|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-1487 |
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: 1522.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 17 ELKPVFVVCLLILAAIDLSLALTEDTGQATIPPVKYTNPILYLCTWLL-VLVIQHCRQCCIQkNSWFLSMFWILSLLCGI 95
Cdd:TIGR00957 66 KTKTALGFLLWIVCWADLFYSFWERSHGRAPAPVFLVSPTLLGITMLLaTFLIQLERRKGVQ-SSGIMLTFWLVALVCAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 96 FQFQT-LIRALLQDSKSNMTYSCLFFVSYGFQIVILILSAFSESS--------DSTHAPSATASFLSSVTFSWYDSTVLK 166
Cdd:TIGR00957 145 AILRSkILLALKEDAIVDPFRDTTFYIYFALVLSQLVLSCFSDKSplfsetnhDPNPCPESSASFLSRITFWWITGMAVY 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 167 GYKHPLTIEDVWDIEENLKAKSLTSKFKTIMTKDLQKARQALQRRL--KKSQQSPEGTShgltkKQSQSQDVLVLedskk 244
Cdd:TIGR00957 225 GYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKTRKQPVSAVygKKDPSKPKGSS-----QLDANEEVEAL----- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 245 kkKKSEATKDFPKSwLVKALFKTFYVVILKSFILKLAHDILLFLNPQLLKFLIGFVKDPDSYPWVGYIYAILMFSVTLIQ 324
Cdd:TIGR00957 295 --IVKSPHKPRKPS-LFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPDWQGYFYTGLLFVCACLQ 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 325 SFFLQCYFQFCFVLGMTVRTTIIASVYKKALTLSNLARRQYTIGETVNLMSVDSQKLMDVTNYIHLLWSSVLQIALSIFF 404
Cdd:TIGR00957 372 TLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYF 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 405 LWRELGPSILAGVGLMVLLVPVNGVLATKIRKIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFKEQVNSIRKKELR 484
Cdd:TIGR00957 452 LWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELK 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 485 NLLRFSQLQTILIFILHLTPTLVSVITFSVYVLVDSQNVLNAEKAFTSITLFNILRFPLAMLPMVISSVIQASVSVDRLE 564
Cdd:TIGR00957 532 VLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNILDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLR 611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 565 QYLGSDDLDLSAIRHVCHFD---KAVQFSEASFTWDRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENV 641
Cdd:TIGR00957 612 IFLSHEELEPDSIERRTIKPgegNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKV 691
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 642 HGHITIKGSIAYVPQQAWIQNGTIKDNILFGSEYDEKKYQRVIEACALLPDLEMLPGGDMAEIGEKGINLSGGQKHRVSL 721
Cdd:TIGR00957 692 EGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSL 771
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 722 ARATYQDADIYILDDPLSAVDTHVGKHIFNKVVGPNGLLSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGSYSDLMDK 801
Cdd:TIGR00957 772 ARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQR 851
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 802 KGVFAKNWKTFmkhsgpegeATVDNDSEEEDGDCGLI--PTVEEIP-DDAASLTMRRENSLRRTLSRSSRSGSRRGKSLK 878
Cdd:TIGR00957 852 DGAFAEFLRTY---------APDEQQGHLEDSWTALVsgEGKEAKLiENGMLVTDVVGKQLQRQLSASSSDSGDQSRHHG 922
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 879 SSLKIKSVNAlnkKEEVvkgQKLIKKEFVETGKVKFSIYLKYLQAVGWWSLLFIVIFYVLNYVAFIGTNLWLSAWTSDSe 958
Cdd:TIGR00957 923 SSAELQKAEA---KEET---WKLMEADKAQTGQVELSVYWDYMKAIGLFITFLSIFLFVCNHVSALASNYWLSLWTDDP- 995
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 959 KQNGTDNSpsqRDMRIGVFGALGIAQGIFLLSSSLWSIYACRNASKTLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDI 1038
Cdd:TIGR00957 996 MVNGTQNN---TSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKEL 1072
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1039 STVDDTLPQTLRSWLLCFFGIVSTLVMICMATPIFIIIIIPLSILYVSVQVFYVATSRQLRRLDSVTKSPIYSHFSETVS 1118
Cdd:TIGR00957 1073 DTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLL 1152
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1119 GLPVIRAFEHQQRFLANSEKQIDTNQKCVFSWITSNRWLAIRLELVGNLIVFCSALLLVIYKNSLTGDTVGFVLSNALNI 1198
Cdd:TIGR00957 1153 GVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQV 1232
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1199 TQTLNWLVRMTSEVETNIVAVERINEYINVDNEAPW-VTDKKPPADWPKKGEIQFNNYQVRYRPELDLVLKGITCNIKST 1277
Cdd:TIGR00957 1233 TFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWqIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGG 1312
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1278 EKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTIIPQDPILFSGNLRMNLDPFNKYSDEEIW 1357
Cdd:TIGR00957 1313 EKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVW 1392
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1358 RALELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRNEFSQCT 1437
Cdd:TIGR00957 1393 WALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCT 1472
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|
gi 569006289 1438 VITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELLSNMGPFYLMAKEAGI 1487
Cdd:TIGR00957 1473 VLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAKDAGL 1522
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
43-1476 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 1050.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 43 GQATIPPVKYTNPILYLCTWLLVLV-IQHCRQCCIQKNSWFLSmFWILSLLCGIFQFQTLIRALLQ--DSKSNMTYSCLF 119
Cdd:PLN03130 103 GQTSLPPFEIVSLIVEALTWCSMLVmIGVETKIYIREFRWYVR-FAVIYVLVGDAVMLNLVLSVKEyySSFVLYLYISEV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 120 FVSYGFQIVILI----LSAF-------SESSDSTH----------APSATASFLSSVTFSWYDSTVLKGYKHPLTIEDVW 178
Cdd:PLN03130 182 AAQVLFGILLLVyfpnLDPYpgytpigSESVDDYEyeelpggeqiCPERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVW 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 179 DIEENLKAKSLTSKFKTIMTKDLQKarqalqrrlkksqqspegtshgltkkqsqsqdvlvledskkkkkkseatkdfPKS 258
Cdd:PLN03130 262 KLDTWDQTETLYRSFQKCWDEELKK----------------------------------------------------PKP 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 259 WLVKALFKTFYVVILKSFILKLAHDILLFLNPQLLKFLIGFVKDPDSyPWVGYIYAILMFSVTLIQSFFLQCYFQFCFVL 338
Cdd:PLN03130 290 WLLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQNGEP-AWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 339 GMTVRTTIIASVYKKALTLSNLARRQYTIGETVNLMSVDSQKLMDVTNYIHLLWSSVLQIALSIFFLWRELGPSILAGVG 418
Cdd:PLN03130 369 GFRLRSTLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSL 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 419 LMVLLVPVNGVLATKIRKIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFKEQVNSIRKKELRNLLRFSQLQTILIF 498
Cdd:PLN03130 449 MLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSF 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 499 ILHLTPTLVSVITFSVYVLVDSqnVLNAEKAFTSITLFNILRFPLAMLPMVISSVIQASVSVDRLEQYLGSDDLDLSAIR 578
Cdd:PLN03130 529 ILNSIPVLVTVVSFGVFTLLGG--DLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEERVLLPNP 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 579 HVCHFDKAVQFSEASFTWDRDLE-ATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENV-HGHITIKGSIAYVPQ 656
Cdd:PLN03130 607 PLEPGLPAISIKNGYFSWDSKAErPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRsDASVVIRGTVAYVPQ 686
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 657 QAWIQNGTIKDNILFGSEYDEKKYQRVIEACALLPDLEMLPGGDMAEIGEKGINLSGGQKHRVSLARATYQDADIYILDD 736
Cdd:PLN03130 687 VSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDD 766
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 737 PLSAVDTHVGKHIFNKVVgpNGLLSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGSYSDLMDKKGVFAKnwktFMKHS 816
Cdd:PLN03130 767 PLSALDAHVGRQVFDKCI--KDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQK----LMENA 840
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 817 GpEGEATVDNDSEEEDGDCGLIPTVEEIPDDaasltmrrenslrrtlsrssrsgsrrgkslkssLKIKSVNALNKKEevv 896
Cdd:PLN03130 841 G-KMEEYVEENGEEEDDQTSSKPVANGNANN---------------------------------LKKDSSSKKKSKE--- 883
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 897 KGQKLIKKEFVETGKVKFSIYLKYLQAVG-WWSLLFIVIFYVLNYVAFIGTNLWLSAWTSDSEKQngtDNSPSqrdMRIG 975
Cdd:PLN03130 884 GKSVLIKQEERETGVVSWKVLERYKNALGgAWVVMILFLCYVLTEVFRVSSSTWLSEWTDQGTPK---THGPL---FYNL 957
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 976 VFGALGIAQGIFLLSSSLWSIYACRNASKTLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDTLPQTLRSWLLC 1055
Cdd:PLN03130 958 IYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQ 1037
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1056 FFGIVSTLVMICMATPIFIIIIIPLSILYVSVQVFYVATSRQLRRLDSVTKSPIYSHFSETVSGLPVIRAFEHQQRFLAN 1135
Cdd:PLN03130 1038 IFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEI 1117
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1136 SEKQIDTNQKCVFSWITSNRWLAIRLELVGNLIVFCSALLLVIyKNSLTGD------TVGFVLSNALNITQTLNWLVRMT 1209
Cdd:PLN03130 1118 NGRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVM-QNGRAENqaafasTMGLLLSYALNITSLLTAVLRLA 1196
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1210 SEVETNIVAVERINEYINVDNEAPWVT-DKKPPADWPKKGEIQFNNYQVRYRPELDLVLKGITCNIKSTEKVGVVGRTGA 1288
Cdd:PLN03130 1197 SLAENSLNAVERVGTYIDLPSEAPLVIeNNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGA 1276
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1289 GKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTIIPQDPILFSGNLRMNLDPFNKYSDEEIWRALELAHLKSF 1368
Cdd:PLN03130 1277 GKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDV 1356
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1369 VAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTI 1448
Cdd:PLN03130 1357 IRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTI 1436
|
1450 1460
....*....|....*....|....*...
gi 569006289 1449 MDSDKIMVLDSGKIVEYGSPEELLSNMG 1476
Cdd:PLN03130 1437 IDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
34-1492 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 974.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 34 LSLALTEDTGQATIPPVKYTNPILYLCTW--LLVLVIQHCRQCcIQKNSWFLSmFWILSLLCGIFQFQTLIRALLQDSKS 111
Cdd:PLN03232 94 MGISLFDMDEETDLPPFEVASLMVEAFAWfsMLVLIGLETKQY-VKEFRWYVR-FGVVYVLVADAVLLDLVLPLKNSINR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 112 NMTYSCLFF----VSYGFQIVILI--LSAFS-------ESSDSTH----------APSATASFLSSVTFSWYDSTVLKGY 168
Cdd:PLN03232 172 TALYLCISSrccqALFGILLLVYIpeLDPYPgyhilnnESLDNVEydalrggeniCPERYASIFSRIYFSWMTPLMQLGY 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 169 KHPLTIEDVWDIEENLKAKSLTSKFKTIMTKDLQKarqalqrrlkksqqspegtshgltkkqsqsqdvlvledskkkkkk 248
Cdd:PLN03232 252 RKPITEKDVWQLDQWDQTETLIKRFQRCWTEESRR--------------------------------------------- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 249 seatkdfPKSWLVKALFKTFYVVILKSFILKLAHDILLFLNPQLLKFLIGFVKDPDSyPWVGYIYAILMFSVTLIQSFFL 328
Cdd:PLN03232 287 -------PKPWLLRALNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMQEGDP-AWVGYVYAFLIFFGVTFGVLCE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 329 QCYFQFCFVLGMTVRTTIIASVYKKALTLSNLARRQYTIGETVNLMSVDSQKLMDVTNYIHLLWSSVLQIALSIFFLWRE 408
Cdd:PLN03232 359 SQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQ 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 409 LGPSILAGVGLMVLLVPVNGVLATKIRKIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFKEQVNSIRKKELrNLLR 488
Cdd:PLN03232 439 LGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEEL-SWFR 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 489 FSQLQTIL-IFILHLTPTLVSVITFSVYVLVDSQnvLNAEKAFTSITLFNILRFPLAMLPMVISSVIQASVSVDRLEQYL 567
Cdd:PLN03232 518 KAQLLSAFnSFILNSIPVVVTLVSFGVFVLLGGD--LTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELL 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 568 GSDDLDLSAIRHVCHFDKAVQFSEASFTWDRDLE-ATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVH-GHI 645
Cdd:PLN03232 596 LSEERILAQNPPLQPGAPAISIKNGYFSWDSKTSkPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtSSV 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 646 TIKGSIAYVPQQAWIQNGTIKDNILFGSEYDEKKYQRVIEACALLPDLEMLPGGDMAEIGEKGINLSGGQKHRVSLARAT 725
Cdd:PLN03232 676 VIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAV 755
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 726 YQDADIYILDDPLSAVDTHVGKHIFNKVVGPNglLSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGSYSDLMDKKGVF 805
Cdd:PLN03232 756 YSNSDIYIFDDPLSALDAHVAHQVFDSCMKDE--LKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLF 833
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 806 AKnwktFMKHSGpEGEATVDNDSEEEDGDcGLIPTVEeipddaasltmrrenslrrtlsrssrsGSRRGKSLKSSLKIKS 885
Cdd:PLN03232 834 KK----LMENAG-KMDATQEVNTNDENIL-KLGPTVT---------------------------IDVSERNLGSTKQGKR 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 886 VNALnkkeevvkgqkLIKKEFVETGKVKFSIYLKYLQAV-GWWSLLFIVIFYVLNYVAFIGTNLWLSAWTSDSEKQNgtd 964
Cdd:PLN03232 881 GRSV-----------LVKQEERETGIISWNVLMRYNKAVgGLWVVMILLVCYLTTEVLRVSSSTWLSIWTDQSTPKS--- 946
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 965 NSPSqrdMRIGVFGALGIAQGIFLLSSSLWSIYACRNASKTLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDT 1044
Cdd:PLN03232 947 YSPG---FYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRN 1023
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1045 LPQTLRSWLLCFFGIVSTLVMICMATPIFIIIIIPLSILYVSVQVFYVATSRQLRRLDSVTKSPIYSHFSETVSGLPVIR 1124
Cdd:PLN03232 1024 VANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIR 1103
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1125 AFEHQQRFLANSEKQIDTNQKCVFSWITSNRWLAIRLELVGNLIVFCSALLLVIyKNSLTGDTVGF------VLSNALNI 1198
Cdd:PLN03232 1104 AYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVL-RNGNAENQAGFastmglLLSYTLNI 1182
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1199 TQTLNWLVRMTSEVETNIVAVERINEYINVDNEAPWV-TDKKPPADWPKKGEIQFNNYQVRYRPELDLVLKGITCNIKST 1277
Cdd:PLN03232 1183 TTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIiENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPS 1262
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1278 EKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTIIPQDPILFSGNLRMNLDPFNKYSDEEIW 1357
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLW 1342
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1358 RALELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRNEFSQCT 1437
Cdd:PLN03232 1343 EALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCT 1422
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|....*.
