATASIDNAT-DLILQ--KTIRREFaDCTVITVAHRIPTV-MDCTMVLSISDGRIVE 1421
Cdd:cd03257 148 GGQRQRVAIARALALNPKLLIADEPTSALDVSVqAQILDllKKLQEEL-GLTLLFITHDLGVVaKIADRVAVMYAGKIVE 226
|
.
gi 22331862 1422 Y 1422
Cdd:cd03257 227 E 227
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
540-825 |
5.87e-29 |
|
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: 125.24 E-value: 5.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 540 VFTFVATLRLVQDPVRMIPDVIGVTIQAKVAFSRIAtflEAPELQGGERRRKQRSEGNQ--NAIIIKSASFSWeekGSTK 617
Cdd:TIGR01193 414 LITFNALLSYFLTPLENIINLQPKLQAARVANNRLN---EVYLVDSEFINKKKRTELNNlnGDIVINDVSYSY---GYGS 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 618 PNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-------------IAYVSQTAWIQTGTIRDN 684
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFslkdidrhtlrqfINYLPQEPYIFSGSILEN 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 685 ILFGGV--MDEHRYRETIQKSSLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTA 762
Cdd:TIGR01193 568 LLLGAKenVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE 647
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331862 763 SSLFQEYVmdALAGKAVLLVTHQVDFLPAFDSVLLMSDGEITEADTYQELLARSRDFQDLVNA 825
Cdd:TIGR01193 648 KKIVNNLL--NLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
607-802 |
6.00e-29 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 115.64 E-value: 6.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 607 SFSWEekGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTI-------------DFYGTIAYVSQT 673
Cdd:cd03225 6 SFSYP--DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlvdgkdltklslkELRRKVGLVFQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 674 AWIQ--TGTIRDNILFGGvmdEHRY--RETIQKssldKDLELLPDGDQTEIGERGV-NLSGGQKQRIQLARALYQDADIY 748
Cdd:cd03225 84 PDDQffGPTVEEEVAFGL---ENLGlpEEEIEE----RVEEALELVGLEGLRDRSPfTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 749 LLDDPFSAVDAHTASSLFQeyVMDAL--AGKAVLLVTHQVDFLPAF-DSVLLMSDGE 802
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLE--LLKKLkaEGKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
620-804 |
1.20e-28 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 113.68 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-------------IAYVSQTawiqtgtirdnil 686
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaslspkelarkIAYVPQA------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 687 fggvmdehryretiqkssldkdLELLpdgDQTEIGERGVN-LSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSL 765
Cdd:cd03214 82 ----------------------LELL---GLAHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 22331862 766 FQeyVMDALA---GKAVLLVTHQVDFLPAF-DSVLLMSDGEIT 804
Cdd:cd03214 137 LE--LLRRLArerGKTVVMVLHDLNLAARYaDRVILLKDGRIV 177
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1208-1418 |
2.49e-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: 114.10 E-value: 2.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1208 EISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGII 1287
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1288 PQDPT--LFNGTVR----FNLDPLcQHSDAEIWEVLGKCqLKEVvqekenGLDSLVVEDGSNWSMGQRQLFCLGRAVLRR 1361
Cdd:cd03225 81 FQNPDdqFFGPTVEeevaFGLENL-GLPEEEIEERVEEA-LELV------GLEGLRDRSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331862 1362 SRVLVLDEATASID-NATDLILQ--KTIRREFAdcTVITVAHRIPTVMD-CTMVLSISDGR 1418
Cdd:cd03225 153 PDILLLDEPTAGLDpAGRRELLEllKKLKAEGK--TIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
620-813 |
4.45e-28 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 114.76 E-value: 4.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-------------IAYVSQTAWIQTG-TIRDNI 685
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRdlaslsrrelarrIAYVPQEPPAPFGlTVRELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 686 LFGGvmdeHRYRETIQKSSlDKDLEL----LpdgDQTEIG---ERGVN-LSGGQKQRIQLARALYQDADIYLLDDPFSAV 757
Cdd:COG1120 97 ALGR----YPHLGLFGRPS-AEDREAveeaL---ERTGLEhlaDRPVDeLSGGERQRVLIARALAQEPPLLLLDEPTSHL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22331862 758 D-AHtasslfQEYVMDALA------GKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQELL 813
Cdd:COG1120 169 DlAH------QLEVLELLRrlarerGRTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGPPEEVL 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
608-843 |
2.47e-27 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 118.08 E-value: 2.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 608 FSWEEKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPC---VSGTIDFYGT-------------IAYVS 671
Cdd:COG1123 10 LSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRdllelsealrgrrIGMVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 672 QTAWIQ--TGTIRDNILFGGvmdehRYRETIQKSSLDKDLELLPDGDQTEIGERGVN-LSGGQKQRIQLARALYQDADIY 748
Cdd:COG1123 90 QDPMTQlnPVTVGDQIAEAL-----ENLGLSRAEARARVLELLEAVGLERRLDRYPHqLSGGQRQRVAIAMALALDPDLL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 749 LLDDPFSAVDAHTasslfQEYVMDALA------GKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQELLARSRDFQD 821
Cdd:COG1123 165 IADEPTTALDVTT-----QAEILDLLRelqrerGTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEILAAPQALAA 239
|
250 260
....*....|....*....|....*....
gi 22331862 822 L-------VNAHRETAGSERVVAVENPTK 843
Cdd:COG1123 240 VprlgaarGRAAPAAAAAEPLLEVRNLSK 268
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1208-1418 |
2.61e-27 |
|
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: 109.26 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1208 EISDLQIRYrrESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGII 1287
Cdd:cd00267 1 EIENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1288 PQdptLfngtvrfnldplcqhsdaeiwevlgkcqlkevvqekengldslvvedgsnwSMGQRQLFCLGRAVLRRSRVLVL 1367
Cdd:cd00267 79 PQ---L---------------------------------------------------SGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22331862 1368 DEATASIDNATDLILQKTIRREFAD-CTVITVAHRIPTVMD-CTMVLSISDGR 1418
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1207-1421 |
7.50e-27 |
|
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: 108.55 E-value: 7.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGvHDLRSRFGI 1286
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDPTLFNGTVRFNLdplcqhsdaeiwevlgkcqlkevvqekengldslvvedGSNWSMGQRQLFCLGRAVLRRSRVLV 1366
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 1367 LDEATASIDNATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGRIVE 1421
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
601-818 |
1.23e-26 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 110.33 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 601 IIIKSASFSWEEKgstkPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT------------IA 668
Cdd:COG4555 2 IEVENLSKKYGKV----PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEdvrkeprearrqIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 669 YVSQtawiQTG-----TIRDNI-LFGGVMDEHRYRETIQKSSLDKDLELLPDGDQteigeRGVNLSGGQKQRIQLARALY 742
Cdd:COG4555 78 VLPD----ERGlydrlTVRENIrYFAELYGLFDEELKKRIEELIELLGLEEFLDR-----RVGELSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 743 QDADIYLLDDPFSAVDAHtASSLFQEYVMDALA-GKAVLLVTHQVDFLPA-FDSVLLMSDGEITEADTYQELLARSRD 818
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVM-ARRLLREILRALKKeGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1207-1425 |
1.53e-26 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 109.58 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESplVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVE-----PVGGKIVVDGVDISKIGVHD-- 1279
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1280 LRSRFGIIPQDPTLFNGTVRFNLD-PLCQHsdaeiwEVLGKCQLKEVVQE-------KENGLDSLvveDGSNWSMGQRQL 1351
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAyGLRLH------GIKLKEELDERVEEalrkaalWDEVKDRL---HALGLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 1352 FCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIRREFADCTVITVAHRIPT---VMDCTMVLsiSDGRIVEYDEP 1425
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQaarVADRTAFL--LNGRLVEFGPT 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
620-803 |
1.55e-26 |
|
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: 108.76 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILG-ETPCvSGTIDFYGT-----------IAYVSQT-AWIQTGTIRDNIL 686
Cdd:cd03259 16 LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGlERPD-SGEILIDGRdvtgvpperrnIGMVFQDyALFPHLTVAENIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 687 FGgvMDEHRYRETIQKSSLDKDLELLpdgDQTEIGERGVN-LSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSL 765
Cdd:cd03259 95 FG--LKLRGVPKAEIRARVRELLELV---GLEGLLNRYPHeLSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREEL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 22331862 766 fQEYVMDALA--GKAVLLVTH-QVDFLPAFDSVLLMSDGEI 803
Cdd:cd03259 170 -REELKELQRelGITTIYVTHdQEEALALADRIAVMNEGRI 209
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
607-803 |
1.82e-26 |
|
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: 109.10 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 607 SFSWEEKGSTkPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG-------------TIAYVSQT 673
Cdd:cd03248 18 TFAYPTRPDT-LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyehkylhsKVSLVGQE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 674 AWIQTGTIRDNILFG--GVMDEhRYRETIQKSSLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLD 751
Cdd:cd03248 97 PVLFARSLQDNIAYGlqSCSFE-CVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 22331862 752 DPFSAVDAHTASSLfQEYVMDALAGKAVLLVTHQVDFLPAFDSVLLMSDGEI 803
Cdd:cd03248 176 EATSALDAESEQQV-QQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
598-805 |
2.15e-26 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 108.98 E-value: 2.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 598 QNAIIIKSASFSWEEKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLaAILG--ETPCvSGTIDFYGT--------- 666
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLL-NILGglDRPT-SGEVLIDGQdisslsere 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 667 --------IAYVSQTA-WIQTGTIRDNILFGGVMDEHRYRETIQKSsldkdLELLpdgDQTEIGERG----VNLSGGQKQ 733
Cdd:COG1136 80 larlrrrhIGFVFQFFnLLPELTALENVALPLLLAGVSRKERRERA-----RELL---ERVGLGDRLdhrpSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 734 RIQLARALYQDADIYLLDDPFSAVDAHTAsslfqEYVMDALA------GKAVLLVTHQVDFLPAFDSVLLMSDGEITE 805
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTG-----EEVLELLRelnrelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
889-1438 |
2.42e-26 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 118.21 E-value: 2.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 889 GYIFFFIAslaqvtfAVGQILQNSWMAANVDNpqvstlkLILVYLLIGLCSVLCLMVRSVCVVIMCMKSSASLFSQLLNS 968
Cdd:PTZ00265 74 GTLPFFVS-------VFGVIMKNMNLGENVND-------IIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKS 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 969 LFRAPMSFYDSTPLGRILSRVSSDLSIVD--LDVPFGLIFVVASSVntgcslgvLAIVTWQV-------LFVSV--PMVY 1037
Cdd:PTZ00265 140 VFYQDGQFHDNNPGSKLTSDLDFYLEQVNagIGTKFITIFTYASAF--------LGLYIWSLfknarltLCITCvfPLIY 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1038 LAFRL-QKYYFQTAKELMRINGTTRSYVAnhlaESVAGAITIRAFDEEERFFKKsltlidTNASPFFHS---FAANEWLI 1113
Cdd:PTZ00265 212 ICGVIcNKKVKINKKTSLLYNNNTMSIIE----EALVGIRTVVSYCGEKTILKK------FNLSEKLYSkyiLKANFMES 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1114 QRLETVSAIVLASTAF-----CMILL-------PTGTFSSG-FIGMALSYGLSLNMgLVYSVQNqcyLANWIISVERLNQ 1180
Cdd:PTZ00265 282 LHIGMINGFILASYAFgfwygTRIIIsdlsnqqPNNDFHGGsVISILLGVLISMFM-LTIILPN---ITEYMKSLEATNS 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1181 YTHLTPEAPeVIEETRPPVNWPVTGRVEISDLQIRY-RRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVE 1259
Cdd:PTZ00265 358 LYEIINRKP-LVENNDDGKKLKDIKKIQFKNVRFHYdTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1260 PVGGKIVV-DGVDISKIGVHDLRSRFGIIPQDPTLFNGTVRFN----------LDPLCQHS------------------- 1309
Cdd:PTZ00265 437 PTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNikyslyslkdLEALSNYYnedgndsqenknkrnscra 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1310 -----------------------------DAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLR 1360
Cdd:PTZ00265 517 kcagdlndmsnttdsneliemrknyqtikDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIR 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1361 RSRVLVLDEATASIDNATDLILQKTIRREFADCTVIT--VAHRIPTVMDCTMVLSISD---GRIVEYD----EPMKLMKD 1431
Cdd:PTZ00265 597 NPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITiiIAHRLSTIRYANTIFVLSNrerGSTVDVDiigeDPTKDNKE 676
|
....*..
gi 22331862 1432 ENSLFGK 1438
Cdd:PTZ00265 677 NNNKNNK 683
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1208-1425 |
2.53e-26 |
|
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: 109.18 E-value: 2.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1208 EISDLQIRYRreSPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHdLRSRFGII 1287
Cdd:COG4555 3 EVENLSKKYG--KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1288 PQDPTLFNG-TVRFNLDPLcqhsdAEIWEVLGKcQLKEVVQE--KENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRV 1364
Cdd:COG4555 80 PDERGLYDRlTVRENIRYF-----AELYGLFDE-ELKKRIEEliELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 1365 LVLDEATASID-NATDLILQ--KTIRREfaDCTVITVAHRIPTVMD-CTMVLSISDGRIVEYDEP 1425
Cdd:COG4555 154 LLLDEPTNGLDvMARRLLREilRALKKE--GKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSL 216
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
601-821 |
2.87e-26 |
|
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: 108.57 E-value: 2.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 601 IIIKSASFSWEEKgstKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-------------I 667
Cdd:COG1122 1 IELENLSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKditkknlrelrrkV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 668 AYVSQTAWIQ--TGTIRDNILFG----GVmDEHRYRETIQKSsldkdLELLpdgDQTEIGERGV-NLSGGQKQRIQLARA 740
Cdd:COG1122 78 GLVFQNPDDQlfAPTVEEDVAFGpenlGL-PREEIRERVEEA-----LELV---GLEHLADRPPhELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 741 LYQDADIYLLDDPFSAVDAHTASSLFQeyVMDAL--AGKAVLLVTHQVDFLPA-FDSVLLMSDGEITEADTYQELLARSR 817
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLE--LLKRLnkEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDYE 226
|
....
gi 22331862 818 DFQD 821
Cdd:COG1122 227 LLEE 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1207-1425 |
2.98e-26 |
|
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: 115.00 E-value: 2.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRY---RRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIG---VHDL 1280
Cdd:COG1123 261 LEVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1281 RSRFGIIPQDP-TLFN--GTVRFNL-DPLCQH---SDAEIW----EVLGKCQLKEVVqekengLDSLVVEdgsnWSMGQR 1349
Cdd:COG1123 341 RRRVQMVFQDPySSLNprMTVGDIIaEPLRLHgllSRAERRervaELLERVGLPPDL------ADRYPHE----LSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1350 QLFCLGRAVLRRSRVLVLDEATASIDNAT-----DLILQktIRREFaDCTVITVAHriptvmDCTMVLSISD-------G 1417
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVqaqilNLLRD--LQREL-GLTYLFISH------DLAVVRYIADrvavmydG 481
|
....*...
gi 22331862 1418 RIVEYDEP 1425
Cdd:COG1123 482 RIVEDGPT 489
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1207-1435 |
3.32e-26 |
|
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: 114.62 E-value: 3.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEP---VGGKIVVDGVDISKIGVHDLRSR 1283
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1284 FGIIPQDP-TLFNG-TVRFNLdplcqhsdAEIWEVLG--KCQLKEVVQE--KENGLDSLVVEDGSNWSMGQRQLFCLGRA 1357
Cdd:COG1123 85 IGMVFQDPmTQLNPvTVGDQI--------AEALENLGlsRAEARARVLEllEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1358 VLRRSRVLVLDEATASIDNATD---LILQKTIRREFaDCTVITVAHRIPTVMD-CTMVLSISDGRIVEYDEPMKLMKDEN 1433
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQaeiLDLLRELQRER-GTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
..
gi 22331862 1434 SL 1435
Cdd:COG1123 236 AL 237
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
891-1150 |
3.72e-26 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 109.65 E-value: 3.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 891 IFFFIASLAQVTFAV--GQILqnSWMAANVDNPQVSTLKLILVYLLIGLCSVLCLMVRSVCVVIMCMKSSASLFSQLLNS 968
Cdd:pfam00664 6 LLAILSGAISPAFPLvlGRIL--DVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 969 LFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLIFVVASSVNTGCSLGVLAIVTWQVLFVSVPMVYLAFRLQKYYFQ 1048
Cdd:pfam00664 84 ILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1049 TAKELMRINGTTRSYVANHLAESVAGAITIRAFDEEERFFKKSLTLIDTNASPFFHSFAANEWLIQRLE-TVSAIVLAST 1127
Cdd:pfam00664 164 ILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQfIGYLSYALAL 243
|
250 260
....*....|....*....|...
gi 22331862 1128 AFCMILLPTGTFSSGFIGMALSY 1150
Cdd:pfam00664 244 WFGAYLVISGELSVGDLVAFLSL 266
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
495-825 |
4.13e-26 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 115.44 E-value: 4.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 495 ELKSLKAV--QMRKAYNAVLFWSSpvFVSAATfatcyfldiplRASNVFTFVATLR----LVQDPVRMIPDVIGVTIQAK 568
Cdd:PRK13657 217 ETQALRDIadNLLAAQMPVLSWWA--LASVLN-----------RAASTITMLAILVlgaaLVQKGQLRVGEVVAFVGFAT 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 569 VAFSRI--------ATFLEAPELQG--------GERRRKQ--RSEGN-QNAIIIKSASFSWeekGSTKPNLRNVSLEVKF 629
Cdd:PRK13657 284 LLIGRLdqvvafinQVFMAAPKLEEffevedavPDVRDPPgaIDLGRvKGAVEFDDVSFSY---DNSRQGVEDVSFEAKP 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 630 GEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-------------IAYVSQTAWIQTGTIRDNILFG--GVMDEH 694
Cdd:PRK13657 361 GQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirtvtraslrrnIAVVFQDAGLFNRSIEDNIRVGrpDATDEE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 695 RYRETIQKSSLDKdLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLfQEYVMDAL 774
Cdd:PRK13657 441 MRAAAERAQAHDF-IERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKV-KAALDELM 518
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 22331862 775 AGKAVLLVTHQVDFLPAFDSVLLMSDGEITEADTYQELLARSRDFQDLVNA 825
Cdd:PRK13657 519 KGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRA 569
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
614-815 |
6.43e-26 |
|
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: 108.16 E-value: 6.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 614 GSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAI--LGETpcVSGTIDFYG-------------TIAYVSQtawiQT 678
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMInrLIEP--TSGEIFIDGedireqdpvelrrKIGYVIQ----QI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 679 G-----TIRDNIlfGGVMD-EHRYRETIQKSSlDKDLELLpDGDQTEIGER-GVNLSGGQKQRIQLARALYQDADIYLLD 751
Cdd:cd03295 85 GlfphmTVEENI--ALVPKlLKWPKEKIRERA-DELLALV-GLDPAEFADRyPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 752 DPFSAVDAHTASSLFQEYV-MDALAGKAVLLVTHQVDflPAF---DSVLLMSDGEITEADTYQELLAR 815
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKrLQQELGKTIVFVTHDID--EAFrlaDRIAIMKNGEIVQVGTPDEILRS 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1219-1418 |
9.01e-26 |
|
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: 106.40 E-value: 9.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1219 ESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGvdiskigvhdlrsRFGIIPQDPTLFNGTV 1298
Cdd:cd03250 16 ETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------SIAYVSQEPWIQNGTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1299 RFN------LDPlcqhsdAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATA 1372
Cdd:cd03250 83 RENilfgkpFDE------ERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 22331862 1373 SIDNAT-DLILQKTIRREFADC-TVITVAHRIPTVMDCTMVLSISDGR 1418
Cdd:cd03250 157 AVDAHVgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
600-825 |
1.11e-25 |
|
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: 107.58 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 600 AIIIKSASFSWEEKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTI-------------DFYGT 666
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVtfdgrpvtrrrrkAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 667 IAYVSQTAwiqTG------TIRDnilfggVMDE--HRYRETIQKSSLDKDLEL--LPDgdqtEIGERGVN-LSGGQKQRI 735
Cdd:COG1124 81 VQMVFQDP---YAslhprhTVDR------ILAEplRIHGLPDREERIAELLEQvgLPP----SFLDRYPHqLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 736 QLARALYQDADIYLLDDPFSAVDAHTasslfQEYVMDALA------GKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADT 808
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSV-----QAEILNLLKdlreerGLTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELT 222
|
250
....*....|....*....
gi 22331862 809 YQELLARSRD--FQDLVNA 825
Cdd:COG1124 223 VADLLAGPKHpyTRELLAA 241
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
620-802 |
1.37e-25 |
|
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: 104.96 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILG-ETPcVSGTIDFYGT---------------IAYVSQT-AWIQTGTIR 682
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGlEEP-DSGSILIDGEdltdledelpplrrrIGMVFQDfALFPHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 683 DNILFGgvmdehryretiqkssldkdlellpdgdqteigergvnLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTA 762
Cdd:cd03229 95 ENIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 22331862 763 SSLfQEYVMD--ALAGKAVLLVTHQVDFLPAF-DSVLLMSDGE 802
Cdd:cd03229 137 REV-RALLKSlqAQLGITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
614-803 |
2.48e-25 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 106.50 E-value: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 614 GSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT----------------IAYVSQT-AWI 676
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrrqIGMIFQQfNLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 677 QTGTIRDNILFG--GVMDEHR------YRETIQK--SSLDKdLELLPDGDQteigeRGVNLSGGQKQRIQLARALYQDAD 746
Cdd:cd03256 91 ERLSVLENVLSGrlGRRSTWRslfglfPKEEKQRalAALER-VGLLDKAYQ-----RADQLSGGQQQRVAIARALMQQPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22331862 747 IYLLDDPFSAVDAHTAsslfqEYVMDALA------GKAVLLVTHQVDFLPAF-DSVLLMSDGEI 803
Cdd:cd03256 165 LILADEPVASLDPASS-----RQVMDLLKrinreeGITVIVSLHQVDLAREYaDRIVGLKDGRI 223
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1203-1405 |
2.87e-25 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 114.36 E-value: 2.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1203 VTGRVEISDLQIRY-RRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVE---------------------- 1259
Cdd:PTZ00265 1162 IKGKIEIMDVNFRYiSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqd 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1260 -------PVG-------------------------GKIVVDGVDISKIGVHDLRSRFGIIPQDPTLFNGTVRFNLDplCQ 1307
Cdd:PTZ00265 1242 yqgdeeqNVGmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK--FG 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1308 HSDAEIWEVLGKCQ---LKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQK 1384
Cdd:PTZ00265 1320 KEDATREDVKRACKfaaIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1399
|
250 260
....*....|....*....|...
gi 22331862 1385 TIR--REFADCTVITVAHRIPTV 1405
Cdd:PTZ00265 1400 TIVdiKDKADKTIITIAHRIASI 1422
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1207-1420 |
3.18e-25 |
|
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: 104.97 E-value: 3.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRREspLVLKGISCTFEGGhKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKiGVHDLRSRFGI 1286
Cdd:cd03264 1 LQLENLTKRYGKK--RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDPTLF-NGTVRFNLDPLC-------QHSDAEIWEVLGKCQLKEVVQEKENGLdslvvedgsnwSMGQRQLFCLGRAV 1358
Cdd:cd03264 77 LPQEFGVYpNFTVREFLDYIAwlkgipsKEVKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331862 1359 LRRSRVLVLDEATASIDNATDLILQKTIRREFADCTVITVAHRIPTVMD-CTMVLSISDGRIV 1420
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLV 208
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
620-815 |
3.21e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 108.70 E-value: 3.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILG-ETPcVSGTIDFYGTIAYVSQTAwiQ---TG------------TIRD 683
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGlETP-DSGRIVLNGRDLFTNLPP--RerrVGfvfqhyalfphmTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 684 NILFGgvMDEHRYRETIQKSSLDKDLELLpdgdQ-TEIGERGVN-LSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHT 761
Cdd:COG1118 95 NIAFG--LRVRPPSKAEIRARVEELLELV----QlEGLADRYPSqLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331862 762 A-------SSLFQEYvmdalaGKAVLLVTH-QVDFLPAFDSVLLMSDGEITEADTYQELLAR 815
Cdd:COG1118 169 RkelrrwlRRLHDEL------GGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1207-1442 |
3.51e-25 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 105.53 E-value: 3.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRREspLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGvHDLRSRFGI 1286
Cdd:COG1131 1 IEVRGLTKRYGDK--TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDPTLFNG-TVRFNLD---PLCQHSDAE----IWEVLGKCQLKEVvqekengLDSLVvedgSNWSMGQRQLFCLGRAV 1358
Cdd:COG1131 78 VPQEPALYPDlTVRENLRffaRLYGLPRKEarerIDELLELFGLTDA-------ADRKV----GTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1359 LRRSRVLVLDEATASIDNATDLILQKTIRREFAD-CTVITVAHriptVMD-----CTMVLSISDGRIVEYDEPMKLMKDE 1432
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTH----YLEeaerlCDRVAIIDKGRIVADGTPDELKARL 222
|
250
....*....|.
gi 22331862 1433 -NSLFGKLVKE 1442
Cdd:COG1131 223 lEDVFLELTGE 233
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
614-803 |
3.76e-25 |
|
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: 103.45 E-value: 3.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 614 GSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTI-------------DFYGTIAYVSQTAWIQTGT 680
Cdd:cd03246 12 GAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldgadisqwdpnELGDHVGYLPQDDELFSGS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 681 IRDNILfggvmdehryretiqkssldkdlellpdgdqteigergvnlSGGQKQRIQLARALYQDADIYLLDDPFSAVDAH 760
Cdd:cd03246 92 IAENIL-----------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 22331862 761 TASSLFQEYVMDALAGKAVLLVTHQVDFLPAFDSVLLMSDGEI 803
Cdd:cd03246 131 GERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1207-1421 |
3.95e-25 |
|
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: 106.04 E-value: 3.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYR--RESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRF 1284
Cdd:COG1124 2 LEVRNLSVSYGqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1285 GIIPQDPTlfnGTV--RFNLD-----PLCQH----SDAEIWEVLGKCQLKEVVqekengLDSLVVEdgsnWSMGQRQLFC 1353
Cdd:COG1124 82 QMVFQDPY---ASLhpRHTVDrilaePLRIHglpdREERIAELLEQVGLPPSF------LDRYPHQ----LSGGQRQRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331862 1354 LGRAVLRRSRVLVLDEATASIDNAT-DLILQ--KTIRREFaDCTVITVAHRIPtVMD--CTMVLSISDGRIVE 1421
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVqAEILNllKDLREER-GLTYLFVSHDLA-VVAhlCDRVAVMQNGRIVE 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
620-800 |
4.23e-25 |
|
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: 104.48 E-value: 4.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTI------------DFYGTIAYVS-QTAWIQTGTIRDNIL 686
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVlwngepirdareDYRRRLAYLGhADGLKPELTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 687 F-----GGVMDEHRYRETIQKSSLDKDLELLPDgdqteigergvNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHt 761
Cdd:COG4133 98 FwaalyGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 22331862 762 ASSLFQEYVMDALA-GKAVLLVTHQVDFLPAfDSVLLMSD 800
Cdd:COG4133 166 GVALLAELIAAHLArGGAVLLTTHQPLELAA-ARVLDLGD 204
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
589-815 |
5.64e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 111.65 E-value: 5.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 589 RRKQRSEGNqnaIIIKSASFSWEEKgsTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-- 666
Cdd:PRK11176 333 RVIERAKGD---IEFRNVTFTYPGK--EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdl 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 667 -----------IAYVSQTAWIQTGTIRDNILFGGvmDEHRYRETIQKSS-----LDKdLELLPDGDQTEIGERGVNLSGG 730
Cdd:PRK11176 408 rdytlaslrnqVALVSQNVHLFNDTIANNIAYAR--TEQYSREQIEEAArmayaMDF-INKMDNGLDTVIGENGVLLSGG 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 731 QKQRIQLARALYQDADIYLLDDPFSAVDahTASSLFQEYVMDAL-AGKAVLLVTHQVDFLPAFDSVLLMSDGEITEADTY 809
Cdd:PRK11176 485 QRQRIAIARALLRDSPILILDEATSALD--TESERAIQAALDELqKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTH 562
|
....*.
gi 22331862 810 QELLAR 815
Cdd:PRK11176 563 AELLAQ 568
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
609-803 |
9.39e-25 |
|
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: 104.28 E-value: 9.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 609 SWEEKGSTKPN-------LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILG---ETPCVSGTIDFYG----------TIA 668
Cdd:cd03234 5 PWWDVGLKAKNwnkyariLNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGqprkpdqfqkCVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 669 YVSQT-AWIQTGTIRDNILFGGVMDEHRYRETIQKSSLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADI 747
Cdd:cd03234 85 YVRQDdILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 748 YLLDDPFSAVDAHTASSLFQEYVMDALAGKAVLLVTHQ--VDFLPAFDSVLLMSDGEI 803
Cdd:cd03234 165 LILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQprSDLFRLFDRILLLSSGEI 222
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
620-815 |
9.87e-25 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 104.38 E-value: 9.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT------------IAYVSQTAWIQTG-TIRDNI- 685
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvardpaevrrrIGYVPQEPALYPDlTVRENLr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 686 LFGGV--MDEHRYRETIQKssLDKDLELLPDGDQteigeRGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTAS 763
Cdd:COG1131 96 FFARLygLPRKEARERIDE--LLELFGLTDAADR-----KVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 764 SLFQeyVMDALA--GKAVLLVTHQ---VDFLpaFDSVLLMSDGEITEADTYQELLAR 815
Cdd:COG1131 169 ELWE--LLRELAaeGKTVLLSTHYleeAERL--CDRVAIIDKGRIVADGTPDELKAR 221
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
566-836 |
1.01e-24 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 110.96 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 566 QAKVAFSRIATFLEAPELQGGERRRKQRSegnqNAIIIKSASFSWEEKgstKPNLRNVSLEVKFGEKVAVCGEVGSGKST 645
Cdd:PRK10790 310 QAVVAGERVFELMDGPRQQYGNDDRPLQS----GRIDIDNVSFAYRDD---NLVLQNINLSVPSRGFVALVGHTGSGKST 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 646 LLAAILGETPCVSGTIDFYG-------------TIAYVSQTAWIQTGTIRDNILFGGVMDEH---RYRETIQKSSLDKDL 709
Cdd:PRK10790 383 LASLLMGYYPLTEGEIRLDGrplsslshsvlrqGVAMVQQDPVVLADTFLANVTLGRDISEEqvwQALETVQLAELARSL 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 710 ellPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQeyVMDALAGKAVLLV-THQVDF 788
Cdd:PRK10790 463 ---PDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQ--ALAAVREHTTLVViAHRLST 537
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 22331862 789 LPAFDSVLLMSDGEITEADTYQELLA-RSRDFQ--DLVNAHRETAGSERVV 836
Cdd:PRK10790 538 IVEADTILVLHRGQAVEQGTHQQLLAaQGRYWQmyQLQLAGEELAASVREE 588
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
607-815 |
1.13e-24 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 111.07 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 607 SFSWEEKgstKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-IAYVSQT---AWIqtG--- 679
Cdd:COG5265 364 SFGYDPE---RPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQdIRDVTQAslrAAI--Givp 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 680 --------TIRDNILFG--GVMDEhRYRETIQKSSLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYL 749
Cdd:COG5265 439 qdtvlfndTIAYNIAYGrpDASEE-EVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILI 517
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 750 LDDPFSAVDAHTASSLfQEYVMDALAGKAVLLVTHQ----VDflpAfDSVLLMSDGEITEADTYQELLAR 815
Cdd:COG5265 518 FDEATSALDSRTERAI-QAALREVARGRTTLVIAHRlstiVD---A-DEILVLEAGRIVERGTHAELLAQ 582
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
566-822 |
1.46e-24 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 110.99 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 566 QAKVAFSRIATFLEAPelqggerrRKQRSEGN------QNAIIIKSASFSWEEkgSTKPNLRNVSLEVKFGEKVAVCGEV 639
Cdd:TIGR01846 423 QTGIALERLGDILNSP--------TEPRSAGLaalpelRGAITFENIRFRYAP--DSPEVLSNLNLDIKPGEFIGIVGPS 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 640 GSGKSTL-----------LAAIL--GETPCVSGTIDFYGTIAYVSQTAWIQTGTIRDNILFGG-VMDEHRYRETIQKSSL 705
Cdd:TIGR01846 493 GSGKSTLtkllqrlytpqHGQVLvdGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNpGAPFEHVIHAAKLAGA 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 706 DKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQEyvMDAL-AGKAVLLVTH 784
Cdd:TIGR01846 573 HDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRN--MREIcRGRTVIIIAH 650
|
250 260 270
....*....|....*....|....*....|....*...
gi 22331862 785 QVDFLPAFDSVLLMSDGEITEADTYQELLARSRDFQDL 822
Cdd:TIGR01846 651 RLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARL 688
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1207-1419 |
2.56e-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: 101.32 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRResPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVhDLRSRFGI 1286
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE-EVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDPTLFNG-TVRFNLDplcqhsdaeiwevlgkcqlkevvqekengldslvvedgsnWSMGQRQLFCLGRAVLRRSRVL 1365
Cdd:cd03230 78 LPEEPSLYENlTVRENLK----------------------------------------LSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 1366 VLDEATASID-NATDLILQ--KTIRREfaDCTVITVAHRIPTVMD-CTMVLSISDGRI 1419
Cdd:cd03230 118 ILDEPTSGLDpESRREFWEllRELKKE--GKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1206-1437 |
3.04e-24 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 103.58 E-value: 3.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1206 RVEISDLQIRYRRESplVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFG 1285
Cdd:COG1120 1 MLEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1286 IIPQDPTL-FNGTV-------RFN-LDPLCQHSD---AEIWEVLGKCQLKEVvqeKENGLDSLvvedgsnwSMGQRQLFC 1353
Cdd:COG1120 79 YVPQEPPApFGLTVrelvalgRYPhLGLFGRPSAedrEAVEEALERTGLEHL---ADRPVDEL--------SGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1354 LGRAVLRRSRVLVLDEATASIDNATDLILQKTIRR--EFADCTVITVAHriptvmD-------CTMVLSISDGRIVEYDE 1424
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLH------DlnlaaryADRLVLLKDGRIVAQGP 221
|
250
....*....|....*
gi 22331862 1425 PMKLMKDEN--SLFG 1437
Cdd:COG1120 222 PEEVLTPELleEVYG 236
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
289-574 |
8.37e-24 |
|
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: 103.45 E-value: 8.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 289 GFFAFMKIVAVSAGPLLLNAFILVAEGNASF--RYEGLVLAVLLFFSKMIESLSQRQWYFRCRIVGLRVRSLLTAAINKK 366
Cdd:cd18593 3 GIFLFLEEAIRVVQPIFLGKLIRYFEGNGSSisLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIYRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 367 QLRLNNSSRLIHSGSEIMNYATVDAYRIGEFPYWFHQLWTTSFQLLIALGILFHSVGVATFSALAVIILTVLCNAPIAKL 446
Cdd:cd18593 83 ALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFGKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 447 QNKFQSELMTSQDERLKACNESLVNMKVLKLYAWESHFKKVIEKLRNIELKSLKAVQMRKAYNAVLFWSSPVFVSAATFA 526
Cdd:cd18593 163 FSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTFL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 22331862 527 TCYFLDIPLRASNVFTFVATLRLVQDPVRM-IPDVIGVTIQAKVAFSRI 574
Cdd:cd18593 243 AYILLGNILTAERVFVTMALYNAVRLTMTLfFPFAIQFGSELSVSIRRI 291
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1207-1435 |
9.52e-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: 101.42 E-value: 9.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESplVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDL---RSR 1283
Cdd:cd03261 1 IELRGLTKSFGGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1284 FGIIPQDPTLFNG-TVRFNLD-PLCQHSDaeiwevLGKCQLKEVVQEKEN--GLDSlvVED--GSNWSMGQRQLFCLGRA 1357
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAfPLREHTR------LSEEEIREIVLEKLEavGLRG--AEDlyPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1358 VLRRSRVLVLDEATASIDNAT-----DLILqkTIRREFaDCTVITVAHRIPTVMD-CTMVLSISDGRIVEYDEPMKLMKD 1431
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIAsgvidDLIR--SLKKEL-GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRAS 227
|
....
gi 22331862 1432 ENSL 1435
Cdd:cd03261 228 DDPL 231
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
603-805 |
2.19e-23 |
|
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: 100.27 E-value: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 603 IKSASFSWEEKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT---------------- 666
Cdd:cd03257 4 VKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllklsrrlrkirrke 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 667 IAYVSQ---TAWIQTGTIRDNI----LFGGVMDEHRYRETIqkssLDKDLELLPDGDqtEIGERGVN-LSGGQKQRIQLA 738
Cdd:cd03257 84 IQMVFQdpmSSLNPRMTIGEQIaeplRIHGKLSKKEARKEA----VLLLLVGVGLPE--EVLNRYPHeLSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22331862 739 RALYQDADIYLLDDPFSAVDAHTasslfQEYVMDALA------GKAVLLVTHQVDFLPAF-DSVLLMSDGEITE 805
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSV-----QAQILDLLKklqeelGLTLLFITHDLGVVAKIaDRVAVMYAGKIVE 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
620-803 |
2.94e-23 |
|
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: 99.53 E-value: 2.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGTIAYVSQTAWI----QTG------------TIRD 683
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINelrqKVGmvfqqfnlfphlTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 684 NILFGGVMDEHRYRETIQKSSLDKdLEL--LPDGDQTEIGErgvnLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHT 761
Cdd:cd03262 96 NITLAPIKVKGMSKAEAEERALEL-LEKvgLADKADAYPAQ----LSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 22331862 762 ASSLFQeyVMDALA--GKAVLLVTHQVDF-LPAFDSVLLMSDGEI 803
Cdd:cd03262 171 VGEVLD--VMKDLAeeGMTMVVVTHEMGFaREVADRVIFMDDGRI 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
603-804 |
3.96e-23 |
|
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: 98.87 E-value: 3.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 603 IKSASFSWEEKGSTkpnLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG----------TIAYVSQ 672
Cdd:cd03226 2 IENISFSYKKGTEI---LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 673 TAWIQ--TGTIRDNILFGgVMDEHRYRETIQKssLDKDLELLpdgdqtEIGERG-VNLSGGQKQRIQLARALYQDADIYL 749
Cdd:cd03226 79 DVDYQlfTDSVREELLLG-LKELDAGNEQAET--VLKDLDLY------ALKERHpLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 750 LDDPFSAVDAHTASSLfQEYVMD-ALAGKAVLLVTHQVDFLPAF-DSVLLMSDGEIT 804
Cdd:cd03226 150 FDEPTSGLDYKNMERV-GELIRElAAQGKAVIVITHDYEFLAKVcDRVLLLANGAIV 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
571-818 |
4.21e-23 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 104.99 E-value: 4.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 571 FSRIATFLEAPELQGGERRRKQRSEGNQNAIIIKSASFSWEEKGSTKPN-LRNVSLEVKFGEKVAVCGEVGSGKSTLLAA 649
Cdd:COG1123 231 LAAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRGKGGVRaVDDVSLTLRRGETLGLVGESGSGKSTLARL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 650 ILGETPCVSGTIDFYGT----------------IAYVSQ---TAWIQTGTIRDNILFG----GVMDEHRYRETIQkssld 706
Cdd:COG1123 311 LLGLLRPTSGSILFDGKdltklsrrslrelrrrVQMVFQdpySSLNPRMTVGDIIAEPlrlhGLLSRAERRERVA----- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 707 kdlELLpdgDQTEIGERGVN-----LSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTasslfQEYVMDALA------ 775
Cdd:COG1123 386 ---ELL---ERVGLPPDLADrypheLSGGQRQRVAIARALALEPKLLILDEPTSALDVSV-----QAQILNLLRdlqrel 454
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 22331862 776 GKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQELLARSRD 818
Cdd:COG1123 455 GLTYLFISHDLAVVRYIaDRVAVMYDGRIVEDGPTEEVFANPQH 498
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
620-803 |
5.24e-23 |
|
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: 97.47 E-value: 5.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGtiayvsQTAWIQTGTIRDNIlfgGVMdehryret 699
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG------KDIKKEPEEVKRRI---GYL-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 700 IQKSSLDKDL---ELLpdgdqteigergvNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQeyVMDALA- 775
Cdd:cd03230 79 PEEPSLYENLtvrENL-------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWE--LLRELKk 143
|
170 180 190
....*....|....*....|....*....|
gi 22331862 776 -GKAVLLVTHQVDFLPA-FDSVLLMSDGEI 803
Cdd:cd03230 144 eGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
603-805 |
5.54e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 99.94 E-value: 5.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 603 IKSASFSWEEKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGTI--------AYVSQT- 673
Cdd:COG4525 6 VRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVFQKd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 674 ---AWIqtgTIRDNILFG----GVMDEHRYRETIQKssldkdLEL--LPDGDQTEIGErgvnLSGGQKQRIQLARALYQD 744
Cdd:COG4525 86 allPWL---NVLDNVAFGlrlrGVPKAERRARAEEL------LALvgLADFARRRIWQ----LSGGMRQRVGIARALAAD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 745 ADIYLLDDPFSAVDAHTASSLfQEYVMD--ALAGKAVLLVTHQVD---FLPAfdSVLLMSD--GEITE 805
Cdd:COG4525 153 PRFLLMDEPFGALDALTREQM-QELLLDvwQRTGKGVFLITHSVEealFLAT--RLVVMSPgpGRIVE 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1208-1420 |
5.86e-23 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 98.76 E-value: 5.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1208 EISDLQIRYRREspLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIgvhdlRSRFGII 1287
Cdd:cd03235 1 EVEDLTVSYGGH--PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1288 PQ----DPTlFNGTVR----------FNLDPLCQHSD-AEIWEVLGKCQLKEVVQEKengLDSLvvedgsnwSMGQRQLF 1352
Cdd:cd03235 74 PQrrsiDRD-FPISVRdvvlmglyghKGLFRRLSKADkAKVDEALERVGLSELADRQ---IGEL--------SGGQQQRV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331862 1353 CLGRAVLRRSRVLVLDEATASIDNAT--DLI-LQKTIRREfaDCTVITVAHRIPTVMD-CTMVLSIsDGRIV 1420
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTqeDIYeLLRELRRE--GMTILVVTHDLGLVLEyFDRVLLL-NRTVV 210
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1168-1417 |
6.37e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 105.27 E-value: 6.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1168 LANWIISVERLNQYTHLTpEAPEVIEETRPPVNWPVTGRVEISDLQIRYRRESPLVlKGISCTFEGGHKIGIVGRTGSGK 1247
Cdd:COG4178 325 LAEWRATVDRLAGFEEAL-EAADALPEAASRIETSEDGALALEDLTLRTPDGRPLL-EDLSLSLKPGERLLITGPSGSGK 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1248 TTLISALFRLVEPVGGKIVV-DGVDISkigvhdlrsrfgIIPQDPTLFNGTVRFNL---DPLCQHSDAEIWEVLGKCqlk 1323
Cdd:COG4178 403 STLLRAIAGLWPYGSGRIARpAGARVL------------FLPQRPYLPLGTLREALlypATAEAFSDAELREALEAV--- 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1324 evvqekenGLDSLV--VEDGSNW----SMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIRREFADCTVIT 1397
Cdd:COG4178 468 --------GLGHLAerLDEEADWdqvlSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVIS 539
|
250 260
....*....|....*....|.
gi 22331862 1398 VAHRiPTVMD-CTMVLSISDG 1417
Cdd:COG4178 540 VGHR-STLAAfHDRVLELTGD 559
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
620-814 |
9.39e-23 |
|
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: 98.28 E-value: 9.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT--------------IAYVSQTAWIQTG-TIRDN 684
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEGRRIFPElTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 685 ILFGGvmdeHRYRETIQKSSLDKDLELLPDgdqteIGER----GVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVdah 760
Cdd:cd03224 96 LLLGA----YARRRAKRKARLERVYELFPR-----LKERrkqlAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL--- 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 761 taSSLFQEYVMDALA-----GKAVLLVTHQVDF-LPAFDSVLLMSDGEITEADTYQELLA 814
Cdd:cd03224 164 --APKIVEEIFEAIRelrdeGVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
618-812 |
1.63e-22 |
|
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: 98.18 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 618 PNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILG-ETPcVSGTIDFYG-----------TIAYVSQT-AWIQTGTIRDN 684
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGlERP-DSGTILFGGedatdvpvqerNVGFVFQHyALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 685 ILFGgvMDEHRYRETIQKSSLDKDLELLPDGDQTE-IGERGVN-LSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTA 762
Cdd:cd03296 95 VAFG--LRVKPRSERPPEAEIRAKVHELLKLVQLDwLADRYPAqLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22331862 763 SSL--FQEYVMDALaGKAVLLVTH-QVDFLPAFDSVLLMSDGEITEADTYQEL 812
Cdd:cd03296 173 KELrrWLRRLHDEL-HVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
618-798 |
2.77e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.15 E-value: 2.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 618 PNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG--TIAYVSQ-TAWIQT--GTIRDNILFG---- 688
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQrSEVPDSlpLTVRDLVAMGrwar 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 689 -GVMDEHRYREtiqKSSLDKDLELLpdgDQTEIGERGVN-LSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLF 766
Cdd:NF040873 86 rGLWRRLTRDD---RAAVDDALERV---GLADLAGRQLGeLSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERII 159
|
170 180 190
....*....|....*....|....*....|..
gi 22331862 767 QEYVMDALAGKAVLLVTHQVDFLPAFDSVLLM 798
Cdd:NF040873 160 ALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
620-815 |
2.80e-22 |
|
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: 97.41 E-value: 2.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-----------IAYVSQT-AWIQTGTIRDNILF 687
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 688 G----GVMDEHRYRETIQKSSLDKDLELLPDGDQTeigergvnLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTAS 763
Cdd:cd03299 95 GlkkrKVDKKEIERKVLEIAEMLGIDHLLNRKPET--------LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 22331862 764 SLFQEY-VMDALAGKAVLLVTHqvDFLPAF---DSVLLMSDGEITEADTYQELLAR 815
Cdd:cd03299 167 KLREELkKIRKEFGVTVLHVTH--DFEEAWalaDKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
620-814 |
3.42e-22 |
|
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: 97.19 E-value: 3.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-IAYVSQTAWI----------QTG------TIR 682
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdISGLSEAELYrlrrrmgmlfQSGalfdslTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 683 DNILFGgvMDEHR--YRETIQKSSLDKdLEL--LPDGDQTEIGErgvnLSGGQKQRIQLARALYQDADIYLLDDPFSAVD 758
Cdd:cd03261 96 ENVAFP--LREHTrlSEEEIREIVLEK-LEAvgLRGAEDLYPAE----LSGGMKKRVALARALALDPELLLYDEPTAGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 22331862 759 AhTASSLFQEYVMD--ALAGKAVLLVTHQVDF-LPAFDSVLLMSDGEITEADTYQELLA 814
Cdd:cd03261 169 P-IASGVIDDLIRSlkKELGLTSIMVTHDLDTaFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
615-827 |
3.74e-22 |
|
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: 97.67 E-value: 3.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 615 STKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-------------IAYVSQTAWIQTGTI 681
Cdd:cd03288 32 NLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIdisklplhtlrsrLSIILQDPILFSGSI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 682 RDNILFGGVMDEHRYRETIQKSSLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHT 761
Cdd:cd03288 112 RFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 762 aSSLFQEYVMDALAGKAVLLVTHQVDFLPAFDSVLLMSDGEITEADTYQELLARSRD-FQDLVNAHR 827
Cdd:cd03288 192 -ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGvFASLVRTDK 257
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1207-1424 |
4.20e-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: 96.88 E-value: 4.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRY--RRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDI---SKIGVHDLR 1281
Cdd:cd03258 2 IELKNVSKVFgdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1282 SRFGIIPQDPTLFNG-TVRFNLD-PLcqhsdaEIWEVlgkcqLKEVVQEKENGLDSLV-VEDG-----SNWSMGQRQLFC 1353
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVAlPL------EIAGV-----PKAEIEERVLELLELVgLEDKadaypAQLSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 1354 LGRAVLRRSRVLVLDEATASID-NATDLILQ--KTIRREFaDCTVITVAHRIPTVMD-CTMVLSISDGRIVEYDE 1424
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDpETTQSILAllRDINREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGT 224
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
618-808 |
4.41e-22 |
|
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: 95.94 E-value: 4.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 618 PNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-IAYVSQTAWIQTGTI--RDNILFGGvmdeh 694
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdISTIPLEDLRSSLTIipQDPTLFSG----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 695 ryreTIqKSSLDkdlellPDGDQTE--------IGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTaSSLF 766
Cdd:cd03369 97 ----TI-RSNLD------PFDEYSDeeiygalrVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT-DALI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 22331862 767 QEYVMDALAGKAVLLVTHQVDFLPAFDSVLLMSDGEITEADT 808
Cdd:cd03369 165 QKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
598-814 |
4.69e-22 |
|
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: 97.71 E-value: 4.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 598 QNAIIIKSASFSWEE---KGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-IAYVSQT 673
Cdd:cd03294 15 QKAFKLLAKGKSKEEilkKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdIAAMSRK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 674 AWIQTG-----------------TIRDNILFG----GVMDEHRYR---ETIQKSSLDKDLELLPDgdqteigergvNLSG 729
Cdd:cd03294 95 ELRELRrkkismvfqsfallphrTVLENVAFGlevqGVPRAEREEraaEALELVGLEGWEHKYPD-----------ELSG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 730 GQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLfQEYVMD--ALAGKAVLLVTHqvDFLPAF---DSVLLMSDGEIT 804
Cdd:cd03294 164 GMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM-QDELLRlqAELQKTIVFITH--DLDEALrlgDRIAIMKDGRLV 240
|
250
....*....|
gi 22331862 805 EADTYQELLA 814
Cdd:cd03294 241 QVGTPEEILT 250
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1183-1421 |
5.51e-22 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 102.10 E-value: 5.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1183 HLTPEAPEVIEETRPPVNWPVTGRVEISdlQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVG 1262
Cdd:PRK10789 292 AMLAEAPVVKDGSEPVPEGRGELDVNIR--QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1263 GKIVVDGVDISKIGVHDLRSRFGIIPQDPTLFNGTVRFNLDPLC-QHSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDG 1341
Cdd:PRK10789 370 GDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERG 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1342 SNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGRIVE 1421
Cdd:PRK10789 450 VMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQ 529
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
467-823 |
8.96e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 102.11 E-value: 8.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 467 ESLVNMKVLKLYAWE----SHFKkviEKLRNIelkslKAVQMRKAY-NAVLFWSSPVFVSAATFATCYF-----LDIPLR 536
Cdd:TIGR00958 345 EALSGMRTVRSFAAEegeaSRFK---EALEET-----LQLNKRKALaYAGYLWTTSVLGMLIQVLVLYYggqlvLTGKVS 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 537 ASNVFTFVATLRLVQDPVRMIPDVIGVTIQAKVAFSRIATFLE-APELQGGERRRKQRSEGNqnaIIIKSASFSWEEKgS 615
Cdd:TIGR00958 417 SGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDrKPNIPLTGTLAPLNLEGL---IEFQDVSFSYPNR-P 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 616 TKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-------------IAYVSQTAWIQTGTIR 682
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplvqydhhylhrqVALVGQEPVLFSGSVR 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 683 DNILFG-GVMDEHRYRETIQKSSLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHT 761
Cdd:TIGR00958 573 ENIAYGlTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC 652
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331862 762 ASSLFQEyvmDALAGKAVLLVTHQVDFLPAFDSVLLMSDGEITEADTYQELLARSRDFQDLV 823
Cdd:TIGR00958 653 EQLLQES---RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1208-1420 |
9.43e-22 |
|
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: 94.04 E-value: 9.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1208 EISDLQIRYRRESplVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGII 1287
Cdd:cd03214 1 EVENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1288 PQdptlfngtvrfnldplcqhsdaeiweVLGKCQLKEVvqeKENGLDSLvvedgsnwSMGQRQLFCLGRAVLRRSRVLVL 1367
Cdd:cd03214 79 PQ--------------------------ALELLGLAHL---ADRPFNEL--------SGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 22331862 1368 DEATASIDNATDLILQKTIRREFAD--CTVITVAHRI-PTVMDCTMVLSISDGRIV 1420
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARErgKTVVMVLHDLnLAARYADRVILLKDGRIV 177
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1208-1425 |
1.89e-21 |
|
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: 94.94 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1208 EISDLQIRYRRESPlVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDL---RSRF 1284
Cdd:cd03256 2 EVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1285 GIIPQDPTLFNG-TVRFNLdpLC----QHSdaeIWEVLGKcQLKEvvQEKEN--------GLDSLVVEDGSNWSMGQRQL 1351
Cdd:cd03256 81 GMIFQQFNLIERlSVLENV--LSgrlgRRS---TWRSLFG-LFPK--EEKQRalaalervGLLDKAYQRADQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 1352 FCLGRAVLRRSRVLVLDEATASIDNATDLI---LQKTIRREFADcTVITVAHRIPTVMD-CTMVLSISDGRIVeYDEP 1425
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQvmdLLKRINREEGI-TVIVSLHQVDLAREyADRIVGLKDGRIV-FDGP 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
624-818 |
2.13e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 94.82 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 624 SLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG---TIAYVSQ---TAWIQTG------TIRDNILFG--- 688
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdlTALPPAErpvSMLFQENnlfphlTVAQNIGLGlrp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 689 ----GVMDEHRYRETIQKSSLDKDLELLPDgdqteigergvNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAhtasS 764
Cdd:COG3840 99 glklTAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDP----A 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331862 765 LFQEyvMDAL-------AGKAVLLVTHQV-DFLPAFDSVLLMSDGEITEADTYQELLARSRD 818
Cdd:COG3840 164 LRQE--MLDLvdelcreRGLTVLMVTHDPeDAARIADRVLLVADGRIAADGPTAALLDGEPP 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
620-812 |
2.85e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 97.08 E-value: 2.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-----------IAYVSQT-AWIQTGTIRDNILF 687
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHyALFRHMTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 688 GGVMDEHRYRETiqKSSLDKDLELLPDGDQ-TEIGER-GVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSL 765
Cdd:PRK10851 98 GLTVLPRRERPN--AAAIKAKVTQLLEMVQlAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKEL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22331862 766 --FQEYVMDALAGKAVlLVTH-QVDFLPAFDSVLLMSDGEITEADTYQEL 812
Cdd:PRK10851 176 rrWLRQLHEELKFTSV-FVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
620-818 |
3.23e-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: 3.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-----------IAYVSQ--------Tawiqtgt 680
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppekrnVGMVFQdyalfphlT------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 681 IRDNILFG---GVMDEHRYRETIQkssldkdlELLpdgDQTEI---GERGVN-LSGGQKQRIQLARALYQDADIYLLDDP 753
Cdd:COG3842 94 VAENVAFGlrmRGVPKAEIRARVA--------ELL---ELVGLeglADRYPHqLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 754 FSAVDAHTASSLfQEYVMDALA--GKAVLLVTHqvDFLPAF---DSVLLMSDGEITEADTYQELLARSRD 818
Cdd:COG3842 163 LSALDAKLREEM-REELRRLQRelGITFIYVTH--DQEEALalaDRIAVMNDGRIEQVGTPEEIYERPAT 229
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
620-805 |
4.13e-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: 93.78 E-value: 4.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAI------LGETPcVSGTIDFYG---------------TIAYVSQTAWIQT 678
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndlIPGAP-DEGEVLLDGkdiydldvdvlelrrRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 679 GTIRDNILFG----GvMDEHRYRETIQKSSLDKDLelLPDgdqtEIGER--GVNLSGGQKQRIQLARALYQDADIYLLDD 752
Cdd:cd03260 95 GSIYDNVAYGlrlhG-IKLKEELDERVEEALRKAA--LWD----EVKDRlhALGLSGGQQQRLCLARALANEPEVLLLDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 753 PFSAVDAHTASSLfqEYVMDALAGK-AVLLVTH---QVDFLPafDSVLLMSDGEITE 805
Cdd:cd03260 168 PTSALDPISTAKI--EELIAELKKEyTIVIVTHnmqQAARVA--DRTAFLLNGRLVE 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
601-817 |
4.78e-21 |
|
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: 93.80 E-value: 4.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 601 IIIKSASFSWEEKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILG-ETPcVSGTIDFYGT------------- 666
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGlERP-TSGSVLVDGTdltllsgkelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 667 ---IAYVSQT-AWIQTGTIRDNILF----GGVMDEHRYRetiqkssldKDLELLPDGDQTEIGER-GVNLSGGQKQRIQL 737
Cdd:cd03258 81 rrrIGMIFQHfNLLSSRTVFENVALpleiAGVPKAEIEE---------RVLELLELVGLEDKADAyPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 738 ARALYQDADIYLLDDPFSAVDAHTASSlfqeyVMDALA------GKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQ 810
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQS-----ILALLRdinrelGLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVE 226
|
....*..
gi 22331862 811 ELLARSR 817
Cdd:cd03258 227 EVFANPQ 233
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1207-1423 |
7.33e-21 |
|
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: 92.58 E-value: 7.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRreSPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHdlRSRFGI 1286
Cdd:cd03259 1 LELKGLSKTYG--SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDPTLF-NGTVRFNLD-PLCQHSdaeiwevLGKCQLKEVVQE--KENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRS 1362
Cdd:cd03259 77 VFQDYALFpHLTVAENIAfGLKLRG-------VPKAEIRARVREllELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22331862 1363 RVLVLDEATASIDNATDLILQKTIRR--EFADCTVITVAHRIPTVM---DCTMVLsiSDGRIVEYD 1423
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEEALalaDRIAVM--NEGRIVQVG 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
620-819 |
9.10e-21 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 93.13 E-value: 9.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILG-ETPCvSGTIDFYGTIAYVSQTAWIQ----TG------------TIR 682
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLlEEPD-SGTITVDGEDLTDSKKDINKlrrkVGmvfqqfnlfphlTVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 683 DNILFGGVmdehryreTIQKssLDKD------LELLpdgDQTEIGERG----VNLSGGQKQRIQLARALYQDADIYLLDD 752
Cdd:COG1126 96 ENVTLAPI--------KVKK--MSKAeaeeraMELL---ERVGLADKAdaypAQLSGGQQQRVAIARALAMEPKVMLFDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 753 PFSAVDAhtasslfqEY------VMDALA--GKAVLLVTHQVDFlpAF---DSVLLMSDGEITEADTYQELLA-----RS 816
Cdd:COG1126 163 PTSALDP--------ELvgevldVMRDLAkeGMTMVVVTHEMGF--ARevaDRVVFMDGGRIVEEGPPEEFFEnpqheRT 232
|
...
gi 22331862 817 RDF 819
Cdd:COG1126 233 RAF 235
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
620-803 |
9.30e-21 |
|
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: 92.36 E-value: 9.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKF---GEKVAVCGEVGSGKSTLLAAILG-ETPCVsGTIDFYGT-----------------IAYVSQTAWIQT 678
Cdd:cd03297 10 LPDFTLKIDFdlnEEVTGIFGASGAGKSTLLRCIAGlEKPDG-GTIVLNGTvlfdsrkkinlppqqrkIGLVFQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 679 G-TIRDNILFGgvMDEHRYREtiQKSSLDKDLELLpdgDQTEIGERGV-NLSGGQKQRIQLARALYQDADIYLLDDPFSA 756
Cdd:cd03297 89 HlNVRENLAFG--LKRKRNRE--DRISVDELLDLL---GLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 22331862 757 VDAHTASSLfQEYVMDALA--GKAVLLVTHQVD--FLPAfDSVLLMSDGEI 803
Cdd:cd03297 162 LDRALRLQL-LPELKQIKKnlNIPVIFVTHDLSeaEYLA-DRIVVMEDGRL 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1207-1433 |
1.00e-20 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 93.23 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRREspLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKigvhdLRSRFGI 1286
Cdd:COG1121 7 IELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDPTL---FNGTVR----FNLDP-------LCQHSDAEIWEVLGKCQLKEVVQEKengLDSLvvedgsnwSMGQRQLF 1352
Cdd:COG1121 80 VPQRAEVdwdFPITVRdvvlMGRYGrrglfrrPSRADREAVDEALERVGLEDLADRP---IGEL--------SGGQQQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1353 CLGRAVLRRSRVLVLDEATASIDNAT-DLILQ--KTIRREfaDCTVITVAHRIPTVMD-CTMVLSIsDGRIVEYDEPMKL 1428
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATeEALYEllRELRRE--GKTILVVTHDLGAVREyFDRVLLL-NRGLVAHGPPEEV 225
|
....*
gi 22331862 1429 MKDEN 1433
Cdd:COG1121 226 LTPEN 230
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1206-1418 |
1.25e-20 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 91.77 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1206 RVEISDLQIRYRREspLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVhDLRSRFG 1285
Cdd:COG4133 2 MLEAENLSCRRGER--LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1286 IIPQDPTLFNG-TVRFNLDPLCQ-----HSDAEIWEVLGKCQLKEVvqekengLDSLVvedgSNWSMGQRQLFCLGRAVL 1359
Cdd:COG4133 79 YLGHADGLKPElTVRENLRFWAAlyglrADREAIDEALEAVGLAGL-------ADLPV----RQLSAGQKRRVALARLLL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 22331862 1360 RRSRVLVLDEATASIDNATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGR 1418
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVLDLGDFK 206
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
620-807 |
4.34e-20 |
|
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: 90.67 E-value: 4.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGTIAYVSQtawIQTG-----TIRDNILFGGVM--- 691
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG---LGGGfnpelTGRENIYLNGRLlgl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 692 ----DEHRYRETIQKSSLDKDLELlpdgdqteigeRGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHtasslFQ 767
Cdd:cd03220 115 srkeIDEKIDEIIEFSELGDFIDL-----------PVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA-----FQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 22331862 768 EYVMDALA-----GKAVLLVTHQVDFLPAF-DSVLLMSDGEITEAD 807
Cdd:cd03220 179 EKCQRRLRellkqGKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1208-1431 |
4.56e-20 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 90.57 E-value: 4.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1208 EISDLQIRYRrESPlVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDlRSRFGI- 1286
Cdd:cd03224 2 EVENLNAGYG-KSQ-ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARAGIg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 -IPQDPTLFNG-TVRFNLD----PLCQHSDAEIWEVLgkCQLKEVVQEKENGLdslvvedGSNWSMGQRQLFCLGRAVLR 1360
Cdd:cd03224 79 yVPEGRRIFPElTVEENLLlgayARRRAKRKARLERV--YELFPRLKERRKQL-------AGTLSGGEQQMLAIARALMS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1361 RSRVLVLDEATAS-----IDNATDLIlqKTIRREfaDCTVITVAHRIptvmdcTMVLSISD-------GRIVEYDEPMKL 1428
Cdd:cd03224 150 RPKLLLLDEPSEGlapkiVEEIFEAI--RELRDE--GVTILLVEQNA------RFALEIADrayvlerGRVVLEGTAAEL 219
|
...
gi 22331862 1429 MKD 1431
Cdd:cd03224 220 LAD 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
620-804 |
4.63e-20 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 88.64 E-value: 4.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGTIayvsqtawiqtgtirdnILFGGVMDEHRyret 699
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE-----------------VSFASPRDARR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 700 iqkssldkdlellpdgdqteigeRGVN----LSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQeyVMDALA 775
Cdd:cd03216 75 -----------------------AGIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK--VIRRLR 129
|
170 180 190
....*....|....*....|....*....|..
gi 22331862 776 --GKAVLLVTHQVDFLPAF-DSVLLMSDGEIT 804
Cdd:cd03216 130 aqGVAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
615-804 |
4.85e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.47 E-value: 4.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 615 STKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT--------------IAYVS----QTAWI 676
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVPedrkGEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 677 QTGTIRDNILF--------GGVMDEHRYRETIQKSSldKDLELLPDGDQTEIGergvNLSGGQKQRIQLARALYQDADIY 748
Cdd:COG1129 343 LDLSIRENITLasldrlsrGGLLDRRRERALAEEYI--KRLRIKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 22331862 749 LLDDPFSAVDAHTASSLFQeyVMDALA--GKAVLLVTHQVDFLPAF-DSVLLMSDGEIT 804
Cdd:COG1129 417 ILDEPTRGIDVGAKAEIYR--LIRELAaeGKAVIVISSELPELLGLsDRILVMREGRIV 473
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
620-806 |
6.00e-20 |
|
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: 90.91 E-value: 6.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGET-PCVSGTIDFYGT-------------IAYVSQ--TAWIQTG-TIR 682
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLFGErrggedvwelrkrIGLVSPalQLRFPRDeTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 683 DNILFG--GVMDehRYRE--TIQKSSLDKDLELLpdgDQTEIGERGVN-LSGGQKQRIQLARALYQDADIYLLDDPFSAV 757
Cdd:COG1119 99 DVVLSGffDSIG--LYREptDEQRERARELLELL---GLAHLADRPFGtLSQGEQRRVLIARALVKDPELLILDEPTAGL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22331862 758 DAHTASSLFQeyVMDALAG---KAVLLVTHQV-DFLPAFDSVLLMSDGEITEA 806
Cdd:COG1119 174 DLGARELLLA--LLDKLAAegaPTLVLVTHHVeEIPPGITHVLLLKDGRVVAA 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1207-1418 |
8.37e-20 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 88.40 E-value: 8.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRREspLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIG--VHDLRSRF 1284
Cdd:cd03229 1 LELKNVSKRYGQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1285 GIIPQDPTLFNG-TVRFNLdplcqhsdaeiweVLGkcqlkevvqekengldslvvedgsnWSMGQRQLFCLGRAVLRRSR 1363
Cdd:cd03229 79 GMVFQDFALFPHlTVLENI-------------ALG-------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1364 VLVLDEATASIDNATDLILQKTIRREFAD--CTVITVAHRIPTVM---DCTMVLsiSDGR 1418
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAArlaDRVVVL--RDGK 178
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
620-824 |
8.54e-20 |
|
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: 89.83 E-value: 8.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG------------TIAYVSQTAWIqtgTIRDNILF 687
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGkqitepgpdrmvVFQNYSLLPWL---TVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 688 GGVMDEHRYRETIQKSSLDKDLELLpdGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLfQ 767
Cdd:TIGR01184 78 AVDRVLPDLSKSERRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL-Q 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 768 EYVMDAL--AGKAVLLVTHQVD---FLPafDSVLLMSD------GEITEADtyqelLARSRDFQDLVN 824
Cdd:TIGR01184 155 EELMQIWeeHRVTVLMVTHDVDealLLS--DRVVMLTNgpaaniGQILEVP-----FPRPRDRLEVVE 215
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1207-1421 |
1.04e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 89.72 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESPLV--LKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDL---- 1280
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1281 RSRFGIIPQDPTLFNG-TVRFNLD-PL----CQHSDAEIW--EVLGKCQLKEVVQEKENGLdslvvedgsnwSMGQRQLF 1352
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENVAlPLllagVSRKERRERarELLERVGLGDRLDHRPSQL-----------SGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331862 1353 CLGRAVLRRSRVLVLDEATASIDNAT-DLILQ--KTIRREFaDCTVITVAHRiPTVMD-CTMVLSISDGRIVE 1421
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTgEEVLEllRELNREL-GTTIVMVTHD-PELAArADRVIRLRDGRIVS 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
620-815 |
1.16e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 92.44 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILG-ETPcVSGTIDFYGT-----------IAYVSQT-AWIQTGTIRDNIL 686
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGlEDP-TSGEILIGGRdvtdlppkdrnIAMVFQSyALYPHMTVYENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 687 FG----GVmdehrYRETIQKSsLDKDLELLpdgDQTEIGERGV-NLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHT 761
Cdd:COG3839 98 FPlklrKV-----PKAEIDRR-VREAAELL---GLEDLLDRKPkQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 762 A-------SSLFQEYvmdalaGKAVLLVTH-QVDflpAF---DSVLLMSDGEITEADTYQELLAR 815
Cdd:COG3839 169 RvemraeiKRLHRRL------GTTTIYVTHdQVE---AMtlaDRIAVMNDGRIQQVGTPEELYDR 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1207-1443 |
1.29e-19 |
|
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: 89.65 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRY-RREsplVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDL---RS 1282
Cdd:COG1127 6 IEVRNLTKSFgDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyelRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1283 RFGIIPQDPTLFNG-TVRFNLD-PLCQHSDaeiwevLGKCQLKEVVQEKEN--GLdslvveDGSNWSM------GQRQLF 1352
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAfPLREHTD------LSEAEIRELVLEKLElvGL------PGAADKMpselsgGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1353 CLGRAVLRRSRVLVLDEATASIDNAT-----DLILqkTIRREFaDCTVITVAHRIPTVMD-CTMVLSISDGRIVEYDEPM 1426
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITsavidELIR--ELRDEL-GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPE 227
|
250
....*....|....*..
gi 22331862 1427 KLMKDENslfgKLVKEY 1443
Cdd:COG1127 228 ELLASDD----PWVRQF 240
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
620-803 |
1.45e-19 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 88.85 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG-----------TIAYVSQT-AWIQTGTIRDNILF 687
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkdrDIAMVFQNyALYPHMTVYDNIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 688 G--------GVMDEhRYRETIQKSSLDKDLELLPDgdqteigergvNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDA 759
Cdd:cd03301 96 GlklrkvpkDEIDE-RVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 22331862 760 HTASSLFQEYV-MDALAGKAVLLVTH-QVDFLPAFDSVLLMSDGEI 803
Cdd:cd03301 164 KLRVQMRAELKrLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
615-803 |
2.27e-19 |
|
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: 87.10 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 615 STKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT--------------IAYVS----QTAWI 676
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairagIAYVPedrkREGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 677 QTGTIRDNILFGGVmdehryretiqkssldkdlellpdgdqteigergvnLSGGQKQRIQLARALYQDADIYLLDDPFSA 756
Cdd:cd03215 91 LDLSVAENIALSSL------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22331862 757 VDAHTASSLFQeyVMDALA--GKAVLLVTHQVDFLPAF-DSVLLMSDGEI 803
Cdd:cd03215 135 VDVGAKAEIYR--LIRELAdaGKAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1207-1419 |
2.51e-19 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 88.32 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESP--LVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDL---- 1280
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1281 RSRFGIIPQDPTLFNG-TVRFNLD-PLcqhsdaeiweVLGKCQLKEVVQEKENGLDSLVVEDG-----SNWSMGQRQLFC 1353
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVElPL----------LLAGVPKKERRERAEELLERVGLGDRlnhypSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 1354 LGRAVLRRSRVLVLDEATASIDNATDLILQKTIRR--EFADCTVITVAHRIPTVMDCTMVLSISDGRI 1419
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
617-805 |
3.98e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 88.60 E-value: 3.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 617 KPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGTI--------AYVSQT-AWIQTGTIRDNILF 687
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPvegpgaerGVVFQNeGLLPWRNVQDNVAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 688 G----GVMDEHRyretiqkssLDKDLELLPDGDQTEIGERGV-NLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTA 762
Cdd:PRK11248 94 GlqlaGVEKMQR---------LEIAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 22331862 763 SSLfQEYVMDALA--GKAVLLVTHQVD---FLpAFDSVLLMSD-GEITE 805
Cdd:PRK11248 165 EQM-QTLLLKLWQetGKQVLLITHDIEeavFM-ATELVLLSPGpGRVVE 211
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1207-1435 |
4.41e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 88.89 E-value: 4.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGI 1286
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDP-TLFNG-TVR----FNLDPLCQHSDaEIWEVlgkcqLKEVVqeKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLR 1360
Cdd:PRK13632 88 IFQNPdNQFIGaTVEddiaFGLENKKVPPK-KMKDI-----IDDLA--KKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 1361 RSRVLVLDEATASIDNATDLILQKTIR--REFADCTVITVAHRIPTVMDCTMVLSISDGRIVEYDEPMKLMKDENSL 1435
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEIL 236
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
601-789 |
4.63e-19 |
|
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: 85.19 E-value: 4.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 601 IIIKSASFSWEEKgstkPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT--IAYVSQtawiqt 678
Cdd:cd03221 1 IELENLSKTYGGK----LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTvkIGYFEQ------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 679 gtirdnilfggvmdehryretiqkssldkdlellpdgdqteigergvnLSGGQKQRIQLARALYQDADIYLLDDPFSAVD 758
Cdd:cd03221 71 ------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180 190
....*....|....*....|....*....|....
gi 22331862 759 AHTASSL---FQEYvmdalaGKAVLLVTHQVDFL 789
Cdd:cd03221 103 LESIEALeeaLKEY------PGTVILVSHDRYFL 130
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
573-801 |
4.90e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 92.95 E-value: 4.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 573 RIATF---LEAPELQGGERRRKQRSEGNqnAIIIKSASFsweekgsTKPN----LRNVSLEVKFGEKVAVCGEVGSGKST 645
Cdd:COG4178 334 RLAGFeeaLEAADALPEAASRIETSEDG--ALALEDLTL-------RTPDgrplLEDLSLSLKPGERLLITGPSGSGKST 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 646 LLAAILGETPCVSGTIDF--YGTIAYVSQTAWIQTGTIRDNILF---GGVMDEHRYRETIQKSSLDKdleLLPDGDQTEI 720
Cdd:COG4178 405 LLRAIAGLWPYGSGRIARpaGARVLFLPQRPYLPLGTLREALLYpatAEAFSDAELREALEAVGLGH---LAERLDEEAD 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 721 GERGvnLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQeYVMDALAGKAVLLVTHQVDFLPAFDSVLLMSD 800
Cdd:COG4178 482 WDQV--LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQ-LLREELPGTTVISVGHRSTLAAFHDRVLELTG 558
|
.
gi 22331862 801 G 801
Cdd:COG4178 559 D 559
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1208-1420 |
5.21e-19 |
|
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: 86.93 E-value: 5.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1208 EISDLQIRYRReSPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKigvHDLRSRFGII 1287
Cdd:cd03226 1 RIENISFSYKK-GTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1288 PQDPT--LFNGTVRFNLDplcqhsdaeiwevLGKCQLKEVVQEKENGLDSLVVEDGSNW-----SMGQRQLFCLGRAVLR 1360
Cdd:cd03226 77 MQDVDyqLFTDSVREELL-------------LGLKELDAGNEQAETVLKDLDLYALKERhplslSGGQKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331862 1361 RSRVLVLDEATASIDNATDLILQKTIRREFADCTVITVA-HRIPTVMD-CTMVLSISDGRIV 1420
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVItHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1207-1421 |
8.50e-19 |
|
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: 86.50 E-value: 8.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRREspLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIgvHDLRSRFGI 1286
Cdd:cd03268 1 LKTNDLTKTYGKK--RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN--IEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDPTLF-NGTVRFNLDPLC---QHSDAEIWEVLGKCQLKEVVQEKEngldslvvedgSNWSMGQRQLFCLGRAVLRRS 1362
Cdd:cd03268 77 LIEAPGFYpNLTARENLRLLArllGIRKKRIDEVLDVVGLKDSAKKKV-----------KGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331862 1363 RVLVLDEATASIDNATDLILQKTIRREFAD-CTVITVAHRIPTVMD-CTMVLSISDGRIVE 1421
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKvADRIGIINKGKLIE 206
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
620-814 |
8.79e-19 |
|
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: 87.34 E-value: 8.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-IAYVSQTAWI----------QTG------TIR 682
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQdITGLSEKELYelrrrigmlfQGGalfdslTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 683 DNILFGgvMDEHRY--RETIQKSSLDKdLELLpdgdqteiGERGVN------LSGGQKQRIQLARALYQDADIYLLDDPF 754
Cdd:COG1127 101 ENVAFP--LREHTDlsEAEIRELVLEK-LELV--------GLPGAAdkmpseLSGGMRKRVALARALALDPEILLYDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22331862 755 SAVDAHTASS---LFQEYVmDALaGKAVLLVTHQVDflPAF---DSVLLMSDGEITEADTYQELLA 814
Cdd:COG1127 170 AGLDPITSAVideLIRELR-DEL-GLTSVVVTHDLD--SAFaiaDRVAVLADGKIIAEGTPEELLA 231
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
617-796 |
1.01e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 86.38 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 617 KPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETP---CVSGTIDFYGT-----------IAYVSQTA-----Wiq 677
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRrltalpaeqrrIGILFQDDllfphL-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 678 tgTIRDNILFG---GVMDEHRyRETIQkSSLDkDLELlpdgdqTEIGERGVN-LSGGQKQRIQLARALYQDADIYLLDDP 753
Cdd:COG4136 92 --SVGENLAFAlppTIGRAQR-RARVE-QALE-EAGL------AGFADRDPAtLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 22331862 754 FSAVDAHTASSlFQEYVMDAL--AGKAVLLVTHQVDFLPAFDSVL 796
Cdd:COG4136 161 FSKLDAALRAQ-FREFVFEQIrqRGIPALLVTHDEEDAPAAGRVL 204
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1207-1435 |
1.23e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 88.18 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESPL---VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDIS--KIGVHDLR 1281
Cdd:PRK13637 3 IKIENLTHIYMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1282 SRFGIIPQDP--TLFNGTV---------RFNLdplcqhSDAEIwevlgkcqlKEVVQEKEN--GLDSLVVEDGSNW--SM 1346
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIekdiafgpiNLGL------SEEEI---------ENRVKRAMNivGLDYEDYKDKSPFelSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1347 GQRQLFCLGRAVLRRSRVLVLDEATASID-NATDLILQ--KTIRREFaDCTVITVAHRIPTVMD-CTMVLSISDGRIVEY 1422
Cdd:PRK13637 148 GQKRRVAIAGVVAMEPKILILDEPTAGLDpKGRDEILNkiKELHKEY-NMTIILVSHSMEDVAKlADRIIVMNKGKCELQ 226
|
250
....*....|...
gi 22331862 1423 DEPMKLMKDENSL 1435
Cdd:PRK13637 227 GTPREVFKEVETL 239
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
622-832 |
1.74e-18 |
|
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: 89.00 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 622 NVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-----------------IAYVSQTAwiq-tgTIRD 683
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsargiflpphrrrIGYVFQEArlfphlSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 684 NILFGgvmdEHRYRETIQKSSLDKDLELLpdgdqtEIG---ERGV-NLSGGQKQRIQLARALYQDADIYLLDDPFSAVDA 759
Cdd:COG4148 97 NLLYG----RKRAPRAERRISFDEVVELL------GIGhllDRRPaTLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 760 HTASSLFqEYvMDALAGKA---VLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQELLARSrDFQDLvnAHRETAGS 832
Cdd:COG4148 167 ARKAEIL-PY-LERLRDELdipILYVSHSLDEVARLaDHVVLLEQGRVVASGPLAEVLSRP-DLLPL--AGGEEAGS 238
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1207-1428 |
2.24e-18 |
|
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: 85.63 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKiGVHDLRSRFGI 1286
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDPTLFNG-TVRFNLDPLCQ-------HSDAEIWEVLGKCQLKEVvqekengLDSLVvedgSNWSMGQRQLFCLGRAV 1358
Cdd:cd03263 80 CPQFDALFDElTVREHLRFYARlkglpksEIKEEVELLLRVLGLTDK-------ANKRA----RTLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 1359 LRRSRVLVLDEATASIDNATDLILQKTIRREFADCTVITVAHRiptvMD-----CTMVLSISDGRIVEYDEPMKL 1428
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHS----MDeaealCDRIAIMSDGKLRCIGSPQEL 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1207-1422 |
2.50e-18 |
|
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: 87.80 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESPLV--LKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEP---VGGKIVVDGVDISKIGVHDLR 1281
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1282 ----SRFGIIPQDP-TLFNG--TVRFNL-DPLCQH---SDAEIW----EVLGKCQLkevvQEKENGLDS----Lvvedgs 1342
Cdd:COG0444 82 kirgREIQMIFQDPmTSLNPvmTVGDQIaEPLRIHgglSKAEAReraiELLERVGL----PDPERRLDRypheL------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1343 nwSMGQRQLFCLGRAVLRRSRVLVLDEATASIDnAT------DLIlqKTIRREFaDCTVITVAHriptvmDCTMVLSISD 1416
Cdd:COG0444 152 --SGGMRQRVMIARALALEPKLLIADEPTTALD-VTiqaqilNLL--KDLQREL-GLAILFITH------DLGVVAEIAD 219
|
250
....*....|...
gi 22331862 1417 -------GRIVEY 1422
Cdd:COG0444 220 rvavmyaGRIVEE 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
616-795 |
3.77e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.74 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 616 TKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG--TIAYVSQ-TAWIQTGTIRDNIL--FGGV 690
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQePPLDDDLTVLDTVLdgDAEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 691 MD-EHRYRETIQK-SSLDKDLELLPDgDQTEIGERGV--------------------------NLSGGQKQRIQLARALY 742
Cdd:COG0488 90 RAlEAELEELEAKlAEPDEDLERLAE-LQEEFEALGGweaearaeeilsglgfpeedldrpvsELSGGWRRRVALARALL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 743 QDADIYLLDDPFSAVDAHTASSLfQEYvmdaLAG--KAVLLVTHQVDFLpafDSV 795
Cdd:COG0488 169 SEPDLLLLDEPTNHLDLESIEWL-EEF----LKNypGTVLVVSHDRYFL---DRV 215
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
620-814 |
4.16e-18 |
|
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: 85.03 E-value: 4.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT--------------IAYVSQTAWIQTG-TIRDN 684
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarlgIGYVPEGRRIFPSlTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 685 ILFGGVMdeHRYRETIQKSsLDKDLELLPdgdqtEIGER----GVNLSGGQKQRIQLARALYQDADIYLLDDPFsavdAH 760
Cdd:COG0410 99 LLLGAYA--RRDRAEVRAD-LERVYELFP-----RLKERrrqrAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS----LG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 761 TASSLFQEyVMDALA-----GKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQELLA 814
Cdd:COG0410 167 LAPLIVEE-IFEIIRrlnreGVTILLVEQNARFALEIaDRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
613-812 |
4.54e-18 |
|
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: 84.48 E-value: 4.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 613 KGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT------------IAYVSQtawiqtgt 680
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsirtdrkaarqsLGYCPQ-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 681 irDNILFGG--VMdEHRY--------RETIQKSSLDKDLELLPDGDQ--TEIGergvNLSGGQKQRIQLARALYQDADIY 748
Cdd:cd03263 83 --FDALFDEltVR-EHLRfyarlkglPKSEIKEEVELLLRVLGLTDKanKRAR----TLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 749 LLDDPFSAVDAHTASSLFqEYVMDALAGKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQEL 812
Cdd:cd03263 156 LLDEPTSGLDPASRRAIW-DLILEVRKGRSIILTTHSMDEAEALcDRIAIMSDGKLRCIGSPQEL 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1207-1424 |
4.93e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 84.72 E-value: 4.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESPlVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKI---GVHDLRSR 1283
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1284 FGIIPQD-PTLFNGTVRFNLD-PL--CQHSDAEIW----EVLGKCQLKevvqEKENGL-DSLvvedgsnwSMGQRQLFCL 1354
Cdd:COG2884 81 IGVVFQDfRLLPDRTVYENVAlPLrvTGKSRKEIRrrvrEVLDLVGLS----DKAKALpHEL--------SGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22331862 1355 GRAVLRRSRVLVLDEATASIDNAT-DLILQ--KTIRRefADCTVITVAHRIPTVMDCTM-VLSISDGRIVEYDE 1424
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPETsWEIMEllEEINR--RGTTVLIATHDLELVDRMPKrVLELEDGRLVRDEA 220
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
624-803 |
6.18e-18 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 84.14 E-value: 6.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 624 SLEVKFGEKVAVCGEVGSGKSTLLAAILG-ETPcVSGTI-----DFYGTIAY---VS----QTAWIQTGTIRDNILFG-- 688
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGfIEP-ASGSIkvndqSHTGLAPYqrpVSmlfqENNLFAHLTVRQNIGLGlh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 689 -----GVMDEHRYRETIQKSSLDKDLELLPDgdqteigergvNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDahtaS 763
Cdd:TIGR01277 97 pglklNAEQQEKVVDAAQQVGIADYLDRLPE-----------QLSGGQRQRVALARCLVRPNPILLLDEPFSALD----P 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 22331862 764 SLFQEyvMDALAGK-------AVLLVTHQV-DFLPAFDSVLLMSDGEI 803
Cdd:TIGR01277 162 LLREE--MLALVKQlcserqrTLLMVTHHLsDARAIASQIAVVSQGKI 207
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
620-817 |
7.03e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 84.75 E-value: 7.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGTIAyvsqtaW---IQTG-----TIRDNILFGGVM 691
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVS------AlleLGAGfhpelTGRENIYLNGRL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 692 DEHRYRETIQKssLDKDLELlpdgdqTEIGE------RgvNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHtassl 765
Cdd:COG1134 116 LGLSRKEIDEK--FDEIVEF------AELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAA----- 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 766 FQEYVMDALA-----GKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADT-------YQELLARSR 817
Cdd:COG1134 181 FQKKCLARIRelresGRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDpeeviaaYEALLAGRE 245
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
617-830 |
7.20e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 85.21 E-value: 7.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 617 KPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGtiAYVSQTAWIQTGTIRdnilfgGVMDEH-- 694
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNG--RPLADWSPAELARRR------AVLPQHss 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 695 -----RYRETIQ-----KSSLDKDLELLPDG--DQTEIGE-RGVN---LSGGQKQRIQLARALYQDAD------IYLLDD 752
Cdd:PRK13548 87 lsfpfTVEEVVAmgrapHGLSRAEDDALVAAalAQVDLAHlAGRDypqLSGGEQQRVQLARVLAQLWEpdgpprWLLLDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 753 PFSAVD-AHtasslfQEYVMDAL------AGKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQE-----LLARSRDF 819
Cdd:PRK13548 167 PTSALDlAH------QHHVLRLArqlaheRGLAVIVVLHDLNLAARYaDRIVLLHQGRLVADGTPAEvltpeTLRRVYGA 240
|
250
....*....|.