gi 569006289 1438 VITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELLSNMG-PFYLMAKEAGIESVNH 1492
Cdd:PLN03232 1423 MLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVHSTGPANAQY 1478
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
255-1474 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 785.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 255 FPKSW-LVKALFKTFYVVILKSFILKLAHDILLFLNPQLLKFLIGFVKDPDSYPWVGYIYAILMFSVTLIQSFFLQCYFQ 333
Cdd:PTZ00243 228 TPKRLsLLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRFYY 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 334 FCFVLGMTVRTTIIASVYKKALTLSN--LARRQYTIGETVNLMSVDSQKLMDVTNYIHLLWSSVLQIALSIFFLWRELGP 411
Cdd:PTZ00243 308 ISIRCGLQYRSALNALIFEKCFTISSksLAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGW 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 412 SILAGVGLMVLLVPVNGVLATKIRKIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFKEQVNSIRKKELRNLLRFSQ 491
Cdd:PTZ00243 388 CALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQL 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 492 LQTILIFILHLTPTLVSVITFSVYVLvdSQNVLNAEKAFTSITLFNILRFPLAMLPMVISSVIQASVSVDRLEQYLGSDD 571
Cdd:PTZ00243 468 ARVATSFVNNATPTLMIAVVFTVYYL--LGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLECDN 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 572 LDLSAIR-----------HVCHFDKAVQFSEASFT-----------------WDRDL----------------------- 600
Cdd:PTZ00243 546 ATCSTVQdmeeywreqreHSTACQLAAVLENVDVTafvpvklprapkvktslLSRALrmlcceqcrptkrhpspsvvved 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 601 ----------------------EAT-------------------------IQDVNLDIKPGQLVAVVGTVGSGKSSLISA 633
Cdd:PTZ00243 626 tdygspssasrhiveggtggghEATptsersaktpkmktddffelepkvlLRDVSVSVPRGKLTVVLGATGSGKSTLLQS 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 634 MLGEMENVHGHITIKGSIAYVPQQAWIQNGTIKDNILFGSEYDEKKYQRVIEACALLPDLEMLPGGDMAEIGEKGINLSG 713
Cdd:PTZ00243 706 LLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSG 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 714 GQKHRVSLARATYQDADIYILDDPLSAVDTHVGKHIFNKVVgpNGLLSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKG 793
Cdd:PTZ00243 786 GQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF--LGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSG 863
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 794 SYSDLMDKKgvFAKNWKTFMKHSGPEGEATVDNDSEEEDGDCGLIPTVEEipddaasltmrrenslrrtlsrssrsgsrr 873
Cdd:PTZ00243 864 SSADFMRTS--LYATLAAELKENKDSKEGDADAEVAEVDAAPGGAVDHEP------------------------------ 911
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 874 gKSLKSSLKIKSVNALNKkeEVVKGQkLIKKEFVETGKVKFSIYLKYLQAVG---WWSLLfIVIFYVLNYVAfIGTNLWL 950
Cdd:PTZ00243 912 -PVAKQEGNAEGGDGAAL--DAAAGR-LMTREEKASGSVPWSTYVAYLRFCGglhAAGFV-LATFAVTELVT-VSSGVWL 985
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 951 SAWTSDSEKQNGTDNSPSQrdMRIGVFGALGIAQGIFLlssslwSIYACRNASKTLHRQLLTNILRAPMSFFDTTPTGRI 1030
Cdd:PTZ00243 986 SMWSTRSFKLSAATYLYVY--LGIVLLGTFSVPLRFFL------SYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRI 1057
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1031 VNRFAGDISTVDDTLPQTLRSWLLCFFGIVSTLVMICMATPIFIIIIIPLSILYVSVQVFYVATSRQLRRLDSVTKSPIY 1110
Cdd:PTZ00243 1058 LNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVF 1137
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1111 SHFSETVSGLPVIRAFEHQQRFLANSEKQIDTNQKCVFSWITSNRWLAIRLELVGNLIVFCSALLLVIYK-NSLTGDTVG 1189
Cdd:PTZ00243 1138 TLLEEALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGVIGTmLRATSQEIG 1217
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1190 FV---LSNALNITQTLNWLVRMTSEVETNIVAVERINEYI-NVDNEA-P-----------------------WVTDKKPP 1241
Cdd:PTZ00243 1218 LVslsLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTdEVPHEDmPeldeevdalerrtgmaadvtgtvVIEPASPT 1297
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1242 ADWP---KKGEIQFNNYQVRYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASI 1318
Cdd:PTZ00243 1298 SAAPhpvQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAY 1377
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1319 GLHDLRGRLTIIPQDPILFSGNLRMNLDPFNKYSDEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLG 1398
Cdd:PTZ00243 1378 GLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMA 1457
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 1399 RAVLRK-SKILVLDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELLSN 1474
Cdd:PTZ00243 1458 RALLKKgSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMN 1534
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
144-1478 |
5.12e-156 |
|
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: 512.53 E-value: 5.12e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 144 APSATASFLSSVTFSWYDSTVLKGYKHPLTIEDVWDIEENLKAKSLTSKFKtimtkdlqkarQALQRRLKKSQQSPEgts 223
Cdd:TIGR01271 4 SPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLE-----------REWDRELASAKKNPK--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 224 hgltkkqsqsqdvlvledskkkkkkseatkdfpkswLVKALFKTFYVVILKSFILKLAHDILLFLNPQLLKFLIGFVkDP 303
Cdd:TIGR01271 70 ------------------------------------LLNALRRCFFWRFVFYGILLYFGEATKAVQPLLLGRIIASY-DP 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 304 DSYP--WVGYIYAILMFSVTLIQSFFLQCYFQFCFVLGMTVRTTIIASVYKKALTLSNLARRQYTIGETVNLMSVDSQKL 381
Cdd:TIGR01271 113 FNAPerEIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKF 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 382 MDVTNYIHLLWSSVLQIALSIFFLWRELGPSILAGVGLMVLLVPVNGVLATKIRKIQVQNMKNKDKRLKIMNEILSGIKI 461
Cdd:TIGR01271 193 DEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQS 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 462 LKYFAWEPSFKEQVNSIRKKELRNLLRFSQLQTILIFILHLTPTLVSVITFSVYVLVDSqnvLNAEKAFTSITLFNILRF 541
Cdd:TIGR01271 273 VKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVVFLSVVPYALIKG---IILRRIFTTISYCIVLRM 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 542 PLA-MLPMVISSVIQASVSVDRLEQYLGSDD-------LDLSAIRHVC-----------HFDKAVQFSEASFTWDRD--- 599
Cdd:TIGR01271 350 TVTrQFPGAIQTWYDSLGAITKIQDFLCKEEyktleynLTTTEVEMVNvtaswdegigeLFEKIKQNNKARKQPNGDdgl 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 600 --------LEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGSIAYVPQQAWIQNGTIKDNILF 671
Cdd:TIGR01271 430 ffsnfslyVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIF 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 672 GSEYDEKKYQRVIEACALLPDLEMLPGGDMAEIGEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVDTHVGKHIFN 751
Cdd:TIGR01271 510 GLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFE 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 752 KVVGPngLLSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGSYSDLMDKKGVFAK------------------------ 807
Cdd:TIGR01271 590 SCLCK--LMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSlllgleafdnfsaerrnsiltetl 667
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 808 ------------NW----KTFMKHSGPE-----------------------------GEATVDNDSEEEDGD--CGLIPT 840
Cdd:TIGR01271 668 rrvsidgdstvfSGpetiKQSFKQPPPEfaekrkqsiilnpiasarkfsfvqmgpqkAQATTIEDAVREPSErkFSLVPE 747
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 841 VEE---------IPDDAASLTMRRENSLRRTLSRSSRSGSRRGKSLKSSLKIKSVNALNK-------------------- 891
Cdd:TIGR01271 748 DEQgeeslprgnQYHHGLQHQAQRRQSVLQLMTHSNRGENRREQLQTSFRKKSSITQQNElaseldiysrrlskdsvyei 827
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 892 KEEVvkGQKLIKKEFVETGKVKF-----SIYLKYLQAVGwwSLLFIVIFYVLNYVAFIGTN---LWL---SAWTSDSEKQ 960
Cdd:TIGR01271 828 SEEI--NEEDLKECFADERENVFetttwNTYLRYITTNR--NLVFVLIFCLVIFLAEVAASllgLWLitdNPSAPNYVDQ 903
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 961 N-GTDNSPSQRDMRI--------------GV---FGALGIAQGIFLLSSSLwsiyacrNASKTLHRQLLTNILRAPMSFF 1022
Cdd:TIGR01271 904 QhANASSPDVQKPVIitptsayyifyiyvGTadsVLALGFFRGLPLVHTLL-------TVSKRLHEQMLHSVLQAPMAVL 976
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1023 DTTPTGRIVNRFAGDISTVDDTLPQTLRSWLLCFFGIVSTLVMICMATPIFIIIIIPLSILYVSVQVFYVATSRQLRRLD 1102
Cdd:TIGR01271 977 NTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLE 1056
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1103 SVTKSPIYSHFSETVSGLPVIRAFEHQQRFLANSEKQIDTNQKCVFSWITSNRWLAIRLELVgNLIVFCSALLLVIYKNS 1182
Cdd:TIGR01271 1057 SEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDII-FVFFFIAVTFIAIGTNQ 1135
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1183 LTGDTVGFVLSNALNITQTLNWLVRMTSEVETNIVAVERINEYINVDNEAPWVTDKKPPAD---------------WPKK 1247
Cdd:TIGR01271 1136 DGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRPSGGGGKYQlstvlvienphaqkcWPSG 1215
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1248 GEIQFNNYQVRYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILeSAGGQIIIDGIDIASIGLHDLRGRL 1327
Cdd:TIGR01271 1216 GQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRKAF 1294
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1328 TIIPQDPILFSGNLRMNLDPFNKYSDEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKI 1407
Cdd:TIGR01271 1295 GVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKI 1374
|
1450 1460 1470 1480 1490 1500 1510
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569006289 1408 LVLDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELLSNMGPF 1478
Cdd:TIGR01271 1375 LLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
274-563 |
4.00e-151 |
|
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: 460.78 E-value: 4.00e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 274 KSFILKLAHDILLFLNPQLLKFLIGFVKDPDSYPWVGYIYAILMFSVTLIQSFFLQCYFQFCFVLGMTVRTTIIASVYKK 353
Cdd:cd18595 1 LAALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 354 ALTLSNLARRQYTIGETVNLMSVDSQKLMDVTNYIHLLWSSVLQIALSIFFLWRELGPSILAGVGLMVLLVPVNGVLATK 433
Cdd:cd18595 81 ALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 434 IRKIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFKEQVNSIRKKELRNLLRFSQLQTILIFILHLTPTLVSVITFS 513
Cdd:cd18595 161 IKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 569006289 514 VYVLVDSQNVLNAEKAFTSITLFNILRFPLAMLPMVISSVIQASVSVDRL 563
Cdd:cd18595 241 TYVLSDPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
929-1225 |
8.47e-144 |
|
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: 441.53 E-value: 8.47e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 929 LLFIVIFYVLNYVAFIGTNLWLSAWTSDSEKQNGTDNSpsQRDMRIGVFGALGIAQGIFLLSSSLWSIYACRNASKTLHR 1008
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDTE--QRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1009 QLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDTLPQTLRSWLLCFFGIVSTLVMICMATPIFIIIIIPLSILYVSVQ 1088
Cdd:cd18603 79 KLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1089 VFYVATSRQLRRLDSVTKSPIYSHFSETVSGLPVIRAFEHQQRFLANSEKQIDTNQKCVFSWITSNRWLAIRLELVGNLI 1168
Cdd:cd18603 159 RFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLI 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 1169 VFCSALLLVIYKNSLTGDTVGFVLSNALNITQTLNWLVRMTSEVETNIVAVERINEY 1225
Cdd:cd18603 239 VLFAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEY 295
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1248-1468 |
6.66e-124 |
|
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: 384.92 E-value: 6.66e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1248 GEIQFNNYQVRYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRL 1327
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1328 TIIPQDPILFSGNLRMNLDPFNKYSDEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKI 1407
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569006289 1408 LVLDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSP 1468
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
587-788 |
6.77e-114 |
|
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: 356.78 E-value: 6.77e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 587 VQFSEASFTWDRDLEA---TIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGSIAYVPQQAWIQNG 663
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 664 TIKDNILFGSEYDEKKYQRVIEACALLPDLEMLPGGDMAEIGEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVDT 743
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 569006289 744 HVGKHIFNKVVGPNgLLSGKTRILVTHGIHFLPQVDEIVVLGKGT 788
Cdd:cd03250 161 HVGRHIFENCILGL-LLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
275-563 |
1.65e-112 |
|
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: 356.80 E-value: 1.65e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 275 SFILKLAHDILLFLNPQLLKFLIGFVKDPDSYP-WVGYIYAILMFSVTLIQSFFLQCYFQFCFVLGMTVRTTIIASVYKK 353
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPlSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 354 ALTLSNLARRQYTIGETVNLMSVDSQKLMDVTNYIHLLWSSVLQIALSIFFLWRELGPSILAGVGLMVLLVPVNGVLATK 433
Cdd:cd18579 82 ALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 434 IRKIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFKEQVNSIRKKELRNLLRFSQLQTILIFILHLTPTLVSVITFS 513
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 569006289 514 VYVLVDsqNVLNAEKAFTSITLFNILRFPLAMLPMVISSVIQASVSVDRL 563
Cdd:cd18579 242 TYVLLG--NPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
929-1226 |
7.37e-104 |
|
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: 332.93 E-value: 7.37e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 929 LLFIVIFYVLNYVAFIGTNLWLSAWTSDSekqngTDNSPSQRDMRIGVFGALGIAQGIFL-LSSSLWSIYACRNASKTLH 1007
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDW-----SSSPNSSSGYYLGVYAALLVLASVLLvLLRWLLFVLAGLRASRRLH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1008 RQLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDTLPQTLRSWLLCFFGIVSTLVMICMATPIFIIIIIPLSILYVSV 1087
Cdd:cd18580 76 DKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1088 QVFYVATSRQLRRLDSVTKSPIYSHFSETVSGLPVIRAFEHQQRFLANSEKQIDTNQKCVFSWITSNRWLAIRLELVGNL 1167
Cdd:cd18580 156 QRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGAL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 569006289 1168 IVFCSALLLVIYKNSLTGDTVGFVLSNALNITQTLNWLVRMTSEVETNIVAVERINEYI 1226
Cdd:cd18580 236 LALVVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
918-1479 |
5.39e-100 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 332.90 E-value: 5.39e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 918 LKYLQAVgWWSLLFIVIFYVLNYVAFIGTnLWLSAWTSDsekqNGTDNSPSQRDMRI-GVFGALGIAQGIFLLSSSLWSI 996
Cdd:COG1132 13 LRYLRPY-RGLLILALLLLLLSALLELLL-PLLLGRIID----ALLAGGDLSALLLLlLLLLGLALLRALLSYLQRYLLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 997 YACRNASKTLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDTLPQTLRSWLLCFFGIVSTLVMICMATPIFIII 1076
Cdd:COG1132 87 RLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1077 IIPLSILYVSVQVFYVATSRQLRRLDSVTKSPIYSHFSETVSGLPVIRAFEHQQRFLANSEKQIDTNQKCVFSWITSNRW 1156
Cdd:COG1132 167 VLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1157 LAIRLELVGNL---IVFCSALLLVIyKNSLT-GDTVGFVLSnALNITQTLNWLVRMTSEVETNIVAVERINEYINVDNEA 1232
Cdd:COG1132 247 FFPLMELLGNLglaLVLLVGGLLVL-SGSLTvGDLVAFILY-LLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1233 PWVTDKKPPAdwPKKGEIQFNNYQVRYRPElDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFR------------- 1299
Cdd:COG1132 325 PDPPGAVPLP--PVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRfydptsgrilidg 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1300 --IlesaggqiiidgidiASIGLHDLRGRLTIIPQDPILFSGNLRMNL---DPfnKYSDEEIWRALELAHLKSFVAGLQL 1374
Cdd:COG1132 402 vdI---------------RDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAKAAQAHEFIEALPD 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1375 GLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIMDSDKI 1454
Cdd:COG1132 465 GYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRI 544
|
570 580
....*....|....*....|....*
gi 569006289 1455 MVLDSGKIVEYGSPEELLSNmGPFY 1479
Cdd:COG1132 545 LVLDDGRIVEQGTHEELLAR-GGLY 568
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
929-1225 |
9.81e-94 |
|
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: 304.40 E-value: 9.81e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 929 LLFIVIFYVLNYVAFIGTNLWLSAWTSDSEKQNgtdnspsqRDMRIGVFGALGIAQGIFLLSSSLWSIYACRNASKTLHR 1008
Cdd:cd18606 1 LPLLLLLLILSQFAQVFTNLWLSFWTEDFFGLS--------QGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1009 QLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDTLPQTLRSWLLCFFGIVSTLVMICMATPIFIIIIIPLSILYVSVQ 1088
Cdd:cd18606 73 KALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1089 VFYVATSRQLRRLDSVTKSPIYSHFSETVSGLPVIRAFEHQQRFLANSEKQIDTNQKCVFSWITSNRWLAIRLELVGNLI 1168
Cdd:cd18606 153 NYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 1169 VFCSALLLVIYKNSLTGDTVGFVLSNALNITQTLNWLVRMTSEVETNIVAVERINEY 1225
Cdd:cd18606 233 VLIVALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHY 289
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1244-1468 |
6.62e-92 |
|
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: 295.86 E-value: 6.62e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1244 WPKKGEIQFNNYQVRYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDL 1323
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1324 RGRLTIIPQDPILFSGNLRMNLDPFNKYSDEEIWRALelahlksfvaglqlgllhEVTEGGDNLSIGQRQLLCLGRAVLR 1403
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569006289 1404 KSKILVLDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSP 1468
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
930-1226 |
5.77e-89 |
|
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: 291.29 E-value: 5.77e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 930 LFIVIFYVLNYVAFIGTNLWLSAWTSDSEKQNGTDNSPSQRDMRIGVFGALGIAQGIFLLSSSLWSIYACRNASKTLHRQ 1009
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVSVLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1010 LLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDTLPQTLRSWLLCFFGIVSTLVMICMATPIFIIIIIPLSILYVSVQV 1089
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1090 FYVATSRQLRRLDSVTKSPIYSHFSETVSGLPVIRAFEHQQRFLANSEKQIDTNQKCVFSWITSNRWLAIRLELVGNLIV 1169
Cdd:cd18604 162 LYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFS 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 1170 FCSALLLViYKNSLTGDTVGFVLSNALNITQTLNWLVRMTSEVETNIVAVERINEYI 1226
Cdd:cd18604 242 FATAALLV-YGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
930-1225 |
2.53e-84 |
|
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: 278.72 E-value: 2.53e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 930 LFIVIFYVLNYVAFIGTNLWLSAWTS-----DSEKQNGTDNSPSQRDMR--IGVFGALGIAQGIFLLSSSLWSIYACRNA 1002
Cdd:cd18602 2 ALVLALALLKQGLRVATDFWLADWTEanhdvASVVFNITSSSLEDDEVSyyISVYAGLSLGAVILSLVTNLAGELAGLRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1003 SKTLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDTLPQTLRSWLLCFFGIVSTLVMICMATPIFIIIIIPLSI 1082
Cdd:cd18602 82 ARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIII 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1083 LYVSVQVFYVATSRQLRRLDSVTKSPIYSHFSETVSGLPVIRAFEHQQRFLANSEKQIDTNQKCVFSWITSNRWLAIRLE 1162
Cdd:cd18602 162 VYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLD 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569006289 1163 LVGNLIVFCSAL--LLVIYKNSLTGDTVGFVLSNALNITQTLNWLVRMTSEVETNIVAVERINEY 1225
Cdd:cd18602 242 YLGAVIVFLAALssLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEY 306
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
275-563 |
1.47e-83 |
|
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: 275.87 E-value: 1.47e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 275 SFILKLAHDILLFLNPQLLKFLIGFVKD-----PDSYPWVGYIYAILMFSVTLIQSFFLQCYFQFCFVLGMTVRTTIIAS 349
Cdd:cd18597 2 AGLLKLLADVLQVLSPLLLKYLINFVEDaylggPPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 350 VYKKALTLSNLARRQYTIGETVNLMSVDSQKLMDVTNYIHLLWSSVLQIALSIFFLWRELGPSILAGVGLMVLLVPVNGV 429
Cdd:cd18597 82 IYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 430 LATKIRKIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFKEQVNSIRKKELRNLLRFSQLQTILIFILHLTPTLVSV 509
Cdd:cd18597 162 LMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASM 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 569006289 510 ITFSVYVLVDsqNVLNAEKAFTSITLFNILRFPLAMLPMVISSVIQASVSVDRL 563
Cdd:cd18597 242 LSFITYYATG--HTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
276-563 |
2.13e-82 |
|
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: 273.22 E-value: 2.13e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 276 FILKLAHDILLFLNPQLLKFLIGFVKDPDSYPWV-GYIYAILMFSVTLIQSFFLQCYFQFCFVLGMTVRTTIIASVYKKA 354
Cdd:cd18596 3 ALLAVLSSVLSFAPPFFLNRLLRYLEDPGEDATVrPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 355 LTLSNLA-------------------RRQYTIGETVNLMSVDSQKLMDVTNYIHLLWSSVLQIALSIFFLWRELGPSILA 415
Cdd:cd18596 83 LRRRDKSgssksseskkkdkeededeKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 416 GVGLMVLLVPVNGVLATKIRKIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFKEQVNSIRKKELRNLLRFSQLQTI 495
Cdd:cd18596 163 GLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569006289 496 LIFILHLTPTLVSVITFSVYVLVdSQNVLNAEKAFTSITLFNILRFPLAMLPMVISSVIQASVSVDRL 563
Cdd:cd18596 243 LSLLWFLIPILVTVVTFATYTLV-MGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
974-1484 |
3.86e-80 |
|
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: 280.18 E-value: 3.86e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 974 IGVFGALgIAQGIFLLSSSLWSIYACRNASKTLHRQLLTNILRAPMSFFDTTPTGRIVNRFaGDISTVDDTLP-QTLRSW 1052
Cdd:COG2274 200 IGLLLAL-LFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTgSLLTAL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1053 LLCFFGIVSTLVMIcmatpifiiiiiplsilYVSVQVFYVA-------------TSRQLRRLD---SVTKSPIYSHFSET 1116
Cdd:COG2274 278 LDLLFVLIFLIVLF-----------------FYSPPLALVVllliplyvllgllFQPRLRRLSreeSEASAKRQSLLVET 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1117 VSGLPVIRAFEHQQRFLANSE----KQIDTNQKcVFSWITSNRWLAIRLELVGNLIVFCSALLLVIyKNSLTgdtVG-FV 1191
Cdd:COG2274 341 LRGIETIKALGAESRFRRRWEnllaKYLNARFK-LRRLSNLLSTLSGLLQQLATVALLWLGAYLVI-DGQLT---LGqLI 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1192 LSNALnITQTLNWLVRMTS---EVETNIVAVERINEYINVDNEAPWVTDKKPPAdwPKKGEIQFNNYQVRYRPELDLVLK 1268
Cdd:COG2274 416 AFNIL-SGRFLAPVAQLIGllqRFQDAKIALERLDDILDLPPEREEGRSKLSLP--RLKGDIELENVSFRYPGDSPPVLD 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1269 GITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTIIPQDPILFSGNLRMNL--- 1345
Cdd:COG2274 493 NISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlg 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1346 DPfnKYSDEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLI 1425
Cdd:COG2274 573 DP--DATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAII 650
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 569006289 1426 QTTIRNEFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELLSNMGPFYLMAKE 1484
Cdd:COG2274 651 LENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
277-563 |
1.52e-78 |
|
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: 261.33 E-value: 1.52e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 277 ILKLAHDILLFLNPQLLKFLIGFVKDPDSYPWVGYIYAILMFSVTLIQSFflqCYFQFCFV---LGMTVRTTIIASVYKK 353
Cdd:cd18598 4 LLKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGAL---LSSHYNFQmnkVSLKVRAALVTAVYRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 354 ALTLSNLARRQYTIGETVNLMSVDSQKLMDVTNYIHLLWSSVLQIALSIFFLWRELGPSILAGVGLMVLLVPVNGVLATK 433
Cdd:cd18598 81 ALRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 434 IRKIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFKEQVNSIRKKELRNLLRFSQLQTILIFILHLTPTLVSVITFS 513
Cdd:cd18598 161 IGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPVLISILTFA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 569006289 514 VYVLVdsQNVLNAEKAFTSITLFNILRFPLAMLPMVISSVIQASVSVDRL 563
Cdd:cd18598 241 TYVLM--GNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
929-1226 |
1.42e-77 |
|
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: 259.00 E-value: 1.42e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 929 LLFIVIFYVLNYVAFIGTNLWLSAWTSDSEKQNGTDNSPSQRDMrIGVFGALGIAQGIFLLSSSLWSIYACRNASKTLHR 1008
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWVSHSNNSFFNFINDSFNFF-LTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1009 QLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDTLPQTLRSWLLCFFGIVSTLVMICMATPIFIIIIIPLSILYVSVQ 1088
Cdd:cd18605 80 KLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1089 VFYVATSRQLRRLDSVTKSPIYSHFSETVSGLPVIRAFEHQQRFLANSEKQIDTNQKCVFSWITSNRWLAIRLELVGNLI 1168
Cdd:cd18605 160 RYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVLI 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569006289 1169 VFC---SALLLVIYKNSLTGDTVGFVLSNALNITQTLNWLVRMTSEVETNIVAVERINEYI 1226
Cdd:cd18605 240 VTFvalTAVVQHFFGLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
259-807 |
3.89e-77 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 267.80 E-value: 3.89e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 259 WLVKALFKTFYVVILKSFILKLAHDILLFLNPQLLKFLI--GFVKDPDSYPWvgyIYAILMFSVTLIQSFFLQCYFQFCF 336
Cdd:COG1132 10 RRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIdaLLAGGDLSALL---LLLLLLLGLALLRALLSYLQRYLLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 337 VLGMTVRTTIIASVYKKALTLSNLARRQYTIGETVNLMSVDSQKLMD-VTNYIHLLWSSVLQIALSI---FFLWRELGPS 412
Cdd:COG1132 87 RLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQfLAHGLPQLVRSVVTLIGALvvlFVIDWRLALI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 413 ILAGVGLMVLLVpvnGVLATKIRKIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFKEQVNSIRKKELRNLLRFSQL 492
Cdd:COG1132 167 VLLVLPLLLLVL---RLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 493 QTILIFILHLTPTLVSVITFSVYVLVDSQNVLNAEKAFTSITLFNILRFPLAMLPMVISSVIQASVSVDRLEQYL--GSD 570
Cdd:COG1132 244 SALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLdePPE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 571 DLDLSAIRHVCHFDKAVQFSEASFTWDRDlEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG- 649
Cdd:COG1132 324 IPDPPGAVPLPPVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGv 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 650 ------------SIAYVPQQAWIQNGTIKDNILFGS-EYDEKKYQRVIEACALLPDLEMLPGGDMAEIGEKGINLSGGQK 716
Cdd:COG1132 403 dirdltleslrrQIGVVPQDTFLFSGTIRENIRYGRpDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQR 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 717 HRVSLARATYQDADIYILDDPLSAVDTHVGKHIFNKVvgpNGLLSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGSYS 796
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEAL---ERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHE 559
|
570
....*....|.