gi 22331862 820 QDLVNAHRETA 830
Cdd:PRK13548 241 DVLVQPHPETG 251
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
598-803 |
7.62e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 85.32 E-value: 7.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 598 QNAIIIKSASFSWEeKGSTKpnLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT----------I 667
Cdd:PRK15056 4 QAGIVVNDVTVTWR-NGHTA--LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 668 AYVSQTA---WIQTGTIRDNILFG--GVMDEHRYRETIQKSSLDKDLEL--LPDGDQTEIGErgvnLSGGQKQRIQLARA 740
Cdd:PRK15056 81 AYVPQSEevdWSFPVLVEDVVMMGryGHMGWLRRAKKRDRQIVTAALARvdMVEFRHRQIGE----LSGGQKKRVFLARA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22331862 741 LYQDADIYLLDDPFSAVDAHTAS---SLFQEYVMDalaGKAVLLVTHQVDFLPAFDSVLLMSDGEI 803
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEAriiSLLRELRDE---GKTMLVSTHNLGSVTEFCDYTVMVKGTV 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
601-815 |
1.02e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.20 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 601 IIIKSASFSWEEKgstkPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFyGT---IAYVSQtawiq 677
Cdd:COG0488 316 LELEGLSKSYGDK----TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GEtvkIGYFDQ----- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 678 tgtirdnilfggvmdeHRyretiqkSSLDKDL-------ELLPDGDQTEI----------GER-----GVnLSGGQKQRI 735
Cdd:COG0488 386 ----------------HQ-------EELDPDKtvldelrDGAPGGTEQEVrgylgrflfsGDDafkpvGV-LSGGEKARL 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 736 QLARALYQDADIYLLDDPFSAVDAHTASSLfqeyvMDALA---GkAVLLVTHQVDFLPAF-DSVLLMSDGEITEAD-TYQ 810
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEAL-----EEALDdfpG-TVLLVSHDRYFLDRVaTRILEFEDGGVREYPgGYD 515
|
....*
gi 22331862 811 ELLAR 815
Cdd:COG0488 516 DYLEK 520
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1207-1375 |
2.86e-17 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 82.19 E-value: 2.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESplVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDI--SKIGVHDLRSRF 1284
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1285 GIIPQDPTLF-NGTVRFNLdplcqhSDAEIWeVLGKCQlKEVVQEKENGLDSLVVEDGSNW-----SMGQRQLFCLGRAV 1358
Cdd:cd03262 79 GMVFQQFNLFpHLTVLENI------TLAPIK-VKGMSK-AEAEERALELLEKVGLADKADAypaqlSGGQQQRVAIARAL 150
|
170
....*....|....*..
gi 22331862 1359 LRRSRVLVLDEATASID 1375
Cdd:cd03262 151 AMNPKVMLFDEPTSALD 167
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
602-822 |
2.91e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 83.91 E-value: 2.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 602 IIKSASFSWEEKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGtIAYVSQTAW---IQT 678
Cdd:PRK13635 5 IIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG-MVLSEETVWdvrRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 679 G-------------TIRDNILFG----GV----MDEhRYRETIQKSSLDKDLELLPDgdqteigergvNLSGGQKQRIQL 737
Cdd:PRK13635 84 GmvfqnpdnqfvgaTVQDDVAFGleniGVpreeMVE-RVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 738 ARALYQDADIYLLDDPFSAVDAHTasslfQEYVMDAL------AGKAVLLVTHQVDFLPAFDSVLLMSDGEITEADTYQE 811
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRG-----RREVLETVrqlkeqKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEE 226
|
250
....*....|.
gi 22331862 812 LLARSRDFQDL 822
Cdd:PRK13635 227 IFKSGHMLQEI 237
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
617-800 |
2.94e-17 |
|
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: 80.66 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 617 KPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFY--GTIAYVSQTAWIQTGTIRDNILFggvmdeh 694
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPegEDLLFLPQRPYLPLGTLREQLIY------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 695 ryretiqkssldkdlellPDGDqteigergvNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQeyvMDAL 774
Cdd:cd03223 87 ------------------PWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQ---LLKE 136
|
170 180
....*....|....*....|....*.
gi 22331862 775 AGKAVLLVTHQVDFLPAFDSVLLMSD 800
Cdd:cd03223 137 LGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
599-822 |
2.98e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 83.63 E-value: 2.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 599 NAIIIKSASFSWEEKgSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTI-------------DFYG 665
Cdd:PRK13650 3 NIIEVKNLTFKYKED-QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdllteenvwDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 666 TIAYVSQTAWIQ--TGTIRDNILFGGVMDEHRYREtiQKSSLDKDLELLpdgDQTEIGERG-VNLSGGQKQRIQLARALY 742
Cdd:PRK13650 82 KIGMVFQNPDNQfvGATVEDDVAFGLENKGIPHEE--MKERVNEALELV---GMQDFKEREpARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 743 QDADIYLLDDPFSAVDA-------HTASSLFQEYVMdalagkAVLLVTHQVDFLPAFDSVLLMSDGEITEADTYQELLAR 815
Cdd:PRK13650 157 MRPKIIILDEATSMLDPegrleliKTIKGIRDDYQM------TVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
....*..
gi 22331862 816 SRDFQDL 822
Cdd:PRK13650 231 GNDLLQL 237
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1188-1421 |
4.07e-17 |
|
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: 86.66 E-value: 4.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1188 APEVIEETRPPVnwpvtgrVEISDLQIRY-------RRESPLV--LKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLV 1258
Cdd:COG4172 264 DPRPVPPDAPPL-------LEARDLKVWFpikrglfRRTVGHVkaVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1259 ePVGGKIVVDGVDISKIGVHD---LRSRFGIIPQDPtlfNGTvrfnLDPlcQHSDAEIWE--------VLGKCQLKEVVQ 1327
Cdd:COG4172 337 -PSEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDP---FGS----LSP--RMTVGQIIAeglrvhgpGLSAAERRARVA 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1328 E--KENGLDslvvEDGSN-----WSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNAT-----DLI--LQKtiRREFA-- 1391
Cdd:COG4172 407 EalEEVGLD----PAARHrypheFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVqaqilDLLrdLQR--EHGLAyl 480
|
250 260 270
....*....|....*....|....*....|....*
gi 22331862 1392 ----DCTVI-TVAHRIptvmdctMVLsiSDGRIVE 1421
Cdd:COG4172 481 fishDLAVVrALAHRV-------MVM--KDGKVVE 506
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
620-840 |
4.90e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 86.23 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT--------------IAYVSQ-TAWIQTGTIRDN 684
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvrfrsprdaqaagIAIIHQeLNLVPNLSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 685 ILFG------GVMDehrYRETIQKSS--LDK-DLELLPDgdqTEIGErgvnLSGGQKQRIQLARALYQDADIYLLDDPFS 755
Cdd:COG1129 100 IFLGreprrgGLID---WRAMRRRARelLARlGLDIDPD---TPVGD----LSVAQQQLVEIARALSRDARVLILDEPTA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 756 AVDAHTASSLFQeyVMDALA--GKAVLLVTHQVDFLPAF-DSVLLMSDGEITE----ADTYQELLARS---RDFQDLVNA 825
Cdd:COG1129 170 SLTEREVERLFR--IIRRLKaqGVAIIYISHRLDEVFEIaDRVTVLRDGRLVGtgpvAELTEDELVRLmvgRELEDLFPK 247
|
250
....*....|....*
gi 22331862 826 HRETAGsERVVAVEN 840
Cdd:COG1129 248 RAAAPG-EVVLEVEG 261
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
285-554 |
5.00e-17 |
|
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: 83.08 E-value: 5.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 285 LLTSGFFAFMKIVAVSAGPLLLNAFILVAEGNASFRYEGLV---LAVLLFFSKMIESLSQRQWYFRcrIVGLRVRSLLTA 361
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNvysLALLLLGLAQFILSFLQSYLLN--HTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 362 AINKKQLRLNNSSRLIHSGSEIMNYATVDAYRIGEFPYWFHQLWTTSFQLLIALGILFHSVGVA-TFSALAVIILTVLCN 440
Cdd:pfam00664 79 KLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 441 APIAKLQNKFQSELMTSQDERLKACNESLVNMKVLKLYAWESHFKKVIEKLRNIELKSLKAVQMRKAYNAVLFWSSPVFV 520
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLS 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 22331862 521 SAATFATCYFLDIP--LRASNVFTFVATLRLVQDPV 554
Cdd:pfam00664 239 YALALWFGAYLVISgeLSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1207-1422 |
5.92e-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: 81.17 E-value: 5.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESplVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDG--VDISKigvhdlRSRF 1284
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpLDIAA------RNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1285 GIIPQDPTLF-NGTVRFNLDPLCQ-----HSDA--EIWEVLGKCQLKEVVQEKengLDSLvvedgsnwSMGQRQLFCLGR 1356
Cdd:cd03269 73 GYLPEERGLYpKMKVIDQLVYLAQlkglkKEEArrRIDEWLERLELSEYANKR---VEEL--------SKGNQQKVQFIA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1357 AVLRRSRVLVLDEATASIDNA-TDLIlqKTIRREFAD--CTVITVAHRIPTVMD-CTMVLSISDGRIVEY 1422
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVnVELL--KDVIRELARagKTVILSTHQMELVEElCDRVLLLNKGRAVLY 209
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1237-1423 |
8.60e-17 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 80.80 E-value: 8.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1237 IGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGV--DISKIGVH--DLRSRFGIIPQDPTLF-NGTVRFNLD-PLCQHSD 1310
Cdd:cd03297 26 TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlFDSRKKINlpPQQRKIGLVFQQYALFpHLNVRENLAfGLKRKRN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1311 AEIwevlgKCQLKEVVQEKenGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIRREF 1390
Cdd:cd03297 106 RED-----RISVDELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIK 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 22331862 1391 AD--CTVITVAHRIPTV-MDCTMVLSISDGRIVEYD 1423
Cdd:cd03297 179 KNlnIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1223-1420 |
8.69e-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: 81.33 E-value: 8.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1223 VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDlRSRFGIIP--QDPTLFNG-TVR 1299
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE-IARLGIGRtfQIPRLFPElTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1300 FNLDPLCQHSDAEIWEVLGKCQLKEVVQEKEN------GLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATA- 1372
Cdd:cd03219 94 ENVMVAAQARTGSGLLLARARREEREARERAEellervGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAg 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 22331862 1373 ----SIDNATDLILQktIRREfaDCTVITVAHRiptvMDctMVLSISDgRIV 1420
Cdd:cd03219 174 lnpeETEELAELIRE--LRER--GITVLLVEHD----MD--VVMSLAD-RVT 214
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1207-1429 |
1.23e-16 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 81.19 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESPLVlKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGI 1286
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDPTLF-NGTVRFN--LDPLCQHsdaeiWEvlgkcqlKEVVQEKENGLDSLVVEDGSNW--------SMGQRQLFCLG 1355
Cdd:cd03295 80 VIQQIGLFpHMTVEENiaLVPKLLK-----WP-------KEKIRERADELLALVGLDPAEFadryphelSGGQQQRVGVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1356 RAVLRRSRVLVLDEATASIDNATDLILQ---KTIRREFADcTVITVAH----------RIpTVMDctmvlsisDGRIVEY 1422
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQeefKRLQQELGK-TIVFVTHdideafrladRI-AIMK--------NGEIVQV 217
|
....*..
gi 22331862 1423 DEPMKLM 1429
Cdd:cd03295 218 GTPDEIL 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
620-807 |
1.53e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 80.10 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT----------------IAYVSQTAW-IQTGTIR 682
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsrlkrreipylrrrIGVVFQDFRlLPDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 683 DNILF-----GgvMDEHRYRETIQkssldkdlELLpdgDQTEIGERG----VNLSGGQKQRIQLARALYQDADIYLLDDP 753
Cdd:COG2884 98 ENVALplrvtG--KSRKEIRRRVR--------EVL---DLVGLSDKAkalpHELSGGEQQRVAIARALVNRPELLLADEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 754 FSAVDAHTASSlfqeyVMDAL-----AGKAVLLVTHQVDFLPAFDS-VLLMSDGEITEAD 807
Cdd:COG2884 165 TGNLDPETSWE-----IMELLeeinrRGTTVLIATHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
610-803 |
1.59e-16 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 79.52 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 610 WEEKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILG--ETPCVSGTI----------DFYGTIAYVSQtawiq 677
Cdd:cd03213 15 SSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVlingrpldkrSFRKIIGYVPQ----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 678 tgtirDNILFGgvmdEHRYRETIQKSSldkdlELlpdgdqteigeRGvnLSGGQKQRIQLARALYQDADIYLLDDPFSAV 757
Cdd:cd03213 90 -----DDILHP----TLTVRETLMFAA-----KL-----------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22331862 758 DAHTASSLFQeyVMDALA--GKAVLLVTHQV--DFLPAFDSVLLMSDGEI 803
Cdd:cd03213 143 DSSSALQVMS--LLRRLAdtGRTIICSIHQPssEIFELFDKLLLLSQGRV 190
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1207-1420 |
1.84e-16 |
|
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: 80.10 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESPLV--LKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKiGVHDLRSRF 1284
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1285 GIIPQDPTLFNG-TVRFNLDPLC-------QHSDAEIWEVLGKCQLKEVVQEKENGLdslvvedgsnwSMGQRQLFCLGR 1356
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYFAglyglkgDELTARLEELADRLGMEELLDRRVGGF-----------STGMRQKVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22331862 1357 AVLRRSRVLVLDEATASIDNATDLILQKTIRR-EFADCTVITVAHRIPTVMD-CTMVLSISDGRIV 1420
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQlRALGKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
624-803 |
2.34e-16 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 79.46 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 624 SLEVKFGEKVAVCGEVGSGKSTLLAAILG-ETPcVSGTIDFYG---TIAYVSQ---TAWIQTG------TIRDNILFGGV 690
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGfETP-QSGRVLINGvdvTAAPPADrpvSMLFQENnlfahlTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 691 -------MDEHRYRETIQKSSLDKDLELLPDgdqteigergvNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTAS 763
Cdd:cd03298 97 pglkltaEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 22331862 764 SLfQEYVMDALA--GKAVLLVTHQV-DFLPAFDSVLLMSDGEI 803
Cdd:cd03298 166 EM-LDLVLDLHAetKMTVLMVTHQPeDAKRLAQRVVFLDNGRI 207
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
620-830 |
2.54e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 80.54 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG-------------TIAYVSQtawiQTG-----TI 681
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaawspwelarRRAVLPQ----HSSlafpfTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 682 RDNILFG--GVMDEHRYRETIQKSSLDK-DLELLPDGDQTEigergvnLSGGQKQRIQLARALYQ-------DADIYLLD 751
Cdd:COG4559 93 EEVVALGraPHGSSAAQDRQIVREALALvGLAHLAGRSYQT-------LSGGEQQRVQLARVLAQlwepvdgGPRWLFLD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 752 DPFSAVD-AHtasslfQEYVMDAL-----AGKAVLLVTHqvDF-LPAF--DSVLLMSDGEITEADTYQE-----LLARSR 817
Cdd:COG4559 166 EPTSALDlAH------QHAVLRLArqlarRGGGVVAVLH--DLnLAAQyaDRILLLHQGRLVAQGTPEEvltdeLLERVY 237
|
250
....*....|...
gi 22331862 818 DFQDLVNAHRETA 830
Cdd:COG4559 238 GADLRVLAHPEGG 250
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
620-814 |
3.65e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 80.12 E-value: 3.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILG-ETPcVSGTIDFYGTIayVSQTAWIQTGTIRDNI------LFGGVMD 692
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGlESP-SQGNVSWRGEP--LAKLNRAQRKAFRRDIqmvfqdSISAVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 693 EHRYRETIQK-----SSLDKD------LELLP--DGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDA 759
Cdd:PRK10419 105 RKTVREIIREplrhlLSLDKAerlaraSEMLRavDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331862 760 HtasslFQEYVMDALA------GKAVLLVTHQVDFLPAFDS-VLLMSDGEITEADTYQELLA 814
Cdd:PRK10419 185 V-----LQAGVIRLLKklqqqfGTACLFITHDLRLVERFCQrVMVMDNGQIVETQPVGDKLT 241
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1207-1436 |
4.32e-16 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 79.30 E-value: 4.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRespLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISkiGVHDLRSRFGI 1286
Cdd:cd03299 1 LKVENLSKDWKE---FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDPTLF-NGTVRFNLDPLCQHSDAEiwevlgKCQLKEVVQE--KENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSR 1363
Cdd:cd03299 76 VPQNYALFpHMTVYKNIAYGLKKRKVD------KKEIERKVLEiaEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1364 VLVLDEATASIDNATDLILQ---KTIRREFaDCTVITVAHriptvmDCTMVLSISD-------GRIVEYDEPMKLMKDEN 1433
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLReelKKIRKEF-GVTVLHVTH------DFEEAWALADkvaimlnGKLIQVGKPEEVFKKPK 222
|
...
gi 22331862 1434 SLF 1436
Cdd:cd03299 223 NEF 225
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1223-1420 |
4.37e-16 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 77.08 E-value: 4.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1223 VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRsRFGIipqdptlfnGTVrfnl 1302
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDAR-RAGI---------AMV---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1303 dplcqHsdaeiwevlgkcQLkevvqekengldslvvedgsnwSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLIL 1382
Cdd:cd03216 81 -----Y------------QL----------------------SVGERQMVEIARALARNARLLILDEPTAALTPAEVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 22331862 1383 QKTIRREFAD-CTVITVAHRIPTVMD-CTMVLSISDGRIV 1420
Cdd:cd03216 122 FKVIRRLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
597-813 |
4.95e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 80.03 E-value: 4.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 597 NQNAIIIKSASFSWEEkgSTKPNLRNVSLEVKFGEKVAVCGEVGSGKST---LLAAILGETpcvSGTIDFYGTIAYVSQT 673
Cdd:PRK13632 4 KSVMIKVENVSFSYPN--SENNALKNVSFEINEGEYVAILGHNGSGKSTiskILTGLLKPQ---SGEIKIDGITISKENL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 674 AWIQT---------------GTIRDNILFG--------GVMDEHRYrETIQKSSLDKDLELLPDgdqteigergvNLSGG 730
Cdd:PRK13632 79 KEIRKkigiifqnpdnqfigATVEDDIAFGlenkkvppKKMKDIID-DLAKKVGMEDYLDKEPQ-----------NLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 731 QKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQeyVMDAL---AGKAVLLVTHQVDFLPAFDSVLLMSDGEITEAD 807
Cdd:PRK13632 147 QKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKK--IMVDLrktRKKTLISITHDMDEAILADKVIVFSEGKLIAQG 224
|
....*.
gi 22331862 808 TYQELL 813
Cdd:PRK13632 225 KPKEIL 230
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1207-1430 |
5.01e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 80.06 E-value: 5.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGI 1286
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDP-TLFNGT-----VRFNLdplcqhsdaeiwEVLG--KCQLKEVVQE--KENGLDSLVVEDGSNWSMGQRQLFCLGR 1356
Cdd:PRK13635 86 VFQNPdNQFVGAtvqddVAFGL------------ENIGvpREEMVERVDQalRQVGMEDFLNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22331862 1357 AVLRRSRVLVLDEATASIDNATDLILQKTIRR--EFADCTVITVAHRIPTVMDCTMVLSISDGRIVEYDEPMKLMK 1430
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
949-1369 |
5.02e-16 |
|
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: 83.31 E-value: 5.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 949 CVVIMCmkssASLFSQLLNS------LFRAPMSFYD---STPL--------GRILSRVSSDLSIVdLDVPFGLIFVVASS 1011
Cdd:COG4615 58 LVLLLL----SRLASQLLLTrlgqhaVARLRLRLSRrilAAPLerlerigaARLLAALTEDVRTI-SQAFVRLPELLQSV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1012 VNTGCSLGVLAIVTWQVLFVSVPMVYLAF----------------------RLQKYY---FQTAKELmRINGTTR-SYVA 1065
Cdd:COG4615 133 ALVLGCLAYLAWLSPPLFLLTLVLLGLGVagyrllvrrarrhlrrareaedRLFKHFralLEGFKEL-KLNRRRRrAFFD 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1066 NHLAESVAGA--ITIRAFdeeeRFFKKSLTLIDTnaspFFHS------FAANEWLIQRLETVSAIVLAstafcmILlptg 1137
Cdd:COG4615 212 EDLQPTAERYrdLRIRAD----TIFALANNWGNL----LFFAliglilFLLPALGWADPAVLSGFVLV------LL---- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1138 tFSSGFIGMALSYGLSLNMglvysvqnqcylANwiISVERLNQYTHLTPEAPEVIEETRPPVNWPVTGRVEISDLQIRYR 1217
Cdd:COG4615 274 -FLRGPLSQLVGALPTLSR------------AN--VALRKIEELELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1218 RE---SPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQDPTLF 1294
Cdd:COG4615 339 GEdgdEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 1295 NGtvrfNLDPLCQHSDAEIWEVLGKCQLKEVVQEKENGLDSLvvedgsNWSMGQRQLFCLGRAVLRRSRVLVLDE 1369
Cdd:COG4615 419 DR----LLGLDGEADPARARELLERLELDHKVSVEDGRFSTT------DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
620-812 |
6.80e-16 |
|
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: 78.43 E-value: 6.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILG-ETPcVSGTIDFYGT-----------IAYVSQT-AWIQTGTIRDNIL 686
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGfETP-TSGEILLDGKditnlpphkrpVNTVFQNyALFPHLTVFENIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 687 FGGVMdeHRYRETIQKSSLDKDLELLpdgDQTEIGERGVN-LSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSL 765
Cdd:cd03300 95 FGLRL--KKLPKAEIKERVAEALDLV---QLEGYANRKPSqLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 22331862 766 FQEyvMDAL---AGKAVLLVTH-QVDFLPAFDSVLLMSDGEITEADTYQEL 812
Cdd:cd03300 170 QLE--LKRLqkeLGITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
880-1178 |
9.05e-16 |
|
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: 80.23 E-value: 9.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 880 YIQYMNQNKGYIFFFI-----------ASLAQVTFAVGQILQNSWMAANV--DNPQV---STLKLILVYLLIGLCSVLCL 943
Cdd:cd18600 6 YLRYITSHKSLIFVLIlclvifaievaASLVGLWLLRSQADRVNTTRPESssNTYAVivtFTSSYYVFYIYVGVADSLLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 944 M--VRSVCVVIMCMKSSASLFSQLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLI-FVVASSVNTGCSLGV 1020
Cdd:cd18600 86 MgfFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFdFIQLFLIVIGAITVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1021 LAIVTWqVLFVSVPMVYLAFRLQKYYFQTAKELMRINGTTRSYVANHLAESVAGAITIRAFDEEERF---FKKSLtliDT 1097
Cdd:cd18600 166 SILQPY-IFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFetlFHKAL---NL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1098 NASPFFHSFAANEWLIQRLETVSAIVLASTAFCMILlpTGTFSSGFIGMALSYGLSLNMGLVYSVQNQCYLANWIISVER 1177
Cdd:cd18600 242 HTANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIG--TTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSR 319
|
.
gi 22331862 1178 L 1178
Cdd:cd18600 320 I 320
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
616-814 |
1.49e-15 |
|
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: 77.58 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 616 TKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT--------------IAYVSQTAWIQTG-T 680
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarlgIGYLPQEASIFRKlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 681 IRDNILfgGVMDEHRYRETIQKSSLDkdlELLPDGDQTEIGER-GVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDA 759
Cdd:cd03218 92 VEENIL--AVLEIRGLSKKEREEKLE---ELLEEFHITHLRKSkASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 760 HTASSLfQEYVMD-ALAGKAVLLVTHQV-DFLPAFDSVLLMSDGEITEADTYQELLA 814
Cdd:cd03218 167 IAVQDI-QKIIKIlKDRGIGVLITDHNVrETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1207-1421 |
1.91e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 79.46 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESPLV--LKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRS-- 1282
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1283 -RFGIIPQDptlFN--------GTVRFnldPLcqhsdaeiwEVLGKCqlKEVVQEKENGLDSLV-VEDG-----SNWSMG 1347
Cdd:PRK11153 82 rQIGMIFQH---FNllssrtvfDNVAL---PL---------ELAGTP--KAEIKARVTELLELVgLSDKadrypAQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1348 QRQLFCLGRAVLRRSRVLVLDEATASIDNA-TDLILQ--KTIRREFaDCTVITVAHRiptvMD-----CTMVLSISDGRI 1419
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPAtTRSILEllKDINREL-GLTIVLITHE----MDvvkriCDRVAVIDAGRL 219
|
..
gi 22331862 1420 VE 1421
Cdd:PRK11153 220 VE 221
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
620-803 |
1.99e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 77.80 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILG-ETPCvSGTIdFYGTiAYVSQtawiqtgtIRDNI--LFggvmDEHR- 695
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGlETPS-AGEL-LAGT-APLAE--------AREDTrlMF----QDARl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 696 --YRETIQKSSL-------DKDLELLPD-GDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHT---- 761
Cdd:PRK11247 93 lpWKKVIDNVGLglkgqwrDAALQALAAvGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTriem 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 22331862 762 ---ASSLFQEYvmdalaGKAVLLVTHQVDFLPAF-DSVLLMSDGEI 803
Cdd:PRK11247 173 qdlIESLWQQH------GFTVLLVTHDVSEAVAMaDRVLLIEEGKI 212
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1207-1419 |
2.00e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 80.27 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRyrRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGI 1286
Cdd:PRK09536 4 IDVSDLSVE--FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDPTL-FNGTVR-----------FNLDPLCQHSDAEIWEVLGKCqlkEVVQEKENGLDSLvvedgsnwSMGQRQLFCL 1354
Cdd:PRK09536 82 VPQDTSLsFEFDVRqvvemgrtphrSRFDTWTETDRAAVERAMERT---GVAQFADRPVTSL--------SGGERQRVLL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331862 1355 GRAVLRRSRVLVLDEATASIDnatdliLQKTIR-----REFADC--TVITVAHRIPTVMD-CTMVLSISDGRI 1419
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLD------INHQVRtlelvRRLVDDgkTAVAAIHDLDLAARyCDELVLLADGRV 217
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
601-822 |
2.22e-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: 77.86 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 601 IIIKSASFSWEEkgSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTL---LAAILgeTPcVSGTIDFYGTIAYVSQTAW-- 675
Cdd:TIGR04520 1 IEVENVSFSYPE--SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLaklLNGLL--LP-TSGKVTVDGLDTLDEENLWei 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 676 --------------IQTGTIRDNILFG----GV-----------------MDEHRYRETIqkssldkdlellpdgdqtei 720
Cdd:TIGR04520 76 rkkvgmvfqnpdnqFVGATVEDDVAFGlenlGVpreemrkrvdealklvgMEDFRDREPH-------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 721 gergvNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDA-------HTASSLFQEYvmdalaGKAVLLVTHQVDFLPAFD 793
Cdd:TIGR04520 136 -----LLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPkgrkevlETIRKLNKEE------GITVISITHDMEEAVLAD 204
|
250 260
....*....|....*....|....*....
gi 22331862 794 SVLLMSDGEITEADTYQELLARSRDFQDL 822
Cdd:TIGR04520 205 RVIVMNKGKIVAEGTPREIFSQVELLKEI 233
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
620-785 |
2.36e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.45 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG----------TIAYVS-QTAWIQTGTIRDNILF- 687
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpdvaeACHYLGhRNAMKPALTVAENLEFw 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 688 ----GGvmDEHRYRETIQKSSLDkDLELLPDGdqteigergvNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHtAS 763
Cdd:PRK13539 98 aaflGG--EELDIAAALEAVGLA-PLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AV 163
|
170 180
....*....|....*....|...
gi 22331862 764 SLFQEYVMDALA-GKAVLLVTHQ 785
Cdd:PRK13539 164 ALFAELIRAHLAqGGIVIAATHI 186
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
620-808 |
2.82e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.78 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILG-ETPcVSGTIDFYG-TIAYVSQTAwiqTGTIRDNIL-----FGGVMD 692
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGlDTP-TSGDVIFNGqPMSKLSSAA---KAELRNQKLgfiyqFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 693 EHRYRETI----------QKSSLDKDLELLPD-GDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHT 761
Cdd:PRK11629 101 DFTALENVamplligkkkPAEINSRALEMLAAvGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22331862 762 ASSLFQ---EyvMDALAGKAVLLVTHQVDFLPAFDSVLLMSDGEITEADT 808
Cdd:PRK11629 181 ADSIFQllgE--LNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1207-1421 |
3.19e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 78.58 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESPLV--LKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDL---R 1281
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1282 SRFGIIPQDPTLFNG-TVRFNLD-PLcqhsdaEIWEVlGKCQLKEVVQEkengLDSLVvedG---------SNWSMGQRQ 1350
Cdd:COG1135 82 RKIGMIFQHFNLLSSrTVAENVAlPL------EIAGV-PKAEIRKRVAE----LLELV---GlsdkadaypSQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1351 LFCLGRAVLRRSRVLVLDEATASID-NATDLILQ--KTIRREFaDCTV--IT----VAHRIptvmdCTMVLSISDGRIVE 1421
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDpETTRSILDllKDINREL-GLTIvlIThemdVVRRI-----CDRVAVLENGRIVE 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1207-1435 |
3.71e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 77.46 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESP-LVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFG 1285
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1286 IIPQDP-TLFNGT-----VRFNLDPlcqhsdaeiwEVLGKCQLKEVVQEKEN--GLDSLVVEDGSNWSMGQRQLFCLGRA 1357
Cdd:PRK13650 85 MVFQNPdNQFVGAtveddVAFGLEN----------KGIPHEEMKERVNEALElvGMQDFKEREPARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1358 VLRRSRVLVLDEATASIDNATDLILQKTIR--REFADCTVITVAHRIPTVMDCTMVLSISDGRIVEYDEPMKLMKDENSL 1435
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKgiRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGNDL 234
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
601-820 |
3.82e-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: 77.59 E-value: 3.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 601 IIIKSASFSWEEKGSTKpnLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILgETPCVSGTIDFYG-------------TI 667
Cdd:cd03289 3 MTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwrkAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 668 AYVSQTAWIQTGTIRDNI-LFGGVMDEHRYRETiQKSSLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDAD 746
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLdPYGKWSDEEIWKVA-EEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22331862 747 IYLLDDPFSAVDAHTaSSLFQEYVMDALAGKAVLLVTHQVDFLPAFDSVLLMSDGEITEADTYQELLARSRDFQ 820
Cdd:cd03289 159 ILLLDEPSAHLDPIT-YQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFK 231
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1208-1434 |
4.91e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 75.95 E-value: 4.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1208 EISDLQIRYRREsplvLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDlrsR-FGI 1286
Cdd:COG3840 3 RLDDLTYRYGDF----PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE---RpVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDPTLFNG-TVRFN----LDPLCQHSDAE---IWEVLGKCQLKEVVQEKENGLdslvvedgsnwSMGQRQLFCLGRAV 1358
Cdd:COG3840 76 LFQENNLFPHlTVAQNiglgLRPGLKLTAEQraqVEQALERVGLAGLLDRLPGQL-----------SGGQRQRVALARCL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1359 LRRSRVLVLDEATASIDNA-----TDLIlqKTIRREFaDCTVITVAHRIPTVMD-CTMVLSISDGRIVEYDEPMKLMKDE 1432
Cdd:COG3840 145 VRKRPILLLDEPFSALDPAlrqemLDLV--DELCRER-GLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
|
..
gi 22331862 1433 NS 1434
Cdd:COG3840 222 PP 223
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1207-1428 |
5.08e-15 |
|
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: 75.87 E-value: 5.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYrrESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKiGVHDLRSRFGI 1286
Cdd:cd03265 1 IEVENLVKKY--GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDPTLFNG-TVRFNLdplcqHSDAEIWEVLGKcQLKEVVQEKENGLDSLVVEDG--SNWSMGQRQLFCLGRAVLRRSR 1363
Cdd:cd03265 78 VFQDLSVDDElTGWENL-----YIHARLYGVPGA-ERRERIDELLDFVGLLEAADRlvKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331862 1364 VLVLDEATASIDNATDLILQKTIR---REFaDCTVITVAHriptVMD-----CTMVLSISDGRIVEYDEPMKL 1428
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEklkEEF-GMTILLTTH----YMEeaeqlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
468-825 |
5.18e-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: 81.11 E-value: 5.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 468 SLVNMKVLKLYAWESHFKKVIEKLRNIE-------LKSLKAVQMRKAYNAVLFWSSPVFVSAATFAtcyflDIPLRASNV 540
Cdd:TIGR01271 1070 SLKGLWTIRAFGRQSYFETLFHKALNLHtanwflyLSTLRWFQMRIDIIFVFFFIAVTFIAIGTNQ-----DGEGEVGII 1144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 541 FTFVAT-LRLVQDPVRMIPDVIGVTIQAKVAFSRIATFLEAPELQGG------------ERRRKQRSEGNQNAIIIKSAS 607
Cdd:TIGR01271 1145 LTLAMNiLSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRPSGGggkyqlstvlviENPHAQKCWPSGGQMDVQGLT 1224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 608 FSWEEKGSTKpnLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILgETPCVSGTIDFYG-------------TIAYVSQTA 674
Cdd:TIGR01271 1225 AKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGvswnsvtlqtwrkAFGVIPQKV 1301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 675 WIQTGTIRDNI-LFGGVMDEHRYRETiQKSSLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDP 753
Cdd:TIGR01271 1302 FIFSGTFRKNLdPYEQWSDEEIWKVA-EEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331862 754 FSAVDAHTAsSLFQEYVMDALAGKAVLLVTHQVDFLPAFDSVLLMSDGEITEADTYQELLARSRDFQDLVNA 825
Cdd:TIGR01271 1381 SAHLDPVTL-QIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMSA 1451
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
620-803 |
5.69e-15 |
|
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: 75.39 E-value: 5.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG---------TIAYVSQtawiQTGTIRDNilfgGV 690
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaarnRIGYLPE----ERGLYPKM----KV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 691 MDEHRY--------RETIQKSSLD--KDLELlpdgdqTEIGERGVN-LSGGQKQRIQLARALYQDADIYLLDDPFSAVDA 759
Cdd:cd03269 88 IDQLVYlaqlkglkKEEARRRIDEwlERLEL------SEYANKRVEeLSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 22331862 760 hTASSLFQEYVMD-ALAGKAVLLVTHQVDFLPAF-DSVLLMSDGEI 803
Cdd:cd03269 162 -VNVELLKDVIRElARAGKTVILSTHQMELVEELcDRVLLLNKGRA 206
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1207-1388 |
7.37e-15 |
|
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: 75.66 E-value: 7.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRREspLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDlRSRFGI 1286
Cdd:cd03218 1 LRAENLSKRYGKR--KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 I--PQDPTLFNG-TVRFNLDPLcqhsdAEIWEVLGKCQLKEVVQE-KENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRS 1362
Cdd:cd03218 78 GylPQEASIFRKlTVEENILAV-----LEIRGLSKKEREEKLEELlEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180
....*....|....*....|....*.
gi 22331862 1363 RVLVLDEATASIDNATDLILQKTIRR 1388
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKI 178
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
624-816 |
8.78e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 75.39 E-value: 8.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 624 SLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG---TIAYVSQ---TAWIQTG------TIRDNILFG--- 688
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhTTTPPSRrpvSMLFQENnlfshlTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 689 GVMDEHRYRETIQ----KSSLDKDLELLPdgdqteiGErgvnLSGGQKQRIQLARALYQDADIYLLDDPFSAVDahtaSS 764
Cdd:PRK10771 99 GLKLNAAQREKLHaiarQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVREQPILLLDEPFSALD----PA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 765 LFQEyvMDALAGK-------AVLLVTHQVDflpafDSV------LLMSDGEITEADTYQELLARS 816
Cdd:PRK10771 164 LRQE--MLTLVSQvcqerqlTLLMVSHSLE-----DAAriaprsLVVADGRIAWDGPTDELLSGK 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
620-821 |
9.60e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 75.56 E-value: 9.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAI-LGETPcVSGTI-----DFYGTIAYVSQTAWI-----QTG--------- 679
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInLLEQP-EAGTIrvgdiTIDTARSLSQQKGLIrqlrqHVGfvfqnfnlf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 680 ---TIRDNILFGGVMDEHRYREtiqkSSLDKDLELLP----DGDQTEIGERgvnLSGGQKQRIQLARALYQDADIYLLDD 752
Cdd:PRK11264 98 phrTVLENIIEGPVIVKGEPKE----EATARARELLAkvglAGKETSYPRR---LSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 753 PFSAVDAH-------TASSLFQEyvmdalaGKAVLLVTHQVDFL-PAFDSVLLMSDGEITEADTYQELLA-----RSRDF 819
Cdd:PRK11264 171 PTSALDPElvgevlnTIRQLAQE-------KRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKALFAdpqqpRTRQF 243
|
..
gi 22331862 820 QD 821
Cdd:PRK11264 244 LE 245
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
623-842 |
1.03e-14 |
|
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: 77.46 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 623 VSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-----------------IAYVSQTAWIQTG-TIRDN 684
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrkgiflppekrrIGYVFQEARLFPHlSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 685 ILFGgvmdEHRYRETIQKSSLDKDLELLPDGdqtEIGERGVN-LSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTAS 763
Cdd:TIGR02142 96 LRYG----MKRARPSERRISFERVIELLGIG---HLLGRLPGrLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 764 SL--FQEYVMDALaGKAVLLVTHQVD-FLPAFDSVLLMSDGEITEADTYQELLARSrdfqDLVNAHRETAGS--ERVVAV 838
Cdd:TIGR02142 169 EIlpYLERLHAEF-GIPILYVSHSLQeVLRLADRVVVLEDGRVAAAGPIAEVWASP----DLPWLAREDQGSliEGVVAE 243
|
....
gi 22331862 839 ENPT 842
Cdd:TIGR02142 244 HDQH 247
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
454-814 |
1.12e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 79.69 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 454 LMTSQDERLK----ACNESLVNMKVLKLYAWESHFKKVIEKLRNIELKSlkavQMRKAYNAVLFW----SSPVFVSAATF 525
Cdd:PTZ00265 1010 AYNSDDEIFKdpsfLIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKG----QKRKTLVNSMLWgfsqSAQLFINSFAY 1085
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 526 ATCYFL------DIPLRASNVFTFVATLRLVQDPVRMIPDvigvTIQAKVAFSRIATFLEAPEL-----QGGER-RRKQR 593
Cdd:PTZ00265 1086 WFGSFLirrgtiLVDDFMKSLFTFLFTGSYAGKLMSLKGD----SENAKLSFEKYYPLIIRKSNidvrdNGGIRiKNKND 1161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 594 SEGNqnaIIIKSASFSWeekgSTKPNL---RNVSLEVKFGEKVAVCGEVGSGKSTLLAAIL------------------- 651
Cdd:PTZ00265 1162 IKGK---IEIMDVNFRY----ISRPNVpiyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtn 1234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 652 --------------------------------GETPCV---SGTI-------------DFYGTIAYVSQTAWIQTGTIRD 683
Cdd:PTZ00265 1235 dmtneqdyqgdeeqnvgmknvnefsltkeggsGEDSTVfknSGKIlldgvdicdynlkDLRNLFSIVSQEPMLFNMSIYE 1314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 684 NILFGgvmDEHRYRETIQKSS----LDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDA 759
Cdd:PTZ00265 1315 NIKFG---KEDATREDVKRACkfaaIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDS 1391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331862 760 HTaSSLFQEYVMDA--LAGKAVLLVTHQVDFLPAFDSVLLMSD----GEITEAD-TYQELLA 814
Cdd:PTZ00265 1392 NS-EKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAHgTHEELLS 1452
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
616-821 |
1.13e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 74.75 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 616 TKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLL---AAILGETpcvSGTIDFYGT-------------IAYVSQTAWIQTG 679
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLkivASLISPT---SGTLLFEGEdistlkpeiyrqqVSYCAQTPTLFGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 680 TIRDNILFGGVMDehryRETIQKSSLDKDLEL--LPDgdqtEIGERGVN-LSGGQKQRIQLARALYQDADIYLLDDPFSA 756
Cdd:PRK10247 96 TVYDNLIFPWQIR----NQQPDPAIFLDDLERfaLPD----TILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 757 VDAHT---ASSLFQEYVMDalAGKAVLLVTHQVDflpafdsvllmsdgEITEADTYQELLARSRDFQD 821
Cdd:PRK10247 168 LDESNkhnVNEIIHRYVRE--QNIAVLWVTHDKD--------------EINHADKVITLQPHAGEMQE 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
620-803 |
1.23e-14 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 75.17 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT--------------IAYVSQTAWI-QTGTIRDN 684
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglppheiarlgIGRTFQIPRLfPELTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 685 ILFGGVMDEHRY-----RETIQKSSLDKDLELLpdgDQTEIGERG----VNLSGGQKQRIQLARALYQDADIYLLDDPF- 754
Cdd:cd03219 96 VMVAAQARTGSGlllarARREEREARERAEELL---ERVGLADLAdrpaGELSYGQQRRLEIARALATDPKLLLLDEPAa 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 22331862 755 --SAVDAHTASSLFQEYvmdALAGKAVLLVTHQVDFLPAF-DSVLLMSDGEI 803
Cdd:cd03219 173 glNPEETEELAELIREL---RERGITVLLVEHDMDVVMSLaDRVTVLDQGRV 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
620-819 |
1.50e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 74.74 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGT-----IDFYGTIAYVSQTAwIQTG------------TIR 682
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDlivdgLKVNDPKVDERLIR-QEAGmvfqqfylfphlTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 683 DNILFGGVmdehRYRETIQKSSLDKDLELLpdgDQTEIGERG----VNLSGGQKQRIQLARALYQDADIYLLDDPFSAVD 758
Cdd:PRK09493 96 ENVMFGPL----RVRGASKEEAEKQARELL---AKVGLAERAhhypSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331862 759 AHtassLFQEY--VMDALA--GKAVLLVTHQVDFLPAFDSVLL-MSDGEITEADTYQELLA-----RSRDF 819
Cdd:PRK09493 169 PE----LRHEVlkVMQDLAeeGMTMVIVTHEIGFAEKVASRLIfIDKGRIAEDGDPQVLIKnppsqRLQEF 235
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
620-785 |
1.54e-14 |
|
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: 73.93 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT------------IAYVSQTAWIQTG-TIRDNIL 686
Cdd:TIGR01189 16 FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeqrdephenILYLGHLPGLKPElSALENLH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 687 FggvmdehrYRETIQKSSLDKDlELLPDGDQTEIGERGVN-LSGGQKQRIQLARALYQDADIYLLDDPFSAVDAhTASSL 765
Cdd:TIGR01189 96 F--------WAAIHGGAQRTIE-DALAAVGLTGFEDLPAAqLSAGQQRRLALARLWLSRRPLWILDEPTTALDK-AGVAL 165
|
170 180
....*....|....*....|.
gi 22331862 766 FQEYVMDALA-GKAVLLVTHQ 785
Cdd:TIGR01189 166 LAGLLRAHLArGGIVLLTTHQ 186
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
604-818 |
1.73e-14 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 75.23 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 604 KSASFSWeeKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILG-ETPcVSGTIDFYG----------------T 666
Cdd:TIGR02769 13 RTGGLFG--AKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGlEKP-AQGTVSFRGqdlyqldrkqrrafrrD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 667 IAYVSQTA-----------WIqtgtIRDNILFGGVMDEHRYRETIQKssLDKDLELLPDGDQteigERGVNLSGGQKQRI 735
Cdd:TIGR02769 90 VQLVFQDSpsavnprmtvrQI----IGEPLRHLTSLDESEQKARIAE--LLDMVGLRSEDAD----KLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 736 QLARALYQDADIYLLDDPFSAVDAH-TASSLFQEYVMDALAGKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQELL 813
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVlQAVILELLRKLQQAFGTAYLFITHDLRLVQSFcQRVAVMDKGQIVEECDVAQLL 239
|
....*
gi 22331862 814 ARSRD 818
Cdd:TIGR02769 240 SFKHP 244
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
620-804 |
1.74e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.14 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT--------------IAYVSQ----TAWIQTGTI 681
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsprerrrlgVAYIPEdrlgRGLVPDMSV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 682 RDNILF----------GGVMDEHRYRETIQKssLDKDLELLPDGDQTEIGergvNLSGGQKQRIQLARALYQDADIYLLD 751
Cdd:COG3845 354 AENLILgryrrppfsrGGFLDRKAIRAFAEE--LIEEFDVRTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAA 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 22331862 752 DPFSAVDAHTAsslfqEYVMDAL-----AGKAVLLVTHQVDFLPAF-DSVLLMSDGEIT 804
Cdd:COG3845 428 QPTRGLDVGAI-----EFIHQRLlelrdAGAAVLLISEDLDEILALsDRIAVMYEGRIV 481
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
617-784 |
2.11e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.81 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 617 KPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAI-----LGETPCVSGTIDFYGTIAYVSQTAWIQTG------------ 679
Cdd:PRK14239 18 KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNIYSPRTDTVDLRkeigmvfqqpnp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 680 ---TIRDNILFG----GVMDEHRYRETIQKSSLDKDLEllpDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDD 752
Cdd:PRK14239 98 fpmSIYENVVYGlrlkGIKDKQVLDEAVEKSLKGASIW---DEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190
....*....|....*....|....*....|...