gi 569006289 797 DLMDKKGVFAK 807
Cdd:COG1132 560 ELLARGGLYAR 570
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
275-563 |
3.77e-74 |
|
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: 249.05 E-value: 3.77e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 275 SFILKLAHDILLFLNPQLLKFLIGFVKDPDSYPWVGYIYAILMFSVTLIQSFFLQCYFQFCFVLGMTVRTTIIASVYKKA 354
Cdd:cd18559 2 FLLIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 355 LTLSNLARRQYTIGETVNLMSVDSQKLMDVTNYIHLLWSSVLQIALSIFFLWRELGPSILAGVGLMVLLVPVNGVLATKI 434
Cdd:cd18559 82 LRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 435 RKIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFKEQVNSIRKKELRNLLRFSQLQTILIFILHLTPTLVSVITFSV 514
Cdd:cd18559 162 RQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 569006289 515 YVLVDSQNVLNAEKAFTSITLFNILRFPLAMLPMVISSVIQASVSVDRL 563
Cdd:cd18559 242 YVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
249-810 |
1.29e-72 |
|
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: 258.23 E-value: 1.29e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 249 SEATKDFPKSWLVKALF---KTFYVVILKSFILKLahdiLLFLNPQLLKFLIGFVKDPDSYPWVgYIYAILMFSVTLIQS 325
Cdd:COG2274 136 KRGEKPFGLRWFLRLLRryrRLLLQVLLASLLINL----LALATPLFTQVVIDRVLPNQDLSTL-WVLAIGLLLALLFEG 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 326 FF--LQCYFqfcfVLGMTVR--TTIIASVYKKALTLSNLARRQYTIGETVN-LMSVDS-QKLMdvTNYIHLLWSSVLQIA 399
Cdd:COG2274 211 LLrlLRSYL----LLRLGQRidLRLSSRFFRHLLRLPLSFFESRSVGDLASrFRDVESiREFL--TGSLLTALLDLLFVL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 400 LSIFFLWReLGPSI-LAGVGLMVLLVPVNGVLATKIRKIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFKEQVNSI 478
Cdd:COG2274 285 IFLIVLFF-YSPPLaLVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 479 RKKELRNLLRFSQLQTILIFILHLTPTLVSVIT--FSVYVLVDSQnvlnaekaftsITL-----FNIL--RF--PLAMLP 547
Cdd:COG2274 364 LAKYLNARFKLRRLSNLLSTLSGLLQQLATVALlwLGAYLVIDGQ-----------LTLgqliaFNILsgRFlaPVAQLI 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 548 MVISSVIQASVSVDRLEQYLG--SDDLDLSAIRHVCHFDKAVQFSEASFTWDRDLEATIQDVNLDIKPGQLVAVVGTVGS 625
Cdd:COG2274 433 GLLQRFQDAKIALERLDDILDlpPEREEGRSKLSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGS 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 626 GKSSLISAMLGEMENVHGHITIKG-------------SIAYVPQQAWIQNGTIKDNILFG-SEYDEKKYQRVIEACALLP 691
Cdd:COG2274 513 GKSTLLKLLLGLYEPTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGTIRENITLGdPDATDEEIIEAARLAGLHD 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 692 DLEMLPGGDMAEIGEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVDTHVGKHIFNKVvgpNGLLSGKTRILVTHG 771
Cdd:COG2274 593 FIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENL---RRLLKGRTVIIIAHR 669
|
570 580 590
....*....|....*....|....*....|....*....
gi 569006289 772 IHFLPQVDEIVVLGKGTILEKGSYSDLMDKKGVFAKNWK 810
Cdd:COG2274 670 LSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1248-1478 |
3.59e-70 |
|
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: 235.96 E-value: 3.59e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1248 GEIQFNNYQVRYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRL 1327
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1328 TIIPQDPILFSGNLRMNLDPFNKYSDEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKI 1407
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006289 1408 LVLDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELLSNM-GPF 1478
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVF 249
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
277-563 |
3.76e-67 |
|
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: 229.43 E-value: 3.76e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 277 ILKLAHDILLFLNPQLLKFLIGFVKDP-------DSYPWV-----------GYIYAILMFSVTLIQSFFLQCYFQFCFVL 338
Cdd:cd18591 4 ILKLLGDLLGFVGPLCISGIVDYVEENtysssnsTDKLSVsyvtveeffsnGYVLAVILFLALLLQATFSQASYHIVIRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 339 GMTVRTTIIASVYKKALTLS--NLARRQYTIGETVNLMSVDSQKLMDVTNYIHLLWSSVLQIALSIFFLWRELGPSILAG 416
Cdd:cd18591 84 GIRLKTALQAMIYEKALRLSswNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 417 VGLMVLLVPVNGVLATKIRKIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFKEQVNSIRKKELRNLLRFSQLQTIL 496
Cdd:cd18591 164 AALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSLM 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 497 IFILHLTPTLVSVITFSVYVLVDSQNvLNAEKAFTSITLFNILRFPLAMLPMVISSVIQASVSVDRL 563
Cdd:cd18591 244 TFLTQASPILVTLVTFGLYPYLEGEP-LTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
925-1226 |
4.92e-67 |
|
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: 229.37 E-value: 4.92e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 925 GWWSLLFIVIFYVLNYVAFIGTNLWLSAW------TSDSEKQNGTDNSPSQRD-----MRIGVFGALGIAQGIFLLSSSL 993
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWlkqgsgNTTNNVDNSTVDSGNISDnpdlnFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 994 WSIYACRNASKTLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDTLPQTLRSWLLCFFGIVSTLVMICMATPIF 1073
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1074 IIIIIPLSILYVSVQVFYVATSRQLRRLDSVTKSPIYSHFSETVSGLPVIRAFEHQQRFLANSEKQIDTNQKCVFSWITS 1153
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006289 1154 NRWLAIRLELVGNLIVFCSALLLVIYKNSLTGDTVGFVLSNALNITQTLNWLVRMTSEVETNIVAVERINEYI 1226
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
925-1225 |
1.40e-65 |
|
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: 225.28 E-value: 1.40e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 925 GWWSLLFIVIFYVLNYVAFIGTNLWLSAWTSDSEKQN------------GTDNSPSQRDMRIGVFGALGIAQGIFLLSSS 992
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEEKLNdttdrvqgenstNVDIEDLDRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 993 LWSIYACRNASKTLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDTLPQTLRSWLLCFFGIVSTLVMICMATPI 1072
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1073 FIIIIIPLSILYVSVQVFYVATSRQLRRLDSVTKSPIYSHFSETVSGLPVIRAFEHQQRFLANSEKQIDTNQKCVFSWIT 1152
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006289 1153 SNRWLAIRLELVGNLIVFCSALLLVIYKNSLTGDTVGFVLSNALNITQTLNWLVRMTSEVETNIVAVERINEY 1225
Cdd:cd18601 241 TSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEY 313
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
284-564 |
1.07e-63 |
|
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: 218.66 E-value: 1.07e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 284 ILLFLN-------PQLLKFLIG-FVKDPDSYPWVGYIYAILMFSVTLIQSFFLQCYFQFCFVLGMTVRTTIIASVYKKAL 355
Cdd:cd18594 4 ILLFLEeslkivqPLLLGRLVAyFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 356 TLSNLARRQYTIGETVNLMSVDSQKLMDVTNYIHLLWSSVLQIALSIFFLWRELGPSILAGVGLMVLLVPVNGVLATKIR 435
Cdd:cd18594 84 KLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 436 KIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFKEQVNSIRKKELRNLLRFSQLQTILIFILHLTPTLVSVITFSVY 515
Cdd:cd18594 164 KYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPY 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 569006289 516 VLVDsqNVLNAEKAFTSITLFNILRFPLAM-LPMVISSVIQASVSVDRLE 564
Cdd:cd18594 244 VLTG--NTLTARKVFTVISLLNALRMTITRfFPESIQTLSESRVSLKRIQ 291
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1248-1472 |
1.03e-62 |
|
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: 213.63 E-value: 1.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1248 GEIQFNNYQVRYRPElDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRL 1327
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1328 TIIPQDPILFSGNLRMNLDPFNKYS-DEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSK 1406
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNAtDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006289 1407 ILVLDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELL 1472
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1218-1476 |
2.30e-61 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 221.17 E-value: 2.30e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1218 AVERINEYINVDNEAPWVTDKKPPadWPKKGEIQFNNYQVRYrPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCL 1297
Cdd:COG4988 307 AAEKIFALLDAPEPAAPAGTAPLP--AAGPPSIELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1298 FRILESAGGQIIIDGIDIASIGLHDLRGRLTIIPQDPILFSGNLRMNLDPFN-KYSDEEIWRALELAHLKSFVAGLQLGL 1376
Cdd:COG4988 384 LGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDEFVAALPDGL 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1377 LHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIMDSDKIMV 1456
Cdd:COG4988 464 DTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILV 543
|
250 260
....*....|....*....|
gi 569006289 1457 LDSGKIVEYGSPEELLSNMG 1476
Cdd:COG4988 544 LDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
587-788 |
1.61e-58 |
|
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: 201.02 E-value: 1.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 587 VQFSEASFTWDRDLeATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHI-----------------TIKG 649
Cdd:cd03290 1 VQVTNGYFSWGSGL-ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 650 SIAYVPQQAWIQNGTIKDNILFGSEYDEKKYQRVIEACALLPDLEMLPGGDMAEIGEKGINLSGGQKHRVSLARATYQDA 729
Cdd:cd03290 80 SVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006289 730 DIYILDDPLSAVDTHVGKHIFNKvvgpnGLLS-----GKTRILVTHGIHFLPQVDEIVVLGKGT 788
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQE-----GILKflqddKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
604-806 |
5.40e-56 |
|
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: 196.23 E-value: 5.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGSIAYVPQQAWIQNGTIKDNILFGSEYDEKKYQRV 683
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 684 IEACALLPDLEMLPGGDMAEIGEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVDTHVGKHIFNKVVGPngLLSGK 763
Cdd:cd03291 133 VKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCK--LMANK 210
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 569006289 764 TRILVTHGIHFLPQVDEIVVLGKGTILEKGSYSDLMDKKGVFA 806
Cdd:cd03291 211 TRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFS 253
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
980-1476 |
2.01e-55 |
|
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: 203.79 E-value: 2.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 980 LGIAQGIFLLSSSLWSIYACRNASKTLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGD------------ISTVDDTLPQ 1047
Cdd:TIGR02203 63 LAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDseqvasaatdafIVLVRETLTV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1048 TLRSWLLCFFGIVSTLVMICMATPifiiiiiplsilyVSVQVFYVatSRQLRRLDS---VTKSPIYSHFSETVSGLPVIR 1124
Cdd:TIGR02203 143 IGLFIVLLYYSWQLTLIVVVMLPV-------------LSILMRRV--SKRLRRISKeiqNSMGQVTTVAEETLQGYRVVK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1125 AFEHQ----QRFLANSEkqidtnqkcvfswitSNRWLAIRLELVGNL------IVFCSALLLVIY-------KNSLT-GD 1186
Cdd:TIGR02203 208 LFGGQayetRRFDAVSN---------------RNRRLAMKMTSAGSIsspitqLIASLALAVVLFialfqaqAGSLTaGD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1187 TVGFVLSnALNITQTLNWLVRMTSEVETNIVAVERINEYINVDNEAPWVTDKKPPAdwpkKGEIQFNNYQVRYRPELDLV 1266
Cdd:TIGR02203 273 FTAFITA-MIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDTGTRAIERA----RGDVEFRNVTFRYPGRDRPA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1267 LKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTIIPQDPILFSGNLRMNL- 1345
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIa 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1346 --DPfNKYSDEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDS 1423
Cdd:TIGR02203 428 ygRT-EQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESER 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 569006289 1424 LIQTTIRNEFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELLSNMG 1476
Cdd:TIGR02203 507 LVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNG 559
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1008-1481 |
7.66e-54 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 199.56 E-value: 7.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1008 RQLLTNI----LRAPMSFFDTTPTGRIVNRFAGDISTVDD----TLPQTLRSWLLcffgIVSTLV--------MICMATP 1071
Cdd:PRK10790 98 QQLRTDVmdaaLRQPLSAFDTQPVGQLISRVTNDTEVIRDlyvtVVATVLRSAAL----IGAMLVamfsldwrMALVAIM 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1072 IFIIIIIplsilyvsVQVFYVATSRQL-RRLDSVTkSPIYSHFSETVSGLPVIRAFEHQQRFlanSEKQIDTNQKCVFSw 1150
Cdd:PRK10790 174 IFPAVLV--------VMVIYQRYSTPIvRRVRAYL-ADINDGFNEVINGMSVIQQFRQQARF---GERMGEASRSHYMA- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1151 itsnRWLAIRLE--LVGNLIVFCSAL----LLVIYKNSLTGdTVGF-VLSNALNITQTLNW-LVRMTSE---VETNIVAV 1219
Cdd:PRK10790 241 ----RMQTLRLDgfLLRPLLSLFSALilcgLLMLFGFSASG-TIEVgVLYAFISYLGRLNEpLIELTTQqsmLQQAVVAG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1220 ERINEYINVDNEaPWVTDKKPPAdwpkKGEIQFNNYQVRYRPElDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFR 1299
Cdd:PRK10790 316 ERVFELMDGPRQ-QYGNDDRPLQ----SGRIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMG 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1300 ILESAGGQIIIDGIDIASIGLHDLRGRLTIIPQDPILFSGNLRMNLDPFNKYSDEEIWRALELAHLKSFVAGLQLGLLHE 1379
Cdd:PRK10790 390 YYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTP 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1380 VTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIMDSDKIMVLDS 1459
Cdd:PRK10790 470 LGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHR 549
|
490 500
....*....|....*....|..