gi 22331862 753 PFSAVDAHTASSLfqEYVMDALAGK-AVLLVTH 784
Cdd:PRK14239 175 PTSALDPISAGKI--EETLLGLKDDyTMLLVTR 205
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1207-1420 |
2.48e-14 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 73.68 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRrESPLVLkgiSCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDlrSRFGI 1286
Cdd:cd03298 1 VRLDKIRFSYG-EQPMHF---DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDPTLF-NGTVRFNLDplcqhsdaeiwevLGKC---QLKEVVQEK------ENGLDSLVVEDGSNWSMGQRQLFCLGR 1356
Cdd:cd03298 75 LFQENNLFaHLTVEQNVG-------------LGLSpglKLTAEDRQAievalaRVGLAGLEKRLPGELSGGERQRVALAR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331862 1357 AVLRRSRVLVLDEATASIDNA-----TDLILqkTIRREfADCTVITVAHripTVMDC----TMVLSISDGRIV 1420
Cdd:cd03298 142 VLVRDKPVLLLDEPFAALDPAlraemLDLVL--DLHAE-TKMTVLMVTH---QPEDAkrlaQRVVFLDNGRIA 208
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
590-803 |
2.59e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.78 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 590 RKQRSEGNQNAIIIKSASFS-WEEKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPC---VSGTIDFYG 665
Cdd:TIGR00955 10 VFGRVAQDGSWKQLVSRLRGcFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 666 TI----------AYVSQ-TAWIQTGTIRDNILFGGVMDEHRYRETIQK----SSLDKDLELLPDGDqTEIGERGV--NLS 728
Cdd:TIGR00955 90 MPidakemraisAYVQQdDLFIPTLTVREHLMFQAHLRMPRRVTKKEKrervDEVLQALGLRKCAN-TRIGVPGRvkGLS 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22331862 729 GGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQeyVMDALA--GKAVLLVTHQ--VDFLPAFDSVLLMSDGEI 803
Cdd:TIGR00955 169 GGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQ--VLKGLAqkGKTIICTIHQpsSELFELFDKIILMAEGRV 245
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
612-813 |
3.86e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.42 E-value: 3.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 612 EKGSTkPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-------------IAYVSQTAWIQT 678
Cdd:PRK09536 12 EFGDT-TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsaraasrrVASVPQDTSLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 679 G-TIRDNILFGgvMDEHRYRETIQKSSLDKDLE-LLPDGDQTEIGERGV-NLSGGQKQRIQLARALYQDADIYLLDDPFS 755
Cdd:PRK09536 91 EfDVRQVVEMG--RTPHRSRFDTWTETDRAAVErAMERTGVAQFADRPVtSLSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331862 756 AVDAHTAS---SLFQEYVMDalaGKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQELL 813
Cdd:PRK09536 169 SLDINHQVrtlELVRRLVDD---GKTAVAAIHDLDLAARYcDELVLLADGRVRAAGPPADVL 227
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1206-1421 |
6.70e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 73.41 E-value: 6.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1206 RVEISDLQIRYrrESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVE-----PVGGKIVVDGVDISKIGVHDL 1280
Cdd:PRK14247 3 KIEIRDLKVSF--GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1281 RSRFGIIPQDP------TLF-NGTVRFNLDPLCQhSDAEIWE----VLGKCQLKEvvqEKENGLDSlvveDGSNWSMGQR 1349
Cdd:PRK14247 81 RRRVQMVFQIPnpipnlSIFeNVALGLKLNRLVK-SKKELQErvrwALEKAQLWD---EVKDRLDA----PAGKLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331862 1350 QLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIRREFADCTVITVAHRIPTVMDCT-MVLSISDGRIVE 1421
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISdYVAFLYKGQIVE 225
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
620-808 |
7.05e-14 |
|
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: 72.85 E-value: 7.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILG-ETPcVSGTIDFYGT-----------------IAYVSQT-AWIQTGT 680
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGlDRP-TSGTVRLAGQdlfaldedararlrarhVGFVFQSfQLLPTLT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 681 IRDNI-----LFGGVMDEHRYRETIQKSSLDKDLELLPDGdqteigergvnLSGGQKQRIQLARALYQDADIYLLDDPFS 755
Cdd:COG4181 107 ALENVmlpleLAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFADEPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 22331862 756 AVDAHTAsslfqEYVMDAL------AGKAVLLVTHQVDFLPAFDSVLLMSDGEITEADT 808
Cdd:COG4181 176 NLDAATG-----EQIIDLLfelnreRGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTA 229
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1223-1413 |
7.11e-14 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 71.81 E-value: 7.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1223 VLKGISCTFEGGHKIGIVGRTGSGKTTLISAL--FRLVEPVGGKIVVDGVDISKigvHDLRSRFGIIPQD----PTLfng 1296
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK---RSFRKIIGYVPQDdilhPTL--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1297 TVRFNLDplcqhsdaeiweVLGKCQlkevvqekenGLdslvvedgsnwSMGQRQLFCLGRAVLRRSRVLVLDEATASIDN 1376
Cdd:cd03213 98 TVRETLM------------FAAKLR----------GL-----------SGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 22331862 1377 ATDLILQKTIRReFAD--CTVITVAHRIPTVM----DCTMVLS 1413
Cdd:cd03213 145 SSALQVMSLLRR-LADtgRTIICSIHQPSSEIfelfDKLLLLS 186
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
911-1181 |
7.83e-14 |
|
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: 73.79 E-value: 7.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 911 NSWMAANVDNPQVSTLKLILVYLLI----GLCSVLCLMVRSVCVVIMCMKSSASLFSQLLNSLFRAPMSFYDSTPLGRIL 986
Cdd:cd18559 19 NLWLLLWFDDPVNGPQEHGQVYLSVlgalAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 987 SRVSSDLSIVDLDVPFgLIFVVASSVNTGCSLGVLAIVTWQVLFVSVPMVYLAFRLQKYYFQTAKELMRINGTTRSYVAN 1066
Cdd:cd18559 99 NLFSKDLDRVDSMAPQ-VIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1067 HLAESVAGAITIRAFDEEERFFKKSLTLIDtNASPFFHSFAANEWLIQRLETVS-AIVLASTAFCMILLPTgtfSSGFIG 1145
Cdd:cd18559 178 LFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGpCIVLFASFFAYVSRHS---LAGLVA 253
|
250 260 270
....*....|....*....|....*....|....*.
gi 22331862 1146 MALSYGLSLNMGLVYSVQNQCYLANWIISVERLNQY 1181
Cdd:cd18559 254 LKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLER 289
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1216-1387 |
8.27e-14 |
|
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: 71.62 E-value: 8.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1216 YRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQD---PT 1292
Cdd:TIGR01189 8 CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPglkPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1293 LfngTVRFNLD---PLCQHSDAEIWEVLGKCQLkevvqekeNGLDSLVVedgSNWSMGQRQLFCLGRAVLRRSRVLVLDE 1369
Cdd:TIGR01189 88 L---SALENLHfwaAIHGGAQRTIEDALAAVGL--------TGFEDLPA---AQLSAGQQRRLALARLWLSRRPLWILDE 153
|
170
....*....|....*...
gi 22331862 1370 ATASIDNATDLILQKTIR 1387
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLR 171
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
889-1156 |
8.63e-14 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 73.73 E-value: 8.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 889 GYIFFFIASLAQVT--FAVGQILqnSWMAANVDNPQVStlKLILVYLLIGLCSVLCLMVRSVCVVIMCMKSSASLFSQLL 966
Cdd:cd18572 1 AFVFLVVAALSELAipHYTGAVI--DAVVADGSREAFY--RAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 967 NSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLIFVVASSVNTGCSLGVLAIVTWQ---VLFVSVPMVYLAFRLQ 1043
Cdd:cd18572 77 RSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRltlLAFITVPVIALITKVY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1044 KYYFQTAKELMRingtTRSYVANHLAESVAGAI-TIRAFDEEERFFKKsltlidtnaspffHSFAANEWLiqRLETVSAI 1122
Cdd:cd18572 157 GRYYRKLSKEIQ----DALAEANQVAEEALSNIrTVRSFATEEREARR-------------YERALDKAL--KLSVRQAL 217
|
250 260 270
....*....|....*....|....*....|....
gi 22331862 1123 VLASTAFCMILLPTGTFSsgfigMALSYGLSLNM 1156
Cdd:cd18572 218 AYAGYVAVNTLLQNGTQV-----LVLFYGGHLVL 246
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1188-1431 |
9.06e-14 |
|
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: 75.99 E-value: 9.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1188 APEVIEETRPPVNWPVTGRVEISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVV 1267
Cdd:TIGR03269 264 VSEVEKECEVEVGEPIIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1268 ----DGVDISKIGVhDLRSR----FGIIPQDPTLFngTVRFNLDPLCQHSDAEIWEVLGKcqLKEVVQEKENGLD----- 1334
Cdd:TIGR03269 344 rvgdEWVDMTKPGP-DGRGRakryIGILHQEYDLY--PHRTVLDNLTEAIGLELPDELAR--MKAVITLKMVGFDeekae 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1335 SLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTI--RREFADCTVITVAHRIPTVMD-CTMV 1411
Cdd:TIGR03269 419 EILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRA 498
|
250 260
....*....|....*....|
gi 22331862 1412 LSISDGRIVEYDEPMKLMKD 1431
Cdd:TIGR03269 499 ALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
620-788 |
1.46e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 72.35 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILG-----ETP-----CVSGTIDFYGTIAYVSQTAWIQTG---------- 679
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdKSAgshieLLGRTVQREGRLARDIRKSRANTGyifqqfnlvn 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 680 --TIRDNILFGGVMDEHRYRETIQKSSLDKDLELLPDgdQTEIG------ERGVNLSGGQKQRIQLARALYQDADIYLLD 751
Cdd:PRK09984 100 rlSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQA--LTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 22331862 752 DPFSAVDAHTAsslfqEYVMDALA------GKAVLLVTHQVDF 788
Cdd:PRK09984 178 EPIASLDPESA-----RIVMDTLRdinqndGITVVVTLHQVDY 215
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1214-1441 |
1.58e-13 |
|
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: 72.04 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1214 IRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPV-GGKIVVDGVDISKIGVHDLRSRFGI------ 1286
Cdd:COG1119 9 VTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTyGNDVRLFGERRGGEDVWELRKRIGLvspalq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 --IPQDPT--------LFNGTVRFNldplcQHSDAEI---WEVLGKCQLKEVVQEKENGLdslvvedgsnwSMGQRQLFC 1353
Cdd:COG1119 89 lrFPRDETvldvvlsgFFDSIGLYR-----EPTDEQReraRELLELLGLAHLADRPFGTL-----------SQGEQRRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1354 LGRAVLRRSRVLVLDEATASID-NATDLILQkTIRReFA---DCTVITVAHRIPTVMDC-TMVLSISDGRIVEYDEPMKL 1428
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDlGARELLLA-LLDK-LAaegAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEV 230
|
250
....*....|....*
gi 22331862 1429 MKDEN--SLFGKLVK 1441
Cdd:COG1119 231 LTSENlsEAFGLPVE 245
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1223-1422 |
1.81e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 72.00 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1223 VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVD------GVDISKIGVHDLRSRFGIIPQDPTLF-N 1295
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfGKDIFQIDAIKLRKEVGMVFQQPNPFpH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1296 GTVRFNLD-PLCQHSDAEiwevlgKCQLKEVVQE--KENGLDSLVVE----DGSNWSMGQRQLFCLGRAVLRRSRVLVLD 1368
Cdd:PRK14246 105 LSIYDNIAyPLKSHGIKE------KREIKKIVEEclRKVGLWKEVYDrlnsPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 1369 EATASIDNATDLILQKTIRREFADCTVITVAH---RIPTVMDctMVLSISDGRIVEY 1422
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIAIVIVSHnpqQVARVAD--YVAFLYNGELVEW 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
620-814 |
1.95e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 71.92 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAI-LGETPCvsgtidfYGTIAYVSQtawiQTGTIRDNILFGGVMDEHRYR- 697
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCInFLEKPS-------EGSIVVNGQ----TINLVRDKDGQLKVADKNQLRl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 698 -----------------ETIQKSSLDKDLELLPDG------------DQTEIGERG-----VNLSGGQKQRIQLARALYQ 743
Cdd:PRK10619 90 lrtrltmvfqhfnlwshMTVLENVMEAPIQVLGLSkqeareravkylAKVGIDERAqgkypVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22331862 744 DADIYLLDDPFSAVDAHTASSLFQeyVMDALA--GKAVLLVTHQVDFLPAFDS-VLLMSDGEITEADTYQELLA 814
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLR--IMQQLAeeGKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQLFG 241
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
598-814 |
2.13e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 72.55 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 598 QNAIIIKSASFSWEEKGstkpnLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG------------ 665
Cdd:PRK13641 6 ENVDYIYSPGTPMEKKG-----LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 666 -----TIAYVSQTAWIQ--TGTIRDNILFG----GVMDEH---RYRETIQKSSLDKDLellpdgdqteIGERGVNLSGGQ 731
Cdd:PRK13641 81 kklrkKVSLVFQFPEAQlfENTVLKDVEFGpknfGFSEDEakeKALKWLKKVGLSEDL----------ISKSPFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 732 KQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQEYVMDALAGKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQ 810
Cdd:PRK13641 151 MRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYaDDVLVLEHGKLIKHASPK 230
|
....
gi 22331862 811 ELLA 814
Cdd:PRK13641 231 EIFS 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
620-802 |
2.18e-13 |
|
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: 74.48 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPC--VSGTIDFYGT--------------IAYVSQT-AWIQTGTIR 682
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHgtWDGEIYWSGSplkasnirdteragIVIIHQElTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 683 DNILF-------GGVMDE----HRYRETIQKSSLDKDLELLPDGDqteigergvnLSGGQKQRIQLARALYQDADIYLLD 751
Cdd:TIGR02633 97 ENIFLgneitlpGGRMAYnamyLRAKNLLRELQLDADNVTRPVGD----------YGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22331862 752 DPFSAVDAHTASSLFqEYVMDALA-GKAVLLVTHQVDFLPAF-DSVLLMSDGE 802
Cdd:TIGR02633 167 EPSSSLTEKETEILL-DIIRDLKAhGVACVYISHKLNEVKAVcDTICVIRDGQ 218
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
615-833 |
2.24e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 71.65 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 615 STKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPC----VSGTIDFYGTIAYVSQTAWIQTGTIRDN--ILFG 688
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGRKIATIMQNprSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 689 GV--MDEHRyRETIQKSSLDKDLELLP--------DGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVD 758
Cdd:PRK10418 94 PLhtMHTHA-RETCLALGKPADDATLTaaleavglENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 759 AhtassLFQEYVMDALA------GKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQELLA--RSRDFQDLVNAHRET 829
Cdd:PRK10418 173 V-----VAQARILDLLEsivqkrALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETLFNapKHAVTRSLVSAHLAL 247
|
....
gi 22331862 830 AGSE 833
Cdd:PRK10418 248 YGME 251
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1207-1420 |
2.54e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 72.19 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRrESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDG--VDISKIGVHDLRSRF 1284
Cdd:PRK13636 6 LKVEELNYNYS-DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1285 GIIPQDP--TLFNGTVrfnldplcqHSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSN-----WSMGQRQLFCLGRA 1357
Cdd:PRK13636 85 GMVFQDPdnQLFSASV---------YQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDkpthcLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 1358 VLRRSRVLVLDEATASID--NATDLI-LQKTIRREFaDCTVITVAHRIPTV-MDCTMVLSISDGRIV 1420
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDpmGVSEIMkLLVEMQKEL-GLTIIIATHDIDIVpLYCDNVFVMKEGRVI 221
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1207-1400 |
2.79e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 71.66 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESPL---VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDlRSR 1283
Cdd:COG1101 2 LELKNLSKTFNPGTVNekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK-RAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1284 F-GIIPQDP---TLFNGTV------------RFNLdplcqhsdaeIWEVLGKcqLKEVVQEK--------ENGLDSLVve 1339
Cdd:COG1101 81 YiGRVFQDPmmgTAPSMTIeenlalayrrgkRRGL----------RRGLTKK--RRELFRELlatlglglENRLDTKV-- 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 1340 dgSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNAT-DLILQKT---IRREfaDCTVITVAH 1400
Cdd:COG1101 147 --GLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTaALVLELTekiVEEN--NLTTLMVTH 207
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
889-1086 |
3.32e-13 |
|
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: 71.82 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 889 GYIFFFIASLAQ--VTFAVGQILQNswmAANVDNPQVsTLKLILVYLLIGLCSVLCLMVRSVCVVIMCMKSSASLFSQLL 966
Cdd:cd18557 1 GLLFLLISSAAQllLPYLIGRLIDT---IIKGGDLDV-LNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 967 NSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLIFVVASSVNTGCSLGVLAIVTWQ---VLFVSVPMVYLAFRLQ 1043
Cdd:cd18557 77 SSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKltlVLLLVIPLLLIASKIY 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 22331862 1044 KYYfqtakeLMRINGTTRSYVA--NHLAESVAGAI-TIRAFDEEER 1086
Cdd:cd18557 157 GRY------IRKLSKEVQDALAkaGQVAEESLSNIrTVRSFSAEEK 196
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1223-1406 |
4.47e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.91 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1223 VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIvvdgvdiskigVHDLRSRFGIIPQ----DPTLFNGTV 1298
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVPQklylDTTLPLTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1299 RF-NLDPLCQHSDaeIWEVLGKCQLKEVVQEKENGLdslvvedgsnwSMGQRQLFCLGRAVLRRSRVLVLDEATASID-N 1376
Cdd:PRK09544 88 RFlRLRPGTKKED--ILPALKRVQAGHLIDAPMQKL-----------SGGETQRVLLARALLNRPQLLVLDEPTQGVDvN 154
|
170 180 190
....*....|....*....|....*....|....
gi 22331862 1377 AT----DLILQktIRREFaDCTVITVAHRIPTVM 1406
Cdd:PRK09544 155 GQvalyDLIDQ--LRREL-DCAVLMVSHDLHLVM 185
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
620-784 |
5.06e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 70.89 E-value: 5.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-------------IAYVSQ-----TAwiQTGTI 681
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdvtklpeykrakyIGRVFQdpmmgTA--PSMTI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 682 RDNI-----------LFGGVMDEHR--YRETIqkSSLDKDLEllpDGDQTEIGergvNLSGGQKQRIQLARALYQDADIY 748
Cdd:COG1101 100 EENLalayrrgkrrgLRRGLTKKRRelFRELL--ATLGLGLE---NRLDTKVG----LLSGGQRQALSLLMATLTKPKLL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 22331862 749 LLDDPFSAVDAHTAsslfqEYVMDaLAGKAV-------LLVTH 784
Cdd:COG1101 171 LLDEHTAALDPKTA-----ALVLE-LTEKIVeennlttLMVTH 207
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1207-1433 |
5.13e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.92 E-value: 5.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRrESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGI 1286
Cdd:PRK13647 5 IEVEDLHFRYK-DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDP--TLFNGTVrfnldplcqhsdaeiWE--VLGKCQL----KEVVQEKENGLDSLVVEDGSN-----WSMGQRQLFC 1353
Cdd:PRK13647 84 VFQDPddQVFSSTV---------------WDdvAFGPVNMgldkDEVERRVEEALKAVRMWDFRDkppyhLSYGQKKRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1354 LGRAVLRRSRVLVLDEATASIDNATDLILQKTIRREFADCTVITVA-HRIPTVMD-CTMVLSISDGRIVEYDEPmKLMKD 1431
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDK-SLLTD 227
|
..
gi 22331862 1432 EN 1433
Cdd:PRK13647 228 ED 229
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1224-1431 |
5.53e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.17 E-value: 5.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1224 LKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIG-VHDLRSRFGIIPQDP-TLFNG-TVR- 1299
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVFQNPeTQFVGrTVEe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1300 ---FNLDPLCqhsdaeiwevLGKCQLKEVVQE--KENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASI 1374
Cdd:PRK13644 98 dlaFGPENLC----------LPPIEIRKRVDRalAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 1375 D-NATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGRIVEYDEPMKLMKD 1431
Cdd:PRK13644 168 DpDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
601-812 |
5.69e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 71.27 E-value: 5.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 601 IIIKSASFSWEEKGSTKPN-LRNVSLEVKFGEKVAVCGEVGSGKSTL---LAAILGETpcvSGTIDF------------- 663
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKaLDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALLLPD---TGTIEWifkdeknkkktke 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 664 ---YGT---------------------IAYVSQTAWIQ--TGTIRDNILFG----GVMDEH---RYRETIQKSSLDKD-L 709
Cdd:PRK13651 80 kekVLEklviqktrfkkikkikeirrrVGVVFQFAEYQlfEQTIEKDIIFGpvsmGVSKEEakkRAAKYIELVGLDESyL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 710 ELLPdgdqteigergVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQEYVMDALAGKAVLLVTHQVD-F 788
Cdd:PRK13651 160 QRSP-----------FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDnV 228
|
250 260
....*....|....*....|....*
gi 22331862 789 LPAFDSVLLMSDGEIT-EADTYQEL 812
Cdd:PRK13651 229 LEWTKRTIFFKDGKIIkDGDTYDIL 253
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
620-849 |
6.22e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.14 E-value: 6.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT--------------IAYVSQ--------TAWiq 677
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvrirsprdaialgIGMVHQhfmlvpnlTVA-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 678 tgtirDNIL------FGGVMDEHRYRETIQKSSLDKDLELLPDgdqTEIGErgvnLSGGQKQRIQLARALYQDADIYLLD 751
Cdd:COG3845 99 -----ENIVlgleptKGGRLDRKAARARIRELSERYGLDVDPD---AKVED----LSVGEQQRVEILKALYRGARILILD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 752 DPfsavdahTA-------SSLFQeyVMDALA--GKAVLLVTHQvdflpaFDSVLLMSD-----------GEITEADTYQE 811
Cdd:COG3845 167 EP-------TAvltpqeaDELFE--ILRRLAaeGKSIIFITHK------LREVMAIADrvtvlrrgkvvGTVDTAETSEE 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 22331862 812 LLARS---RDFQDLVNAHRETAGsERVVAVEN-------PTKPVKEIN 849
Cdd:COG3845 232 ELAELmvgREVLLRVEKAPAEPG-EVVLEVENlsvrddrGVPALKDVS 278
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
620-853 |
7.07e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 71.65 E-value: 7.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAI-LGETPcVSGTIDFYGT-IAYVSQTAWIQT----G------------TI 681
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCInLLERP-TSGSVLVDGVdLTALSERELRAArrkiGmifqhfnllssrTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 682 RDNILF-----GgvMDehryRETIQKssldKDLELLpdgDQTEIGERG----VNLSGGQKQRIQLARALYQDADIYLLDD 752
Cdd:COG1135 100 AENVALpleiaG--VP----KAEIRK----RVAELL---ELVGLSDKAdaypSQLSGGQKQRVGIARALANNPKVLLCDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 753 PFSAVDAHTASSlfqeyVMDALA------GKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQELLAR-----SRDF- 819
Cdd:COG1135 167 ATSALDPETTRS-----ILDLLKdinrelGLTIVLITHEMDVVRRIcDRVAVLENGRIVEQGPVLDVFANpqselTRRFl 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 22331862 820 ---------QDLVNAHRETAGSERVVAV----ENPTKPVkeINRVIS 853
Cdd:COG1135 242 ptvlndelpEELLARLREAAGGGRLVRLtfvgESADEPL--LSELAR 286
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
620-803 |
8.22e-13 |
|
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: 68.71 E-value: 8.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGetpcvsgtidFYGTIAyvsqtawiqtgtIRDNILFGGV------MDE 693
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG----------HPKYEV------------TEGEILFKGEditdlpPEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 694 hRYRETIQKSSLD-------KDLELLpdgdqteigeRGVN--LSGGQKQRIQLARALYQDADIYLLDDPFSAVDAhTASS 764
Cdd:cd03217 74 -RARLGIFLAFQYppeipgvKNADFL----------RYVNegFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI-DALR 141
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 22331862 765 LFQEYVMDAL-AGKAVLLVTHQ---VDFLPAfDSVLLMSDGEI 803
Cdd:cd03217 142 LVAEVINKLReEGKSVLIITHYqrlLDYIKP-DRVHVLYDGRI 183
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
620-834 |
9.56e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.64 E-value: 9.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG-TIAYVSQTAWIQTG--------------TIRDN 684
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqEMRFASTTAALAAGvaiiyqelhlvpemTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 685 ILFG------GVMDEH--RYRETIQKSSLDKDLEllPDgdqTEIGErgvnLSGGQKQRIQLARALYQDADIYLLDDPFSA 756
Cdd:PRK11288 100 LYLGqlphkgGIVNRRllNYEAREQLEHLGVDID--PD---TPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 757 VDAHTASSLFQeyVMDAL--AGKAVLLVTHQVDFLPAF-DSVLLMSDGEITE-----ADTYQELLARS---RDFQDLVNA 825
Cdd:PRK11288 171 LSAREIEQLFR--VIRELraEGRVILYVSHRMEEIFALcDAITVFKDGRYVAtfddmAQVDRDQLVQAmvgREIGDIYGY 248
|
....*....
gi 22331862 826 HRETAGSER 834
Cdd:PRK11288 249 RPRPLGEVR 257
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
617-784 |
1.02e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 71.02 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 617 KPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT------------IAYVSQTAWI-QTGTIRD 683
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVpvpararlararIGVVPQFDNLdLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 684 NIL-FGGVMDEH-RYRETIQKSSLD-KDLELLPDGdqteigeRGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAH 760
Cdd:PRK13536 134 NLLvFGRYFGMStREIEAVIPSLLEfARLESKADA-------RVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH 206
|
170 180
....*....|....*....|....*
gi 22331862 761 tASSLFQEYVMDALA-GKAVLLVTH 784
Cdd:PRK13536 207 -ARHLIWERLRSLLArGKTILLTTH 230
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1207-1421 |
1.07e-12 |
|
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: 69.04 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESP--LVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISkigvhDLRSRF 1284
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1285 GIIPQDPTLFN-GTVRFN--LDPLCQ-HSDAEIwevlgkcqlKEVVQE--KENGLDS--------LvvedgsnwSMGQRQ 1350
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNvaLGLELQgVPKAEA---------RERAEEllELVGLSGfenayphqL--------SGGMRQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1351 LFCLGRAVLRRSRVLVLDEATASIDNATDLILQ----KTIRREFAdcTVITVAH----------RIptvmdctMVLSISD 1416
Cdd:cd03293 139 RVALARALAVDPDVLLLDEPFSALDALTREQLQeellDIWRETGK--TVLLVTHdideavfladRV-------VVLSARP 209
|
....*
gi 22331862 1417 GRIVE 1421
Cdd:cd03293 210 GRIVA 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
620-812 |
1.13e-12 |
|
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: 68.94 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG------------TIAYVSQTAWIQTG-TIRDNI- 685
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGWENLy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 686 LFG---GVMDEHRyRETIQkssldkdlELLPDGDQTEIGERGV-NLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHT 761
Cdd:cd03265 96 IHArlyGVPGAER-RERID--------ELLDFVGLLEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 22331862 762 ASSLFqEYV--MDALAGKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQEL 812
Cdd:cd03265 167 RAHVW-EYIekLKEEFGMTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEEL 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
622-812 |
1.21e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.90 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 622 NVSLEVKFGEKVAVCGEVGSGKSTLLAAILG-ETPcVSGTIDFYGT-----------IAYVSQT-AWIQTGTIRDNILFG 688
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGlEKP-TEGQIFIDGEdvthrsiqqrdICMVFQSyALFPHMSLGENVGYG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 689 GVMdEHRYRETIqKSSLDKDLELLpdgDQTEIGERGVN-LSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASS--- 764
Cdd:PRK11432 103 LKM-LGVPKEER-KQRVKEALELV---DLAGFEDRYVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSmre 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 765 ----LFQEYvmdalaGKAVLLVTHqvDFLPAF---DSVLLMSDGEITEADTYQEL 812
Cdd:PRK11432 178 kireLQQQF------NITSLYVTH--DQSEAFavsDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1223-1432 |
1.31e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.15 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1223 VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDlRSRFGI--IPQDPTLFNG-TVR 1299
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA-RARRGIgyLPQEASIFRRlSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1300 FNLDPLCQhsdaeIWEVLGKCQLKEVVQE--KENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNA 1377
Cdd:PRK10895 97 DNLMAVLQ-----IRDDLSAEQREDRANElmEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 1378 TDLILQKTIR--REFADCTVITvAHRIPTVMD-CTMVLSISDGRIVEYDEPMKLMKDE 1432
Cdd:PRK10895 172 SVIDIKRIIEhlRDSGLGVLIT-DHNVRETLAvCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
620-826 |
1.38e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 69.48 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDF------YGTIAYVSQ----------TAW---IQTGT 680
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILInghkleYGDYKYRCKhirmifqdpnTSLnprLNIGQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 681 IRDNIL-FGGVMDEHRYRETIqKSSLdKDLELLPDGDQTEIGErgvnLSGGQKQRIQLARALYQDADIYLLDDPFSAVDA 759
Cdd:COG4167 109 ILEEPLrLNTDLTAEEREERI-FATL-RLVGLLPEHANFYPHM----LSSGQKQRVALARALILQPKIIIADEALAALDM 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22331862 760 HTASSL------FQEYVmdalaGKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQELLARSRD--FQDLVNAH 826
Cdd:COG4167 183 SVRSQIinlmleLQEKL-----GISYIYVSQHLGIVKHIsDKVLVMHQGEVVEYGKTAEVFANPQHevTKRLIESH 253
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
620-814 |
1.42e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 69.72 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG-TIAY-------VSQTAWIQ---------TGTIR 682
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGePIKYdkkslleVRKTVGIVfqnpddqlfAPTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 683 DNILFGGV-----MDE--HRYRETIQKSSLDKDLELLPDgdqteigergvNLSGGQKQRIQLARALYQDADIYLLDDPFS 755
Cdd:PRK13639 98 EDVAFGPLnlglsKEEveKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 756 AVDAHTASSLFQEYVMDALAGKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQELLA 814
Cdd:PRK13639 167 GLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYaDKVYVMSDGKIIKEGTPKEVFS 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1223-1421 |
1.62e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.59 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1223 VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHD-LRSRFGIIPQDPTLFNG-TVRF 1300
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQELNLVPNlSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1301 NL------------DPLCQHSDAEiwEVLGKCQLKEvvqekenGLDSLVvedgSNWSMGQRQLFCLGRAVLRRSRVLVLD 1368
Cdd:COG1129 99 NIflgreprrggliDWRAMRRRAR--ELLARLGLDI-------DPDTPV----GDLSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 1369 EATASIDNA-TDlILQKTIRReFAD--CTVITVAHRIPTVMD-CTMVLSISDGRIVE 1421
Cdd:COG1129 166 EPTASLTEReVE-RLFRIIRR-LKAqgVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
618-784 |
1.63e-12 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 68.20 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 618 PNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT---------IAYVSQT--------AWIQTGT 680
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdlrgraIPYLRRKigvvfqdfRLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 681 IRDNILFGGVMDEHRYREtIQKSSLDKdLELLpdGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAH 760
Cdd:cd03292 95 VYENVAFALEVTGVPPRE-IRKRVPAA-LELV--GLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
170 180
....*....|....*....|....*....
gi 22331862 761 TASSlfqeyVMDAL-----AGKAVLLVTH 784
Cdd:cd03292 171 TTWE-----IMNLLkkinkAGTTVVVATH 194
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1219-1431 |
2.20e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 69.35 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1219 ESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIG-VHDLRSRFGIIPQDP------ 1291
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQNPdnqiva 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1292 TLFNGTVRFNLDPLCQHSDaEIWEVLGKCqLKEV-VQEKENGLDSLVvedgsnwSMGQRQLFCLGRAVLRRSRVLVLDEA 1370
Cdd:PRK13633 101 TIVEEDVAFGPENLGIPPE-EIRERVDES-LKKVgMYEYRRHAPHLL-------SGGQKQRVAIAGILAMRPECIIFDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22331862 1371 TASIDNATDLILQKTIR---REFAdCTVITVAHRIPTVMDCTMVLSISDGRIVEYDEPMKLMKD 1431
Cdd:PRK13633 172 TAMLDPSGRREVVNTIKelnKKYG-ITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
620-758 |
2.21e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 68.52 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT--------------IAYVSQTAWIQTG-TIRDN 684
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIGYLPQEASIFRKlTVEDN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 685 ILfgGVMDEHRYRETIQKSSLDkdlELLPDGDQTEIGE-RGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVD 758
Cdd:COG1137 99 IL--AVLELRKLSKKEREERLE---ELLEEFGITHLRKsKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
926-1098 |
2.26e-12 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 69.50 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 926 LKLILVYLLIGLCSVLCLMVRSVCVVIMCMKSSASLFSQLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLI 1005
Cdd:cd07346 39 LWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1006 FVVASSVNTGCSLGVLAIVTWQ---VLFVSVPMVYLAFRlqkYYFQTAKELMRINGTTRSYVANHLAESVAGAITIRAF- 1081
Cdd:cd07346 119 QLLSDVLTLIGALVILFYLNWKltlVALLLLPLYVLILR---YFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFa 195
|
170 180
....*....|....*....|
gi 22331862 1082 ---DEEERFFKKSLTLIDTN 1098
Cdd:cd07346 196 aeeREIERFREANRDLRDAN 215
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
928-1086 |
2.38e-12 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 69.43 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 928 LILVYLLIGLCSVLCLMVRSVCVVIMCMKSSASLFSQLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLiFV 1007
Cdd:cd18543 41 LVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGP-FL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1008 VASSVNTGCSLGVLAIVTWQ----VLFVSVPMVYLAFRLQKYYFQTAKELMRINGTtrsyVANHLAESVAGAITIRAFDE 1083
Cdd:cd18543 120 LGNLLTLVVGLVVMLVLSPPlalvALASLPPLVLVARRFRRRYFPASRRAQDQAGD----LATVVEESVTGIRVVKAFGR 195
|
...
gi 22331862 1084 EER 1086
Cdd:cd18543 196 ERR 198
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1224-1417 |
2.41e-12 |
|
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: 68.13 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1224 LKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSR----FGIIPQDPTLFNGTVR 1299
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1300 FNLDPLCQHSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASID-NAT 1378
Cdd:cd03290 97 ENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDiHLS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 22331862 1379 DLILQKTIRREFAD--CTVITVAHRIPTVMDCTMVLSISDG 1417
Cdd:cd03290 177 DHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1207-1421 |
2.65e-12 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 68.23 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRY-RRESPL-VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGvHDLRSRF 1284
Cdd:COG4181 9 IELRGLTKTVgTGAGELtILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD-EDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1285 -----GIIPQD----PTLfngTVRFN----LdPLCQHSDAEI--WEVLGKCQLKEVVQEKENGLdslvvedgsnwSMGQR 1349
Cdd:COG4181 88 rarhvGFVFQSfqllPTL---TALENvmlpL-ELAGRRDARAraRALLERVGLGHRLDHYPAQL-----------SGGEQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 1350 QLFCLGRAVLRRSRVLVLDEATASIDNAT-----DLILQktIRREfADCTVITVAHRIPTVMDCTMVLSISDGRIVE 1421
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATgeqiiDLLFE--LNRE-RGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
616-813 |
3.62e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 68.12 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 616 TKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLL---AAILgeTPcVSGTIDFYGT-------------IAYVSQTAWIQTG 679
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLkcfARLL--TP-QSGTVFLGDKpismlssrqlarrLALLPQHHLTPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 680 -TIRDNILFG-----------GVMDEHRYRETIQKSSLDkdlellpdgdqtEIGERGV-NLSGGQKQRIQLARALYQDAD 746
Cdd:PRK11231 91 iTVRELVAYGrspwlslwgrlSAEDNARVNQAMEQTRIN------------HLADRRLtDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331862 747 IYLLDDPFSAVD-AHTAS--SLFQEyvMDAlAGKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQELL 813
Cdd:PRK11231 159 VVLLDEPTTYLDiNHQVElmRLMRE--LNT-QGKTVVTVLHDLNQASRYcDHLVVLANGHVMAQGTPEEVM 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
620-826 |
4.27e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 68.61 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFyGTIAYVSQTAWIQTGTIRDNIlfgGVM----DEHR 695
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQKEIKPVRKKV---GVVfqfpESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 696 YRETI--------QKSSLDKD---------LELLpdGDQTEIGERG-VNLSGGQKQRIQLARALYQDADIYLLDDPFSAV 757
Cdd:PRK13643 98 FEETVlkdvafgpQNFGIPKEkaekiaaekLEMV--GLADEFWEKSpFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22331862 758 DAHTASSLFQEYVMDALAGKAVLLVTHQVDFLPAF-DSVLLMSDGEI----TEADTYQELlarsrdfqDLVNAH 826
Cdd:PRK13643 176 DPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYaDYVYLLEKGHIiscgTPSDVFQEV--------DFLKAH 241
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1210-1425 |
4.41e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.11 E-value: 4.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1210 SDLQIRYRRESplVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDG--VDISKIGVHDLRSRFGII 1287
Cdd:PRK13638 5 SDLWFRYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1288 PQDP------TLFNGTVRFNLDPLCQHSDAEIWEVLGKCQLKEVVQEKENGLDSLvvedgsnwSMGQRQLFCLGRAVLRR 1361
Cdd:PRK13638 83 FQDPeqqifyTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCL--------SHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22331862 1362 SRVLVLDEATASIDNATDLILQKTIRREFADCT-VITVAHRIPTVMDCT-MVLSISDGRIVEYDEP 1425
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNhVIISSHDIDLIYEISdAVYVLRQGQILTHGAP 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1222-1400 |
4.92e-12 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 67.30 E-value: 4.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1222 LVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVG---GKIVVDGVDISKigvHDLRSRFGIIPQDPTLFNG-T 1297
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKP---DQFQKCVAYVRQDDILLPGlT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1298 VRFNLD-----PLCQHSDAEIwevlgKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATA 1372
Cdd:cd03234 98 VRETLTytailRLPRKSSDAI-----RKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190
....*....|....*....|....*....|
gi 22331862 1373 SIDNATDLILQKTIRReFA--DCTVITVAH 1400
Cdd:cd03234 173 GLDSFTALNLVSTLSQ-LArrNRIVILTIH 201
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1222-1425 |
5.08e-12 |
|
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: 67.26 E-value: 5.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1222 LVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHdlRSRFGIIPQDPTLFN-----G 1296
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALFPhltvfE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1297 TVRFNLDpLCQHSDAEI----WEVLGKCQLKEVVQEKENGLdslvvedgsnwSMGQRQLFCLGRAVLRRSRVLVLDEATA 1372
Cdd:cd03300 92 NIAFGLR-LKKLPKAEIkervAEALDLVQLEGYANRKPSQL-----------SGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331862 1373 sidnATDLILQKTIRREFAD------CTVITVAHriptvmDCTMVLSISD-------GRIVE-------YDEP 1425
Cdd:cd03300 160 ----ALDLKLRKDMQLELKRlqkelgITFVFVTH------DQEEALTMSDriavmnkGKIQQigtpeeiYEEP 222
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
620-784 |
5.32e-12 |
|
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: 68.54 E-value: 5.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILG---ETPCVSGTIDFYGT-----------------IAYVSQ------- 672
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEdllklsekelrkirgreIQMIFQdpmtsln 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 673 ---TAWIQtgtIRDNILFGGVMDEHRYRETIqkssldkdLELLpdgDQTEI--GERGVN-----LSGGQKQRIQLARALY 742
Cdd:COG0444 101 pvmTVGDQ---IAEPLRIHGGLSKAEARERA--------IELL---ERVGLpdPERRLDrypheLSGGMRQRVMIARALA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 22331862 743 QDADIYLLDDPFSAVDAHTasslfQEYVMDALA------GKAVLLVTH 784
Cdd:COG0444 167 LEPKLLIADEPTTALDVTI-----QAQILNLLKdlqrelGLAILFITH 209
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
618-801 |
6.40e-12 |
|
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: 66.69 E-value: 6.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 618 PNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFY---------------------GTIAYVSQ---- 672
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggwvdlaqaspreilalrrRTIGYVSQflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 673 ----TAwiqtgtiRDNilfggVMDEHRYRETIQKSSLDKDLELLpdgDQTEIGERGVNL-----SGGQKQRIQLARALYQ 743
Cdd:COG4778 105 iprvSA-------LDV-----VAEPLLERGVDREEARARARELL---ARLNLPERLWDLppatfSGGEQQRVNIARGFIA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22331862 744 DADIYLLDDPFSAVDAHTAsslfqEYVMDAL-----AGKAVLLVTHQVDFLPAF-DSVLLMSDG 801
Cdd:COG4778 170 DPPLLLLDEPTASLDAANR-----AVVVELIeeakaRGTAIIGIFHDEEVREAVaDRVVDVTPF 228
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
623-785 |
6.49e-12 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 66.36 E-value: 6.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 623 VSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT------------IAYVSQTAWIQTG-TIRDNILFgg 689
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldfqrdsiargLLYLGHAPGIKTTlSVLENLRF-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 690 VMDEHRyRETIqkssldkdLELLPDGDQTEIGERGVN-LSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQE 768
Cdd:cd03231 97 WHADHS-DEQV--------EEALARVGLNGFEDRPVAqLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
170
....*....|....*..
gi 22331862 769 YVMDALAGKAVLLVTHQ 785
Cdd:cd03231 168 MAGHCARGGMVVLTTHQ 184
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1207-1435 |
7.14e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 67.90 E-value: 7.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTT---LISALFRLVEPVGGKIVVDGVDISKIGVHDLRSR 1283
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1284 FGIIPQDP-TLFNGT-----VRFNLDPlcqhsdaeiwEVLGKCQLKEVVQEKENGLDSLVVEDG--SNWSMGQRQLFCLG 1355
Cdd:PRK13640 86 VGIVFQNPdNQFVGAtvgddVAFGLEN----------RAVPRPEMIKIVRDVLADVGMLDYIDSepANLSGGQKQRVAIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1356 RAVLRRSRVLVLDEATASIDNATDLILQKTIR--REFADCTVITVAHRIPTVMDCTMVLSISDGRIVEYDEPMKLMKDEN 1433
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRklKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
..
gi 22331862 1434 SL 1435
Cdd:PRK13640 236 ML 237
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1217-1421 |
1.09e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 67.02 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1217 RRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKI---GVHDLRSRFGIIPQD-PT 1292
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDsIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1293 LFN--GTVRFNLDPLCQH----SDAE----IWEVLGKCQLKEVVQEKENGldslvvedgsNWSMGQRQLFCLGRAVLRRS 1362
Cdd:PRK10419 101 AVNprKTVREIIREPLRHllslDKAErlarASEMLRAVDLDDSVLDKRPP----------QLSGGQLQRVCLARALAVEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 1363 RVLVLDEATASIdnatDLILQ-------KTIRREFAD-CTVITvaHRIPTVMD-CTMVLSISDGRIVE 1421
Cdd:PRK10419 171 KLLILDEAVSNL----DLVLQagvirllKKLQQQFGTaCLFIT--HDLRLVERfCQRVMVMDNGQIVE 232
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
601-813 |
1.37e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 66.26 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 601 IIIKSASFSWeekgSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG-------------TI 667
Cdd:COG4604 2 IEIKNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvattpsrelakRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 668 AYVSQTAWIQTG-TIRDNILFGgvmdehRY-----RETIQ-KSSLDKDLELLpdgDQTEIGERGVN-LSGGQKQRIQLAR 739
Cdd:COG4604 78 AILRQENHINSRlTVRELVAFG------RFpyskgRLTAEdREIIDEAIAYL---DLEDLADRYLDeLSGGQRQRAFIAM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 740 ALYQDADIYLLDDPFSAVD-AHTASslfqeyVMDAL------AGKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQE 811
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDmKHSVQ------MMKLLrrladeLGKTVVIVLHDINFASCYaDHIVAMKDGRVVAQGTPEE 222
|
..
gi 22331862 812 LL 813
Cdd:COG4604 223 II 224
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
620-805 |
1.69e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.57 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG-----------------TIAYVSQT-AWIQTGTI 681
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqmdeearaklrakHVGFVFQSfMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 682 RDNILFGGVMdehryRETIQKSSLDKDLELLpdgDQTEIGER----GVNLSGGQKQRIQLARALYQDADIYLLDDPFSAV 757
Cdd:PRK10584 106 LENVELPALL-----RGESSRQSRNGAKALL---EQLGLGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 758 DAHTAS-------SLFQEYvmdalaGKAVLLVTHQVDFLPAFDSVLLMSDGEITE 805
Cdd:PRK10584 178 DRQTGDkiadllfSLNREH------GTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1206-1435 |
1.71e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.03 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1206 RVEISDLQIRYRRESPLVLK---GISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKI----------------- 1265
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTELKaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkeke 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1266 -VVDGVDISKI------GVHDLRSRFGIIPQ--DPTLFNGTVRFNL--DPLCQHSDAEIWEVLGKCQLKEVvqekenGLD 1334
Cdd:PRK13651 82 kVLEKLVIQKTrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIifGPVSMGVSKEEAKKRAAKYIELV------GLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1335 -SLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASID-NATDLILQ--KTIRREFAdcTVITVAHRIPTVMDCT- 1409
Cdd:PRK13651 156 eSYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILEifDNLNKQGK--TIILVTHDLDNVLEWTk 233
|
250 260
....*....|....*....|....*.
gi 22331862 1410 MVLSISDGRIVEYDEPMKLMKDENSL 1435
Cdd:PRK13651 234 RTIFFKDGKIIKDGDTYDILSDNKFL 259
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1219-1420 |
1.75e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 68.98 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1219 ESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDL----RSRFGIIPQdptlf 1294
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQ----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1295 ngtvRFNLDP-LCQHSDAEIWEV---LGKCQLKEVVQE--KENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLD 1368
Cdd:PRK10535 94 ----RYHLLShLTAAQNVEVPAVyagLERKQRLLRAQEllQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 22331862 1369 EATASIDNATD----LILQKTIRREFadcTVITVAHRIPTVMDCTMVLSISDGRIV 1420
Cdd:PRK10535 170 EPTGALDSHSGeevmAILHQLRDRGH---TVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
622-784 |
2.16e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 66.75 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 622 NVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG-TIAYVSQTAWIQTG------------TIRDNIL-- 686
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGePVPSRARHARQRVGvvpqfdnldpdfTVRENLLvf 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 687 ---FGgvMDEHRYRETIQKSSLDKDLELLPDGdqtEIGErgvnLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHtAS 763
Cdd:PRK13537 105 gryFG--LSAAAARALVPPLLEFAKLENKADA---KVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ-AR 174
|
170 180
....*....|....*....|..
gi 22331862 764 SLFQEYVMDALA-GKAVLLVTH 784
Cdd:PRK13537 175 HLMWERLRSLLArGKTILLTTH 196
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
611-802 |
2.31e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.03 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 611 EEKGSTK-----PNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPC--VSGTIDFYGT--------------IAY 669
Cdd:PRK13549 7 EMKNITKtfggvKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgtYEGEIIFEGEelqasnirdteragIAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 670 VSQT-AWIQTGTIRDNILFG------GVMDE----HRYRETIQKSSLDKDlellPDgdqTEIGergvNLSGGQKQRIQLA 738
Cdd:PRK13549 87 IHQElALVKELSVLENIFLGneitpgGIMDYdamyLRAQKLLAQLKLDIN----PA---TPVG----NLGLGQQQLVEIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22331862 739 RALYQDADIYLLDDPFSAVDAHTASSLFqEYVMDALA-GKAVLLVTHQVDFLPAF-DSVLLMSDGE 802
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTESETAVLL-DIIRDLKAhGIACIYISHKLNEVKAIsDTICVIRDGR 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1207-1435 |
2.47e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 65.93 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGI 1286
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDP-TLFNGT-----VRFNLDPLCQHSDaeiwevlgkcQLKEVVQEKENGLDSLVVEDGSNWSM--GQRQLFCLGRAV 1358
Cdd:PRK13648 88 VFQNPdNQFVGSivkydVAFGLENHAVPYD----------EMHRRVSEALKQVDMLERADYEPNALsgGQKQRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22331862 1359 LRRSRVLVLDEATASIDNATDLILQKTIRR--EFADCTVITVAHRIPTVMDCTMVLSISDGRIVEYDEPMKLMKDENSL 1435
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKvkSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
599-815 |
2.93e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.91 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 599 NAIIIKSASFSWeeKGSTKPnLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGTIAYVSQTAWIQ- 677
Cdd:PRK13647 3 NIIEVEDLHFRY--KDGTKA-LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 678 --------------TGTIRDNILFGGVMDEHRYRETIQKSSldkdlELLPDGDQTEIGERG-VNLSGGQKQRIQLARALY 742
Cdd:PRK13647 80 kvglvfqdpddqvfSSTVWDDVAFGPVNMGLDKDEVERRVE-----EALKAVRMWDFRDKPpYHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22331862 743 QDADIYLLDDPFSAVDAHTASSLFQeyVMDAL--AGKAVLLVTHQVDFLPAF-DSVLLMSDGEiTEADTYQELLAR 815
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLME--ILDRLhnQGKTVIVATHDVDLAAEWaDQVIVLKEGR-VLAEGDKSLLTD 227
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
926-1090 |
2.98e-11 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 65.87 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 926 LKLILVYLLIGLCSVLCLMVRSVCVVIMCMKSSASLFSQLLNSLFRAPMSFYDSTPLGRILSRVSSDL-SIVDLdvpF-- 1002
Cdd:cd18544 41 LLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTeALNEL---Fts 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1003 GLIFVVASSVNTGCSLGVLAIVTWQ---VLFVSVPMVYLAFrlqkYYFQtaKELMRINGTTRSYVAN---HLAESVAGAI 1076
Cdd:cd18544 118 GLVTLIGDLLLLIGILIAMFLLNWRlalISLLVLPLLLLAT----YLFR--KKSRKAYREVREKLSRlnaFLQESISGMS 191
|
170
....*....|....
gi 22331862 1077 TIRAFDEEERFFKK 1090
Cdd:cd18544 192 VIQLFNREKREFEE 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
620-815 |
3.10e-11 |
|
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: 67.79 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCvSGTIDFYGT-IAYVSQTAWiqtgtirdnilfggvmdeHRYRE 698
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQdLDGLSRRAL------------------RPLRR 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 699 TIQ------KSSLD----------KDLELL-PDGDQTEIGER------GVNL------------SGGQKQRIQLARALYQ 743
Cdd:COG4172 363 RMQvvfqdpFGSLSprmtvgqiiaEGLRVHgPGLSAAERRARvaealeEVGLdpaarhryphefSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22331862 744 DADIYLLDDPFSAVDAHTasslfQEYVMDALA------GKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQELLAR 815
Cdd:COG4172 443 EPKLLVLDEPTSALDVSV-----QAQILDLLRdlqrehGLAYLFISHDLAVVRALaHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
620-872 |
3.10e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 67.91 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILG------------------------ETPCVSGT-------------ID 662
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqyeptsgriiyhvalcekcgyvERPSKVGEpcpvcggtlepeeVD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 663 FYGT-----------IAYVSQTAWIQTG--TIRDNILfgGVMDEHRYRetiQKSSLDKDLELLpdgDQTEIGER----GV 725
Cdd:TIGR03269 96 FWNLsdklrrrirkrIAIMLQRTFALYGddTVLDNVL--EALEEIGYE---GKEAVGRAVDLI---EMVQLSHRithiAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 726 NLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTAsslfqEYVMDAL------AGKAVLLVTHQVDFLPAF-DSVLLM 798
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTA-----KLVHNALeeavkaSGISMVLTSHWPEVIEDLsDKAIWL 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 799 SDGEITEADTYQELLARsrdFQDLVNAHREtagsERVVAVENPTKPVKEIN-RVISSQSKVLKPSRLIKQEEREK 872
Cdd:TIGR03269 243 ENGEIKEEGTPDEVVAV---FMEGVSEVEK----ECEVEVGEPIIKVRNVSkRYISVDRGVVKAVDNVSLEVKEG 310
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
622-814 |
3.55e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.91 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 622 NVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDF--------------YGTIAYVSQTAWIqtgtIRDNILF 687
Cdd:PRK10895 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllplharaRRGIGYLPQEASI----FRRLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 688 GGVMDEHRYRETI-QKSSLDKDLELLPDGDQTEIGER-GVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSL 765
Cdd:PRK10895 97 DNLMAVLQIRDDLsAEQREDRANELMEEFHIEHLRDSmGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 22331862 766 FQ--EYVMDalAGKAVLLVTHQV-DFLPAFDSVLLMSDGEITEADTYQELLA 814
Cdd:PRK10895 177 KRiiEHLRD--SGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
624-814 |
3.56e-11 |
|
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: 65.12 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 624 SLEVKFG-----EKVAVCGEVGSGKST---LLAAILgeTPCVSGTIDFYGTIAYVSQTAWI-QTGTIRDniLFGGVMDEH 694
Cdd:cd03237 14 TLEVEGGsisesEVIGILGPNGIGKTTfikMLAGVL--KPDEGDIEIELDTVSYKPQYIKAdYEGTVRD--LLSSITKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 695 rYRETIQKSSLDKDLELLPdgdqteIGERGVN-LSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHT---ASSLFQEYV 770
Cdd:cd03237 90 -YTHPYFKTEIAKPLQIEQ------ILDREVPeLSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQrlmASKVIRRFA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 22331862 771 MDalAGKAVLLVTHQVDFLPAFDSVLLMSDGE---ITEADTYQELLA 814
Cdd:cd03237 163 EN--NEKTAFVVEHDIIMIDYLADRLIVFEGEpsvNGVANPPQSLRS 207
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1224-1378 |
4.38e-11 |
|
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: 63.97 E-value: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1224 LKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKI---GVHDLRSRFGIIPQDPTLF-NGTVR 1299
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRKIGVVFQDFRLLpDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1300 FNLdplcqhsdAEIWEVLGKCQlKEVVQEKENGLDSLVVEDGSN-----WSMGQRQLFCLGRAVLRRSRVLVLDEATASI 1374
Cdd:cd03292 97 ENV--------AFALEVTGVPP-REIRKRVPAALELVGLSHKHRalpaeLSGGEQQRVAIARAIVNSPTILIADEPTGNL 167
|
....
gi 22331862 1375 DNAT 1378
Cdd:cd03292 168 DPDT 171
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
621-805 |
4.45e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 4.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 621 RNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT--------------IAYVSQ----TAWIQTGTIR 682
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprspldavkkgMAYITEsrrdNGFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 683 DNIL---------FGGVM---DEHRYRETIQKSSldKDLELLPDGDQTEIGErgvnLSGGQKQRIQLARALYQDADIYLL 750
Cdd:PRK09700 360 QNMAisrslkdggYKGAMglfHEVDEQRTAENQR--ELLALKCHSVNQNITE----LSGGNQQKVLISKWLCCCPEVIIF 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 751 DDPFSAVDAHTASSLFQeyVMDALA--GKAVLLVTHQV-DFLPAFDSVLLMSDGEITE 805
Cdd:PRK09700 434 DEPTRGIDVGAKAEIYK--VMRQLAddGKVILMVSSELpEIITVCDRIAVFCEGRLTQ 489
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
620-803 |
4.47e-11 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 64.31 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGtIAYVSQTAWIQTG--------------TIRDNI 685
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG-FDVVKEPAEARRRlgfvsdstglydrlTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 686 LFGGvmDEHRYRETIQKSSLDKDLELLPDGDQTEigERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSL 765
Cdd:cd03266 100 EYFA--GLYGLKGDELTARLEELADRLGMEELLD--RRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 22331862 766 FQeyVMDAL--AGKAVLLVTHQVDFLPAF-DSVLLMSDGEI 803
Cdd:cd03266 176 RE--FIRQLraLGKCILFSTHIMQEVERLcDRVVVLHRGRV 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
589-804 |
4.82e-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: 64.28 E-value: 4.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 589 RRKQRSEGnqnaiIIKSASFSWEEKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKST---LLAAIL----GETPcVSGTI 661
Cdd:cd03267 11 RVYSKEPG-----LIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTtlkILSGLLqptsGEVR-VAGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 662 DFYGTIAYVSQTAWI--QTGTI------RDNILFGGVM---DEHRYRETiqkssLDKDLELLPDGDQTEIGERgvNLSGG 730
Cdd:cd03267 85 PWKRRKKFLRRIGVVfgQKTQLwwdlpvIDSFYLLAAIydlPPARFKKR-----LDELSELLDLEELLDTPVR--QLSLG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 731 QKQRIQLARALYQDADIYLLDDPFSAVDAHTASSL---FQEYVMDalAGKAVLLVTHQVDFLPAF-DSVLLMSDGEIT 804
Cdd:cd03267 158 QRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIrnfLKEYNRE--RGTTVLLTSHYMKDIEALaRRVLVIDKGRLL 233
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
620-801 |
5.77e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 64.80 E-value: 5.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAI-----LGETPCVSGTIDFYGTIAYVSQTAWIQT---------------G 679
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYAPDVDPVEVrrrigmvfqkpnpfpK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 680 TIRDNILFG-------GVMDEHRYRETIQKSSLD--KDlellpdgdqtEIGERGVNLSGGQKQRIQLARALYQDADIYLL 750
Cdd:PRK14243 106 SIYDNIAYGaringykGDMDELVERSLRQAALWDevKD----------KLKQSGLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 751 DDPFSAVDAhtASSLFQEYVMDALAGK-AVLLVTH------QVDFLPAFDSVLLMSDG 801
Cdd:PRK14243 176 DEPCSALDP--ISTLRIEELMHELKEQyTIIIVTHnmqqaaRVSDMTAFFNVELTEGG 231
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
607-813 |
6.07e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 66.21 E-value: 6.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 607 SFSWEEKGSTKP----------NLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT---------- 666
Cdd:PRK10070 21 AFKYIEQGLSKEqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVdiakisdael 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 667 -------IAYVSQT-AWIQTGTIRDNILFG----GVMDEHRYR---ETIQKSSLDKDLELLPDgdqteigergvNLSGGQ 731
Cdd:PRK10070 101 revrrkkIAMVFQSfALMPHMTVLDNTAFGmelaGINAEERREkalDALRQVGLENYAHSYPD-----------ELSGGM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 732 KQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQEYV-MDALAGKAVLLVTHQVD-FLPAFDSVLLMSDGEITEADTY 809
Cdd:PRK10070 170 RQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVkLQAKHQRTIVFISHDLDeAMRIGDRIAIMQNGEVVQVGTP 249
|
....
gi 22331862 810 QELL 813
Cdd:PRK10070 250 DEIL 253
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
613-804 |
7.18e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.47 E-value: 7.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 613 KGSTKPNLRN-VSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG-TIAYVSQTAWIQTG----------- 679
Cdd:PRK11288 261 DGLKGPGLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkPIDIRSPRDAIRAGimlcpedrkae 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 680 ------TIRDNI---------LFGGVMDEHRYRETIqksslDKDLELL----PDGDQtEIGergvNLSGGQKQRIQLARA 740
Cdd:PRK11288 341 giipvhSVADNInisarrhhlRAGCLINNRWEAENA-----DRFIRSLniktPSREQ-LIM----NLSGGNQQKAILGRW 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 741 LYQDADIYLLDDPFSAVDAHTASSLFQeyVMDALA--GKAVLLVTHQvdfLPAF----DSVLLMSDGEIT 804
Cdd:PRK11288 411 LSEDMKVILLDEPTRGIDVGAKHEIYN--VIYELAaqGVAVLFVSSD---LPEVlgvaDRIVVMREGRIA 475
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
621-785 |
7.27e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.28 E-value: 7.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 621 RNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-I-----AYVSQTAWI--QTG-----TIRDNILF 687
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEpIrrqrdEYHQDLLYLghQPGiktelTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 688 ----GGVMDEHRYRETIQKSSLdKDLELLPDGdqteigergvNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHtAS 763
Cdd:PRK13538 98 yqrlHGPGDDEALWEALAQVGL-AGFEDVPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ-GV 165
|
170 180
....*....|....*....|...
gi 22331862 764 SLFQEYVMDALA-GKAVLLVTHQ 785
Cdd:PRK13538 166 ARLEALLAQHAEqGGMVILTTHQ 188
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
620-860 |
9.36e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.96 E-value: 9.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT--------------IAYVSQT-AWIQTGTIRDN 684
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhklaaqlgIGIIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 685 ILFG----------GVMDehrYRETIQKSSLdkdlELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPF 754
Cdd:PRK09700 101 LYIGrhltkkvcgvNIID---WREMRVRAAM----MLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 755 SAVDAHTASSLFqeYVMDAL--AGKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQEL-------LARSRDFQDLVN 824
Cdd:PRK09700 174 SSLTNKEVDYLF--LIMNQLrkEGTAIVYISHKLAEIRRIcDRYTVMKDGSSVCSGMVSDVsnddivrLMVGRELQNRFN 251
|
250 260 270
....*....|....*....|....*....|....*.
gi 22331862 825 AHRETAGSErvvavenPTKPVKEINRVISSQSKVLK 860
Cdd:PRK09700 252 AMKENVSNL-------AHETVFEVRNVTSRDRKKVR 280
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
285-574 |
9.55e-11 |
|
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: 64.49 E-value: 9.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 285 LLTSGFFAFMKIVAVSAGPLLLNAFI--LVAEGNASFRYEGLVLAVLLFFSKMIESLSQRQWYFRcriVGLRVRSLLTAA 362
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIddVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAAR---LGQRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 363 INKKQLRLNNSSRLIHSGSEIMNYATVDAYRIGEFPYW-FHQLWTTSFQLLIALGILFHSVGVATFSALAVIILTVLCNA 441
Cdd:cd07346 78 LFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSgLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 442 PIAKLQNKFQSELMTSQDERLKACNESLVNMKVLKLYAWESHFKKVIEKLrnieLKSLKAVQMRKAYNAVLFWSSPVFVS 521
Cdd:cd07346 158 YFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREA----NRDLRDANLRAARLSALFSPLIGLLT 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 22331862 522 AATFAT-----CYF-LDIPLRASNVFTFVATLRLVQDPVRMIPDVIGVTIQAKVAFSRI 574
Cdd:cd07346 234 ALGTALvllygGYLvLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1207-1425 |
1.08e-10 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 65.12 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYrrESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDlRsRFGI 1286
Cdd:COG3842 6 LELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK-R-NVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDPTLF-------NgtVRFnldPLCQH--SDAEI----WEVLGKCQLKEVVQEKENGLdslvvedgsnwSMGQRQLFC 1353
Cdd:COG3842 82 VFQDYALFphltvaeN--VAF---GLRMRgvPKAEIrarvAELLELVGLEGLADRYPHQL-----------SGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1354 LGRAVLRRSRVLVLDEATASIDNATDLILQ---KTIRREFaDCTVITVAH----------RIpTVMDctmvlsisDGRIV 1420
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMReelRRLQREL-GITFIYVTHdqeealaladRI-AVMN--------DGRIE 215
|
....*
gi 22331862 1421 EYDEP 1425
Cdd:COG3842 216 QVGTP 220
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
624-767 |
1.13e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 66.31 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 624 SLEVKFGEKVAVCGEVGSGKSTLLAaILGET-PCVSG--TIDFYGTIAYVSQTAWIQTGTIRDNILFGGVMDEHryretI 700
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFR-ILGELwPVYGGrlTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDM-----K 545
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 701 QKSSLDKDLE-LLPDGDQTEIGERGVN----------LSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQ 767
Cdd:TIGR00954 546 RRGLSDKDLEqILDNVQLTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYR 623
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1209-1431 |
1.30e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 65.05 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1209 ISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLR------- 1281
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrkki 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1282 ----SRFGIIPQDPTLFNGTVRFNLDPLCQHSDAEiwevlgkcqlKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRA 1357
Cdd:PRK10070 109 amvfQSFALMPHMTVLDNTAFGMELAGINAEERRE----------KALDALRQVGLENYAHSYPDELSGGMRQRVGLARA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 1358 VLRRSRVLVLDEATASIDNATDLILQKTIRREFA--DCTVITVAHRIPTVMDCTMVLSI-SDGRIVEYDEPMKLMKD 1431
Cdd:PRK10070 179 LAINPDILLMDEAFSALDPLIRTEMQDELVKLQAkhQRTIVFISHDLDEAMRIGDRIAImQNGEVVQVGTPDEILNN 255
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
620-753 |
1.48e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.97 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGTIAYVSQTAWIQTG---------------TIRDN 684
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREavaivpegrrvfsrmTVEEN 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 685 ILFGGVM-DEHRYRETIQKSsldkdLELLPDGDQTEIgERGVNLSGGQKQRIQLARALYQDADIYLLDDP 753
Cdd:PRK11614 101 LAMGGFFaERDQFQERIKWV-----YELFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
616-785 |
1.49e-10 |
|
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: 62.23 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 616 TKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGTIAYVSQTAWIQTGTI------------RD 683
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALieapgfypnltaRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 684 NILFGGVMdehrYRetIQKSSLDKDLELLpdGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTAS 763
Cdd:cd03268 92 NLRLLARL----LG--IRKKRIDEVLDVV--GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIK 163
|
170 180
....*....|....*....|...
gi 22331862 764 SLfQEYVMD-ALAGKAVLLVTHQ 785
Cdd:cd03268 164 EL-RELILSlRDQGITVLISSHL 185
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
620-804 |
1.52e-10 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 62.60 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEvkFGEKV-AVCGEVGSGKSTLLAAILGETPCVSGTIDFYG------------TIAYVSQT-AWIQTGTIRDNI 685
Cdd:cd03264 16 LDGVSLT--LGPGMyGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQEfGVYPNFTVREFL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 686 ----LFGGVMDEHryretiQKSSLDKDLELLpdgDQTEIGERGVN-LSGGQKQRIQLARALYQDADIYLLDDPFSAVDA- 759
Cdd:cd03264 94 dyiaWLKGIPSKE------VKARVDEVLELV---NLGDRAKKKIGsLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPe 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 22331862 760 --HTASSLFQEyvmdALAGKAVLLVTHQV-DFLPAFDSVLLMSDGEIT 804
Cdd:cd03264 165 erIRFRNLLSE----LGEDRIVILSTHIVeDVESLCNQVAVLNKGKLV 208
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
611-804 |
1.57e-10 |
|
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: 62.28 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 611 EEKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPcvsGTIDFYGTIAYVSQTAWIQTGTIRDNILFGGV 690
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTE---GNVSVEGDIHYNGIPYKEFAEKYPGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 691 MDEH----RYRETIqkssldkDLELLPDGDQTEigeRGVnlSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLF 766
Cdd:cd03233 91 EDVHfptlTVRETL-------DFALRCKGNEFV---RGI--SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEIL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 22331862 767 QEYVMDALAGKAVLLVT-HQ--VDFLPAFDSVLLMSDGEIT 804
Cdd:cd03233 159 KCIRTMADVLKTTTFVSlYQasDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
620-803 |
1.62e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.52 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAaILGetpCV----SGTIDFYGT-IAYVSQTAWIQTGtiRDNilFGGVMDEH 694
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILG---CLdkptSGTYRVAGQdVATLDADALAQLR--REH--FGFIFQRY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 695 R----------------YRETIQKSSLDKDLELLPD-GDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAV 757
Cdd:PRK10535 96 HllshltaaqnvevpavYAGLERKQRLLRAQELLQRlGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 22331862 758 DAHTAsslfqEYVMDAL-----AGKAVLLVTHQVDFLPAFDSVLLMSDGEI 803
Cdd:PRK10535 176 DSHSG-----EEVMAILhqlrdRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1223-1423 |
1.67e-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: 62.55 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1223 VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHdlrsrFGIipqDPTLfngTVRFNL 1302
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLG-----GGF---NPEL---TGRENI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1303 DPLCQ---HSDAEIWEVlgkcqLKEVVQ--EKENGLDSLVvedgSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNA 1377
Cdd:cd03220 106 YLNGRllgLSRKEIDEK-----IDEIIEfsELGDFIDLPV----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 22331862 1378 TDLILQKTIRREFADC-TVITVAHRIPTVMD-CTMVLSISDGRIVEYD 1423
Cdd:cd03220 177 FQEKCQRRLRELLKQGkTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1207-1400 |
1.78e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.94 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESplVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVE-----PVGGKIVVDGVDISKIGVH--D 1279
Cdd:PRK14267 5 IETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDpiE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1280 LRSRFGIIPQDPTLF-------NGTVRFNLDPLCQhSDAEIWEV----LGKCQLKEVVQEKENgldslvvEDGSNWSMGQ 1348
Cdd:PRK14267 83 VRREVGMVFQYPNPFphltiydNVAIGVKLNGLVK-SKKELDERvewaLKKAALWDEVKDRLN-------DYPSNLSGGQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 22331862 1349 RQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIRREFADCTVITVAH 1400
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1209-1423 |
1.90e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.09 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1209 ISDLQIRYrrESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGvdiskigvhdlRSRFGIIP 1288
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1289 QDPTLF-NGTVRFNLdplcQHSDAEIWEVLgkcQLKEVVQEKENGLDSLVVE-----------DGsnWSM---------- 1346
Cdd:COG0488 68 QEPPLDdDLTVLDTV----LDGDAELRALE---AELEELEAKLAEPDEDLERlaelqeefealGG--WEAearaeeilsg 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1347 -----------------GQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIRREfaDCTVITVAHriptvmD-- 1407
Cdd:COG0488 139 lgfpeedldrpvselsgGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNY--PGTVLVVSH------Dry 210
|
250 260
....*....|....*....|.
gi 22331862 1408 -----CTMVLSISDGRIVEYD 1423
Cdd:COG0488 211 fldrvATRILELDRGKLTLYP 231
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1216-1375 |
1.95e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 63.27 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1216 YRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISkIGVHDLRS-RFGIIPQDP-TL 1293
Cdd:PRK15112 21 FRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSYRSqRIRMIFQDPsTS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1294 FNGTVRFN--LD-PLCQHSDAEiwevlGKCQLKEVVQE-KENGLdslvVEDGSNW-----SMGQRQLFCLGRAVLRRSRV 1364
Cdd:PRK15112 100 LNPRQRISqiLDfPLRLNTDLE-----PEQREKQIIETlRQVGL----LPDHASYyphmlAPGQKQRLGLARALILRPKV 170
|
170
....*....|.
gi 22331862 1365 LVLDEATASID 1375
Cdd:PRK15112 171 IIADEALASLD 181
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
616-811 |
2.19e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 64.20 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 616 TKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILG-ETPcVSGTIDFYG-TIAYVS-----------QTAWIQTGTIR 682
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGfETP-DSGRIMLDGqDITHVPaenrhvntvfqSYALFPHMTVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 683 DNILFGGVMD-------EHRYRETIQKSSLDkdlellpdgdqtEIGERGV-NLSGGQKQRIQLARALYQDADIYLLDDPF 754
Cdd:PRK09452 105 ENVAFGLRMQktpaaeiTPRVMEALRMVQLE------------EFAQRKPhQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331862 755 SAVDAHTASSLFQEyvMDALA---GKAVLLVTH-QVDFLPAFDSVLLMSDGEITEADTYQE 811
Cdd:PRK09452 173 SALDYKLRKQMQNE--LKALQrklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
614-842 |
2.21e-10 |
|
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: 65.09 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 614 GSTKPNLRNVSLEVKFGEKVAVCGEVGSGKS-TLLaAILGETP----CVSGTIDFYGT-----------------IAYVS 671
Cdd:COG4172 20 GGTVEAVKGVSFDIAAGETLALVGESGSGKSvTAL-SILRLLPdpaaHPSGSILFDGQdllglserelrrirgnrIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 672 Q---TAWIQTGTIRDNIlfGGVMDEHRyretiqksSLDKD------LELLpdgDQTEI--GERGVN-----LSGGQKQRI 735
Cdd:COG4172 99 QepmTSLNPLHTIGKQI--AEVLRLHR--------GLSGAaararaLELL---ERVGIpdPERRLDayphqLSGGQRQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 736 QLARALYQDADIYLLDDPFSAVDAHTasslfQEYVMDALA------GKAVLLVTHqvDfLP-----AfDSVLLMSDGEIT 804
Cdd:COG4172 166 MIAMALANEPDLLIADEPTTALDVTV-----QAQILDLLKdlqrelGMALLLITH--D-LGvvrrfA-DRVAVMRQGEIV 236
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 22331862 805 EADTYQELLARSRD--FQDLVNAhrETAGSERVVAVENPT 842
Cdd:COG4172 237 EQGPTAELFAAPQHpyTRKLLAA--EPRGDPRPVPPDAPP 274
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
620-784 |
2.38e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 62.75 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAI-----LGETPCVSGTIDFYGT---------------IAYVSQTAWIQTG 679
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndLIPGARVEGEILLDGEdiydpdvdvvelrrrVGMVFQKPNPFPK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 680 TIRDNILFG---------GVMDEhRYRETIQKSSL-D--KDlellpdgdqtEIGERGVNLSGGQKQRIQLARALYQDADI 747
Cdd:COG1117 107 SIYDNVAYGlrlhgikskSELDE-IVEESLRKAALwDevKD----------RLKKSALGLSGGQQQRLCIARALAVEPEV 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 22331862 748 YLLDDPFSAVDAHTASSLfqEYVMDALAGK-AVLLVTH 784
Cdd:COG1117 176 LLMDEPTSALDPISTAKI--EELILELKKDyTIVIVTH 211
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
607-789 |
2.56e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.90 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 607 SFSWEEKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPC--VSGTIDfygtiayVSQTAWIQTGTIRDN 684
Cdd:COG2401 33 AFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGtpVAGCVD-------VPDNQFGREASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 685 ILfggvmdehryretiQKSSLDKDLELLPD---GDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHT 761
Cdd:COG2401 106 IG--------------RKGDFKDAVELLNAvglSDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180 190
....*....|....*....|....*....|.
gi 22331862 762 A---SSLFQEYVMDalAGKAVLLVTHQVDFL 789
Cdd:COG2401 172 AkrvARNLQKLARR--AGITLVVATHHYDVI 200
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
620-806 |
2.67e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 62.64 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT------IAYVSQ--------TAWiqtGTIRDN- 684
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrdLYALSEaerrrllrTEW---GFVHQHp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 685 -------ILFGGVMDE------HRYRETIQKSSLD--KDLELlpdgDQTEIGERGVNLSGGQKQRIQLARALYQDADIYL 749
Cdd:PRK11701 99 rdglrmqVSAGGNIGErlmavgARHYGDIRATAGDwlERVEI----DAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVF 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 750 LDDPFSAVDAHTasslfQEYVMDAL------AGKAVLLVTHQ--VDFLPAfDSVLLMSDGEITEA 806
Cdd:PRK11701 175 MDEPTGGLDVSV-----QARLLDLLrglvreLGLAVVIVTHDlaVARLLA-HRLLVMKQGRVVES 233
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1207-1428 |
2.69e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 62.80 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESPL-VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFG 1285
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1286 IIPQDP--TLFNGTVRFNLDPLCQHSDAEIWEVLGKCQLKEVVQekeNGLDsLVVEDGSNWSMGQRQLFCLGRAVLRRSR 1363
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAV---NMLD-FKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 1364 VLVLDEATASIDNATDLILQKTIrREFAD---CTVITVAHRIPTVMDCTMVLSISDGRIVEYDEPMKL 1428
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVI-HEIKEkyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
891-1090 |
2.73e-10 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 63.19 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 891 IFFFIASLAQVTF------AVGQILQNSWMAANVDNPQVstLKLILVYLLIGLCSVLCLMVRSVCVVIMCMKSSASLFSQ 964
Cdd:cd18547 6 ILAIISTLLSVLGpyllgkAIDLIIEGLGGGGGVDFSGL--LRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 965 LLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLIFVVASSVNTGCSLGVLAIVTWQ---VLFVSVPMVYLAFR 1041
Cdd:cd18547 84 LFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLltlIVLVTVPLSLLVTK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 22331862 1042 L-----QKYYFQTAKELMRINGttrsyvanHLAESVAGAITIRAFDEEERFFKK 1090
Cdd:cd18547 164 FiakrsQKYFRKQQKALGELNG--------YIEEMISGQKVVKAFNREEEAIEE 209
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1223-1421 |
3.24e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 62.81 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1223 VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGG-----KIVVDGVDISKI-GVHDLRSRFGIIPQDPTLFNG 1296
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1297 TVRFNLdplcqHSDAEIWEVLGKCQLKEVVQEK--ENGLDSLVVEDGSN----WSMGQRQLFCLGRAVLRRSRVLVLDEA 1370
Cdd:PRK14271 116 SIMDNV-----LAGVRAHKLVPRKEFRGVAQARltEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 22331862 1371 TASIDNATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSI-SDGRIVE 1421
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALfFDGRLVE 242
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
612-822 |
3.67e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 62.42 E-value: 3.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 612 EKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTL-------------LAAILGETPCVSGTIDFYGTIAYVSQTAWIQ- 677
Cdd:PRK13642 15 EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTarlidglfeefegKVKIDGELLTAENVWNLRRKIGMVFQNPDNQf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 678 -TGTIRDNILFGgVMDEHRYRETIQKSSldkDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSA 756
Cdd:PRK13642 95 vGATVEDDVAFG-MENQGIPREEMIKRV---DEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSM 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22331862 757 VDAHTASSLFQeyVMDALAGK---AVLLVTHQVDFLPAFDSVLLMSDGEITEADTYQELLARSRDFQDL 822
Cdd:PRK13642 171 LDPTGRQEIMR--VIHEIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVEI 237
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1207-1432 |
3.70e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 62.34 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESplVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGI 1286
Cdd:PRK11231 3 LRTENLTVGYGTKR--ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDPTLFNG-TVR----FNLDPLCQHsdaeiWEVLGKCQLKEVVQEKEN-GLDSLVVEDGSNWSMGQRQLFCLGRAVLR 1360
Cdd:PRK11231 81 LPQHHLTPEGiTVRelvaYGRSPWLSL-----WGRLSAEDNARVNQAMEQtRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22331862 1361 RSRVLVLDEATASIDNATDLILQKTIRR-EFADCTVITVAHRIPTVMD-CTMVLSISDGRIVEYDEPMKLMKDE 1432
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRElNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1207-1375 |
3.77e-10 |
|
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: 61.97 E-value: 3.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYrrESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKigvHDLRSR-FG 1285
Cdd:cd03296 3 IEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD---VPVQERnVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1286 IIPQDPTLF-NGTVRFNL------DPLCQH-SDAEIWEVLGkcQLKEVVQekengLDSLVVEDGSNWSMGQRQLFCLGRA 1357
Cdd:cd03296 78 FVFQHYALFrHMTVFDNVafglrvKPRSERpPEAEIRAKVH--ELLKLVQ-----LDWLADRYPAQLSGGQRQRVALARA 150
|
170
....*....|....*...
gi 22331862 1358 VLRRSRVLVLDEATASID 1375
Cdd:cd03296 151 LAVEPKVLLLDEPFGALD 168
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1223-1421 |
3.95e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 64.34 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1223 VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVePVGGKIVVDGVDISKIGVHDL---RSRFGIIPQDPtlfNGTV- 1298
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDP---NSSLn 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1299 -RFNLdplcQHSDAEIWEV----LGKCQLKEVVQE--KENGLDSLVVED-GSNWSMGQRQLFCLGRAVLRRSRVLVLDEA 1370
Cdd:PRK15134 377 pRLNV----LQIIEEGLRVhqptLSAAQREQQVIAvmEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 1371 TASID---NATDLILQKTIRREFaDCTVITVAHRIPTVMD-CTMVLSISDGRIVE 1421
Cdd:PRK15134 453 TSSLDktvQAQILALLKSLQQKH-QLAYLFISHDLHVVRAlCHQVIVLRQGEVVE 506
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
600-805 |
3.97e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 62.36 E-value: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 600 AIIIKSASFSWEekgsTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAI-----LGETPCVSGTIDFYGTIAYVS--- 671
Cdd:PRK14258 7 AIKVNNLSFYYD----TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmneLESEVRVEGRVEFFNQNIYERrvn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 672 ------QTAWIQTG------TIRDNILFGGVMDEHRYR---ETIQKSSLdKDLELLpDGDQTEIGERGVNLSGGQKQRIQ 736
Cdd:PRK14258 83 lnrlrrQVSMVHPKpnlfpmSVYDNVAYGVKIVGWRPKleiDDIVESAL-KDADLW-DEIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 737 LARALYQDADIYLLDDPFSAVDAhtASSLFQEYVMDALAGKA---VLLVTH---QVDFLPAFDSVLLMSDGEITE 805
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDP--IASMKVESLIQSLRLRSeltMVIVSHnlhQVSRLSDFTAFFKGNENRIGQ 233
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
597-812 |
4.07e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 62.51 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 597 NQNAIIIKSASFSWeeKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKST---LLAAIL--GETPCVSGTIDfygTIAYVS 671
Cdd:PRK13640 2 KDNIVEFKHVSFTY--PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLlpDDNPNSKITVD---GITLTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 672 QTAW---------IQT-------GTIRDNILFGgvmDEHRY--RETIQKSSLDkdleLLPDGDQTE-IGERGVNLSGGQK 732
Cdd:PRK13640 77 KTVWdirekvgivFQNpdnqfvgATVGDDVAFG---LENRAvpRPEMIKIVRD----VLADVGMLDyIDSEPANLSGGQK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 733 QRIQLARALYQDADIYLLDDPFSAVDAHTAS---SLFQEYVMDalAGKAVLLVTHQVDFLPAFDSVLLMSDGEITEADTY 809
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEqilKLIRKLKKK--NNLTVISITHDIDEANMADQVLVLDDGKLLAQGSP 227
|
...
gi 22331862 810 QEL 812
Cdd:PRK13640 228 VEI 230
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
620-803 |
4.42e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 62.37 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTI---------------DFYGTIAYVSQTAWIQ--TGTIR 682
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgvditdkkvklsDIRKKVGLVFQYPEYQlfEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 683 DNILFG----GVMDEH---RYRETIQKSSLDKdlELLPDGDQTEigergvnLSGGQKQRIQLARALYQDADIYLLDDPFS 755
Cdd:PRK13637 103 KDIAFGpinlGLSEEEienRVKRAMNIVGLDY--EDYKDKSPFE-------LSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 22331862 756 AVDAHT-------ASSLFQEYVMdalagkAVLLVTHQVDFLPAF-DSVLLMSDGEI 803
Cdd:PRK13637 174 GLDPKGrdeilnkIKELHKEYNM------TIILVSHSMEDVAKLaDRIIVMNKGKC 223
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
599-821 |
4.56e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 62.09 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 599 NAIIIKSASFSweeKGStKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG-TIAYVSQTAW-- 675
Cdd:PRK11831 6 NLVDMRGVSFT---RGN-RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGeNIPAMSRSRLyt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 676 --------IQTG------TIRDNILFGgvMDEH-RYRETIQKSSLDKDLEllpdgdqtEIGERGV------NLSGGQKQR 734
Cdd:PRK11831 82 vrkrmsmlFQSGalftdmNVFDNVAYP--LREHtQLPAPLLHSTVMMKLE--------AVGLRGAaklmpsELSGGMARR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 735 IQLARALYQDADIYLLDDPFSAVDAHTASSLFQeyVMDAL---AGKAVLLVTHQV-DFLPAFDSVLLMSDGEITEADTYQ 810
Cdd:PRK11831 152 AALARAIALEPDLIMFDEPFVGQDPITMGVLVK--LISELnsaLGVTCVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQ 229
|
250
....*....|....*
gi 22331862 811 ELLA----RSRDFQD 821
Cdd:PRK11831 230 ALQAnpdpRVRQFLD 244
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
630-801 |
5.11e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.13 E-value: 5.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 630 GEKVAVCGEVGSGKSTLLAAILG--ETPCVSGTI---------DFYGTIAYVSQTAWIQTG-TIRDNILFGGVMDEHRYR 697
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGriQGNNFTGTIlannrkptkQILKRTGFVTQDDILYPHlTVRETLVFCSLLRLPKSL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 698 ETIQKSSLDKDL--EL-LPDGDQTEIGE---RGVnlSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQEYVM 771
Cdd:PLN03211 174 TKQEKILVAESVisELgLTKCENTIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGS 251
|
170 180 190
....*....|....*....|....*....|..
gi 22331862 772 DALAGKAVLLVTHQVD--FLPAFDSVLLMSDG 801
Cdd:PLN03211 252 LAQKGKTIVTSMHQPSsrVYQMFDSVLVLSEG 283
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1218-1377 |
5.17e-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: 60.58 E-value: 5.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1218 RESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQDPTLFNGT 1297
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1298 VRFNLDPLCQ-HSDAEIWEVLGKCQLkevvqekeNGLDSLVVedgSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDN 1376
Cdd:cd03231 90 VLENLRFWHAdHSDEQVEEALARVGL--------NGFEDRPV---AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
.