gi 569006289 1460 GKIVEYGSPEELLSNMGPFYLM 1481
Cdd:PRK10790 550 GQAVEQGTHQQLLAAQGRYWQM 571
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1027-1479 |
1.07e-52 |
|
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: 195.76 E-value: 1.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1027 TGRIVNRFAGDISTVDDTLpqtLR---------------SWLLCFFGIVSTLVM-ICMATPIFIIIIiplsilyvsvqVF 1090
Cdd:COG4987 111 SGDLLNRLVADVDALDNLY---LRvllpllvallvilaaVAFLAFFSPALALVLaLGLLLAGLLLPL-----------LA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1091 YVATSRQLRRLdSVTKSPIYSHFSETVSGLPVIRAFEHQQRFLAN---SEKQIDTNQKcvfswiTSNRWLAIR---LELV 1164
Cdd:COG4987 177 ARLGRRAGRRL-AAARAALRARLTDLLQGAAELAAYGALDRALARldaAEARLAAAQR------RLARLSALAqalLQLA 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1165 GNLIVFCsALLLVIY---KNSLTG-DTVGFVLSnALNITQTLNWLVRMTSEVETNIVAVERINEyinVDNEAPWVTDKKP 1240
Cdd:COG4987 250 AGLAVVA-VLWLAAPlvaAGALSGpLLALLVLA-ALALFEALAPLPAAAQHLGRVRAAARRLNE---LLDAPPAVTEPAE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1241 PADWPKKGEIQFNNYQVRYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGL 1320
Cdd:COG4987 325 PAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDE 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1321 HDLRGRLTIIPQDPILFSGNLRMNL---DPfnKYSDEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCL 1397
Cdd:COG4987 405 DDLRRRIAVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLAL 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1398 GRAVLRKSKILVLDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELLSNMGP 1477
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGR 562
|
..
gi 569006289 1478 FY 1479
Cdd:COG4987 563 YR 564
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1250-1479 |
1.26e-52 |
|
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: 184.74 E-value: 1.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTI 1329
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1330 IPQDPILFSGNLRMNLdpfnKY-----SDEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRK 1404
Cdd:cd03251 81 VSQDVFLFNDTVAENI----AYgrpgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569006289 1405 SKILVLDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELLSNMGPFY 1479
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYA 231
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
586-803 |
9.10e-52 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 192.67 E-value: 9.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 586 AVQFSEASFTWDRDLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-------------SIA 652
Cdd:COG4988 336 SIELEDVSFSYPGGRPA-LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpaswrrQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 653 YVPQQAWIQNGTIKDNILFGS-EYDEKKYQRVIEACALLPDLEMLPGGDMAEIGEKGINLSGGQKHRVSLARATYQDADI 731
Cdd:COG4988 415 WVPQNPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPL 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006289 732 YILDDPLSAVDTHVGKHIFNKVvgpNGLLSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGSYSDLMDKKG 803
Cdd:COG4988 495 LLLDEPTAHLDAETEAEILQAL---RRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
350-810 |
1.38e-50 |
|
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: 189.21 E-value: 1.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 350 VYKKALTLSNLARRQYTIGETVNLMSVDSQKLMDVtnYIHLL---WSSVLQIALSIFFLWR---ELGPSILAGVGLMVLL 423
Cdd:COG4987 94 LYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNL--YLRVLlplLVALLVILAAVAFLAFfspALALVLALGLLLAGLL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 424 VPVNGVLATKIRKIQVQNMKNkDKRLKIMnEILSGIKILKYFAWEPSFKEQVNSIRKKELRNLLRFSQL----QTILIFI 499
Cdd:COG4987 172 LPLLAARLGRRAGRRLAAARA-ALRARLT-DLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLsalaQALLQLA 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 500 LHLTptLVSVITFSVYVLVDSQ--NVLNAEKAFTSITLFNILrfplAMLPMVISSVIQASVSVDRLEQYLG-SDDLDLSA 576
Cdd:COG4987 250 AGLA--VVAVLWLAAPLVAAGAlsGPLLALLVLAALALFEAL----APLPAAAQHLGRVRAAARRLNELLDaPPAVTEPA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 577 IRHVCHFDKAVQFSEASFTWDRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG------- 649
Cdd:COG4987 324 EPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrdld 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 650 ------SIAYVPQQAWIQNGTIKDNILFGSEY-DEKKYQRVIEACALLPDLEMLPGGDMAEIGEKGINLSGGQKHRVSLA 722
Cdd:COG4987 404 eddlrrRIAVVPQRPHLFDTTLRENLRLARPDaTDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALA 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 723 RATYQDADIYILDDPLSAVDTHVGKHIFNKVVgpnGLLSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGSYSDLMDKK 802
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLL---EALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
....*...
gi 569006289 803 GVFAKNWK 810
Cdd:COG4987 561 GRYRQLYQ 568
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
275-563 |
6.73e-50 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350036 [Multi-domain] Cd Length: 287 Bit Score: 178.91 E-value: 6.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 275 SFILKLAHDILLFLNPQ-LLKFLIGFVKDPDSYPWVGYIYAILMFSVTLIQSFFLQCYFQFCFVLGMTVRTTIIASVYKK 353
Cdd:cd18592 2 SILLLLISLIFGFIGPTiLIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 354 ALTLSNLarRQYTIGETVNLMSVDSQKLMDVTNYIHLLWSSVLQIALSIFFLWRELGPSILAGVGLMVLLVPVNGVLATK 433
Cdd:cd18592 82 ILRLRSL--GDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 434 IRKIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFKEQVNSIRKKELRNLLRFSQLQTILIFILHLTPTLVSVITFS 513
Cdd:cd18592 160 TGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 569006289 514 VYVLvdSQNVLNAEKAFTSITLFNILRFPLAMLPMVISSVIQASVSVDRL 563
Cdd:cd18592 240 AHVA--LGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1250-1481 |
7.28e-50 |
|
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: 177.04 E-value: 7.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELDlVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTI 1329
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1330 IPQDPILFSGNLRMNLdpfnKY-----SDEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRK 1404
Cdd:cd03253 80 VPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 1405 SKILVLDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELLSNMGPFYLM 1481
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
301-563 |
1.48e-49 |
|
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: 178.18 E-value: 1.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 301 KDPDSYpWVGYIYAILMFSVTLIQSFFLQCYFQFCFVLGMTVRTTIIASVYKKALTLSNLARRQYTIGETVNLMSVDSQK 380
Cdd:cd18593 31 GSSISL-TEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIYRKALRLSQAALGKTTVGQIVNLLSNDVNR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 381 LMDVTNYIHLLWSSVLQIALSIFFLWRELGPSILAGVGLMVLLVPVNGVLATKIRKIQVQNMKNKDKRLKIMNEILSGIK 460
Cdd:cd18593 110 FDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAARTDKRIRIMNEIINGIR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 461 ILKYFAWEPSFKEQVNSIRKKELRNLLRFSQLQTILIFILHLTPTLVSVITFSVYVLVDsqNVLNAEKAFTSITLFNILR 540
Cdd:cd18593 190 VIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTFLAYILLG--NILTAERVFVTMALYNAVR 267
|
250 260
....*....|....*....|....
gi 569006289 541 FPLAM-LPMVISSVIQASVSVDRL 563
Cdd:cd18593 268 LTMTLfFPFAIQFGSELSVSIRRI 291
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1006-1481 |
4.74e-48 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 184.54 E-value: 4.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1006 LHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDTLPQTLRSWLL-CFFGIVSTLVMICMATPIFIIIIIPLSILY 1084
Cdd:TIGR00958 236 IREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRnLVMLLGLLGFMLWLSPRLTMVTLINLPLVF 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1085 VSVQVF---YVATSRQLRrlDSVTKSPIYSHfsETVSGLPVIRAF--EHQ--QRFLANSEKQIDTNQK-----CVFSWIT 1152
Cdd:TIGR00958 316 LAEKVFgkrYQLLSEELQ--EAVAKANQVAE--EALSGMRTVRSFaaEEGeaSRFKEALEETLQLNKRkalayAGYLWTT 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1153 SNRWLAIRLelvgnLIVFCSALLLVIYKNSlTGDTVGFVLSNaLNITQTLNWLVRMTSEVETNIVAVERINEYINVDNEA 1232
Cdd:TIGR00958 392 SVLGMLIQV-----LVLYYGGQLVLTGKVS-SGNLVSFLLYQ-EQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNI 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1233 PWVTDKKPPadwPKKGEIQFNNYQVRY--RPELdLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIII 1310
Cdd:TIGR00958 465 PLTGTLAPL---NLEGLIEFQDVSFSYpnRPDV-PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1311 DGIDIASIGLHDLRGRLTIIPQDPILFSGNLRMNLD-PFNKYSDEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNLSI 1389
Cdd:TIGR00958 541 DGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSG 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1390 GQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTirNEFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPE 1469
Cdd:TIGR00958 621 GQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHK 698
|
490
....*....|..
gi 569006289 1470 ELLSNMGPFYLM 1481
Cdd:TIGR00958 699 QLMEDQGCYKHL 710
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1250-1485 |
7.74e-47 |
|
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: 168.49 E-value: 7.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRY--RPELdLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRL 1327
Cdd:cd03249 1 IEFKNVSFRYpsRPDV-PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1328 TIIPQDPILFSGNLRMNLdpfnKY-----SDEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVL 1402
Cdd:cd03249 80 GLVSQEPVLFDGTIAENI----RYgkpdaTDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1403 RKSKILVLDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELLSNMGPFYLMA 1482
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
|
...
gi 569006289 1483 KEA 1485
Cdd:cd03249 236 KAQ 238
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1250-1461 |
1.81e-46 |
|
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: 164.48 E-value: 1.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTI 1329
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1330 IPQDPILFSGNLRMNLdpfnkysdeeiwralelahlksfvaglqlgllhevteggdnLSIGQRQLLCLGRAVLRKSKILV 1409
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569006289 1410 LDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIMDSDKIMVLDSGK 1461
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1187-1481 |
4.05e-46 |
|
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: 176.93 E-value: 4.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1187 TVG-FVLSNA--LNITQTLNWLVRMTSEVETNIVAVERINEYINVDNEapwVTDKKPPADWP-KKGEIQFNNYQVRYRPE 1262
Cdd:COG5265 294 TVGdFVLVNAylIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPE---VADAPDAPPLVvGGGEVRFENVSFGYDPE 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1263 lDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTIIPQDPILFSGNLR 1342
Cdd:COG5265 371 -RPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIA 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1343 MNLdpfnKY-----SDEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAV 1417
Cdd:COG5265 450 YNI----AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSAL 525
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006289 1418 DLETDSLIQTTIRNEFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELLSNMGPFYLM 1481
Cdd:COG5265 526 DSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
931-1226 |
8.99e-46 |
|
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: 167.01 E-value: 8.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 931 FIVIFYVLNYVAFIG-TNLWLSAWTSDSEKQngtdnSPSQRDMRIGVFGALGIAQGIFLLSSSLWSIYACRNASKTLHRQ 1009
Cdd:cd18559 2 FLLIKLVLCNHVFSGpSNLWLLLWFDDPVNG-----PQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1010 LLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDTLPQTLRSWLLCFFGIVSTLVMICMATPIFIIIIIPLSIlYVSVQV 1089
Cdd:cd18559 77 LYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLL-YVPVNR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1090 FYVATSRQLRRLDSVTKSPIYSHFSETVSGLPVIRAFEHQQRFLANSEKQIDtNQKCVFSWITSNRWLAIRLELVGNLIV 1169
Cdd:cd18559 156 VYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIV 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 1170 FCSALLLVIYKNSLTGdTVGFVLSNALNITQTLNWLVRMTSEVETNIVAVERINEYI 1226
Cdd:cd18559 235 LFASFFAYVSRHSLAG-LVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1250-1479 |
3.05e-44 |
|
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: 160.73 E-value: 3.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTI 1329
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1330 IPQDPILFSGNLRMNL---DPfnKYSDEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSK 1406
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006289 1407 ILVLDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELLSNMGPFY 1479
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1248-1473 |
4.75e-44 |
|
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: 161.56 E-value: 4.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1248 GEIQFNNYQVRYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILeSAGGQIIIDGIDIASIGLHDLRGRL 1327
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1328 TIIPQDPILFSGNLRMNLDPFNKYSDEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKI 1407
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006289 1408 LVLDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELLS 1473
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLN 225
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1248-1463 |
1.37e-43 |
|
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: 158.14 E-value: 1.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1248 GEIQFNNYQVRYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRL 1327
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1328 TIIPQDPILFSGNLRMNLDPFNKY-SDEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSK 1406
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 1407 ILVLDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIMDSDKIMVLDSGKIV 1463
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
587-803 |
1.91e-43 |
|
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: 158.16 E-value: 1.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 587 VQFSEASFTWDRDlEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-------------SIAY 653
Cdd:cd03254 3 IEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 654 VPQQAWIQNGTIKDNILFGSEYDEKKyqRVIEACALL---PDLEMLPGGDMAEIGEKGINLSGGQKHRVSLARATYQDAD 730
Cdd:cd03254 82 VLQDTFLFSGTIMENIRLGRPNATDE--EVIEAAKEAgahDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006289 731 IYILDDPLSAVDTHVGKHIFNKVvgpNGLLSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGSYSDLMDKKG 803
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEAL---EKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
587-810 |
5.05e-43 |
|
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: 157.39 E-value: 5.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 587 VQFSEASFTWDRDLEaTIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-------------SIAY 653
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 654 VPQQAWIQNGTIKDNILFG--SEYDEKkyqrVIEAC--ALLPDLEM-LPGGDMAEIGEKGINLSGGQKHRVSLARATYQD 728
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGrpDATDEE----VIEAAkaAQIHDKIMrFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 729 ADIYILDDPLSAVDTHVGKHIFNKVvgpNGLLSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGSYSDLMDKKGVFAKN 808
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAAL---RDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
..
gi 569006289 809 WK 810
Cdd:cd03253 233 WK 234
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
587-809 |
7.27e-43 |
|
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: 156.62 E-value: 7.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 587 VQFSEASFTWDRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-------------SIAY 653
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 654 VPQQAWIQNGTIKDNILFG-SEYDEKKYQRVIEACALLPDLEMLPGGDMAEIGEKGINLSGGQKHRVSLARATYQDADIY 732
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGrPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 733 ILDDPLSAVDTHVGKHIFNKVvgpNGLLSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGSYSDLMDKKGVFAKNW 809
Cdd:cd03251 161 ILDEATSALDTESERLVQAAL---ERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1014-1479 |
1.31e-41 |
|
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: 164.91 E-value: 1.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1014 ILRAPMSFFDTTPTGRIVNRFAgDISTVDDTLPQTLRSWLLCFFGIVSTLVMICMATPIFIIIIIPLSILYVSVQVFYVA 1093
Cdd:TIGR01193 239 LFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1094 TSRQLRRLDSVTKSPIYSHFSETVSGLPVIRAFEHQQrflaNSEKQIDTN-----QKCVFSWITSNRWLAIR--LELVGN 1166
Cdd:TIGR01193 318 TFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEA----ERYSKIDSEfgdylNKSFKYQKADQGQQAIKavTKLILN 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1167 LIVFCSALLLVIYKNSLTGDTVGFvlsNAL--NITQTLNWLVRMTSEVETNIVAVERINEYINVDNEapWVTDKKPPADW 1244
Cdd:TIGR01193 394 VVILWTGAYLVMRGKLTLGQLITF---NALlsYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSE--FINKKKRTELN 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1245 PKKGEIQFNNYQVRYRPElDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLR 1324
Cdd:TIGR01193 469 NLNGDIVINDVSYSYGYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLR 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1325 GRLTIIPQDPILFSGNLRMNLDPFNK--YSDEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVL 1402
Cdd:TIGR01193 548 QFINYLPQEPYIFSGSILENLLLGAKenVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALL 627
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 1403 RKSKILVLDEATAAVDLETDSLIQTTIRNeFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELLSNMGPFY 1479
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYA 703
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
587-787 |
2.49e-40 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 147.14 E-value: 2.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 587 VQFSEASFTWDRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-------------SIAY 653
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 654 VPQQAWIQNGTIKDNIlfgseydekkyqrvieacallpdlemlpggdmaeigekginLSGGQKHRVSLARATYQDADIYI 733
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 569006289 734 LDDPLSAVDTHVGKHIFNKVvgpNGLLSGKTRILVTHGIHFLPQVDEIVVLGKG 787
Cdd:cd03228 120 LDEATSALDPETEALILEAL---RALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
586-793 |
3.35e-40 |
|
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: 148.51 E-value: 3.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 586 AVQFSEASFTWDRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-------------SIA 652
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 653 YVPQQAWIQNGTIKDNILFGSEY-DEKKYQRVIEACALLPDLEMLPGGDMAEIGEKGINLSGGQKHRVSLARATYQDADI 731
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006289 732 YILDDPLSAVDTHVGKHIFNKVvgpNGLLSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKG 793
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERL---RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
587-810 |
6.00e-39 |
|
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: 145.76 E-value: 6.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 587 VQFSEASFTWDRDLEATI-QDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS-------------IA 652
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPIlKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 653 YVPQQAWIQNGTIKDNILFGSEYDEKKyqRVIEAC--ALLPD-LEMLPGGDMAEIGEKGINLSGGQKHRVSLARATYQDA 729
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDE--EVEEAAkkANIHDfIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 730 DIYILDDPLSAVDTHVGKHIFNKVvgpNGLLSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGSYSDLMDKKGVFAKNW 809
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEAL---DRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
|
.
gi 569006289 810 K 810
Cdd:cd03249 236 K 236
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
976-1483 |
1.98e-38 |
|
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: 154.73 E-value: 1.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 976 VFGALGIAQGIFLLSSSLWSIYACRNASKTLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGdISTVDDTLP-QTLRSWLL 1054
Cdd:TIGR03797 181 ALLAAAVGAAAFQLAQSLAVLRLETRMDASLQAAVWDRLLRLPVSFFRQYSTGDLASRAMG-ISQIRRILSgSTLTTLLS 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1055 CFFGIVS-----------TLVMICMATpifiiiiiplsilyVSVQVFYVATSRQLR--RLDSVTKSPIYSHFSETVSGLP 1121
Cdd:TIGR03797 260 GIFALLNlglmfyyswklALVAVALAL--------------VAIAVTLVLGLLQVRkeRRLLELSGKISGLTVQLINGIS 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1122 VIRAFEHQQRFLANSEKQIDTNQKCVFSWITSNRWLAIRLELvgnLIVFCSALLLVI----YKNSL--TGDTVGF----- 1190
Cdd:TIGR03797 326 KLRVAGAENRAFARWAKLFSRQRKLELSAQRIENLLTVFNAV---LPVLTSAALFAAaislLGGAGlsLGSFLAFntafg 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1191 -VLSNALNITQTLnwlvrmtSEVETNIVAVERINEYINVDNEAPwvTDKKPPADWpkKGEIQFNNYQVRYRPELDLVLKG 1269
Cdd:TIGR03797 403 sFSGAVTQLSNTL-------ISILAVIPLWERAKPILEALPEVD--EAKTDPGKL--SGAIEVDRVTFRYRPDGPLILDD 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1270 ITCNIKSTEKVGVVGRTGAGKSSLtnclFRIL------ESAGGQIIIDGIdiASIGLHDLRGRLTIIPQDPILFSGNLRM 1343
Cdd:TIGR03797 472 VSLQIEPGEFVAIVGPSGSGKSTL----LRLLlgfetpESGSVFYDGQDL--AGLDVQAVRRQLGVVLQNGRLMSGSIFE 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1344 NLDPFNKYSDEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETds 1423
Cdd:TIGR03797 546 NIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRT-- 623
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006289 1424 liQTTIRNEFSQ--CTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELLSNMGPFYLMAK 1483
Cdd:TIGR03797 624 --QAIVSESLERlkVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLAR 683
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
586-784 |
1.08e-37 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 150.13 E-value: 1.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 586 AVQFSEASFTwDRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-------------SIA 652
Cdd:TIGR02857 321 SLEFSGVSVA-YPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 653 YVPQQAWIQNGTIKDNILFG-SEYDEKKYQRVIEACALLPDLEMLPGGDMAEIGEKGINLSGGQKHRVSLARATYQDADI 731
Cdd:TIGR02857 400 WVPQHPFLFAGTIAENIRLArPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 569006289 732 YILDDPLSAVDTHVGKHIFNKVvgpNGLLSGKTRILVTHGIHFLPQVDEIVVL 784
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEAL---RALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1005-1476 |
1.13e-37 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 150.94 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1005 TLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDTLPQTL-------------------RSWLLcffgivsTLVM 1065
Cdd:PRK11176 99 TMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALitvvregasiiglfimmfyYSWQL-------SLIL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1066 ICMATPifiiiiiplsilyVSVQVFYVatSRQLRRLD--------SVTKSPiyshfSETVSGLPVIRAFEHQQ----RFL 1133
Cdd:PRK11176 172 IVIAPI-------------VSIAIRVV--SKRFRNISknmqntmgQVTTSA-----EQMLKGHKEVLIFGGQEvetkRFD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1134 ANSEKQIDTNQKCVFSWITSNrwlaIRLELVGNLivfcsALLLVIY-------KNSLTGDTVGFVLSNALNITQTLNWLV 1206
Cdd:PRK11176 232 KVSNRMRQQGMKMVSASSISD----PIIQLIASL-----ALAFVLYaasfpsvMDTLTAGTITVVFSSMIALMRPLKSLT 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1207 RMTSEVETNIVAVERINEYINVDNEAPWVTDKKPPAdwpkKGEIQFNNYQVRYRPELDLVLKGITCNIKSTEKVGVVGRT 1286
Cdd:PRK11176 303 NVNAQFQRGMAACQTLFAILDLEQEKDEGKRVIERA----KGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRS 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1287 GAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTIIPQDPILFSGNLRMNLD--PFNKYSDEEIWRALELAH 1364
Cdd:PRK11176 379 GSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAyaRTEQYSREQIEEAARMAY 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1365 LKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHR 1444
Cdd:PRK11176 459 AMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHR 538
|
490 500 510
....*....|....*....|....*....|..
gi 569006289 1445 LHTIMDSDKIMVLDSGKIVEYGSPEELLSNMG 1476
Cdd:PRK11176 539 LSTIEKADEILVVEDGEIVERGTHAELLAQNG 570
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1107-1487 |
2.18e-37 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 150.11 E-value: 2.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1107 SPIYSHFSETVSGLPVIRAF---EHQQRFLANSEKQIDTNQKCVFSWitsnrW-LAIRLELVGNLIVFCSALLLVIY--- 1179
Cdd:PRK13657 192 HDLFAHVSDAIGNVSVVQSYnriEAETQALRDIADNLLAAQMPVLSW-----WaLASVLNRAASTITMLAILVLGAAlvq 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1180 KNSLT-GDTVGFVLSNALNITQtlnwLVRMTSEVETNIVAVERINEYINVDNEAPWVTDKKPPADWPK-KGEIQFNNYQV 1257
Cdd:PRK13657 267 KGQLRvGEVVAFVGFATLLIGR----LDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDLGRvKGAVEFDDVSF 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1258 RY---RPELDlvlkGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTIIPQDP 1334
Cdd:PRK13657 343 SYdnsRQGVE----DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDA 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1335 ILFSGNLRMNL-----DPfnkySDEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILV 1409
Cdd:PRK13657 419 GLFNRSIEDNIrvgrpDA----TDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILI 494
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569006289 1410 LDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELLSNMGPFYLMAKEAGI 1487
Cdd:PRK13657 495 LDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQGM 572
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1216-1481 |
4.35e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 146.14 E-value: 4.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1216 IVAVERINEYINVDNEAPWVTDKKPPADWPKkgEIQFNNYQVrYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTN 1295
Cdd:PRK11174 318 VGAAESLVTFLETPLAHPQQGEKELASNDPV--TIEAEDLEI-LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLN 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1296 CLFRILesaggqIIIDGIDIASIGLHDL-----RGRLTIIPQDPILFSGNLRMNLDPFNK-YSDEEIWRALELAHLKSFV 1369
Cdd:PRK11174 395 ALLGFL------PYQGSLKINGIELRELdpeswRKHLSWVGQNPQLPHGTLRDNVLLGNPdASDEQLQQALENAWVSEFL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1370 AGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIM 1449
Cdd:PRK11174 469 PLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLA 548
|
250 260 270
....*....|....*....|....*....|..
gi 569006289 1450 DSDKIMVLDSGKIVEYGSPEELLSNMGPFYLM 1481
Cdd:PRK11174 549 QWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
929-1199 |
1.16e-35 |
|
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: 137.39 E-value: 1.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 929 LLFIVIFYVLNYVAFIGTNLWLSAWTSDSEKQNgtDNSPSQRDMRIGVFGALGIAQGIFLLSSSLWSIYACRNASKTLHR 1008
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDG--DPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1009 QLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDTLPQTLRSWLLCFFGIVSTLVMICMATPIFIIIIIPLSILYVSVQ 1088
Cdd:pfam00664 79 KLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1089 VFYVATSRQLRRLDSVTKSPIYSHFSETVSGLPVIRAFEHQQRFLANSEKQIDTNQKCVFSWITSNRWLAIRLELVGNLI 1168
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLS 238
|
250 260 270
....*....|....*....|....*....|....