gi 22331862 1377 A 1377
Cdd:cd03231 159 A 159
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1213-1433 |
5.58e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 61.71 E-value: 5.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1213 QIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQDPT 1292
Cdd:PRK13548 7 NLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1293 L-FNGTVR----FNLDPLCQHSDaeiwevlgkcQLKEVVQEK--ENGLDSLVVEDGSNWSMGQRQLFCLGRaVL------ 1359
Cdd:PRK13548 87 LsFPFTVEevvaMGRAPHGLSRA----------EDDALVAAAlaQVDLAHLAGRDYPQLSGGEQQRVQLAR-VLaqlwep 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22331862 1360 -RRSRVLVLDEATASIDNATDLILQKTIRReFAD---CTVITVAHRIP-TVMDCTMVLSISDGRIVEYDEPMKLMKDEN 1433
Cdd:PRK13548 156 dGPPRWLLLDEPTSALDLAHQHHVLRLARQ-LAHergLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLTPET 233
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
601-815 |
5.87e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 61.95 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 601 IIIKSASFSWEEKGSTK-PNLRNVSLEVKFGEKVAVCGEVGSGKSTLLA------------AILGETPCVSG------TI 661
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEfKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqTIVGDYAIPANlkkikeVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 662 DFYGTIAYVSQTAWIQ--TGTIRDNILFGGVMDEHRYRETIQKSSLDKDLELLPDgdqtEIGERG-VNLSGGQKQRIQLA 738
Cdd:PRK13645 87 RLRKEIGLVFQFPEYQlfQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPE----DYVKRSpFELSGGQKRRVALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 739 RALYQDADIYLLDDPFSAVDAHTASSLFQEYV-MDALAGKAVLLVTHQVD-FLPAFDSVLLMSDGEIT------EADTYQ 810
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFErLNKEYKKRIIMVTHNMDqVLRIADEVIVMHEGKVIsigspfEIFSNQ 242
|
....*
gi 22331862 811 ELLAR 815
Cdd:PRK13645 243 ELLTK 247
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1223-1400 |
6.00e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 60.33 E-value: 6.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1223 VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGvdiskigvhdlRSRFGIIPQ---DPTLFNGTVR 1299
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrseVPDSLPLTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1300 fNLDPLCQHSDAEIWEVLGKCQLKEVVQEKEN-GLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNAT 1378
Cdd:NF040873 76 -DLVAMGRWARRGLWRRLTRDDRAAVDDALERvGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180
....*....|....*....|...
gi 22331862 1379 DLILQKTIRREFAD-CTVITVAH 1400
Cdd:NF040873 155 RERIIALLAEEHARgATVVVVTH 177
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1207-1424 |
7.79e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.21 E-value: 7.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYrrESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVE-----PVGGKIVVDGVDI--SKIGVHD 1279
Cdd:PRK14258 8 IKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1280 LRSRFGIIPQDPTLFNGTV---------------RFNLDPLCQHS--DAEIWEvlgkcqlkevvqEKENGLDSLVVEdgs 1342
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVydnvaygvkivgwrpKLEIDDIVESAlkDADLWD------------EIKHKIHKSALD--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1343 nWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIR--REFADCTVITVAHRIPTVM---DCTMVLSISDG 1417
Cdd:PRK14258 151 -LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSrlsDFTAFFKGNEN 229
|
....*..
gi 22331862 1418 RIVEYDE 1424
Cdd:PRK14258 230 RIGQLVE 236
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1223-1417 |
8.20e-10 |
|
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: 61.41 E-value: 8.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1223 VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGvdiskigvhdlrsRFGIIPQDPTLFNGTVRFNL 1302
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1303 DPLCQHSDAEIWEVLGKCQLKEVVQ---EKENgldSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATD 1379
Cdd:cd03291 119 IFGVSYDEYRYKSVVKACQLEEDITkfpEKDN---TVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190
....*....|....*....|....*....|....*....
gi 22331862 1380 L-ILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDG 1417
Cdd:cd03291 196 KeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1177-1423 |
8.74e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.16 E-value: 8.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1177 RLNQYTHLTPEAPEVIEETrPPVNWPVTGR-----VEISDLQIRYrrESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLI 1251
Cdd:COG0488 282 RIKALEKLEREEPPRRDKT-VEIRFPPPERlgkkvLELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1252 SALFRLVEPVGGKIvvdgvdisKIGvHDLrsRFGIIPQDPTLFNG--TVrfnLDPLCQHSD----AEIWEVLGK------ 1319
Cdd:COG0488 359 KLLAGELEPDSGTV--------KLG-ETV--KIGYFDQHQEELDPdkTV---LDELRDGAPggteQEVRGYLGRflfsgd 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1320 CQLKEVvqekenglDSLvvedgsnwSMGQRQLFCLGRAVLRRSRVLVLDEAT-----ASIDNATDLILqktirrEFaDCT 1394
Cdd:COG0488 425 DAFKPV--------GVL--------SGGEKARLALAKLLLSPPNVLLLDEPTnhldiETLEALEEALD------DF-PGT 481
|
250 260 270
....*....|....*....|....*....|....*
gi 22331862 1395 VITVAH------RIptvmdCTMVLSISDGRIVEYD 1423
Cdd:COG0488 482 VLLVSHdryfldRV-----ATRILEFEDGGVREYP 511
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
630-802 |
8.82e-10 |
|
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: 58.54 E-value: 8.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 630 GEKVAVCGEVGSGKSTLLAAILGETPCVSgtidfyGTIAYVSqtawiqtgtirdnilfggvMDEHRYRETIQKSsldkdl 709
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPG------GGVIYID-------------------GEDILEEVLDQLL------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 710 ellpdgdQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQEYVMDAL------AGKAVLLVT 783
Cdd:smart00382 51 -------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLlllkseKNLTVILTT 123
|
170 180
....*....|....*....|....*
gi 22331862 784 HQVDFL------PAFDSVLLMSDGE 802
Cdd:smart00382 124 NDEKDLgpallrRRFDRRIVLLLIL 148
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1208-1406 |
1.02e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 59.80 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1208 EISDLQIRyRRESPLVlKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEP---VGGKIVVDGVDISKIGVHdlRSRF 1284
Cdd:COG4136 3 SLENLTIT-LGGRPLL-APLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1285 GIIPQDPTLF-NGTVRFNLD---PlcqhsdaeiwEVLGKCQLKEVVQE--KENGLDSLVVEDGSNWSMGQRQLFCLGRAV 1358
Cdd:COG4136 79 GILFQDDLLFpHLSVGENLAfalP----------PTIGRAQRRARVEQalEEAGLAGFADRDPATLSGGQRARVALLRAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 22331862 1359 LRRSRVLVLDEATASIDnatdlilqKTIRREFADCTVITVAHR-IPTVM 1406
Cdd:COG4136 149 LAEPRALLLDEPFSKLD--------AALRAQFREFVFEQIRQRgIPALL 189
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1223-1432 |
1.06e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.16 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1223 VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQDPTLFNG-TV--- 1298
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVqel 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1299 ----RFNLDPLCQHSDAEIWEVLGKCQlkevvqeKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASI 1374
Cdd:PRK10253 102 vargRYPHQPLFTRWRKEDEEAVTKAM-------QATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331862 1375 D--NATDLI-LQKTIRREfADCTVITVAHRIPTVMD-CTMVLSISDGRIVEYDEPMKLMKDE 1432
Cdd:PRK10253 175 DisHQIDLLeLLSELNRE-KGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIVTAE 235
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1207-1435 |
1.12e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 61.33 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESPL---VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDI-SKIG---VHD 1279
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1280 LRSRFGIIPQDP--TLFNGTVrfnldplcqhsDAEIweVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRA 1357
Cdd:PRK13646 83 VRKRIGMVFQFPesQLFEDTV-----------EREI--IFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1358 VLRR----------SRVLVLDEATASID-NATDLILQ--KTIRREfADCTVITVAHRIPTV---MDCTMVLsiSDGRIVE 1421
Cdd:PRK13646 150 QMRKiaivsilamnPDIIVLDEPTAGLDpQSKRQVMRllKSLQTD-ENKTIILVSHDMNEVaryADEVIVM--KEGSIVS 226
|
250
....*....|....
gi 22331862 1422 YDEPMKLMKDENSL 1435
Cdd:PRK13646 227 QTSPKELFKDKKKL 240
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
617-789 |
1.21e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.65 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 617 KPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGetpcvsgtID--FYG--------TIAYVSQTAWI-QTGTIRDNI 685
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--------VDkdFNGearpqpgiKVGYLPQEPQLdPTKTVRENV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 686 LFG-----GVMDEH----------------------RYRETIQKS---SLDKDLEL------LPDGDQteigeRGVNLSG 729
Cdd:TIGR03719 90 EEGvaeikDALDRFneisakyaepdadfdklaaeqaELQEIIDAAdawDLDSQLEIamdalrCPPWDA-----DVTKLSG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331862 730 GQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSL---FQEYvmdalAGkAVLLVTHQVDFL 789
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLerhLQEY-----PG-TVVAVTHDRYFL 221
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1238-1420 |
1.40e-09 |
|
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: 61.66 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1238 GIVGRTGSGKTTLISALFRLVEPVGGKIVVDG---VDISK---IGVHdlRSRFGIIPQDPTLFNG-TVRFNLD------- 1303
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARgifLPPH--RRRIGYVFQEARLFPHlSVRGNLLygrkrap 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1304 -PLCQHSDAEIWEVLGkcqLKEVVQEKENGLdslvvedgsnwSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNAT-DLI 1381
Cdd:COG4148 107 rAERRISFDEVVELLG---IGHLLDRRPATL-----------SGGERQRVAIGRALLSSPRLLLMDEPLAALDLARkAEI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 22331862 1382 LQ--KTIRREFaDCTVITVAHRIPTVM---DcTMVLsISDGRIV 1420
Cdd:COG4148 173 LPylERLRDEL-DIPILYVSHSLDEVArlaD-HVVL-LEQGRVV 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
600-805 |
1.50e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 60.03 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 600 AIIIKSASFSWeekGSTKPnLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAI-LGETPcVSGTIDFYGTIAYVSQTAWIQT 678
Cdd:PRK11124 2 SIQLNGINCFY---GAHQA-LFDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMP-RSGTLNIAGNHFDFSKTPSDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 679 G-TIRDNIlfGGVMDEH-----------------RYRETIQKSSLDKDLELLPDGDQTEIGER-GVNLSGGQKQRIQLAR 739
Cdd:PRK11124 77 IrELRRNV--GMVFQQYnlwphltvqqnlieapcRVLGLSKDQALARAEKLLERLRLKPYADRfPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331862 740 ALYQDADIYLLDDPFSAVDAH-TAS--SLFQEyvmdaLAGKAV--LLVTHQVDFLPAFDS-VLLMSDGEITE 805
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEiTAQivSIIRE-----LAETGItqVIVTHEVEVARKTASrVVYMENGHIVE 221
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1207-1425 |
1.82e-09 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 61.32 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESplVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDIsKIGVHDLRSRFGI 1286
Cdd:COG1118 3 IEVRNISKRFGSFT--LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPPRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDPTLF-NGTVR----FNLDPLcQHSDAEIwevlgkcqlKEVVQE--KENGLDSLvvED--GSNWSMGQRQLFCLGRA 1357
Cdd:COG1118 80 VFQHYALFpHMTVAeniaFGLRVR-PPSKAEI---------RARVEEllELVQLEGL--ADryPSQLSGGQRQRVALARA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22331862 1358 VLRRSRVLVLDEATASIDNAtdliLQKTIRR-------EFaDCTVITVAHRIPTVMD-CTMVLSISDGRIVEYDEP 1425
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDAK----VRKELRRwlrrlhdEL-GGTTVFVTHDQEEALElADRVVVMNQGRIEQVGTP 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
601-815 |
1.88e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 60.97 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 601 IIIKSASFSWEEKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAI-LGETPcVSGTIDFYGT-IAYVSQTAWI-- 676
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCInLLERP-TSGRVLVDGQdLTALSEKELRka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 677 --QTG------------TIRDNILFGGVMDeHRYRETIQKssldKDLELLpdgDQTEIGERG----VNLSGGQKQRIQLA 738
Cdd:PRK11153 81 rrQIGmifqhfnllssrTVFDNVALPLELA-GTPKAEIKA----RVTELL---ELVGLSDKAdrypAQLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 739 RALYQDADIYLLDDPFSAVDAHTASSlfqeyVMDALA------GKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQE 811
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRS-----ILELLKdinrelGLTIVLITHEMDVVKRIcDRVAVIDAGRLVEQGTVSE 227
|
....
gi 22331862 812 LLAR 815
Cdd:PRK11153 228 VFSH 231
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
626-756 |
1.90e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.13 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 626 EVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGTIAYVSQtaWI---QTGTIRDniLFGGVMDehRYRETIQK 702
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQ--YIkpdYDGTVED--LLRSITD--DLGSSYYK 434
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 703 SSLDKDLELlpdgdqTEIGERGVN-LSGGQKQRIQLARALYQDADIYLLDDPfSA 756
Cdd:PRK13409 435 SEIIKPLQL------ERLLDKNVKdLSGGELQRVAIAACLSRDADLYLLDEP-SA 482
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1223-1423 |
1.91e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.99 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1223 VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIG---VHDLrsrfGI--IPQDPTLF-NG 1296
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakAHQL----GIylVPQEPLLFpNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1297 TVRFN-LDPLCQHSDAeiwevlgKCQLKEVVQEKENGLD------SLVVEDgsnwsmgqRQLFCLGRAVLRRSRVLVLDE 1369
Cdd:PRK15439 102 SVKENiLFGLPKRQAS-------MQKMKQLLAALGCQLDldssagSLEVAD--------RQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 1370 ATASIDNATDLILQKTIRREFA-DCTVITVAHRIP---------TVM-DCTMVLSisdGRIVEYD 1423
Cdd:PRK15439 167 PTASLTPAETERLFSRIRELLAqGVGIVFISHKLPeirqladriSVMrDGTIALS---GKTADLS 228
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
615-813 |
2.04e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.95 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 615 STKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPcVSGTIDFYGTI-------------AYVSQtawiqtgti 681
Cdd:PRK03695 7 AVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPleawsaaelarhrAYLSQ--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 682 RDNILFggVMDEHRYretiqkssldkdLEL-LPDGDQTEIGERGVN------------------LSGGQKQRIQLARALY 742
Cdd:PRK03695 77 QQTPPF--AMPVFQY------------LTLhQPDKTRTEAVASALNevaealglddklgrsvnqLSGGEWQRVRLAAVVL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 743 Q-------DADIYLLDDPFSAVDahtassLFQEYVMDAL------AGKAVLLVTHQVDF-LPAFDSVLLMSDGEITEADT 808
Cdd:PRK03695 143 QvwpdinpAGQLLLLDEPMNSLD------VAQQAALDRLlselcqQGIAVVMSSHDLNHtLRHADRVWLLKQGKLLASGR 216
|
....*
gi 22331862 809 YQELL 813
Cdd:PRK03695 217 RDEVL 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1207-1420 |
2.11e-09 |
|
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: 59.19 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYrrESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDlRSrFGI 1286
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-RD-IAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDPTLF-NGTVRFNLD-PLCQHS------DAEIWEVLGKCQLKEVVQEKENGLdslvvedgsnwSMGQRQLFCLGRAV 1358
Cdd:cd03301 77 VFQNYALYpHMTVYDNIAfGLKLRKvpkdeiDERVREVAELLQIEHLLDRKPKQL-----------SGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 1359 LRRSRVLVLDEATASIDNAtdliLQKTIRREFA------DCTVITVAHriptvmDCTMVLSISDgRIV 1420
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAK----LRVQMRAELKrlqqrlGTTTIYVTH------DQVEAMTMAD-RIA 202
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
602-817 |
2.25e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.20 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 602 IIKSASFSWEEKGSTKPnLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG-------------TIA 668
Cdd:PRK13652 3 LIETRDLCYSYSGSKEA-LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkenirevrkFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 669 YVSQTA--WIQTGTIRDNILFGGV---MDE----HRYRETIQKSSLDKDLELLPDgdqteigergvNLSGGQKQRIQLAR 739
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPInlgLDEetvaHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 740 ALYQDADIYLLDDPFSAVDAHTASSLFQeyVMDALA---GKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQE---- 811
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELID--FLNDLPetyGMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEiflq 228
|
....*...
gi 22331862 812 --LLARSR 817
Cdd:PRK13652 229 pdLLARVH 236
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
622-758 |
2.51e-09 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 60.52 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 622 NVSLEVKFGEKVAVCGEVGSGKSTLLAAILG-ETPcVSGTIDFYGT-IAYVSQTAW------IQT------------GTI 681
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRlEEP-TSGEILFDGQdITGLSGRELrplrrrMQMvfqdpyaslnprMTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 682 RDNILFG----GVMDEHRYRETIQkssldkdlELLpdgdqteigER-GVN----------LSGGQKQRIQLARALYQDAD 746
Cdd:COG4608 115 GDIIAEPlrihGLASKAERRERVA--------ELL---------ELvGLRpehadrypheFSGGQRQRIGIARALALNPK 177
|
170
....*....|..
gi 22331862 747 IYLLDDPFSAVD 758
Cdd:COG4608 178 LIVCDEPVSALD 189
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
620-822 |
2.53e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.18 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG-TIAYVSQTAWIQTgtIRDNIlfGGVM---DEHR 695
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDiTITHKTKDKYIRP--VRKRI--GMVFqfpESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 696 YRETIQKSSL--------------DKDLELLPD-GDQTEIGERG-VNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDA 759
Cdd:PRK13646 99 FEDTVEREIIfgpknfkmnldevkNYAHRLLMDlGFSRDVMSQSpFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 760 ---HTASSLFQEYVMDalAGKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQELLARSRDFQDL 822
Cdd:PRK13646 179 qskRQVMRLLKSLQTD--ENKTIILVSHDMNEVARYaDEVIVMKEGSIVSQTSPKELFKDKKKLADW 243
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
622-784 |
2.53e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 61.00 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 622 NVSLEVKFGEKVAVCGEVGSGKSTLLAAILG-ETPcVSGTIDFYGT-----------IAYVSQT-AWIQTGTIRDNILFG 688
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQP-TAGQIMLDGVdlshvppyqrpINMMFQSyALFPHMTVEQNIAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 689 GVMDEHRYRETIQKSSldkdlELLPDGDQTEIGERGVN-LSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLfQ 767
Cdd:PRK11607 116 LKQDKLPKAEIASRVN-----EMLGLVHMQEFAKRKPHqLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRM-Q 189
|
170
....*....|....*....
gi 22331862 768 EYVMDAL--AGKAVLLVTH 784
Cdd:PRK11607 190 LEVVDILerVGVTCVMVTH 208
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1213-1400 |
2.55e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 58.96 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1213 QIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQDPT 1292
Cdd:PRK10247 12 NVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1293 LFNGTVRFNLdplcqhsdAEIWEVLGKC-QLKEVVQEKEN-GLDSLVVEDGSN-WSMGQRQLFCLGRAVLRRSRVLVLDE 1369
Cdd:PRK10247 92 LFGDTVYDNL--------IFPWQIRNQQpDPAIFLDDLERfALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190
....*....|....*....|....*....|...
gi 22331862 1370 ATASIDNATDLILQKTIRREFAD--CTVITVAH 1400
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREqnIAVLWVTH 196
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1207-1400 |
3.80e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 59.02 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESplVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRL--VEP---VGGKIVVDGVDI--SKIGVHD 1279
Cdd:PRK14239 6 LQVSDLSVYYNKKK--ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIysPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1280 LRSRFGIIPQDPTLFNGTVRFN---------------LDPLCQHS--DAEIWEvlgkcQLKEVVQEKENGLdslvvedgs 1342
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIYENvvyglrlkgikdkqvLDEAVEKSlkGASIWD-----EVKDRLHDSALGL--------- 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 1343 nwSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIRREFADCTVITVAH 1400
Cdd:PRK14239 150 --SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR 205
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1221-1419 |
4.24e-09 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 57.44 E-value: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1221 PLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDL-----------RSRFGIIPQ 1289
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiragiayvpedRKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1290 DPTLFNGTVRFNLdplcqhsdaeiwevlgkcqlkevvqekengldslvvedgsnwSMGQRQLFCLGRAVLRRSRVLVLDE 1369
Cdd:cd03215 93 LSVAENIALSSLL------------------------------------------SGGNQQKVVLARWLARDPRVLILDE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22331862 1370 ATASIDNATDLILQKTIrREFAD--CTVITVAHRIPTVMD-CTMVLSISDGRI 1419
Cdd:cd03215 131 PTRGVDVGAKAEIYRLI-RELADagKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
620-803 |
4.35e-09 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 58.90 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT--------------IAYVSQTAWIQTG-TIRDN 684
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRditglpphriarlgIARTFQNPRLFPElTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 685 ILFGGvmdEHRYRETIQKSSL-------------DKDLELLpdgDQTEIGERG----VNLSGGQKQRIQLARALYQDADI 747
Cdd:COG0411 100 VLVAA---HARLGRGLLAALLrlprarreerearERAEELL---ERVGLADRAdepaGNLSYGQQRRLEIARALATEPKL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 748 YLLDDPF---SAVDAHTASSLFQEyvMDALAGKAVLLVTHQVDFLPAF-DSVLLMSDGEI 803
Cdd:COG0411 174 LLLDEPAaglNPEETEELAELIRR--LRDERGITILLIEHDMDLVMGLaDRIVVLDFGRV 231
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1216-1435 |
4.66e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 59.46 E-value: 4.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1216 YRRESPLVLKG---ISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDI----SKIGVHDLRSRFGIIP 1288
Cdd:PRK13641 12 YSPGTPMEKKGldnISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKKLRKKVSLVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1289 QDP--TLFNGTV----RF---NLDPLCQHSDAEIWEVLGKCQLKEVVQEKENgldslvvedgSNWSMGQRQLFCLGRAVL 1359
Cdd:PRK13641 92 QFPeaQLFENTVlkdvEFgpkNFGFSEDEAKEKALKWLKKVGLSEDLISKSP----------FELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 1360 RRSRVLVLDEATASID-NATDLILQKTIRREFADCTVITVAHRIPTVMD-CTMVLSISDGRIVEYDEPMKLMKDENSL 1435
Cdd:PRK13641 162 YEPEILCLDEPAAGLDpEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDKEWL 239
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1173-1390 |
4.92e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 60.76 E-value: 4.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1173 ISVERLNQYtHLTPEAPEvIEETRPPVNWPvtgRVEISDLQIRYRRESpLVLKGISCTFEGGHKIGIVGRTGSGKTTLIS 1252
Cdd:PRK10522 294 VAFNKLNKL-ALAPYKAE-FPRPQAFPDWQ---TLELRNVTFAYQDNG-FSVGPINLTIKRGELLFLIGGNGSGKSTLAM 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1253 ALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQDPTLFNGTvrfnLDPLCQHSDAEIWEV-LGKCQLKEVVQEKEN 1331
Cdd:PRK10522 368 LLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALVEKwLERLKMAHKLELEDG 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 22331862 1332 GLDSLvvedgsNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDnatdlilqKTIRREF 1390
Cdd:PRK10522 444 RISNL------KLSKGQKKRLALLLALAEERDILLLDEWAADQD--------PHFRREF 488
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
412-815 |
5.79e-09 |
|
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: 60.58 E-value: 5.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 412 LIALGILfhSVGVATFSALAVIILTVLCNAPIAKLQNKFQsELMTSQDERLKACnESLVN-MKVLKLYA------WESHF 484
Cdd:COG4615 139 LAYLAWL--SPPLFLLTLVLLGLGVAGYRLLVRRARRHLR-RAREAEDRLFKHF-RALLEgFKELKLNRrrrrafFDEDL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 485 KKVIEKLRNIELKSlkavqmrkaynAVLFWSSPVFVSAATFAT---CYFL---DIPLRASNVFTFVATLRLVQDPVRMIP 558
Cdd:COG4615 215 QPTAERYRDLRIRA-----------DTIFALANNWGNLLFFALiglILFLlpaLGWADPAVLSGFVLVLLFLRGPLSQLV 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 559 DVIGVTIQAKVAFSRIATF---LEAPELQGGERRRKQRSEGNQnAIIIKSASFS-WEEKGSTKPNLRNVSLEVKFGEKVA 634
Cdd:COG4615 284 GALPTLSRANVALRKIEELelaLAAAEPAAADAAAPPAPADFQ-TLELRGVTYRyPGEDGDEGFTLGPIDLTIRRGELVF 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 635 VCGEVGSGKSTLLAAILGETPCVSGTIDFYGTI-------AYVSQTAWIQTgtirDNILFGGVMDEHRYRETIQKSSLDK 707
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPvtadnreAYRQLFSAVFS----DFHLFDRLLGLDGEADPARARELLE 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 708 DLELlpdGDQTEIgERG----VNLSGGQKQRIQLARALYQDADIYLLD------DP-FSAVdahtasslFQEYVMDAL-- 774
Cdd:COG4615 439 RLEL---DHKVSV-EDGrfstTDLSQGQRKRLALLVALLEDRPILVFDewaadqDPeFRRV--------FYTELLPELka 506
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 22331862 775 AGKAVLLVTHQVDFLPAFDSVLLMSDGEITEADTYQELLAR 815
Cdd:COG4615 507 RGKTVIAISHDDRYFDLADRVLKMDYGKLVELTGPAALAAS 547
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
595-812 |
6.19e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 58.61 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 595 EGNQNAIIIKSASFSWEekGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTI------------- 661
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYQ--SDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 662 DFYGTIAYVSQTAWIQ--TGTIRDNILFGgvMDEHR--YRETIQKSSldkdlELLPDGDQTEIGERGVN-LSGGQKQRIQ 736
Cdd:PRK13648 80 KLRKHIGIVFQNPDNQfvGSIVKYDVAFG--LENHAvpYDEMHRRVS-----EALKQVDMLERADYEPNaLSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 737 LARALYQDADIYLLDDPFSAVDAHTASSLFqEYVMDALAGKAVLL--VTHQVDFLPAFDSVLLMSDGEITEADTYQEL 812
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLL-DLVRKVKSEHNITIisITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
635-810 |
6.48e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 59.09 E-value: 6.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 635 VCGEVGSGKSTLLAAILGETPCVSGTI---DFYG--------------------------TIAYVSQTAWIQ--TGTIRD 683
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIqvgDIYIgdkknnhelitnpyskkiknfkelrrRVSMVFQFPEYQlfKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 684 NILFGGV-MDEHRYRET------IQKSSLDKD-LELLPDGdqteigergvnLSGGQKQRIQLARALYQDADIYLLDDPFS 755
Cdd:PRK13631 137 DIMFGPVaLGVKKSEAKklakfyLNKMGLDDSyLERSPFG-----------LSGGQKRRVAIAGILAIQPEILIFDEPTA 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 756 AVDAHTASSLFQeYVMDALA-GKAVLLVTHQVD-FLPAFDSVLLMSDGEI-TEADTYQ 810
Cdd:PRK13631 206 GLDPKGEHEMMQ-LILDAKAnNKTVFVITHTMEhVLEVADEVIVMDKGKIlKTGTPYE 262
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
607-801 |
6.61e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 57.25 E-value: 6.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 607 SFSWEE-------KGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLL--AAILGETPCVSGTI---------DFYGTIA 668
Cdd:cd03232 3 VLTWKNlnytvpvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLdvLAGRKTAGVITGEIlingrpldkNFQRSTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 669 YVSQT-AWIQTGTIRDNILFGGVMdehryretiqkssldkdlellpdgdqteigeRGvnLSGGQKQRIQLARALYQDADI 747
Cdd:cd03232 83 YVEQQdVHSPNLTVREALRFSALL-------------------------------RG--LSVEQRKRLTIGVELAAKPSI 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 22331862 748 YLLDDPFSAVDAHTASSLFQEYVMDALAGKAVLLVTHQ--VDFLPAFDSVLLMSDG 801
Cdd:cd03232 130 LFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQpsASIFEKFDRLLLLKRG 185
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
597-812 |
7.16e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 58.56 E-value: 7.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 597 NQNAIIIKSASFSWE--EKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTL---LAAILGETpcvSGTIDFYGTIAYVS 671
Cdd:PRK13633 1 MNEMIKCKNVSYKYEsnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALLIPS---EGKVYVDGLDTSDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 672 QTAWiqtgTIR----------DNILFGGVMDEhryretiqkssldkDLELLPDG---DQTEIGER------GVN------ 726
Cdd:PRK13633 78 ENLW----DIRnkagmvfqnpDNQIVATIVEE--------------DVAFGPENlgiPPEEIRERvdeslkKVGmyeyrr 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 727 -----LSGGQKQRIQLARALYQDADIYLLDDPFSAVDA-------HTASSLFQEYvmdalaGKAVLLVTHQVDFLPAFDS 794
Cdd:PRK13633 140 haphlLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPsgrrevvNTIKELNKKY------GITIILITHYMEEAVEADR 213
|
250
....*....|....*...
gi 22331862 795 VLLMSDGEITEADTYQEL 812
Cdd:PRK13633 214 IIVMDSGKVVMEGTPKEI 231
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
620-815 |
7.30e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 58.97 E-value: 7.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-IAYvsqtawiqtgTIRDNIlfgGVMDEHR--Y 696
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEpLDP----------EDRRRI---GYLPEERglY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 697 -----RETIQ-------------KSSLDKDLELLpdgdqtEIGERG---V-NLSGGQKQRIQLARALYQDADIYLLDDPF 754
Cdd:COG4152 84 pkmkvGEQLVylarlkglskaeaKRRADEWLERL------GLGDRAnkkVeELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331862 755 SAVDAhTASSLFQEYVMD-ALAGKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQELLAR 815
Cdd:COG4152 158 SGLDP-VNVELLKDVIRElAAKGTTVIFSSHQMELVEELcDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
928-1098 |
7.93e-09 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 58.63 E-value: 7.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 928 LILVYLLIGLCSVLCLMVRSVCVVIMCMKSSASLFSQLLNSLFRAPMSFYDSTPLGRILSRVSSDL-SIVDLdVPFGLIF 1006
Cdd:cd18545 42 IALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVnSLSDL-LSNGLIN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1007 VVASSVNTGCSLGVLAIVTWQ---VLFVSVP-MVYLAFRLQKYyfqtAKELMRINGTTRSYVANHLAESVAGAITIRAFD 1082
Cdd:cd18545 121 LIPDLLTLVGIVIIMFSLNVRlalVTLAVLPlLVLVVFLLRRR----ARKAWQRVRKKISNLNAYLHESISGIRVIQSFA 196
|
170 180
....*....|....*....|
gi 22331862 1083 EE----ERFFKKSLTLIDTN 1098
Cdd:cd18545 197 REdeneEIFDELNRENRKAN 216
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1209-1423 |
8.19e-09 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 57.73 E-value: 8.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1209 ISDLQIRYRRESPLV--LKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKiGVHDLRSRFGI 1286
Cdd:cd03267 20 IGSLKSLFKRKYREVeaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK-RRKKFLRRIGV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 I------------PQDPTLFNGTVrFNLDPL-CQHSDAEIWEVLgkcQLKEVvqekengLDSLVvedgSNWSMGQRQLFC 1353
Cdd:cd03267 99 VfgqktqlwwdlpVIDSFYLLAAI-YDLPPArFKKRLDELSELL---DLEEL-------LDTPV----RQLSLGQRMRAE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331862 1354 LGRAVLRRSRVLVLDEATASIDNATDLILQKTIRREFAD--CTVITVAHRIPTVMD-CTMVLSISDGRIVeYD 1423
Cdd:cd03267 164 IAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErgTTVLLTSHYMKDIEAlARRVLVIDKGRLL-YD 235
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
566-789 |
1.02e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.56 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 566 QAKvAFSRIATFleaPELQGGERrrKQRSEGNQnaIIIKSAsfsweekgstkPNLRNVSLEVK-----FGEK-------- 632
Cdd:TIGR03719 283 QAK-SKARLARY---EELLSQEF--QKRNETAE--IYIPPG-----------PRLGDKVIEAEnltkaFGDKlliddlsf 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 633 -------VAVCGEVGSGKSTLLAAILG-ETPcVSGTIDFYGT--IAYVSQTawiqtgtiRDnilfggvmdehryretiqk 702
Cdd:TIGR03719 344 klppggiVGVIGPNGAGKSTLFRMITGqEQP-DSGTIEIGETvkLAYVDQS--------RD------------------- 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 703 sSLDKD---LELLPDG-DQTEIGERGVN---------------------LSGGQKQRIQLARALYQDADIYLLDDPFSAV 757
Cdd:TIGR03719 396 -ALDPNktvWEEISGGlDIIKLGKREIPsrayvgrfnfkgsdqqkkvgqLSGGERNRVHLAKTLKSGGNVLLLDEPTNDL 474
|
250 260 270
....*....|....*....|....*....|..
gi 22331862 758 DAHTASSLfqEYVMDALAGKAVlLVTHQVDFL 789
Cdd:TIGR03719 475 DVETLRAL--EEALLNFAGCAV-VISHDRWFL 503
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1223-1432 |
1.02e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 57.88 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1223 VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQD-PTLFNGTVR-- 1299
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlPAAEGMTVRel 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1300 ---------FNLDPLCQHSDAEIWEVLGKCQLKEVVQEKengLDSLvvedgsnwSMGQRQLFCLGRAVLRRSRVLVLDEA 1370
Cdd:PRK10575 106 vaigrypwhGALGRFGAADREKVEEAISLVGLKPLAHRL---VDSL--------SGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22331862 1371 TASIDNATD---LILQKTIRREFAdCTVITVAHRIPTVMD-CTMVLSISDGRIVEYDEPMKLMKDE 1432
Cdd:PRK10575 175 TSALDIAHQvdvLALVHRLSQERG-LTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1230-1427 |
1.05e-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: 57.80 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1230 TFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDIS-KigvhdlrsrfgiiPQDPTL-FNGTVRFNL----D 1303
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSyK-------------PQYIKAdYEGTVRDLLssitK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1304 PLCQHSDAEIwEVLGKCQLKEVvqekengLDSLVVEdgsnWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQ 1383
Cdd:cd03237 88 DFYTHPYFKT-EIAKPLQIEQI-------LDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMAS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 22331862 1384 KTIRR--EFADCTVITVAHriptvmDCTMVLSISDGRIVEYDEPMK 1427
Cdd:cd03237 156 KVIRRfaENNEKTAFVVEH------DIIMIDYLADRLIVFEGEPSV 195
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1190-1436 |
1.06e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 59.08 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1190 EVIEETRPPVNWPVTGRVEISDLQIRYrrESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDG 1269
Cdd:PRK11607 3 DAIPRPQAKTRKALTPLLEIRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1270 VDISKigVHDLRSRFGIIPQDPTLF-NGTVRFNL------DPLcqhSDAEI----WEVLGKCQLKEVVQEKENGLdslvv 1338
Cdd:PRK11607 81 VDLSH--VPPYQRPINMMFQSYALFpHMTVEQNIafglkqDKL---PKAEIasrvNEMLGLVHMQEFAKRKPHQL----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1339 edgsnwSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNAtdliLQKTIRREFAD------CTVITVAHRIPTVMDCTMVL 1412
Cdd:PRK11607 151 ------SGGQRQRVALARSLAKRPKLLLLDEPMGALDKK----LRDRMQLEVVDilervgVTCVMVTHDQEEAMTMAGRI 220
|
250 260
....*....|....*....|....*
gi 22331862 1413 SISD-GRIVEYDEPMKLMKDENSLF 1436
Cdd:PRK11607 221 AIMNrGKFVQIGEPEEIYEHPTTRY 245
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1206-1375 |
1.09e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 57.67 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1206 RVEISDLQIRYRRESplVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDIS-------KIGVH 1278
Cdd:PRK10619 5 KLNVIDLHKRYGEHE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLKVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1279 D------LRSRFGIIPQDPTLFNG-TVRFNLdplcqhSDAEIwEVLGKCQlKEVVQEKENGLDSLVVEDGS------NWS 1345
Cdd:PRK10619 83 DknqlrlLRTRLTMVFQHFNLWSHmTVLENV------MEAPI-QVLGLSK-QEARERAVKYLAKVGIDERAqgkypvHLS 154
|
170 180 190
....*....|....*....|....*....|
gi 22331862 1346 MGQRQLFCLGRAVLRRSRVLVLDEATASID 1375
Cdd:PRK10619 155 GGQQQRVSIARALAMEPEVLLFDEPTSALD 184
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1207-1435 |
1.16e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 57.89 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRrESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGI 1286
Cdd:PRK13652 4 IETRDLCYSYS-GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDP--TLFNGTVR---------FNLD-PLCQHSDAEIWEVLGKCQLKEVVQEKENGldslvvedgsnwsmGQRQLFCL 1354
Cdd:PRK13652 83 VFQNPddQIFSPTVEqdiafgpinLGLDeETVAHRVSSALHMLGLEELRDRVPHHLSG--------------GEKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1355 GRAVLRRSRVLVLDEATASID--NATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISD-GRIVEYDEPMKLMKD 1431
Cdd:PRK13652 149 AGVIAMEPQVLVLDEPTAGLDpqGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDkGRIVAYGTVEEIFLQ 228
|
....
gi 22331862 1432 ENSL 1435
Cdd:PRK13652 229 PDLL 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1223-1431 |
1.23e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 57.45 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1223 VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDI--------SKIGVHDLRSRFGIIPQDptlf 1294
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQKGLIRQLRQHVGFVFQN---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1295 ngtvrFNLDPlcqHSDA--EIWE--VLGKCQLKEVVQEKENGLDSLVVEDGSN------WSMGQRQLFCLGRAVLRRSRV 1364
Cdd:PRK11264 94 -----FNLFP---HRTVleNIIEgpVIVKGEPKEEATARARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1365 LVLDEATASIDNATDLILQKTIrREFAD--CTVITVAHRIPTVMDCT-MVLSISDGRIVEYDEPMKLMKD 1431
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNTI-RQLAQekRTMVIVTHEMSFARDVAdRAIFMDQGRIVEQGPAKALFAD 234
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1207-1423 |
1.41e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 57.48 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYrrESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFR---LVEP--VGGKIVVDGVDI--SKIGVHD 1279
Cdd:PRK14243 11 LRTENLNVYY--GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGfrVEGKVTFHGKNLyaPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1280 LRSRFGIIPQDPTLF--------------NGtVRFNLDPLCQHS--DAEIW-EVLGKCqlkevvqeKENGLdSLvvedgs 1342
Cdd:PRK14243 89 VRRRIGMVFQKPNPFpksiydniaygariNG-YKGDMDELVERSlrQAALWdEVKDKL--------KQSGL-SL------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1343 nwSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIRREFADCTVITVAHRIPT---VMDCTMVLSIS---- 1415
Cdd:PRK14243 153 --SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQaarVSDMTAFFNVElteg 230
|
250
....*....|.
gi 22331862 1416 ---DGRIVEYD 1423
Cdd:PRK14243 231 ggrYGYLVEFD 241
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
889-1090 |
1.45e-08 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 58.23 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 889 GYIFFFIASLAQVTFAV--GQILqNSWMAANVDNPQVSTLKLILVYLLIGLCSVLCLMVRSVCVVIMCMKSSASLFSQLL 966
Cdd:cd18578 14 GLIGAIIAGAVFPVFAIlfSKLI-SVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 967 NSLFRAPMSFYD----STplGRILSRVSSDLSIVD--LDVPFGLIFVVASSVNTGCslgVLAIVT-WQ---VLFVSVPMV 1036
Cdd:cd18578 93 RAILRQDIAWFDdpenST--GALTSRLSTDASDVRglVGDRLGLILQAIVTLVAGL---IIAFVYgWKlalVGLATVPLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 22331862 1037 YLAFRLQKYYFQTAKELMRingTTRSYVANHLAESVAGAITIRAFDEEERFFKK 1090
Cdd:cd18578 168 LLAGYLRMRLLSGFEEKNK---KAYEESSKIASEAVSNIRTVASLTLEDYFLEK 218
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1222-1414 |
1.62e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 56.42 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1222 LVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDiskIGVHDLRSRFGII-PQD---PTLfngT 1297
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD---IDDPDVAEACHYLgHRNamkPAL---T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1298 VRFNLdplcqhsdaEIW-EVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDN 1376
Cdd:PRK13539 90 VAENL---------EFWaAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 22331862 1377 ATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSI 1414
Cdd:PRK13539 161 AAVALFAELIRAHLAQGGIVIAATHIPLGLPGARELDL 198
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
598-817 |
1.68e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 57.23 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 598 QNAIIIKSASFSWeekGSTKPnLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAI-----LGETPCVSGTIDFYGT------ 666
Cdd:PRK14247 1 MNKIEIRDLKVSF---GQVEV-LDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQdifkmd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 667 -------IAYVSQTA-WIQTGTIRDNILFGGVMD---------EHRYRETIQKSSLDKDLellpdgdQTEIGERGVNLSG 729
Cdd:PRK14247 77 vielrrrVQMVFQIPnPIPNLSIFENVALGLKLNrlvkskkelQERVRWALEKAQLWDEV-------KDRLDAPAGKLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 730 GQKQRIQLARALYQDADIYLLDDPFSAVD-AHTA--SSLFQEYVMDAlagkAVLLVTHqvdfLPA-----FDSVLLMSDG 801
Cdd:PRK14247 150 GQQQRLCIARALAFQPEVLLADEPTANLDpENTAkiESLFLELKKDM----TIVLVTH----FPQqaariSDYVAFLYKG 221
|
250
....*....|....*.
gi 22331862 802 EITEADTYQELLARSR 817
Cdd:PRK14247 222 QIVEWGPTREVFTNPR 237
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
617-785 |
1.72e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.11 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 617 KPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT------IAYVSQTAWI--QTG-----TIRD 683
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlCTYQKQLCFVghRSGinpylTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 684 NILFggvmDEHRYRETIQKSSLDKDLEL-----LPDGdqteigergvNLSGGQKQRIQLARALYQDADIYLLDDPFSAVD 758
Cdd:PRK13540 94 NCLY----DIHFSPGAVGITELCRLFSLehlidYPCG----------LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
170 180
....*....|....*....|....*..
gi 22331862 759 AHTASSLFQEYVMDALAGKAVLLVTHQ 785
Cdd:PRK13540 160 ELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
625-787 |
1.98e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 59.26 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 625 LEVKFGEK--VAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGTIAYVSQTAWIQTGTI--RDNILFGGV-MDEHR--YR 697
Cdd:TIGR01257 949 LNITFYENqiTAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMcpQHNILFHHLtVAEHIlfYA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 698 ETIQKSSLDKDLEL---LPD-GDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFqEYVMDA 773
Cdd:TIGR01257 1029 QLKGRSWEEAQLEMeamLEDtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW-DLLLKY 1107
|
170
....*....|....
gi 22331862 774 LAGKAVLLVTHQVD 787
Cdd:TIGR01257 1108 RSGRTIIMSTHHMD 1121
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1217-1269 |
2.09e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 56.63 E-value: 2.09e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 22331862 1217 RRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDG 1269
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG 87
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1208-1422 |
2.65e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 57.41 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1208 EISDLQIRYRRES--------PLVLK---GISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIG 1276
Cdd:PRK15079 10 EVADLKVHFDIKDgkqwfwqpPKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1277 ---VHDLRSRFGIIPQDPTLfngtvrfNLDPLCQHSD--AEIWEV----LGKCQLKEVVQE---KENGLDSLVVEDGSNW 1344
Cdd:PRK15079 90 ddeWRAVRSDIQMIFQDPLA-------SLNPRMTIGEiiAEPLRTyhpkLSRQEVKDRVKAmmlKVGLLPNLINRYPHEF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1345 SMGQRQLFCLGRAVLRRSRVLVLDEATASID---NATDLILQKTIRREFaDCTVITVAHriptvmDCTMVLSISDGRIVE 1421
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDvsiQAQVVNLLQQLQREM-GLSLIFIAH------DLAVVKHISDRVLVM 235
|
.
gi 22331862 1422 Y 1422
Cdd:PRK15079 236 Y 236
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1208-1286 |
3.02e-08 |
|
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: 55.61 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1208 EISDLqiRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISAL--FRLVEPVGGKIVVDGVDISKIGVHDlRSRFG 1285
Cdd:cd03217 2 EIKDL--HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE-RARLG 78
|
.