gi 569006289 1169 VFCSALL---LVIYKNSLTGDTVGFVLSNALNIT 1199
Cdd:pfam00664 239 YALALWFgayLVISGELSVGDLVAFLSLFAQLFG 272
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1231-1457 |
2.44e-35 |
|
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: 142.81 E-value: 2.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1231 EAPWVTDKKPPADWPKKGEIQFNNYQVRYrPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIII 1310
Cdd:TIGR02857 303 AAPRPLAGKAPVTAAPASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1311 DGIDIASIGLHDLRGRLTIIPQDPILFSGNLRMNLDPFNKY-SDEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNLSI 1389
Cdd:TIGR02857 382 NGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSG 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569006289 1390 GQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIMDSDKIMVL 1457
Cdd:TIGR02857 462 GQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
587-794 |
5.22e-35 |
|
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: 133.77 E-value: 5.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 587 VQFSEASFTWDRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-------------SIAY 653
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 654 VPQQAWIQNGTIKDNILFGSEYDEKKYQRVIEACALLPDLEMLPGGDMAEIGEKGINLSGGQKHRVSLARATYQDADIYI 733
Cdd:cd03244 83 IPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569006289 734 LDDPLSAVDTHVGKHIfNKVVGPNglLSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGS 794
Cdd:cd03244 163 LDEATASVDPETDALI-QKTIREA--FKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
272-543 |
1.03e-34 |
|
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: 134.69 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 272 ILKSFILKLAHDILLFLNPQLLKFLIGFVKDPDSYPWV-GYIYAILMFSVTLIQSFFLQCYFQFCFVLGMTVRTTIIASV 350
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQaLNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 351 YKKALTLSNLARRQYTIGETVNLMSVDSQKLMDVTNYIHLLWSSVLQIALSIFFLWRELGPSI-LAGVGLMVLLVPVNGV 429
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLtLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 430 LATKIRKIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFKEQVNSIRKKELRNLLRFSQLQTILIFILHLTPTLVSV 509
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 569006289 510 ITFSVYVLVDSQNVLNAEKAFTSITLFNILRFPL 543
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
607-806 |
1.43e-34 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 141.52 E-value: 1.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 607 VNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMeNVHGHITIKG------SIAYVPQQ-AWI-QN-----GTIKDNILFG- 672
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGielrelDPESWRKHlSWVgQNpqlphGTLRDNVLLGn 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 673 SEYDEKKYQRVIEACALLPDLEMLPGGDMAEIGEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVDTHVGKHIFNK 752
Cdd:PRK11174 448 PDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 569006289 753 VvgpNGLLSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGSYSDLMDKKGVFA 806
Cdd:PRK11174 528 L---NAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFA 578
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1247-1462 |
2.47e-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: 131.82 E-value: 2.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1247 KGEIQFNNYQVRYRPELD-LVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILEsagGQIIIDGIDIASIGLHD--- 1322
Cdd:cd03248 9 KGIVKFQNVTFAYPTRPDtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQ---PQGGQVLLDGKPISQYEhky 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1323 LRGRLTIIPQDPILFSGNLRMNLD-PFNKYSDEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAV 1401
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569006289 1402 LRKSKILVLDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIMDSDKIMVLDSGKI 1462
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
584-789 |
3.96e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 131.75 E-value: 3.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 584 DKAVQFSEASFTWDRdlEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG--------SIAYVP 655
Cdd:COG1121 4 MPAIELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 656 QQAWIQNG---TIKDNILFG--------SEYDEKKYQRVIEAcallpdLEMLpggDMAEIGEKGIN-LSGGQKHRVSLAR 723
Cdd:COG1121 82 QRAEVDWDfpiTVRDVVLMGrygrrglfRRPSRADREAVDEA------LERV---GLEDLADRPIGeLSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006289 724 ATYQDADIYILDDPLSAVDTHVGKHIFNkvvgpngLLS-----GKTRILVTHGIHFLPQ-VDEIVVLGKGTI 789
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYE-------LLRelrreGKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
587-806 |
1.12e-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: 127.60 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 587 VQFSEASFTWDRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-------------SIAY 653
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 654 VPQQAWIQNGTIKDNILFGSEydEKKYQRVIEACALLPDLEM---LPGGDMAEIGEKGINLSGGQKHRVSLARATYQDAD 730
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADP--GMSMERVIEAAKLAGAHDFiseLPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006289 731 IYILDDPLSAVDTHVGKHIFNKVvgpNGLLSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGSYSDLMDKKGVFA 806
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNM---HDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1216-1479 |
2.17e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 134.57 E-value: 2.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1216 IVAVERINEYINVDNEAPWVTDKKPPADwpkKGEIQFNNYQVRYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTN 1295
Cdd:PRK11160 308 IASARRINEITEQKPEVTFPTTSTAAAD---QVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1296 CLFRILESAGGQIIIDGIDIASIGLHDLRGRLTIIPQDPILFSGNLRMNL---DPfnKYSDEEIWRALE---LAHLKSFV 1369
Cdd:PRK11160 385 LLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQqvgLEKLLEDD 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1370 AGLQLGLlhevTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIM 1449
Cdd:PRK11160 463 KGLNAWL----GEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLE 538
|
250 260 270
....*....|....*....|....*....|
gi 569006289 1450 DSDKIMVLDSGKIVEYGSPEELLSNMGPFY 1479
Cdd:PRK11160 539 QFDRICVMDNGQIIEQGTHQELLAQQGRYY 568
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
913-1226 |
3.22e-32 |
|
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: 128.77 E-value: 3.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 913 KFSIYLKYLQAVGwwSLLFIVIFYVLNYVA----------FIGTNLWLSAWTSDSEKQNGTDNSPSQRD------MRIGV 976
Cdd:cd18600 2 TWNTYLRYITSHK--SLIFVLILCLVIFAIevaaslvglwLLRSQADRVNTTRPESSSNTYAVIVTFTSsyyvfyIYVGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 977 ---FGALGIAQGIFLLSSSLwsiyacrNASKTLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDTLPQTLRSWL 1053
Cdd:cd18600 80 adsLLAMGFFRGLPLVHTLI-------TVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1054 LCFFGIVSTLVMICMATPIFIIIIIPLSILYVSVQVFYVATSRQLRRLDSVTKSPIYSHFSETVSGLPVIRAFEHQQRFL 1133
Cdd:cd18600 153 QLFLIVIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1134 ANSEKQIDTNQKCVFSWITSNRWLAIRLELVgNLIVFCSALLLVIYKNSLTGDTVGFVLSNALNITQTLNWLVRMTSEVE 1213
Cdd:cd18600 233 TLFHKALNLHTANWFLYLSTLRWFQMRIEMI-FVIFFTAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVD 311
|
330
....*....|...
gi 569006289 1214 TNIVAVERINEYI 1226
Cdd:cd18600 312 SLMRSVSRIFKFI 324
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
604-787 |
1.57e-31 |
|
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: 123.41 E-value: 1.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG--------SIAYVPQQA---WIQNGTIKDNIL-- 670
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRRsidRDFPISVRDVVLmg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 671 ------FGSEYDEKKYQRVIEAcallpdLEMLPGGDMAE--IGEkginLSGGQKHRVSLARATYQDADIYILDDPLSAVD 742
Cdd:cd03235 95 lyghkgLFRRLSKADKAKVDEA------LERVGLSELADrqIGE----LSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 569006289 743 THvGKHIFNKVVgpNGL-LSGKTRILVTHGIH-FLPQVDEIVVLGKG 787
Cdd:cd03235 165 PK-TQEDIYELL--RELrREGMTILVVTHDLGlVLEYFDRVLLLNRT 208
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
368-806 |
8.86e-31 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 131.00 E-value: 8.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 368 GETVNLMSVDSQKLMD-VTNYIH-LLWSSVLQIALSIFFLWreLGPSiLAGVGL--MVLLVPVNGVLATKIRKIQVQNMK 443
Cdd:TIGR00958 258 GELTSRLSSDTQTMSRsLSLNVNvLLRNLVMLLGLLGFMLW--LSPR-LTMVTLinLPLVFLAEKVFGKRYQLLSEELQE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 444 NKDKRLKIMNEILSGIKILKYFAWEPS----FKEQVNSI----RKKELRNLL-----RFSQLqTILIFILHLTPTLV--- 507
Cdd:TIGR00958 335 AVAKANQVAEEALSGMRTVRSFAAEEGeasrFKEALEETlqlnKRKALAYAGylwttSVLGM-LIQVLVLYYGGQLVltg 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 508 -----SVITFSVYVLVDSQNVLNaekaftsitlfnilrfplamLPMVISSVIQASVSVDRLEQYLGSD-DLDLSAIRHVC 581
Cdd:TIGR00958 414 kvssgNLVSFLLYQEQLGEAVRV--------------------LSYVYSGMMQAVGASEKVFEYLDRKpNIPLTGTLAPL 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 582 HFDKAVQFSEASFTW-DRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG----------- 649
Cdd:TIGR00958 474 NLEGLIEFQDVSFSYpNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhyl 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 650 --SIAYVPQQAWIQNGTIKDNILFGSEY--DEKKYQRVIEACALLPDLEMlPGGDMAEIGEKGINLSGGQKHRVSLARAT 725
Cdd:TIGR00958 554 hrQVALVGQEPVLFSGSVRENIAYGLTDtpDEEIMAAAKAANAHDFIMEF-PNGYDTEVGEKGSQLSGGQKQRIAIARAL 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 726 YQDADIYILDDPLSAVDTHVgkhifNKVVGPNGLLSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGSYSDLMDKKGVF 805
Cdd:TIGR00958 633 VRKPRVLILDEATSALDAEC-----EQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCY 707
|
.
gi 569006289 806 A 806
Cdd:TIGR00958 708 K 708
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1027-1445 |
2.03e-29 |
|
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: 124.78 E-value: 2.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1027 TGRIVNRFAGDISTVDDTLPQTLrswllcFFGIVSTLVMI--CMATPIFIIIIIPLSILYVSVQVFYV-ATSRQLRRLDS 1103
Cdd:TIGR02868 109 RGDLLGRLGADVDALQDLYVRVI------VPAGVALVVGAaaVAAIAVLSVPAALILAAGLLLAGFVApLVSLRAARAAE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1104 VTKSPIYSHFS----ETVSGLPVIRAFEHQQRFLANSEKQ------IDTNQKCVFSWITSNRWLAIRLELVGNLIVFCSA 1173
Cdd:TIGR02868 183 QALARLRGELAaqltDALDGAAELVASGALPAALAQVEEAdreltrAERRAAAATALGAALTLLAAGLAVLGALWAGGPA 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1174 LLlviyKNSLTGDTVGFVLSNALNITQTLNWLVRMTSEVETNIVAVERINEYINVDNEAPWVTDKKPPADWPKKGEIQFN 1253
Cdd:TIGR02868 263 VA----DGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1254 NYQVRYrPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTIIPQD 1333
Cdd:TIGR02868 339 DLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQD 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1334 PILFSGNLRMNLDPFNK-YSDEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDE 1412
Cdd:TIGR02868 418 AHLFDTTVRENLRLARPdATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDE 497
|
410 420 430
....*....|....*....|....*....|...