gi 22331862 1286 I 1286
Cdd:cd03217 79 I 79
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
626-756 |
3.82e-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: 57.87 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 626 EVKFGEKVAVCGEVGSGKST---LLAAILgeTPcVSGTIDFYGTIAYVSQtaWIQT---GTIRDNI--LFGGVMDEHRYR 697
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTfakILAGVL--KP-DEGEVDEDLKISYKPQ--YISPdydGTVEEFLrsANTDDFGSSYYK 436
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331862 698 -ETIQKSSLDKdlellpdgdqteIGERGV-NLSGGQKQRIQLARALYQDADIYLLDDPfSA 756
Cdd:COG1245 437 tEIIKPLGLEK------------LLDKNVkDLSGGELQRVAIAACLSRDADLYLLDEP-SA 484
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1223-1431 |
4.01e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 55.87 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1223 VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDI--SKIGVHDLR-------SRFGIIPQDPTL 1293
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRqeagmvfQQFYLFPHLTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1294 FNgtVRFNldPL----CQHSDAE--IWEVLGKCQLKEVVQEKENGLdslvvedgsnwSMGQRQLFCLGRAVLRRSRVLVL 1367
Cdd:PRK09493 96 EN--VMFG--PLrvrgASKEEAEkqARELLAKVGLAERAHHYPSEL-----------SGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1368 DEATASIDnaTDL---ILqkTIRREFAD--CTVITVAHRIPTVMDC-TMVLSISDGRIVEYDEPMKLMKD 1431
Cdd:PRK09493 161 DEPTSALD--PELrheVL--KVMQDLAEegMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1223-1418 |
4.05e-08 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 55.52 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1223 VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVD----GVDISKIG---VHDLR-------SRF-GII 1287
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASpreILALRrrtigyvSQFlRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1288 PQDPTLfnGTVrfnLDPLCQH------SDAEIWEVLGKCQLKEvvqekengldSLvvedgsnW-------SMGQRQLFCL 1354
Cdd:COG4778 106 PRVSAL--DVV---AEPLLERgvdreeARARARELLARLNLPE----------RL-------WdlppatfSGGEQQRVNI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331862 1355 GRAVLRRSRVLVLDEATASIDNAT-----DLILQKTIRrefaDCTVITVAHRiPTVMD--CTMVLSISDGR 1418
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANravvvELIEEAKAR----GTAIIGIFHD-EEVREavADRVVDVTPFS 229
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
621-759 |
4.09e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 56.96 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 621 RNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIdFYG------------TIAYVSQT-AWIQTGTIRDNILF 687
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL-FIGekrmndvppaerGVGMVFQSyALYPHLSVAENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 688 G----GVMDEHRYR------ETIQkssLDKDLELLPDGdqteigergvnLSGGQKQRIQLARALYQDADIYLLDDPFSAV 757
Cdd:PRK11000 99 GlklaGAKKEEINQrvnqvaEVLQ---LAHLLDRKPKA-----------LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
..
gi 22331862 758 DA 759
Cdd:PRK11000 165 DA 166
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
603-801 |
4.40e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.20 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 603 IKSASFSWEE-------KGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAA---------ILGETPCVSG-TID--F 663
Cdd:TIGR00956 755 SGEDIFHWRNltyevkiKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVlaervttgvITGGDRLVNGrPLDssF 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 664 YGTIAYVSQT-AWIQTGTIRDNILFGGVMdehRYRETIQKSS----LDKDLELLPDGDQTE--IGERGVNLSGGQKQRIQ 736
Cdd:TIGR00956 835 QRSIGYVQQQdLHLPTSTVRESLRFSAYL---RQPKSVSKSEkmeyVEEVIKLLEMESYADavVGVPGEGLNVEQRKRLT 911
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 737 LARALYQDADIYL-LDDPFSAVDAHTASSLFQEYVMDALAGKAVLLVTHQ--VDFLPAFDSVLLMSDG 801
Cdd:TIGR00956 912 IGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQpsAILFEEFDRLLLLQKG 979
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
620-822 |
4.82e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 56.18 E-value: 4.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAI------------LGETPCVSGT-----IDFYGTIAYVSQTAWIQ--TGT 680
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLngllqptsgtvtIGERVITAGKknkklKPLRKKVGIVFQFPEHQlfEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 681 IRDNILFG----GVMDEH---RYRETIQKSSLDKD-LELLPdgdqteigergVNLSGGQKQRIQLARALYQDADIYLLDD 752
Cdd:PRK13634 103 VEKDICFGpmnfGVSEEDakqKAREMIELVGLPEElLARSP-----------FELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 753 PFSAVDAHTasslfQEYVMDALA------GKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQELLARSRDFQDL 822
Cdd:PRK13634 172 PTAGLDPKG-----RKEMMEMFYklhkekGLTTVLVTHSMEDAARYaDQIVVMHKGTVFLQGTPREIFADPDELEAI 243
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1234-1425 |
4.99e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 55.36 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1234 GHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVD-----ISKIGVhdlrsrfGIIPQDPTLFNG-TVRFN----LD 1303
Cdd:PRK10771 25 GERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhtttpPSRRPV-------SMLFQENNLFSHlTVAQNiglgLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1304 PLCQHSDAEiwevlgKCQLKEVVQEKenGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATD---L 1380
Cdd:PRK10771 98 PGLKLNAAQ------REKLHAIARQM--GIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRqemL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 22331862 1381 ILQKTIRREfADCTVITVAHRIPTVMD-CTMVLSISDGRIVeYDEP 1425
Cdd:PRK10771 170 TLVSQVCQE-RQLTLLMVSHSLEDAARiAPRSLVVADGRIA-WDGP 213
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
599-753 |
5.47e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.21 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 599 NAIIIKSASFSWEEKgstkPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFY--GTIAYVSQ---- 672
Cdd:PRK15064 318 NALEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSenANIGYYAQdhay 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 673 --------TAWI-QTGTIRDNilfggvmdehryrETIQKSSLDKdleLLPDGDqtEIGERGVNLSGGQKQRIQLARALYQ 743
Cdd:PRK15064 394 dfendltlFDWMsQWRQEGDD-------------EQAVRGTLGR---LLFSQD--DIKKSVKVLSGGEKGRMLFGKLMMQ 455
|
170
....*....|
gi 22331862 744 DADIYLLDDP 753
Cdd:PRK15064 456 KPNVLVMDEP 465
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1207-1401 |
6.16e-08 |
|
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: 53.70 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIrYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGvdiskigvhdlRSRFGI 1286
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 IPQDPTLFNGTVRfnlDPLCQHSDaeiwEVLgkcqlkevvqekengldslvvedgsnwSMGQRQLFCLGRAVLRRSRVLV 1366
Cdd:cd03223 69 LPQRPYLPLGTLR---EQLIYPWD----DVL---------------------------SGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*
gi 22331862 1367 LDEATASIDNATDLILQKTIRREFAdcTVITVAHR 1401
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
889-1098 |
6.23e-08 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 55.90 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 889 GYIFFFIASLAQvtFAVGQILQNSwmaanVDNPQVSTLKLILVYLLIGLcsVLCLMVRSVCVVIMCMksSASLFSQ---- 964
Cdd:cd18542 4 AILALLLATALN--LLIPLLIRRI-----IDSVIGGGLRELLWLLALLI--LGVALLRGVFRYLQGY--LAEKASQkvay 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 965 -LLNSLF----RAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLIFVVASSVNTGCSLGVLAIVTWQ---VLFVSVP-M 1035
Cdd:cd18542 73 dLRNDLYdhlqRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKltlISLAIIPfI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331862 1036 VYLAF----RLQKYYFQTAKELMRINGTtrsyvanhLAESVAGAITIRAF----DEEERFFKKSLTLIDTN 1098
Cdd:cd18542 153 ALFSYvffkKVRPAFEEIREQEGELNTV--------LQENLTGVRVVKAFaredYEIEKFDKENEEYRDLN 215
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
891-1149 |
6.27e-08 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 55.89 E-value: 6.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 891 IFFFIASLAQVTFA--VGQILQNSWMAANVDNPQVSTLKLILVYLLIGLCSVLclmvRSVCVVIMCMKSSASLFSQLLNS 968
Cdd:cd18552 6 LGMILVAATTAALAwlLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYL----QTYLMAYVGQRVVRDLRNDLFDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 969 LFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLIFVVASSVNTGCSLGVLAIVTWQ---VLFVSVP-MVYLAFRLQK 1044
Cdd:cd18552 82 LLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKltlIALVVLPlAALPIRRIGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1045 YYFQTAKELMRINGTtrsyVANHLAESVAGAITIRAFDEEERFFKKsltlidtnaspFFHSFAANEWLIQRLETVSAI-- 1122
Cdd:cd18552 162 RLRKISRRSQESMGD----LTSVLQETLSGIRVVKAFGAEDYEIKR-----------FRKANERLRRLSMKIARARALss 226
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 22331862 1123 ----VLASTAFCMIL-----------LPTGTFSSgFIGMALS 1149
Cdd:cd18552 227 plmeLLGAIAIALVLwyggyqvisgeLTPGEFIS-FITALLL 267
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1207-1435 |
6.33e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 55.85 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESpLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDG--VDISKIGVHDLRSRF 1284
Cdd:PRK13639 2 LETRDLKYSYPDGT-EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1285 GIIPQDP--TLFNGTVRFNL--DPLCQHSDAEIWEVLGKCQLKEVvqekenGLDSLVVEDGSNWSMGQRQLFCLGRAVLR 1360
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEEDVafGPLNLGLSKEEVEKRVKEALKAV------GMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1361 RSRVLVLDEATASID--NATDLI-LQKTIRREfaDCTVITVAHRI---PTVMDctMVLSISDGRIVEYDEPMKLMKDENS 1434
Cdd:PRK13639 155 KPEIIVLDEPTSGLDpmGASQIMkLLYDLNKE--GITIIISTHDVdlvPVYAD--KVYVMSDGKIIKEGTPKEVFSDIET 230
|
.
gi 22331862 1435 L 1435
Cdd:PRK13639 231 I 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1224-1420 |
6.63e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.96 E-value: 6.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1224 LKGISCTFEGG--HkiGIVGRTGSGKTTLISALFRLVEPVGGKIVVDG--VDIS--------KIG-VHdlrsrfgiipQD 1290
Cdd:COG3845 21 NDDVSLTVRPGeiH--ALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRsprdaialGIGmVH----------QH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1291 PTLFNG-TVRFNL----DPLCQHsdaeiweVLGKCQLKEVVQE--KENGLD---SLVVEDgsnWSMGQRQLFCLGRAVLR 1360
Cdd:COG3845 89 FMLVPNlTVAENIvlglEPTKGG-------RLDRKAARARIRElsERYGLDvdpDAKVED---LSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331862 1361 RSRVLVLDEATA--SIDNATDLIlqKTIRReFAD--CTVITVAHRIPTVMDctmvlsISD-------GRIV 1420
Cdd:COG3845 159 GARILILDEPTAvlTPQEADELF--EILRR-LAAegKSIIFITHKLREVMA------IADrvtvlrrGKVV 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1224-1433 |
6.65e-08 |
|
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: 57.14 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1224 LKGISCTFEGGHKIGIVGRTGSGKTTLISALFRlVEPVG---GKIVVDGVDISKIGVHDL-RSRFGIIPQDPTLF-NGTV 1298
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1299 RFNLdplcqHSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSN------WSMGQRQLFCLGRAVLRRSRVLVLDEATA 1372
Cdd:TIGR02633 96 AENI-----FLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVtrpvgdYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 1373 SIDNATDLILQKTIR---REFADCtvITVAHRIPTVMD-CTMVLSISDGRIVEyDEPMKLMKDEN 1433
Cdd:TIGR02633 171 SLTEKETEILLDIIRdlkAHGVAC--VYISHKLNEVKAvCDTICVIRDGQHVA-TKDMSTMSEDD 232
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
620-815 |
6.82e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 56.72 E-value: 6.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGET--PCVSGTIDFYGT--------------IAYVS----QTAWIQTG 679
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKevdvstvsdaidagLAYVTedrkGYGLNLID 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 680 TIRDNILF--------GGVMDEHR-------YRETIQ-KSSldkdlellpdgdqtEIGERGVNLSGGQKQRIQLARALYQ 743
Cdd:NF040905 356 DIKRNITLanlgkvsrRGVIDENEeikvaeeYRKKMNiKTP--------------SVFQKVGNLSGGNQQKVVLSKWLFT 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 744 DADIYLLDDPFSAVDahtASSLFQEY-VMDALA--GKAVLLVTHQvdfLPAF----DSVLLMSDGEIT----EADTYQEL 812
Cdd:NF040905 422 DPDVLILDEPTRGID---VGAKYEIYtIINELAaeGKGVIVISSE---LPELlgmcDRIYVMNEGRITgelpREEASQER 495
|
...
gi 22331862 813 LAR 815
Cdd:NF040905 496 IMR 498
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1223-1448 |
7.41e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 56.25 E-value: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1223 VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKigVHDLRSRFGIIPQDPTLFN-----GT 1297
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR--LHARDRKVGFVFQHYALFRhmtvfDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1298 VRFNLDPLCQHSDAEIWEVLGKC-QLKEVVQekengLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDN 1376
Cdd:PRK10851 95 IAFGLTVLPRRERPNAAAIKAKVtQLLEMVQ-----LAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 1377 ATDLILQKTIRR--EFADCTVITVAHRIPTVMDCT-MVLSISDGRIVEYDEPMKLMKDENSLFgklVKEYWSHYN 1448
Cdd:PRK10851 170 QVRKELRRWLRQlhEELKFTSVFVTHDQEEAMEVAdRVVVMSQGNIEQAGTPDQVWREPATRF---VLEFMGEVN 241
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
620-796 |
8.02e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 55.12 E-value: 8.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT--IAYVSQTAWIQT--------------GTIRD 683
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlrIGYVPQKLYLDTtlpltvnrflrlrpGTKKE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 684 NIL--FGGVMDEHRYRETIQKssldkdlellpdgdqteigergvnLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHT 761
Cdd:PRK09544 100 DILpaLKRVQAGHLIDAPMQK------------------------LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 22331862 762 ASSLFQeyVMDALA---GKAVLLVTHQVDFLPA-FDSVL 796
Cdd:PRK09544 156 QVALYD--LIDQLRrelDCAVLMVSHDLHLVMAkTDEVL 192
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1224-1375 |
8.90e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 55.74 E-value: 8.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1224 LKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDI---SKIGVHDLRSRFGIIPQDP--TLfN--G 1296
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNPygSL-NprK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1297 TVRFNL-DPLCQHSDaeiwevLGKCQLKEVVQE--KENGLDSlvvEDGSNW----SMGQRQLFCLGRAVLRRSRVLVLDE 1369
Cdd:PRK11308 110 KVGQILeEPLLINTS------LSAAERREKALAmmAKVGLRP---EHYDRYphmfSGGQRQRIAIARALMLDPDVVVADE 180
|
....*.
gi 22331862 1370 ATASID 1375
Cdd:PRK11308 181 PVSALD 186
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
620-784 |
9.27e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 54.85 E-value: 9.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAI-----LGETPCVSGTIDFYGTIAYVSQTAWIQTG--------------- 679
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIEVRrevgmvfqypnpfph 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 680 -TIRDNILFG----------GVMDEhRYRETIQKSSLDKDLellpdgdQTEIGERGVNLSGGQKQRIQLARALYQDADIY 748
Cdd:PRK14267 100 lTIYDNVAIGvklnglvkskKELDE-RVEWALKKAALWDEV-------KDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 22331862 749 LLDDPFSAVDAHTASSLfQEYVMDALAGKAVLLVTH 784
Cdd:PRK14267 172 LMDEPTANIDPVGTAKI-EELLFELKKEYTIVLVTH 206
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1207-1265 |
9.82e-08 |
|
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: 52.45 E-value: 9.82e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 22331862 1207 VEISDLQIRYrrESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKI 1265
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV 57
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
613-796 |
1.01e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 54.93 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 613 KGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGetPCVS----------GTIDFYGTIAYVSQTAWIQTGTI- 681
Cdd:cd03271 4 KGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLY--PALArrlhlkkeqpGNHDRIEGLEHIDKVIVIDQSPIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 682 ---RDNIL-FGGVMDE-----------HRY-RETIQ-----KS--------------------SLDKDLELLPD-G-DQT 718
Cdd:cd03271 82 rtpRSNPAtYTGVFDEirelfcevckgKRYnRETLEvrykgKSiadvldmtveealeffenipKIARKLQTLCDvGlGYI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 719 EIGERGVNLSGGQKQRIQLARALYQDAD---IYLLDDPFSAVDAHTASSLFQeyVMDAL--AGKAVLLVTHQVDFLPAFD 793
Cdd:cd03271 162 KLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLE--VLQRLvdKGNTVVVIEHNLDVIKCAD 239
|
...
gi 22331862 794 SVL 796
Cdd:cd03271 240 WII 242
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
565-818 |
1.40e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.13 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 565 IQAKVAFSRIATFLEAPELQGGERrrkQRSEGNQNAIIIKSASFSWEEKG-STKPnlrnVSLEVKFGEKVAVCGEVGSGK 643
Cdd:PRK10522 290 LSAQVAFNKLNKLALAPYKAEFPR---PQAFPDWQTLELRNVTFAYQDNGfSVGP----INLTIKRGELLFLIGGNGSGK 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 644 STLLAAILGETPCVSGTIDFYG-TIAYVSQTAWIQtgtirdniLFGGVM-DEHRYRETIQKSSLDKD-------LELLPD 714
Cdd:PRK10522 363 STLAMLLTGLYQPQSGEILLDGkPVTAEQPEDYRK--------LFSAVFtDFHLFDQLLGPEGKPANpalvekwLERLKM 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 715 GDQTEI-GERGVN--LSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQEYV--MDAlAGKAVLLVTHQVDFL 789
Cdd:PRK10522 435 AHKLELeDGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLplLQE-MGKTIFAISHDDHYF 513
|
250 260
....*....|....*....|....*....
gi 22331862 790 PAFDSVLLMSDGEITEAdTYQELLARSRD 818
Cdd:PRK10522 514 IHADRLLEMRNGQLSEL-TGEERDAASRD 541
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1215-1419 |
1.59e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 54.30 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1215 RYRRESPLVLKGISCTFEG-------------GHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIgVHDLR 1281
Cdd:PRK11247 6 RLNQGTPLLLNAVSKRYGErtvlnqldlhipaGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-REDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1282 SRFgiipQDPTLFngtvrfnldPlcqhsdaeiWevlgkcqlKEVV------------QEKENGLDSLVVEDGSN-W---- 1344
Cdd:PRK11247 85 LMF----QDARLL---------P---------W--------KKVIdnvglglkgqwrDAALQALAAVGLADRANeWpaal 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 1345 SMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIRREFAD--CTVITVAHRIP-TVMDCTMVLSISDGRI 1419
Cdd:PRK11247 135 SGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhgFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
598-813 |
1.61e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.41 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 598 QNAIIIKSASFSWEEKGSTKPN---LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTI------------- 661
Cdd:PRK10575 2 QEYTNHSDTTFALRNVSFRVPGrtlLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaqpleswssk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 662 DFYGTIAYVSQTAWIQTG-TIRDNILFG-----------GVMDEHRYRETIQKSSLDKDLELLPDgdqteigergvNLSG 729
Cdd:PRK10575 82 AFARKVAYLPQQLPAAEGmTVRELVAIGrypwhgalgrfGAADREKVEEAISLVGLKPLAHRLVD-----------SLSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 730 GQKQRIQLARALYQDADIYLLDDPFSAVD-AHTASSLFQEYVMDALAGKAVLLVTHQVDFLPAF-DSVLLMSDGEITEAD 807
Cdd:PRK10575 151 GERQRAWIAMLVAQDSRCLLLDEPTSALDiAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYcDYLVALRGGEMIAQG 230
|
....*.
gi 22331862 808 TYQELL 813
Cdd:PRK10575 231 TPAELM 236
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1209-1375 |
1.70e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 54.81 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1209 ISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKiGVHDLRSRFGIIP 1288
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1289 Q----DPTLfngTVRFNLDPLCQH---SDAEIWEVLGKcqLKEVVQeKENGLDSLVVEdgsnWSMGQRQLFCLGRAVLRR 1361
Cdd:PRK13537 87 QfdnlDPDF---TVRENLLVFGRYfglSAAAARALVPP--LLEFAK-LENKADAKVGE----LSGGMKRRLTLARALVND 156
|
170
....*....|....
gi 22331862 1362 SRVLVLDEATASID 1375
Cdd:PRK13537 157 PDVLVLDEPTTGLD 170
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
620-814 |
1.93e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.03 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDF------YGTIAYVSQtawiqtgtiRDNILFGGVMDE 693
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIddhplhFGDYSYRSQ---------RIRMIFQDPSTS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 694 HRYRETIQKSsLDKDLELLPDGDQTEiGERGVN-------------------LSGGQKQRIQLARALYQDADIYLLDDPF 754
Cdd:PRK15112 100 LNPRQRISQI-LDFPLRLNTDLEPEQ-REKQIIetlrqvgllpdhasyyphmLAPGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22331862 755 SAVDAHTASSLFQeyVMDALAGK---AVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQELLA 814
Cdd:PRK15112 178 ASLDMSMRSQLIN--LMLELQEKqgiSYIYVTQHLGMMKHIsDQVLVMHQGEVVERGSTADVLA 239
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
928-1090 |
1.97e-07 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 54.37 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 928 LILVYLLIGLCSVLCLMVRSVCVVIMCMKSSASLFSQLLNSLFRAPMSFYDSTPLGRILSRVsSDLS---------IVDL 998
Cdd:cd18570 44 ISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRF-NDANkireaisstTISL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 999 DVPFGLIFVvassvntgcSLGVLAIVTWQ---VLFVSVP-MVYLAFRLQKYYFQTAKELMRINGTTRSYvanhLAESVAG 1074
Cdd:cd18570 123 FLDLLMVII---------SGIILFFYNWKlflITLLIIPlYILIILLFNKPFKKKNREVMESNAELNSY----LIESLKG 189
|
170
....*....|....*.
gi 22331862 1075 AITIRAFDEEERFFKK 1090
Cdd:cd18570 190 IETIKSLNAEEQFLKK 205
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1224-1420 |
2.07e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 53.34 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1224 LKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIG---VHDLRSRFGIIPQD-PTLFNGTVR 1299
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRRQIGMIFQDhHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1300 FNLD-PLcqhsdaeiweVLGKCQLKEVVQEKENGLDSL-VVEDGSNW----SMGQRQLFCLGRAVLRRSRVLVLDEATAS 1373
Cdd:PRK10908 98 DNVAiPL----------IIAGASGDDIRRRVSAALDKVgLLDKAKNFpiqlSGGEQQRVGIARAVVNKPAVLLADEPTGN 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22331862 1374 IDNAtdliLQKTIRREFAD-----CTVITVAHRIPTVMDCTM-VLSISDGRIV 1420
Cdd:PRK10908 168 LDDA----LSEGILRLFEEfnrvgVTVLMATHDIGLISRRSYrMLTLSDGHLH 216
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
620-803 |
2.67e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 53.31 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPcVSGTIDFYGTI-------------AYVSQTawiQTGTirdnil 686
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPlsdwsaaelarhrAYLSQQ---QSPP------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 687 fgGVMDEHRYRETIQKSSLDkdlellPDGDQTEIGE------------RGVN-LSGGQKQRIQLARALYQ-------DAD 746
Cdd:COG4138 82 --FAMPVFQYLALHQPAGAS------SEAVEQLLAQlaealgledklsRPLTqLSGGEWQRVRLAAVLLQvwptinpEGQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331862 747 IYLLDDPFSAVD-AHTAS--SLFQEYvmdALAGKAVLLVTHqvDF---LPAFDSVLLMSDGEI 803
Cdd:COG4138 154 LLLLDEPMNSLDvAQQAAldRLLREL---CQQGITVVMSSH--DLnhtLRHADRVWLLKQGKL 211
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
614-789 |
2.94e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.12 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 614 GSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGetpcvsgtID--FYGTiayvsqtAWIQTG------------ 679
Cdd:PRK11819 17 PPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--------VDkeFEGE-------ARPAPGikvgylpqepql 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 680 ----TIRDNI-------------------LFGGVMDEH--------RYRETIQKSS---LDKDLEL------LPDGDqTE 719
Cdd:PRK11819 82 dpekTVRENVeegvaevkaaldrfneiyaAYAEPDADFdalaaeqgELQEIIDAADawdLDSQLEIamdalrCPPWD-AK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331862 720 IGergvNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSL---FQEYvmdalAGkAVLLVTHQVDFL 789
Cdd:PRK11819 161 VT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLeqfLHDY-----PG-TVVAVTHDRYFL 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1223-1383 |
3.38e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 52.90 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1223 VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVH---DLRSR-FGIIPQDPTL---FN 1295
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELRNQkLGFIYQFHHLlpdFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1296 GTVRFNLdPLcqhsdaeiweVLGKCQLKEvVQEKEN------GLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDE 1369
Cdd:PRK11629 104 ALENVAM-PL----------LIGKKKPAE-INSRALemlaavGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
170
....*....|....*
gi 22331862 1370 ATASIDNAT-DLILQ 1383
Cdd:PRK11629 172 PTGNLDARNaDSIFQ 186
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1224-1426 |
3.60e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.53 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1224 LKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHD-LRSRFGIIPQD----PTLfngTV 1298
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQElhlvPEM---TV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1299 RFNLdPLCQ--HSDAeiweVLGKCQLKEVVQE--KENGLD--------SLvvedgsnwSMGQRQLFCLGRAVLRRSRVLV 1366
Cdd:PRK11288 97 AENL-YLGQlpHKGG----IVNRRLLNYEAREqlEHLGVDidpdtplkYL--------SIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22331862 1367 LDEATASIDNATDLILQKTIRREFADCTVIT-VAHRiptvMD-----CTMVLSISDGRIVEYDEPM 1426
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIRELRAEGRVILyVSHR----MEeifalCDAITVFKDGRYVATFDDM 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
620-815 |
3.82e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 53.31 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG---------------TIAYVSQTAWIQ--TGTIR 682
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpidysrkglmklreSVGMVFQDPDNQlfSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 683 DNILFGGV---MDEHRYRETIQKSSLDKDLELLPDGDQTEigergvnLSGGQKQRIQLARALYQDADIYLLDDPFSAVDA 759
Cdd:PRK13636 102 QDVSFGAVnlkLPEDEVRKRVDNALKRTGIEHLKDKPTHC-------LSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 760 HTASSLFQEYV-MDALAGKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQELLAR 815
Cdd:PRK13636 175 MGVSEIMKLLVeMQKELGLTIIIATHDIDIVPLYcDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
618-803 |
3.83e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 53.45 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 618 PNLRNVSLEVKFGEKVAVCGEVGSGKSTL---LAAIL--------------GETPCVSGTIDFYGTIAYVSQTAWIQTgT 680
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLalhLNGLLrpqkgkvlvsgidtGDFSKLQGIRKLVGIVFQNPETQFVGR-T 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 681 IRDNILFGG-------VMDEHRYRETIQKSSLDKDLELLPDgdqteigergvNLSGGQKQRIQLARALYQDADIYLLDDP 753
Cdd:PRK13644 95 VEEDLAFGPenlclppIEIRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22331862 754 FSAVDAHTASSLFQEYVMDALAGKAVLLVTHQVDFLPAFDSVLLMSDGEI 803
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKI 213
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1215-1375 |
3.96e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.48 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1215 RYRRESPLVLKgISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDI---SKIGVHDLRSRFGIIPQDP 1291
Cdd:PRK10261 332 RVTREVHAVEK-VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDP 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1292 TLfngtvrfNLDP--LCQHSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNW------SMGQRQLFCLGRAVLRRSR 1363
Cdd:PRK10261 411 YA-------SLDPrqTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWryphefSGGQRQRICIARALALNPK 483
|
170
....*....|..
gi 22331862 1364 VLVLDEATASID 1375
Cdd:PRK10261 484 VIIADEAVSALD 495
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1223-1384 |
4.02e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 53.68 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1223 VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKiGVHDLRSRFGIIPQDPTL-FNGTVRFN 1301
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQFDNLdLEFTVREN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1302 L---DPLCQHSDAEIWEVLGkcQLKEVVQeKENGLDSLVvedgSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASID-NA 1377
Cdd:PRK13536 135 LlvfGRYFGMSTREIEAVIP--SLLEFAR-LESKADARV----SDLSGGMKRRLTLARALINDPQLLILDEPTTGLDpHA 207
|
....*..
gi 22331862 1378 TDLILQK 1384
Cdd:PRK13536 208 RHLIWER 214
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
603-812 |
4.27e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 53.56 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 603 IKSASFSWEEKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-IAYVSQTAWIQTgti 681
Cdd:PRK15079 20 IKDGKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdLLGMKDDEWRAV--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 682 RDNI--LFGGVMDEHRYRETIQksslDKDLELL----PDGDQTEIGER--------GV--NL--------SGGQKQRIQL 737
Cdd:PRK15079 97 RSDIqmIFQDPLASLNPRMTIG----EIIAEPLrtyhPKLSRQEVKDRvkammlkvGLlpNLinryphefSGGQCQRIGI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 738 ARALYQDADIYLLDDPFSAVDAHtasslFQEYVMDALA------GKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQ 810
Cdd:PRK15079 173 ARALILEPKLIICDEPVSALDVS-----IQAQVVNLLQqlqremGLSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYD 247
|
..
gi 22331862 811 EL 812
Cdd:PRK15079 248 EV 249
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
624-842 |
4.73e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.25 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 624 SLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSG--TIDFYgTIAYVS--QTAWIQTGTIRDN---ILFGGVMDEHRY 696
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerQSQFS-HITRLSfeQLQKLVSDEWQRNntdMLSPGEDDTGRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 697 -RETIQKSSLDKDL-ELLPD--GDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQeyVMD 772
Cdd:PRK10938 102 tAEIIQDEVKDPARcEQLAQqfGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAE--LLA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331862 773 ALAGK--AVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQELLARSRdFQDLvnAHRETAGSERVVAVENPT 842
Cdd:PRK10938 180 SLHQSgiTLVLVLNRFDEIPDFvQFAGVLADCTLAETGEREEILQQAL-VAQL--AHSEQLEGVQLPEPDEPS 249
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
620-803 |
5.01e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.29 E-value: 5.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT--------------IAYVSQTAWI-QTGTIRDN 684
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLfPNLSVKEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 685 ILFGGVMDEHRYRETIQK-SSLDKDLELLPDGDQTEIGERgvnlsggqkQRIQLARALYQDADIYLLDDPFSAVDAHTAS 763
Cdd:PRK15439 107 ILFGLPKRQASMQKMKQLlAALGCQLDLDSSAGSLEVADR---------QIVEILRGLMRDSRILILDEPTASLTPAETE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 22331862 764 SLFQEyvMDALAGKAVLLV--THQvdfLPAF----DSVLLMSDGEI 803
Cdd:PRK15439 178 RLFSR--IRELLAQGVGIVfiSHK---LPEIrqlaDRISVMRDGTI 218
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
620-756 |
5.47e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.03 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPcvSGTIDfyGTIAYVSQTAwiQTGTIRD---------------- 683
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP--HGSYE--GEILFDGEVC--RFKDIRDsealgiviihqelali 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 684 -------NILFG------GVMD----EHRYRETIQKSSLDKDlellPDgdqTEIGERGVnlsgGQKQRIQLARALYQDAD 746
Cdd:NF040905 91 pylsiaeNIFLGnerakrGVIDwnetNRRARELLAKVGLDES----PD---TLVTDIGV----GKQQLVEIAKALSKDVK 159
|
170
....*....|
gi 22331862 747 IYLLDDPFSA 756
Cdd:NF040905 160 LLILDEPTAA 169
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
926-1098 |
6.10e-07 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 52.80 E-value: 6.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 926 LKLILVYLLIGLCSVLCLMVRSVCVVIMCMKSSASLFSQLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLI 1005
Cdd:cd18541 40 LRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGIL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1006 FVVASSVNTGCSLGVLAIVTWQV-LFVSVPMVYLAF-------RLQKYYFQTAKELMRINGTTRsyvanhlaESVAGAIT 1077
Cdd:cd18541 120 YLVDALFLGVLVLVMMFTISPKLtLIALLPLPLLALlvyrlgkKIHKRFRKVQEAFSDLSDRVQ--------ESFSGIRV 191
|
170 180
....*....|....*....|....*
gi 22331862 1078 IRAF----DEEERFFKKSLTLIDTN 1098
Cdd:cd18541 192 IKAFvqeeAEIERFDKLNEEYVEKN 216
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
620-802 |
6.34e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.97 E-value: 6.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-IAYVSQTAWIQTG--------------TIRDN 684
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeIDFKSSKEALENGismvhqelnlvlqrSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 685 ILFG-----GVMDEHR--YRETiqKSSLDK-DLELLPDgdqteigERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSA 756
Cdd:PRK10982 94 MWLGryptkGMFVDQDkmYRDT--KAIFDElDIDIDPR-------AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 22331862 757 VDAHTASSLFQeyVMDALA--GKAVLLVTHQVD-FLPAFDSVLLMSDGE 802
Cdd:PRK10982 165 LTEKEVNHLFT--IIRKLKerGCGIVYISHKMEeIFQLCDEITILRDGQ 211
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
619-801 |
6.45e-07 |
|
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: 51.17 E-value: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 619 NLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPC---VSGTIDFYgtiayvsqtawiqtgtiRDNILFGGVMdehr 695
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKarlISFLPKFS-----------------RNKLIFIDQL---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 696 yretiqKSSLDKDLELLPdgdqteIGERGVNLSGGQKQRIQLARALYQDAD--IYLLDDPFSAVDAHTASSLFQeyVMDA 773
Cdd:cd03238 69 ------QFLIDVGLGYLT------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLE--VIKG 134
|
170 180 190
....*....|....*....|....*....|
gi 22331862 774 L--AGKAVLLVTHQVDFLPAFDSVLLMSDG 801
Cdd:cd03238 135 LidLGNTVILIEHNLDVLSSADWIIDFGPG 164
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
621-804 |
6.75e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.10 E-value: 6.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 621 RNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIdFYGT---IAYVSQTAwIQTGTIRDNIL------FGGVM 691
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-FRSAkvrMAVFSQHH-VDGLDLSSNPLlymmrcFPGVP 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 692 dEHRYRETIQKSSLDKDLELLPdgdqteigerGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQEYVm 771
Cdd:PLN03073 604 -EQKLRAHLGSFGVTGNLALQP----------MYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLV- 671
|
170 180 190
....*....|....*....|....*....|....
gi 22331862 772 daLAGKAVLLVTHQVDFLP-AFDSVLLMSDGEIT 804
Cdd:PLN03073 672 --LFQGGVLMVSHDEHLISgSVDELWVVSEGKVT 703
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
608-819 |
7.10e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.74 E-value: 7.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 608 FSWEEKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGTIAYVSQTAWIQ---TGTirDN 684
Cdd:PRK13545 28 FFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNgqlTGI--EN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 685 ILFGGVMdEHRYRETIQkssldkdlELLPDG-DQTEIGeRGVN-----LSGGQKQRIQLARALYQDADIYLLDDPFSAVD 758
Cdd:PRK13545 106 IELKGLM-MGLTKEKIK--------EIIPEIiEFADIG-KFIYqpvktYSSGMKSRLGFAISVHINPDILVIDEALSVGD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 759 ahtasSLFQEYVMDAL-----AGKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQELLARSRDF 819
Cdd:PRK13545 176 -----QTFTKKCLDKMnefkeQGKTIFFISHSLSQVKSFcTKALWLHYGQVKEYGDIKEVVDHYDEF 237
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1227-1428 |
7.47e-07 |
|
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: 54.25 E-value: 7.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1227 ISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDIsKIGVHDLRSRFGIIPQDPTLFNGTVRFNLDPLC 1306
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1307 QHSDAEIWEvlgKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNAT-----DLI 1381
Cdd:TIGR01257 1028 AQLKGRSWE---EAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSrrsiwDLL 1104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 22331862 1382 LQKTIRRefadcTVITVAHRiptvMDCTMVLS-----ISDGRIVEYDEPMKL 1428
Cdd:TIGR01257 1105 LKYRSGR-----TIIMSTHH----MDEADLLGdriaiISQGRLYCSGTPLFL 1147
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1207-1375 |
7.59e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 52.71 E-value: 7.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLQIRYRRESP---LVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIvvdgvdisKIGVH----- 1278
Cdd:PRK13634 3 ITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV--------TIGERvitag 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1279 -------DLRSRFGIIPQDP--TLFNGTV---------RFNLdplcqhSDAEiwevlGKCQLKEVVqeKENGLDSLVVEd 1340
Cdd:PRK13634 75 kknkklkPLRKKVGIVFQFPehQLFEETVekdicfgpmNFGV------SEED-----AKQKAREMI--ELVGLPEELLA- 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 22331862 1341 gsnwsmgqRQLFCLGRAVLRR----------SRVLVLDEATASID 1375
Cdd:PRK13634 141 --------RSPFELSGGQMRRvaiagvlamePEVLVLDEPTAGLD 177
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
617-813 |
7.73e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 7.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 617 KPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG-TIAYVSQTAWIQTGtirdnilFGGVMDEHR 695
Cdd:PRK10982 261 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGkKINNHNANEAINHG-------FALVTEERR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 696 ---------------------YRETI---QKSSLDKDLELLPD-------GDQTEIGergvNLSGGQKQRIQLARALYQD 744
Cdd:PRK10982 334 stgiyayldigfnslisnirnYKNKVgllDNSRMKSDTQWVIDsmrvktpGHRTQIG----SLSGGNQQKVIIGRWLLTQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 745 ADIYLLDDPFSAVDAHTASSLFQEYVMDALAGKAVLLVTHQV-DFLPAFDSVLLMSDGEI-----TEADTYQELL 813
Cdd:PRK10982 410 PEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMpELLGITDRILVMSNGLVagivdTKTTTQNEIL 484
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
928-1098 |
8.26e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 52.51 E-value: 8.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 928 LILVYLLIGLCSVLCLMVRSVCVVIMCMKSSASLFSQLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLIFV 1007
Cdd:cd18563 45 LVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDF 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1008 VASSVNTGCSLGVLAIVTWQV-LFVSVPM---VYLAFRLQKYYFQtakeLMRINGTTRSYVANHLAESVAGAITIRAF-- 1081
Cdd:cd18563 125 LTNILMIIGIGVVLFSLNWKLaLLVLIPVplvVWGSYFFWKKIRR----LFHRQWRRWSRLNSVLNDTLPGIRVVKAFgq 200
|
170
....*....|....*....
gi 22331862 1082 --DEEERFFKKSLTLIDTN 1098
Cdd:cd18563 201 ekREIKRFDEANQELLDAN 219
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
963-1096 |
9.83e-07 |
|
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: 52.05 E-value: 9.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 963 SQLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLIFVVASSVNTGCSLGVLAIVTWQ---VLFVSVPMVYLA 1039
Cdd:cd18551 73 RRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVltlVTLAVVPLAFLI 152
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331862 1040 F-----RLQKYYFQTAKELMRINGTTrsyvanhlaESVAGAI-TIRAFDEEERFFKKSLTLID 1096
Cdd:cd18551 153 IlplgrRIRKASKRAQDALGELSAAL---------ERALSAIrTVKASNAEERETKRGGEAAE 206
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1239-1375 |
1.29e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 52.18 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1239 IVGRTGSGKTTLISALFRLVEPVGGKIVVDG---VDI-SKIGVHDLRSRFGIIPQDPTLF-NGTVRFNLDPLCQHSDAEi 1313
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAeKGICLPPEKRRIGYVFQDARLFpHYKVRGNLRYGMAKSMVA- 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331862 1314 wevlgkcQLKEVVQEKenGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASID 1375
Cdd:PRK11144 108 -------QFDKIVALL--GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
617-818 |
1.31e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.59 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 617 KPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAA------ILGETPCVSGTIDFYGTIAY--------------VSQTAWI 676
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVlnrlieIYDSKIKVDGKVLYFGKDIFqidaiklrkevgmvFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 677 QTGTIRDNILF----GGVMDEHRYRETIQKSsldkdleLLPDGDQTEIGER----GVNLSGGQKQRIQLARALYQDADIY 748
Cdd:PRK14246 103 PHLSIYDNIAYplksHGIKEKREIKKIVEEC-------LRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331862 749 LLDDPFSAVDAhTASSLFQEYVMDALAGKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQELLARSRD 818
Cdd:PRK14246 176 LMDEPTSMIDI-VNSQAIEKLITELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEIFTSPKN 245
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
621-806 |
1.54e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.75 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 621 RNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG----------------------------------- 665
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGkeinalstaqrlarglvylpedrqssglyldapla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 666 ----TIAYVSQTAWIQTGtiRDNILFggvmdeHRYRETIQKSsldkdlelLPDGDQTEigeRGvnLSGGQKQRIQLARAL 741
Cdd:PRK15439 360 wnvcALTHNRRGFWIKPA--RENAVL------ERYRRALNIK--------FNHAEQAA---RT--LSGGNQQKVLIAKCL 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22331862 742 YQDADIYLLDDPFSAVDAHTASSLFQEYVMDALAGKAVLLVTHQVDFLPAF-DSVLLMSDGEITEA 806
Cdd:PRK15439 419 EASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMaDRVLVMHQGEISGA 484
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
889-1090 |
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 22331862 889 GYIFFFIASLAQVTFAV--GQILQ--NSWMAANVDNPQV--STLKLILVYLLIGLCSVLCLMVRSVCVVIMCMKSSASLF 962
Cdd:cd18577 4 GLLAAIAAGAALPLMTIvfGDLFDafTDFGSGESSPDEFldDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 963 SQLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDV--PFGLIFvvaSSVNTGCSLGVLAIVT-WQ---VLFVSVP-- 1034
Cdd:cd18577 84 KRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIgeKLGLLI---QSLSTFIAGFIIAFIYsWKltlVLLATLPli 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331862 1035 ---MVYLAFRLQKYyfqTAKELmringttRSY-VANHLAESVAGAI-TIRAFDEEERFFKK 1090
Cdd:cd18577 161 aivGGIMGKLLSKY---TKKEQ-------EAYaKAGSIAEEALSSIrTVKAFGGEEKEIKR 211
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
620-806 |
2.59e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 50.26 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILG-ETPCvSGTIDFYG----------------TIAYVSQTA-WIQTGTI 681
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGiERPS-AGKIWFSGhditrlknrevpflrrQIGMIFQDHhLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 682 RDN-----ILFGGVMDEHRYRETiqkSSLDKdLELLPDGDQTEIgergvNLSGGQKQRIQLARALYQDADIYLLDDPFSA 756
Cdd:PRK10908 97 YDNvaiplIIAGASGDDIRRRVS---AALDK-VGLLDKAKNFPI-----QLSGGEQQRVGIARAVVNKPAVLLADEPTGN 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 22331862 757 VDAHTASS---LFQEYvmdALAGKAVLLVTHQVDFLPAFD-SVLLMSDGEITEA 806
Cdd:PRK10908 168 LDDALSEGilrLFEEF---NRVGVTVLMATHDIGLISRRSyRMLTLSDGHLHGG 218
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1234-1420 |
2.60e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.52 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1234 GHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQDPTLFNGtvrfnldplcqhsdaei 1313
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGE----------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1314 wevlgkcqlkevvqekengldslvvedgsnwsMGQRQLFclGRAVLRRSRVLVLDEATASIDNATDLILQKTIR------ 1387
Cdd:smart00382 65 --------------------------------LRLRLAL--ALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllll 110
|
170 180 190
....*....|....*....|....*....|....
gi 22331862 1388 -REFADCTVITVAHRIPTVMDcTMVLSISDGRIV 1420
Cdd:smart00382 111 lKSEKNLTVILTTNDEKDLGP-ALLRRRFDRRIV 143
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
623-759 |
2.62e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 51.38 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 623 VSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-----------IAYVSQT-AWIQTGTIRDNILFG-- 688
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnelepadrdIAMVFQNyALYPHMSVRENMAYGlk 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331862 689 --GVMDEHRyRETIQKSSldKDLELLPDGDQteigeRGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDA 759
Cdd:PRK11650 103 irGMPKAEI-EERVAEAA--RILELEPLLDR-----KPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
678-784 |
2.79e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.71 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 678 TGTIRDniLFGGVmDEH-RYRETIQK----SSLDKDLEllpdgdqteigergvNLSGGQKQRIQLARALYQDADIYLLDD 752
Cdd:COG1245 177 KGTVRE--LLEKV-DERgKLDELAEKlgleNILDRDIS---------------ELSGGELQRVAIAAALLRDADFYFFDE 238
|
90 100 110
....*....|....*....|....*....|....*
gi 22331862 753 PFSAVDAH---TASSLFQEYvmdALAGKAVLLVTH 784
Cdd:COG1245 239 PSSYLDIYqrlNVARLIREL---AEEGKYVLVVEH 270
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
711-802 |
3.06e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 49.11 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 711 LLPDGDQTE-------IGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAH---TASSLFQEYVMDalAGKAVL 780
Cdd:cd03222 49 LIPNGDNDEwdgitpvYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlNAARAIRRLSEE--GKKTAL 126
|
90 100
....*....|....*....|..
gi 22331862 781 LVTHQVDFLPAFDSVLLMSDGE 802
Cdd:cd03222 127 VVEHDLAVLDYLSDRIHVFEGE 148
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
617-830 |
3.51e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 50.48 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 617 KPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSG-------------------TIDFYGTIAYVSQTAWIQ 677
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdvllggrsifnyrdVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 678 TGTIRDNILFGGVMDEHRYRETIQKSSLDKDLEL-LPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSA 756
Cdd:PRK14271 114 PMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVgLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 757 VDAHTASSLfQEYVMDALAGKAVLLVTHQVDFLPAF-DSVLLMSDGEITEADTYQELLARSRdfqdlvnaHRETA 830
Cdd:PRK14271 194 LDPTTTEKI-EEFIRSLADRLTVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQLFSSPK--------HAETA 259
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1190-1291 |
3.90e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.18 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1190 EVIEETRPPVnwPVTGRV--EISDLQIRYRRESPlVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVV 1267
Cdd:COG3845 241 EVLLRVEKAP--AEPGEVvlEVENLSVRDDRGVP-ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRL 317
|
90 100
....*....|....*....|....*.
gi 22331862 1268 DGVDISKIGVHDLRsRFGI--IPQDP 1291
Cdd:COG3845 318 DGEDITGLSPRERR-RLGVayIPEDR 342
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1204-1435 |
4.00e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 50.39 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1204 TGRVEISDLQIRYRRESPLVLKGI---SCTFEGGHKIGIVGRTGSGKTTLISALFRL-VEPVGGKIVVD---GVDISKIG 1276
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTPFEFKALnntSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiISETGQTIVGDyaiPANLKKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1277 -VHDLRSRFGIIPQDP--TLFNGTVRFNLDPLCQHSDAEIWEVLGKC-QLKEVVQEKENGLDSLVVEdgsnWSMGQRQLF 1352
Cdd:PRK13645 84 eVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVpELLKLVQLPEDYVKRSPFE----LSGGQKRRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1353 CLGRAVLRRSRVLVLDEATASID--NATDLI-LQKTIRREFADcTVITVAHRIPTVMDCT-MVLSISDGRIVEYDEPMKL 1428
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDpkGEEDFInLFERLNKEYKK-RIIMVTHNMDQVLRIAdEVIVMHEGKVISIGSPFEI 238
|
....*..
gi 22331862 1429 MKDENSL 1435
Cdd:PRK13645 239 FSNQELL 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
622-814 |
4.41e-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: 50.96 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 622 NVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGTIAYVSQTAWIQTGTIRDNILFGGVMDEHR---YRE 698
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGPDGRGRAKRYIGILHQEYDlypHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 699 TIQKSSLDKDLELlPD--------------GDQTEIGERGVN-----LSGGQKQRIQLARALYQDADIYLLDDPFSAVDA 759
Cdd:TIGR03269 382 VLDNLTEAIGLEL-PDelarmkavitlkmvGFDEEKAEEILDkypdeLSEGERHRVALAQVLIKEPRIVILDEPTGTMDP 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 760 HTASSLfQEYVMDALA--GKAVLLVTHQVDF-LPAFDSVLLMSDGEITEADTYQELLA 814
Cdd:TIGR03269 461 ITKVDV-THSILKAREemEQTFIIVSHDMDFvLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1214-1401 |
5.55e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 49.19 E-value: 5.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1214 IRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVE--PVGGKIVVDGVDiskigvhdlrsrfgiIPQDP 1291
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQ---------------FGREA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1292 TLfngtvrfnLDPLCQHSD-AEIWEVLGKCQLKEVVqekengldsLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEA 1370
Cdd:COG2401 101 SL--------IDAIGRKGDfKDAVELLNAVGLSDAV---------LWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEF 163
|
170 180 190
....*....|....*....|....*....|....*
gi 22331862 1371 TASIDNAT----DLILQKTIRRefADCTVITVAHR 1401
Cdd:COG2401 164 CSHLDRQTakrvARNLQKLARR--AGITLVVATHH 196
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
620-758 |
6.55e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.96 E-value: 6.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTL---LAAIlgETPcVSGTIDFYGTIAYVSQTAWIQTGTIRDNILFggvmdEHRY 696
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLarlLTMI--ETP-TGGELYYQGQDLLKADPEAQKLLRQKIQIVF-----QNPY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 697 -----RETIQkSSLDKDLELLPDGDQTEIGERG------VNL------------SGGQKQRIQLARALYQDADIYLLDDP 753
Cdd:PRK11308 103 gslnpRKKVG-QILEEPLLINTSLSAAERREKAlammakVGLrpehydryphmfSGGQRQRIAIARALMLDPDVVVADEP 181
|
....*
gi 22331862 754 FSAVD 758
Cdd:PRK11308 182 VSALD 186
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
603-850 |
6.60e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.47 E-value: 6.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 603 IKSASFSWEEKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILG--ETPCV---SGTIDFYG-TIAYVSQTAWI 676
Cdd:PRK15134 8 IENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRllPSPPVvypSGDIRFHGeSLLHASEQTLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 677 QtgtIRDN---ILFGGVMDEHRYRETIQKS-----SLDKDL-------ELLPDGDQTEI--GERGVN-----LSGGQKQR 734
Cdd:PRK15134 88 G---VRGNkiaMIFQEPMVSLNPLHTLEKQlyevlSLHRGMrreaargEILNCLDRVGIrqAAKRLTdyphqLSGGERQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 735 IQLARALYQDADIYLLDDPFSAVDAHTasslfQEYVMDALA------GKAVLLVTHQVDFLPAF-DSVLLMSDGEITEAD 807
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSV-----QAQILQLLRelqqelNMGLLFITHNLSIVRKLaDRVAVMQNGRCVEQN 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 22331862 808 TYQELLARSRD--FQDLVNAhrETAGseRVVAVENPTKPVKEINR 850
Cdd:PRK15134 240 RAATLFSAPTHpyTQKLLNS--EPSG--DPVPLPEPASPLLDVEQ 280
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
618-812 |
6.96e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 49.36 E-value: 6.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 618 PNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-----------------IAYVSQTAWIQ--T 678
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitstsknkdikqirkkVGLVFQFPESQlfE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 679 GTIRDNILFG----GVMDEH---RYRETIQKSSLDKDLellpdgdqteIGERGVNLSGGQKQRIQLARALYQDADIYLLD 751
Cdd:PRK13649 101 ETVLKDVAFGpqnfGVSQEEaeaLAREKLALVGISESL----------FEKNPFELSGGQMRRVAIAGILAMEPKILVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22331862 752 DPFSAVDAHTASSLFQEYVMDALAGKAVLLVTHQVDFLPAF-DSVLLMSDGEI----TEADTYQEL 812
Cdd:PRK13649 171 EPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYaDFVYVLEKGKLvlsgKPKDIFQDV 236
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
698-784 |
7.51e-06 |
|
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: 49.29 E-value: 7.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 698 ETIQKSSLDKDLELLPdgdqteIGERGV-NLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAH---TASSLFQEYVMDa 773
Cdd:cd03236 116 ERGKLDELVDQLELRH------VLDRNIdQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqrlNAARLIRELAED- 188
|
90
....*....|.
gi 22331862 774 laGKAVLLVTH 784
Cdd:cd03236 189 --DNYVLVVEH 197
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
889-1085 |
9.13e-06 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 49.23 E-value: 9.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 889 GYIFFFIASLAQ--VTFAVGQILQNswMAANVDNPQVStlKLILVYLLIGLCSVLCLMVRSvCVVIMCMkssASLFSQLL 966
Cdd:cd18784 1 AFFFLLAAAVGEifIPYYTGQVIDG--IVIEKSQDKFS--RAIIIMGLLAIASSVAAGIRG-GLFTLAM---ARLNIRIR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 967 NSLFRA----PMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLIFVVASSVNTGCSLGVLAIVTWQ---VLFVSVPMVYLA 1039
Cdd:cd18784 73 NLLFRSivsqEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQlslVTLIGLPLIAIV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 22331862 1040 FRLQ-KYYFQTAKELMringtTRSYVANHLAESVAGAI-TIRAFDEEE 1085
Cdd:cd18784 153 SKVYgDYYKKLSKAVQ-----DSLAKANEVAEETISSIrTVRSFANED 195
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1223-1421 |
9.69e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 48.93 E-value: 9.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1223 VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGvhdlrSRFGIIPQDPTLF-----NGT 1297
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVVFQNEGLLpwrnvQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1298 VRFNLdplcqhsdaEIWEVlGKCQLKEVVQEKENGLDSLVVEDGSNW--SMGQRQLFCLGRAVLRRSRVLVLDEATASID 1375
Cdd:PRK11248 91 VAFGL---------QLAGV-EKMQRLEIAHQMLKKVGLEGAEKRYIWqlSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 22331862 1376 NATDLILQKTIRREFADC--TVITVAHRI--PTVMDCTMVL-SISDGRIVE 1421
Cdd:PRK11248 161 AFTREQMQTLLLKLWQETgkQVLLITHDIeeAVFMATELVLlSPGPGRVVE 211
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
634-796 |
9.98e-06 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 48.03 E-value: 9.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 634 AVCGEVGSGKSTLLAAI----LGETPCVSGTIDFYGTIAYVSQTAWIQtgtirdnilFGGVMDEHRYReTIQKSSLDKD- 708
Cdd:cd03279 32 LICGPTGAGKSTILDAItyalYGKTPRYGRQENLRSVFAPGEDTAEVS---------FTFQLGGKKYR-VERSRGLDYDq 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 709 ---LELLPDGDQTEIGERGV-NLSGGQKQRIQLARAL-----YQDA-----DIYLLDDPFSAVDAHTAsslfqEYVMDAL 774
Cdd:cd03279 102 ftrIVLLPQGEFDRFLARPVsTLSGGETFLASLSLALalsevLQNRggarlEALFIDEGFGTLDPEAL-----EAVATAL 176
|
170 180
....*....|....*....|....*..
gi 22331862 775 A-----GKAVLLVTHQVDFLPAFDSVL 796
Cdd:cd03279 177 ElirteNRMVGVISHVEELKERIPQRL 203
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1208-1291 |
1.05e-05 |
|
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: 50.07 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1208 EISDLQIRYRRESPL--VLKGISCTFEGGHKIGIVGRTGSGKT-TLISALfRLVEP----VGGKIVVDGVDISKIGVHDL 1280
Cdd:COG4172 8 SVEDLSVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDpaahPSGSILFDGQDLLGLSEREL 86
|
90
....*....|....*
gi 22331862 1281 R----SRFGIIPQDP 1291
Cdd:COG4172 87 RrirgNRIAMIFQEP 101
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
586-818 |
1.23e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 50.40 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 586 GERRRKQRSEGNQNAIIiKSASFSWEEKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYG 665
Cdd:TIGR01257 1922 AEERQRIISGGNKTDIL-RLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG 2000
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 666 -----TIAYVSQT-AWIQTGTIRDNILFGgvmDEHRYRETIQKSSLDKDLELLPDGDQTEIG------ERGVNLSGGQKQ 733
Cdd:TIGR01257 2001 ksiltNISDVHQNmGYCPQFDAIDDLLTG---REHLYLYARLRGVPAEEIEKVANWSIQSLGlslyadRLAGTYSGGNKR 2077
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 734 RIQLARALYQDADIYLLDDPFSAVDAHTASSLFQEYVMDALAGKAVLLVTHQVDFLPAFDSVL-LMSDGEITEADTYQEL 812
Cdd:TIGR01257 2078 KLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLaIMVKGAFQCLGTIQHL 2157
|
....*.
gi 22331862 813 LARSRD 818
Cdd:TIGR01257 2158 KSKFGD 2163
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1238-1420 |
1.41e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 49.25 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1238 GIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHD-LRSRFGIIPQD-------PTLfngTVRFN-----LDP 1304
Cdd:COG1129 282 GIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVPEDrkgeglvLDL---SIRENitlasLDR 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1305 LCQHSdaeiweVLGKCQLKEVVQE-------KENGLDSLVvedgSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASID-N 1376
Cdd:COG1129 359 LSRGG------LLDRRRERALAEEyikrlriKTPSPEQPV----GNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvG 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 22331862 1377 ATDLILQktIRREFAD--CTVI----------TVAHRIptvmdctMVLsiSDGRIV 1420
Cdd:COG1129 429 AKAEIYR--LIRELAAegKAVIvisselpellGLSDRI-------LVM--REGRIV 473
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
622-803 |
1.57e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 49.44 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 622 NVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCvsgtiDFYGTIaYVSQTAwIQTGTIRDNILFGGVM-DEHRYRE-- 698
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPG-----KFEGNV-FINGKP-VDIRNPAQAIRAGIAMvPEDRKRHgi 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 699 --------TIQKSSLDKDLELLPDGDQTEIG--ERGVN---------------LSGGQKQRIQLARALYQDADIYLLDDP 753
Cdd:TIGR02633 351 vpilgvgkNITLSVLKSFCFKMRIDAAAELQiiGSAIQrlkvktaspflpigrLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 22331862 754 FSAVDAHTASSLFQEYVMDALAGKAVLLVTHQV-DFLPAFDSVLLMSDGEI 803
Cdd:TIGR02633 431 TRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELaEVLGLSDRVLVIGEGKL 481
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
726-784 |
1.94e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.04 E-value: 1.94e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331862 726 NLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAH---TASSLFQEYVmdalAGKAVLLVTH 784
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRqrlNVARLIRELA----EGKYVLVVEH 269
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1189-1425 |
2.42e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.65 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1189 PEVIE-ETRPPVNWPVTGR-VEISDLQIRYrresplvlKGISCTFEGG--HK---IGIVGRTGSGKTTLISALFRLVEPV 1261
Cdd:PRK13409 321 PEPIEfEERPPRDESERETlVEYPDLTKKL--------GDFSLEVEGGeiYEgevIGIVGPNGIGKTTFAKLLAGVLKPD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1262 GGKIVVDgVDIS-KigvhdlrsrfgiiPQ----DptlFNGTVRFNLDPLCQHSDAEIW--EVLGKCQLKEVvqekengLD 1334
Cdd:PRK13409 393 EGEVDPE-LKISyK-------------PQyikpD---YDGTVEDLLRSITDDLGSSYYksEIIKPLQLERL-------LD 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1335 SLVvedgSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIRR--EFADCTVITVAHriptvmDCTMVL 1412
Cdd:PRK13409 449 KNV----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRiaEEREATALVVDH------DIYMID 518
|
250
....*....|...
gi 22331862 1413 SISDGRIVEYDEP 1425
Cdd:PRK13409 519 YISDRLMVFEGEP 531
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
597-812 |
2.48e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.70 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 597 NQNAIIIKSASFSWEEKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAIL-------GETPCVS--------GTI 661
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMrlleqagGLVQCDKmllrrrsrQVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 662 DFY------------GTIAYVSQ---TAWIQTGTIRDNI-----LFGGVMDEHRYRETiqKSSLDkdLELLPDGdQTEIG 721
Cdd:PRK10261 89 ELSeqsaaqmrhvrgADMAMIFQepmTSLNPVFTVGEQIaesirLHQGASREEAMVEA--KRMLD--QVRIPEA-QTILS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 722 ERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQEY-VMDALAGKAVLLVTHQVDFLPAF-DSVLLMS 799
Cdd:PRK10261 164 RYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIkVLQKEMSMGVIFITHDMGVVAEIaDRVLVMY 243
|
250
....*....|...
gi 22331862 800 DGEITEADTYQEL 812
Cdd:PRK10261 244 QGEAVETGSVEQI 256
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
963-1125 |
4.15e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 47.09 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 963 SQLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLIFVVASSVNTGCSLGVLAIVTWQVLFVSVPMVYLAF-- 1040
Cdd:cd18550 76 VQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVlp 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1041 --RLQKYYFQTAKELMRINGTTRSYVANHLaeSVAGAITIRAF----DEEERFFKKSLTLIDTNASpffhSFAANEWLIQ 1114
Cdd:cd18550 156 trRVGRRRRKLTREQQEKLAELNSIMQETL--SVSGALLVKLFgredDEAARFARRSRELRDLGVR----QALAGRWFFA 229
|
170
....*....|.
gi 22331862 1115 RLETVSAIVLA 1125
Cdd:cd18550 230 ALGLFTAIGPA 240
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
927-1091 |
4.37e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 47.09 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 927 KLILVYLLIGLcsVLCLMVRSVcvVIMCMKSSASLFSQLLNSLF----RAPMSFYDSTPLGRILSRVSSD-------LSI 995
Cdd:cd18540 43 GFILLYLGLIL--IQALSVFLF--IRLAGKIEMGVSYDLRKKAFehlqTLSFSYFDKTPVGWIMARVTSDtqrlgeiISW 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 996 VDLDVPFGLIFVVAssvntgcSLGVLAIVTWQ---VLFVSVPMVYLAFrlqkYYFQtaKELMRINGTTR---SYVANHLA 1069
Cdd:cd18540 119 GLVDLVWGITYMIG-------ILIVMLILNWKlalIVLAVVPVLAVVS----IYFQ--KKILKAYRKVRkinSRITGAFN 185
|
170 180
....*....|....*....|....*.
gi 22331862 1070 ESVAGAITIRAFDEEER----FFKKS 1091
Cdd:cd18540 186 EGITGAKTTKTLVREEKnlreFKELT 211
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
924-1086 |
4.77e-05 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 46.86 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 924 STLKLILVYLLIGLCSvlclMVRSVCVVIMCMKSSASLFSQLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFG 1003
Cdd:cd18780 44 AVLILLGVVLIGSIAT----FLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1004 LIFVVASSVNTGCSLGVLAIVTWQ---VLFVSVPMVYLAFRLQKYYFQTAKELMRingtTRSYVANHLAESVAGAI-TIR 1079
Cdd:cd18780 120 LSMLLRYLVQIIGGLVFMFTTSWKltlVMLSVVPPLSIGAVIYGKYVRKLSKKFQ----DALAAASTVAEESISNIrTVR 195
|
....*..
gi 22331862 1080 AFDEEER 1086
Cdd:cd18780 196 SFAKETK 202
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
923-1090 |
5.40e-05 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 46.72 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 923 VSTLKLILVYLL-IGLCSVLCLMVRSVCVVIMCMKSSASLFSQLLNSLFRAPMSFYDSTPLGRILSRV-----------S 990
Cdd:cd18588 38 LSTLDVLAIGLLvVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVGDTVARVrelesirqfltG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 991 SDLSIVdLDVPFGLIFvvassvntgcsLGVLAIVTWQ---VLFVSVP-MVYLAFRLQKYYFQTAKELMRINGTTRSYvan 1066
Cdd:cd18588 118 SALTLV-LDLVFSVVF-----------LAVMFYYSPTltlIVLASLPlYALLSLLVTPILRRRLEEKFQRGAENQSF--- 182
|
170 180
....*....|....*....|....
gi 22331862 1067 hLAESVAGAITIRAFDEEERFFKK 1090
Cdd:cd18588 183 -LVETVTGIETVKSLAVEPQFQRR 205
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1209-1421 |
5.67e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.54 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1209 ISDLQIRYRRESPLV--LKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKI-------------VVDGVDIS 1273
Cdd:PRK10261 15 VENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1274 KIGVHDLR-SRFGIIPQDPTLfngtvrfNLDPLCQHSD--AEIWEVLGKCQLKEVVQEKENGLDSLVVEDGS-------- 1342
Cdd:PRK10261 95 AAQMRHVRgADMAMIFQEPMT-------SLNPVFTVGEqiAESIRLHQGASREEAMVEAKRMLDQVRIPEAQtilsryph 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1343 NWSMGQRQLFCLGRAVLRRSRVLVLDEATASID---NATDLILQKTIRREFaDCTVITVAHRIPTVMDCT-MVLSISDGR 1418
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDvtiQAQILQLIKVLQKEM-SMGVIFITHDMGVVAEIAdRVLVMYQGE 246
|
...
gi 22331862 1419 IVE 1421
Cdd:PRK10261 247 AVE 249
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1224-1429 |
5.93e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.47 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1224 LKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGvHDLRSRFG--IIPQDPTLFNG-TVRF 1300
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQLGigIIYQELSVIDElTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1301 NLdPLCQHSDAEIWEV----LGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDN 1376
Cdd:PRK09700 100 NL-YIGRHLTKKVCGVniidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTN 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22331862 1377 ATDLILQKTIRREFADCT-VITVAHRIP---------TVM-DCTMVLS--ISDgriVEYDEPMKLM 1429
Cdd:PRK09700 179 KEVDYLFLIMNQLRKEGTaIVYISHKLAeirricdryTVMkDGSSVCSgmVSD---VSNDDIVRLM 241
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1207-1416 |
6.06e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 46.68 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1207 VEISDLqiRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDI---SKIGVHDLRSR 1283
Cdd:PRK11831 8 VDMRGV--SFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamSRSRLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1284 FGIIPQDPTLFNG-TVRFNLD-PLCQHSDaeiwevLGKCQLKEVVQEKEN--GLDSLVVEDGSNWSMGQRQLFCLGRAVL 1359
Cdd:PRK11831 86 MSMLFQSGALFTDmNVFDNVAyPLREHTQ------LPAPLLHSTVMMKLEavGLRGAAKLMPSELSGGMARRAALARAIA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 22331862 1360 RRSRVLVLDEATASIDNATDLILQKTIRR--EFADCTVITVAHRIPTvmdctmVLSISD 1416
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISElnSALGVTCVVVSHDVPE------VLSIAD 212
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
891-1086 |
6.38e-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: 46.74 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 891 IFFFIASLAQVT--FAVGQILqNSWMAANVDNPQV-STLKLILVYLL-IGLCSVLCLMVRSVCVVIMCMKSSASLFSQLL 966
Cdd:cd18573 3 ALLLVSSAVTMSvpFAIGKLI-DVASKESGDIEIFgLSLKTFALALLgVFVVGAAANFGRVYLLRIAGERIVARLRKRLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 967 NSLFRAPMSFYDSTPLGRILSRVSSDLSIV----DLDVPFGLIFVVASSVntgcSLGVLAIVTWQ---VLFVSVPMVYLA 1039
Cdd:cd18573 82 KSILRQDAAFFDKNKTGELVSRLSSDTSVVgkslTQNLSDGLRSLVSGVG----GIGMMLYISPKltlVMLLVVPPIAVG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22331862 1040 FRLqkyYFQTAKELmringtTRSYV-----ANHLAESVAGAI-TIRAFDEEER 1086
Cdd:cd18573 158 AVF---YGRYVRKL------SKQVQdaladATKVAEERLSNIrTVRAFAAERK 201
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1223-1451 |
7.02e-05 |
|
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: 47.10 E-value: 7.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1223 VLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRL--VEPVGGKIV---------------------------------V 1267
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtlepeeV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1268 DGVDISKIGVHDLRSRFGIIPQDP-TLF-NGTVRFNLDPLCQHSDAEIWEVLGKC-QLKEVVQekengLDSLVVEDGSNW 1344
Cdd:TIGR03269 95 DFWNLSDKLRRRIRKRIAIMLQRTfALYgDDTVLDNVLEALEEIGYEGKEAVGRAvDLIEMVQ-----LSHRITHIARDL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1345 SMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIRR--EFADCTVITVAHrIPTVMD--CTMVLSISDGRIV 1420
Cdd:TIGR03269 170 SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSH-WPEVIEdlSDKAIWLENGEIK 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 22331862 1421 EYDEPM----KLM-------KDENSLFGK---LVKEYWSHYNSAD 1451
Cdd:TIGR03269 249 EEGTPDevvaVFMegvseveKECEVEVGEpiiKVRNVSKRYISVD 293
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
923-1090 |
7.38e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 46.40 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 923 VSTLKLILVYLLI-GLCSVLCLMVRSVCVVIMCMKSSASLFSQLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVP 1001
Cdd:cd18568 38 ISLLNLILIGLLIvGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFQENQKIRRFLTR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1002 fGLIFVVASSVNTGCSLGVLAIVTWQ---VLFVSVPM-----VYLAFRLQKYY---FQTAKELMringttrsyvaNHLAE 1070
Cdd:cd18568 118 -SALTTILDLLMVFIYLGLMFYYNLQltlIVLAFIPLyvlltLLSSPKLKRNSreiFQANAEQQ-----------SFLVE 185
|
170 180
....*....|....*....|
gi 22331862 1071 SVAGAITIRAFDEEERFFKK 1090
Cdd:cd18568 186 ALTGIATIKALAAERPIRWR 205
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1223-1400 |
7.53e-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: 47.24 E-value: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1223 VLKGISCTFEGGHKIGIVGRTGSGKTTLIsalfrlvepvggKIVVdGVDISKIGVHDLRS--RFGIIPQDPTL-FNGTVR 1299
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLL------------RIMA-GVDKDFNGEARPQPgiKVGYLPQEPQLdPTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1300 FNLDPLCQH-----------------SDAEiWEVLGKCQ--LKEVVQEK---------ENGLDSLVVEDG----SNWSMG 1347
Cdd:TIGR03719 87 ENVEEGVAEikdaldrfneisakyaePDAD-FDKLAAEQaeLQEIIDAAdawdldsqlEIAMDALRCPPWdadvTKLSGG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22331862 1348 QRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIrREFADcTVITVAH 1400
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL-QEYPG-TVVAVTH 216
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
889-1087 |
1.63e-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: 45.17 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 889 GYIFFFIASLAQVTF--AVGQILQNSWMAANVDNPQVSTLKLILVYLLIGLCSvlclMVRSVCVVIMCMKSSASLFSQLL 966
Cdd:cd18576 1 GLILLLLSSAIGLVFplLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFS----FFRIYLFARVGERVVADLRKDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 967 NSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLIFVVASSVNTGCSLGVLAIVTWQ---VLFVSVPMVYLAF--- 1040
Cdd:cd18576 77 RHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKltlLMLATVPVVVLVAvlf 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22331862 1041 --RLQKYYFQTAKELMRINGTtrsyvanhLAESVAGAITIRAF----DEEERF 1087
Cdd:cd18576 157 grRIRKLSKKVQDELAEANTI--------VEETLQGIRVVKAFtredYEIERY 201
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
891-1090 |
3.27e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 44.42 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 891 IFFFIASLA-QV-TFAVGQILQnsWMAANVDNPQVSTLKLILVYLLIGLCSVLCLM--VRSVCVVIMCMKSSASLFSQLL 966
Cdd:cd18555 5 ISILLLSLLlQLlTLLIPILTQ--YVIDNVIVPGNLNLLNVLGIGILILFLLYGLFsfLRGYIIIKLQTKLDKSLMSDFF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 967 NSLFRAPMSFYDSTPLGRILSRVSSDLSIVD----------LDVPFGLIFVVASSVNTgcslGVLAIVtwqVLFVSVPMV 1036
Cdd:cd18555 83 EHLLKLPYSFFENRSSGDLLFRANSNVYIRQilsnqvisliIDLLLLVIYLIYMLYYS----PLLTLI---VLLLGLLIV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 22331862 1037 YLAFRLQKYYfqtaKELMRINGTTRSYVANHLAESVAGAITIRAFDEEERFFKK 1090
Cdd:cd18555 156 LLLLLTRKKI----KKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKK 205
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
620-801 |
3.83e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.22 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETP--CVSGTIDFYG------TIA----YVSQTAwIQTG--TIRDNI 685
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGfpkkqeTFArisgYCEQND-IHSPqvTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 686 LFGGVMdehRYRETIQKSS----LDKDLEL--LPDGDQTEIGERGVN-LSGGQKQRIQLARALYQDADIYLLDDPFSAVD 758
Cdd:PLN03140 975 IYSAFL---RLPKEVSKEEkmmfVDEVMELveLDNLKDAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 22331862 759 AHTASSLFQEYVMDALAGKAVLLVTHQ--VDFLPAFDSVLLMSDG 801
Cdd:PLN03140 1052 ARAAAIVMRTVRNTVDTGRTVVCTIHQpsIDIFEAFDELLLMKRG 1096
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
928-1086 |
4.69e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 43.99 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 928 LILVYLLIGLCSVLCLMVRSVCVVIMcmksSASLFSQLLNSLF----RAPMSFYDSTPLGRILSRVSSDLSIVDldvpfg 1003
Cdd:cd18567 44 LAIGFGLLLLLQALLSALRSWLVLYL----STSLNLQWTSNLFrhllRLPLSYFEKRHLGDIVSRFGSLDEIQQ------ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1004 liFVVASSVNtgcSL--GVLAIVTWQVLFV-SVPM---------VYLAFRL--QKYYFQTAKELMRINGTTRSyvanHLA 1069
Cdd:cd18567 114 --TLTTGFVE---ALldGLMAILTLVMMFLySPKLalivlaavaLYALLRLalYPPLRRATEEQIVASAKEQS----HFL 184
|
170
....*....|....*..
gi 22331862 1070 ESVAGAITIRAFDEEER 1086
Cdd:cd18567 185 ETIRGIQTIKLFGREAE 201
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
620-766 |
5.42e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.22 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTI-------DFYGTIAyvSQTAWIQ----------TGTIR 682
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSIlylgkevTFNGPKS--SQEAGIGiihqelnlipQLTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 683 DNIL--------FGGVMDEHRYRETiqksslDKDLELL--PDGDQTEIGErgvnLSGGQKQRIQLARALYQDADIYLLDD 752
Cdd:PRK10762 98 ENIFlgrefvnrFGRIDWKKMYAEA------DKLLARLnlRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDE 167
|
170
....*....|....*
gi 22331862 753 PFSAV-DAHTAsSLF 766
Cdd:PRK10762 168 PTDALtDTETE-SLF 181
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
634-816 |
5.47e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 44.09 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 634 AVCGEVGSGKSTLLAAILGETPCVSGTIDFYGT-----------------IAYVSQTAWI-QTGTIRDNILFG--GVMDE 693
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekgiclppekrrIGYVFQDARLfPHYKVRGNLRYGmaKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 694 HrYRETIQKSSLDKDLELLPdgdqteigergVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQeYvMDA 773
Cdd:PRK11144 108 Q-FDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP-Y-LER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 22331862 774 LAGKA---VLLVTHQVD-FLPAFDSVLLMSDGEITEADTYQELLARS 816
Cdd:PRK11144 174 LAREInipILYVSHSLDeILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
728-834 |
5.92e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 728 SGGQKQRIQLARALYQDADIYLLDDPFSAVDAHtASSLFQEYVMDalAGKAVLLVTHQVDFLPAFDSVLLMSDGEitEAD 807
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLH-AVLWLETYLLK--WPKTFIVVSHAREFLNTVVTDILHLHGQ--KLV 420
|
90 100 110
....*....|....*....|....*....|
gi 22331862 808 TYQ---ELLARSRDFQdLVNAHRETAGSER 834
Cdd:PLN03073 421 TYKgdyDTFERTREEQ-LKNQQKAFESNER 449
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
727-816 |
6.56e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 43.46 E-value: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 727 LSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQEYVMDALAGKAVLLVTHQVDFL-PAFDSVLLMSDGEITE 805
Cdd:PRK13638 137 LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILT 216
|
90
....*....|.
gi 22331862 806 ADTYQELLARS 816
Cdd:PRK13638 217 HGAPGEVFACT 227
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1188-1425 |
7.29e-04 |
|
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: 44.00 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1188 APEVIEETRPPVNWPvtgrveisDLQIRYrresplvlKGISCTFEGG--HK---IGIVGRTGSGKTTLISALFRLVEPVG 1262
Cdd:COG1245 331 APRREKEEETLVEYP--------DLTKSY--------GGFSLEVEGGeiREgevLGIVGPNGIGKTTFAKILAGVLKPDE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1263 GKIVVDgVDIS-KigvhdlrsrfgiiPQ----DptlFNGTVRFNLDPLCQHSDAEIW---EVLGKCQLKEVvqekengLD 1334
Cdd:COG1245 395 GEVDED-LKISyK-------------PQyispD---YDGTVEEFLRSANTDDFGSSYyktEIIKPLGLEKL-------LD 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1335 SLVvedgSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIRR--EFADCTVITVAHriptvmDCTMVL 1412
Cdd:COG1245 451 KNV----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRfaENRGKTAMVVDH------DIYLID 520
|
250
....*....|...
gi 22331862 1413 SISDGRIVEYDEP 1425
Cdd:COG1245 521 YISDRLMVFEGEP 533
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
591-721 |
7.31e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.23 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 591 KQRSEGNQNAIIIKsasfsweekGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILgeTPCVsgtidfygtiayv 670
Cdd:TIGR00630 604 AERRPGNGKFLTLK---------GARENNLKNITVSIPLGLFTCITGVSGSGKSTLINDTL--YPAL------------- 659
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 22331862 671 sqtawiqtgtirDNILFGGVMDEHRYRETIQKSSLDKDLELlpdgDQTEIG 721
Cdd:TIGR00630 660 ------------ANRLNGAKTVPGRYTSIEGLEHLDKVIHI----DQSPIG 694
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
961-1086 |
7.55e-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: 43.25 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 961 LFSQLLnslfRAPMSFYDSTPLGRILSRVSSDL-SIVDLdVPFGLIFVVASSVNTGCSLGVLAIVTWQ---VLFVSVPMV 1036
Cdd:cd18546 78 VFAHLQ----RLSLDFHERETSGRIMTRMTSDIdALSEL-LQTGLVQLVVSLLTLVGIAVVLLVLDPRlalVALAALPPL 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 22331862 1037 YLAFRLqkyyFQtaKELMRINGTTRSYVAN---HLAESVAGAITIRAFDEEER 1086
Cdd:cd18546 153 ALATRW----FR--RRSSRAYRRARERIAAvnaDLQETLAGIRVVQAFRRERR 199
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
591-651 |
1.00e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.91 E-value: 1.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331862 591 KQRSEGNQNAIIIKsasfsweekGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAIL 651
Cdd:PRK00349 605 KERRKGNGKFLKLK---------GARENNLKNVDVEIPLGKFTCVTGVSGSGKSTLINETL 656
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
620-758 |
1.17e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.16 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 620 LRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCvSGTIDFYGT----------------IAYVSQTAW-------- 675
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDGQplhnlnrrqllpvrhrIQVVFQDPNsslnprln 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 676 ----IQTGTIRDNILFGGVMDEHRYRETIQKSSLDkdlellPDGDQTEIGErgvnLSGGQKQRIQLARALYQDADIYLLD 751
Cdd:PRK15134 381 vlqiIEEGLRVHQPTLSAAQREQQVIAVMEEVGLD------PETRHRYPAE----FSGGQRQRIAIARALILKPSLIILD 450
|
....*..
gi 22331862 752 DPFSAVD 758
Cdd:PRK15134 451 EPTSSLD 457
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
727-789 |
1.26e-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: 1.26e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331862 727 LSGGQKQRIQLARAL----YQDADIYLLDDPFSAVDAHTASSLFqEYVMDALAGKA-VLLVTHQVDFL 789
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALA-EAILEHLVKGAqVIVITHLPELA 144
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
586-651 |
1.34e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.48 E-value: 1.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22331862 586 GERR---RKQRSEGNQNAIIIKsasfsweekGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAIL 651
Cdd:COG0178 593 GRKRipvPKKRRKGNGKFLTIK---------GARENNLKNVDVEIPLGVLTCVTGVSGSGKSTLVNDIL 652
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
1237-1277 |
1.43e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 42.45 E-value: 1.43e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 22331862 1237 IGIVGRTGSGKTTLISALFrlvepvggkivvdGVDISKIGV 1277
Cdd:COG3596 42 IALVGKTGAGKSSLINALF-------------GAEVAEVGV 69
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1218-1377 |
1.77e-03 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 41.33 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1218 RESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKigvhdLRSRF-----------GI 1286
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-----QRDEYhqdllylghqpGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1287 ipqDPTLfngTVRFNLDPLCQHS----DAEIWEVLGKCQLKEVvqekengLDSLVvedgSNWSMGQRQLFCLGRAVLRRS 1362
Cdd:PRK13538 86 ---KTEL---TALENLRFYQRLHgpgdDEALWEALAQVGLAGF-------EDVPV----RQLSAGQQRRVALARLWLTRA 148
|
170
....*....|....*
gi 22331862 1363 RVLVLDEATASIDNA 1377
Cdd:PRK13538 149 PLWILDEPFTAIDKQ 163
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
603-665 |
2.21e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.32 E-value: 2.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 603 IKSASFSWEEKgstkPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILG--ETPCVSGTIDFYG 665
Cdd:PRK09580 4 IKDLHVSVEDK----AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKG 64
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1234-1291 |
2.72e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 41.45 E-value: 2.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22331862 1234 GHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDL---------RSRFGIIPQDP 1291
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHP 98
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1224-1431 |
3.31e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 41.27 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1224 LKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVH----DLRSRFGIIPQDP--TLFNGT 1297
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdikQIRKKVGLVFQFPesQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1298 V---------RFNLDPlcqhsdaEIWEVLGKCQLKEVvqekenGLD-SLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVL 1367
Cdd:PRK13649 103 VlkdvafgpqNFGVSQ-------EEAEALAREKLALV------GISeSLFEKNPFELSGGQMRRVAIAGILAMEPKILVL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22331862 1368 DEATASIDNATdlilqktiRREFADC---------TVITVAHRIPTVMD-CTMVLSISDGRIVEYDEPMKLMKD 1431
Cdd:PRK13649 170 DEPTAGLDPKG--------RKELMTLfkklhqsgmTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1186-1401 |
3.35e-03 |
|
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: 42.04 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1186 PEAPEVIEETRPPVNWPVTGRVEISDLQIRYRrESPLVL-KGI----SCTFE--GGHKIGIVGRTGSGKttliSALFRLV 1258
Cdd:TIGR00954 424 EEIESGREGGRNSNLVPGRGIVEYQDNGIKFE-NIPLVTpNGDvlieSLSFEvpSGNNLLICGPNGCGK----SSLFRIL 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1259 epvGGKIVVDGVDISKigvhDLRSRFGIIPQDPTLFNGTVRFNL---DPLCQH-----SDAEIWEVLGKCQLKEVVQEkE 1330
Cdd:TIGR00954 499 ---GELWPVYGGRLTK----PAKGKLFYVPQRPYMTLGTLRDQIiypDSSEDMkrrglSDKDLEQILDNVQLTHILER-E 570
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331862 1331 NGLDSLvvedgSNW----SMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIRRefADCTVITVAHR 1401
Cdd:TIGR00954 571 GGWSAV-----QDWmdvlSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHR 638
|
|
| YfjP |
cd11383 |
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
1238-1263 |
5.03e-03 |
|
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They 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. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.
Pssm-ID: 206743 [Multi-domain] Cd Length: 140 Bit Score: 38.86 E-value: 5.03e-03
10 20
....*....|....*....|....*..
gi 22331862 1238 GIVGRTGSGKTTLISALFRL-VEPVGG 1263
Cdd:cd11383 1 GLMGKTGAGKSSLCNALFGTeVAAVGD 27
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1195-1299 |
5.28e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 41.19 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 1195 TRPPVNWPVTGRVEISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISAL-FRL---VEpVGGKIVVDGV 1270
Cdd:TIGR00955 12 GRVAQDGSWKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALaFRSpkgVK-GSGSVLLNGM 90
|
90 100 110
....*....|....*....|....*....|...
gi 22331862 1271 disKIGVHDLRSRFGIIPQD----PTLfngTVR 1299
Cdd:TIGR00955 91 ---PIDAKEMRAISAYVQQDdlfiPTL---TVR 117
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
964-1086 |
5.31e-03 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 40.48 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 964 QLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLIFVVASSVNTGCSLGVLAIVTWQVLFVSVPMVYLAFRLQ 1043
Cdd:cd18554 84 DLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAV 163
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 22331862 1044 KYYFQTAKELMRINGTTRSYVANHLAESVAGAITIRAFDEEER 1086
Cdd:cd18554 164 KYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKH 206
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
1236-1272 |
6.83e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 37.98 E-value: 6.83e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 22331862 1236 KIGIVGRTGSGKTTLISALFRLVEPVG-----------GKIVVDGVDI 1272
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAIVSdypgttrdpneGRLELKGKQI 48
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1210-1254 |
6.95e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 6.95e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 22331862 1210 SDLQIRyrRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISAL 1254
Cdd:PRK10636 5 SSLQIR--RGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALL 47
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
893-1098 |
7.56e-03 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 40.07 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 893 FFIASLAQVTFAVGQILQNSWMA-------ANVDNPQVstLKLILVYLLIGLCSVLClmvrSVCVVIMCMKSSASLFSQL 965
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMAdiidegiANGDLSYI--LRTGLLMLLLALLGLIA----GILAGYFAAKASQGFGRDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 966 LNSLFRAPMSF----YDSTPLGRILSRVSSD-----------LSIVdLDVPFGLIFVVASSVNTGCSLGVLAIVTwqVLF 1030
Cdd:cd18548 75 RKDLFEKIQSFsfaeIDKFGTSSLITRLTNDvtqvqnfvmmlLRML-VRAPIMLIGAIIMAFRINPKLALILLVA--IPI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331862 1031 VSVPMVYLAFRLQKYYFQTAKELMRINGTTRsyvanhlaESVAGAITIRAFD----EEERFFKKSLTLIDTN 1098
Cdd:cd18548 152 LALVVFLIMKKAIPLFKKVQKKLDRLNRVVR--------ENLTGIRVIRAFNredyEEERFDKANDDLTDTS 215
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
632-712 |
9.63e-03 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 38.81 E-value: 9.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331862 632 KVAVCGEVGSGKSTLLAAILGETpcVSgtIDFYGTI--AYVSQTAW-IQTGTIRDNIL-FGGVMDEHRYRETIQKSSLDK 707
Cdd:COG1100 5 KIVVVGTGGVGKTSLVNRLVGDI--FS--LEKYLSTngVTIDKKELkLDGLDVDLVIWdTPGQDEFRETRQFYARQLTGA 80
|
....*
gi 22331862 708 DLELL 712
Cdd:COG1100 81 SLYLF 85
|
|
| |