gi 569006289 1413 ATAAVDLETDSLIQTTIRNEFSQCTVITIAHRL 1445
Cdd:TIGR02868 498 PTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
587-807 |
2.83e-29 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 125.13 E-value: 2.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 587 VQFSEASFTWDRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSlISAMLGEMENV-HGHITIKG-------------SIA 652
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKST-IANLLTRFYDIdEGEILLDGhdlrdytlaslrnQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 653 YVPQQAWIQNGTIKDNILFGSEydeKKYQRV-IEACALLPD----LEMLPGGDMAEIGEKGINLSGGQKHRVSLARATYQ 727
Cdd:PRK11176 421 LVSQNVHLFNDTIANNIAYART---EQYSREqIEEAARMAYamdfINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 728 DADIYILDDPLSAVDTHVGKHIFNKVvgpNGLLSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGSYSDLMDKKGVFAK 807
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAAL---DELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQ 574
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
586-807 |
2.86e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 124.94 E-value: 2.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 586 AVQFSEASFTWDRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-------------SIA 652
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiadyseaalrqAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 653 YVPQQAWIQNGTIKDNILFGS-EYDEKKYQRVIEACALLPDLEMLPGGDmAEIGEKGINLSGGQKHRVSLARATYQDADI 731
Cdd:PRK11160 418 VVSQRVHLFSATLRDNLLLAApNASDEALIEVLQQVGLEKLLEDDKGLN-AWLGEGGRQLSGGEQRRLGIARALLHDAPL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 732 YILDDPLSAVDTHVGKHIFNkvvgpngLL----SGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGSYSDLMDKKGVFAK 807
Cdd:PRK11160 497 LLLDEPTEGLDAETERQILE-------LLaehaQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQ 569
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
529-770 |
1.12e-28 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 122.47 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 529 AFTSITLFNilrfPLAMLPMVISSVIQASVSVDRLEQYL----GSDDLDLSAIRHVCHFDKAVQFSEASFTWDRDLEAtI 604
Cdd:TIGR02868 277 VLLPLAAFE----AFAALPAAAQQLTRVRAAAERIVEVLdaagPVAEGSAPAAGAVGLGKPTLELRDLSAGYPGAPPV-L 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 605 QDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS-------------IAYVPQQAWIQNGTIKDNILF 671
Cdd:TIGR02868 352 DGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVpvssldqdevrrrVSVCAQDAHLFDTTVRENLRL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 672 GS-EYDEKKYQRVIEACALLPDLEMLPGGDMAEIGEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVDTHVGKHIF 750
Cdd:TIGR02868 432 ARpDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELL 511
|
250 260
....*....|....*....|
gi 569006289 751 NKVVGPnglLSGKTRILVTH 770
Cdd:TIGR02868 512 EDLLAA---LSGRTVVLITH 528
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
585-1473 |
2.89e-28 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 124.37 E-value: 2.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 585 KAVQFSEASFTWD--RDLEaTIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS------------ 650
Cdd:PTZ00265 381 KKIQFKNVRFHYDtrKDVE-IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwr 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 651 --IAYVPQQAWIQNGTIKDNILFG-----------SEYDE---------------------------------------K 678
Cdd:PTZ00265 460 skIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsNYYNEdgndsqenknkrnscrakcagdlndmsnttdsneliemrK 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 679 KYQRV-------IEACALLPD-LEMLPGGDMAEIGEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVDTHvGKHIF 750
Cdd:PTZ00265 540 NYQTIkdsevvdVSKKVLIHDfVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK-SEYLV 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 751 NKVVgpNGLLSGKTRI--LVTHGIHFLPQVDEIVVL--------------------------------GKGT-------- 788
Cdd:PTZ00265 619 QKTI--NNLKGNENRItiIIAHRLSTIRYANTIFVLsnrergstvdvdiigedptkdnkennnknnkdDNNNnnnnnnnk 696
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 789 -------ILEKGSYSDLM-DKKGVF---AKNWKTFMKHSGPEGEatvDNDSEEE-----DGDCGliptveEIPDDAASLT 852
Cdd:PTZ00265 697 innagsyIIEQGTHDALMkNKNGIYytmINNQKVSSKKSSNNDN---DKDSDMKssaykDSERG------YDPDEMNGNS 767
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 853 MRRENSLRRTLSRSSRSGSRRGKSLKSSLKIKSvNALNKKEEVVKGQKLIKKEFVETGKVKFSIYLKYLQAVGWWSLlfi 932
Cdd:PTZ00265 768 KHENESASNKKSCKMSDENASENNAGGKLPFLR-NLFKRKPKAPNNLRIVYREIFSYKKDVTIIALSILVAGGLYPV--- 843
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 933 vifYVLNYVAFIGTNLWLSAWTSDSEKQNgtdnspsqrdmrigvFGALGIAQGIFLlSSSLWSIY---ACRNASKTLHRQ 1009
Cdd:PTZ00265 844 ---FALLYAKYVSTLFDFANLEANSNKYS---------------LYILVIAIAMFI-SETLKNYYnnvIGEKVEKTMKRR 904
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1010 LLTNILRAPMSFFDT---TPtGRIVNRFAGDISTVDDTLPQTLRswLLCFFgIVSTLVMICMATPIFIIIIIPLSILY-V 1085
Cdd:PTZ00265 905 LFENILYQEISFFDQdkhAP-GLLSAHINRDVHLLKTGLVNNIV--IFTHF-IVLFLVSMVMSFYFCPIVAAVLTGTYfI 980
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1086 SVQVFYV----ATSRQLRRL--------------DSVTKSPIYShFSETVSGLPVIRAFEHQQRFLANSEKQIDTNQKCV 1147
Cdd:PTZ00265 981 FMRVFAIrarlTANKDVEKKeinqpgtvfaynsdDEIFKDPSFL-IQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQ 1059
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1148 ------------FS-----WITS-NRWLAIRLELVGNLIV--FCSALLLVIYKNSLTGDtvgfvlsnalnitqtlnwLVR 1207
Cdd:PTZ00265 1060 krktlvnsmlwgFSqsaqlFINSfAYWFGSFLIRRGTILVddFMKSLFTFLFTGSYAGK------------------LMS 1121
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1208 MTSEVETNIVAVERINEYI----NVDNEAPWVTDKKPPADWPKKGEIQFNNYQVRYRPELDlVLKGITCNIKSTEKVGVV 1283
Cdd:PTZ00265 1122 LKGDSENAKLSFEKYYPLIirksNIDVRDNGGIRIKNKNDIKGKIEIMDVNFRYISRPNVP-IYKDLTFSCDSKKTTAIV 1200
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1284 GRTGAGKSSLTNCLFRIL--------------------------------------------ESAGGQIIIDGIDIASI- 1318
Cdd:PTZ00265 1201 GETGSGKSTVMSLLMRFYdlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkEGGSGEDSTVFKNSGKIl 1280
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1319 ---------GLHDLRGRLTIIPQDPILFSGNLRMNLDpFNK--YSDEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNL 1387
Cdd:PTZ00265 1281 ldgvdicdyNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGKedATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSL 1359
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1388 SIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRN--EFSQCTVITIAHRLHTIMDSDKIMVLD----SGK 1461
Cdd:PTZ00265 1360 SGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDikDKADKTIITIAHRIASIKRSDKIVVFNnpdrTGS 1439
|
1130
....*....|...
gi 569006289 1462 IVE-YGSPEELLS 1473
Cdd:PTZ00265 1440 FVQaHGTHEELLS 1452
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
586-807 |
3.70e-28 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 121.61 E-value: 3.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 586 AVQFSEASFTWDRDLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-------------SIA 652
Cdd:PRK13657 334 AVEFDDVSFSYDNSRQG-VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtvtraslrrNIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 653 YVPQQAWIQNGTIKDNILFGSE--YDEKKYqRVIEACALLPDLEMLPGGDMAEIGEKGINLSGGQKHRVSLARATYQDAD 730
Cdd:PRK13657 413 VVFQDAGLFNRSIEDNIRVGRPdaTDEEMR-AAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPP 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 731 IYILDDPLSAVD--THVgkhifnKVVGP-NGLLSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGSYSDLMDKKGVFAK 807
Cdd:PRK13657 492 ILILDEATSALDveTEA------KVKAAlDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAA 565
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1181-1476 |
9.92e-28 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 120.20 E-value: 9.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1181 NSLT-GDTVGFVLSNALNITQTLNwLVRMTSEVETNIVAVERINEYINvdnEAPWVTDKKPPADwPKKGEIQFNNYQVRY 1259
Cdd:PRK10789 249 GSLTlGQLTSFVMYLGLMIWPMLA-LAWMFNIVERGSAAYSRIRAMLA---EAPVVKDGSEPVP-EGRGELDVNIRQFTY 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1260 RPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTIIPQDPILFSG 1339
Cdd:PRK10789 324 PQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSD 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1340 NLRMNL---DPfnKYSDEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAA 1416
Cdd:PRK10789 404 TVANNIalgRP--DATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSA 481
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1417 VDLETDSLIQTTIRNEFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELLSNMG 1476
Cdd:PRK10789 482 VDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
593-834 |
1.18e-27 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 119.82 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 593 SFTWDRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITI-------------KGSIAYVPQQAW 659
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFhdipltklqldswRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 660 IQNGTIKDNILFGSEyDEKKYQrvIEACALLP----DLEMLPGGDMAEIGEKGINLSGGQKHRVSLARATYQDADIYILD 735
Cdd:PRK10789 400 LFSDTVANNIALGRP-DATQQE--IEHVARLAsvhdDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 736 DPLSAVDTHVGKHIFNKvvgpnglLS----GKTRILVTHGIHFLPQVDEIVVLGKGTILEKGSYSDLMDKKGvfaknWKT 811
Cdd:PRK10789 477 DALSAVDGRTEHQILHN-------LRqwgeGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG-----WYR 544
|
250 260
....*....|....*....|...
gi 569006289 812 FMKHSgPEGEATVDNDSEEEDGD 834
Cdd:PRK10789 545 DMYRY-QQLEAALDDAPEIREEA 566
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
602-789 |
1.28e-27 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 119.85 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 602 ATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-------------SIAYVPQQAWIQNGTIKDN 668
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGadlsqwdreelgrHIGYLPQDVELFDGTIAEN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 669 I-LFGSEYDEKkyqrVIEAcALLPDL-EM---LPGGDMAEIGEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVDT 743
Cdd:COG4618 426 IaRFGDADPEK----VVAA-AKLAGVhEMilrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 569006289 744 hvgkhifnkvVGPNGLL--------SGKTRILVTHGIHFLPQVDEIVVLGKGTI 789
Cdd:COG4618 501 ----------EGEAALAaairalkaRGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
604-739 |
4.88e-27 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 108.12 E-value: 4.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-------------SIAYVPQQAWIQNG-TIKDNI 669
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006289 670 LFGSE----YDEKKYQRVIEAcallpdLEMLPGGDMAE--IGEKGINLSGGQKHRVSLARATYQDADIYILDDPLS 739
Cdd:pfam00005 81 RLGLLlkglSKREKDARAEEA------LEKLGLGDLADrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
593-789 |
5.70e-27 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 108.84 E-value: 5.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 593 SFTWDRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS-------------IAYVPQQAW 659
Cdd:cd03246 7 SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGYLPQDDE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 660 IQNGTIKDNILfgseydekkyqrvieacallpdlemlpggdmaeigekginlSGGQKHRVSLARATYQDADIYILDDPLS 739
Cdd:cd03246 87 LFSGSIAENIL-----------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNS 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 569006289 740 AVDtHVGKHIFNKVVGpNGLLSGKTRILVTHGIHFLPQVDEIVVLGKGTI 789
Cdd:cd03246 126 HLD-VEGERALNQAIA-ALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
586-810 |
9.59e-27 |
|
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: 117.61 E-value: 9.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 586 AVQFSEASFTWDRDLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-------------SIA 652
Cdd:COG5265 357 EVRFENVSFGYDPERPI-LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdirdvtqaslraAIG 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 653 YVPQQAWIQNGTIKDNILFGS-EYDEKKYQRVIEACALLPDLEMLPGGDMAEIGEKGINLSGGQKHRVSLARATYQDADI 731
Cdd:COG5265 436 IVPQDTVLFNDTIAYNIAYGRpDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPI 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 732 YILDDPLSAVDTHVGKHI---FNKVVgpngllSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGSYSDLMDKKGVFAKN 808
Cdd:COG5265 516 LIFDEATSALDSRTERAIqaaLREVA------RGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
..
gi 569006289 809 WK 810
Cdd:COG5265 590 WA 591
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
453-803 |
7.98e-26 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 114.43 E-value: 7.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 453 NEILSGIKILKYFAWEPSFKEQVNSI-------RKKELR---NLLR-----FSQLqtILIFILHLTpTLVSVITFSVYVL 517
Cdd:PRK10790 208 NEVINGMSVIQQFRQQARFGERMGEAsrshymaRMQTLRldgFLLRpllslFSAL--ILCGLLMLF-GFSASGTIEVGVL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 518 VdsqnvlnaekAFtsITLFNILRFPLAMLPMVISSVIQASVS-------VDRLEQYLGSDDLDLSAIRhvchfdkaVQFS 590
Cdd:PRK10790 285 Y----------AF--ISYLGRLNEPLIELTTQQSMLQQAVVAgervfelMDGPRQQYGNDDRPLQSGR--------IDID 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 591 EASFTWDRDlEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-------------SIAYVPQQ 657
Cdd:PRK10790 345 NVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsslshsvlrqGVAMVQQD 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 658 AWIQNGTIKDNILFGSEYDEKKYQRVIEACALLPDLEMLPGGDMAEIGEKGINLSGGQKHRVSLARATYQDADIYILDDP 737
Cdd:PRK10790 424 PVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEA 503
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 738 LSAVDTHVGKHIFNKVvgpnGLLSGKTRILV-THGIHFLPQVDEIVVLGKGTILEKGSYSDLMDKKG 803
Cdd:PRK10790 504 TANIDSGTEQAIQQAL----AAVREHTTLVViAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQG 566
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
588-788 |
3.10e-25 |
|
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: 105.24 E-value: 3.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 588 QFSEASFTWDRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-------------SIAYV 654
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 655 PQQAWIQ--NGTIKDNILFGSEY----DEKKYQRVIEACALLpdlemlpggDMAEIGEKGI-NLSGGQKHRVSLARATYQ 727
Cdd:cd03225 81 FQNPDDQffGPTVEEEVAFGLENlglpEEEIEERVEEALELV---------GLEGLRDRSPfTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006289 728 DADIYILDDPLSAVDTHVGKHIFNKVVGPNGllSGKTRILVTHGIHFLPQV-DEIVVLGKGT 788
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLKA--EGKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
587-793 |
1.24e-24 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 102.39 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 587 VQFSEASFTWDRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS------------IAYV 654
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 655 PQQAWIQNGTIKDNIlfgseydekkyqrvieacallpdlemlpggdmaeigekGINLSGGQKHRVSLARATYQDADIYIL 734
Cdd:cd03247 81 NQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 569006289 735 DDPLSAVDTHVGKHIFNKVVgpnGLLSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKG 793
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIF---EVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1250-1462 |
4.95e-24 |
|
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: 100.37 E-value: 4.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTI 1329
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1330 IPQDPILFSGNLRMNLdpfnkysdeeiwralelahlksfvaglqlgllhevteggdnLSIGQRQLLCLGRAVLRKSKILV 1409
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 569006289 1410 LDEATAAVDLETDSLIQTTIRN-EFSQCTVITIAHRLHTIMDSDKIMVLDSGKI 1462
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
582-789 |
4.96e-24 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 102.16 E-value: 4.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 582 HFDKAVQFSEASFTW-DRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS---------- 650
Cdd:cd03248 7 HLKGIVKFQNVTFAYpTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkyl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 651 ---IAYVPQQAWIQNGTIKDNILFGseYDEKKYQRVIEAC------ALLPDLEMlpgGDMAEIGEKGINLSGGQKHRVSL 721
Cdd:cd03248 87 hskVSLVGQEPVLFARSLQDNIAYG--LQSCSFECVKEAAqkahahSFISELAS---GYDTEVGEKGSQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569006289 722 ARATYQDADIYILDDPLSAVDTHVGKHIFNKVVGPNgllSGKTRILVTHGIHFLPQVDEIVVLGKGTI 789
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWP---ERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
587-799 |
5.42e-24 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 102.03 E-value: 5.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 587 VQFSEASFTWDRDLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-------------SIAY 653
Cdd:COG1122 1 IELENLSFSYPGGTPA-LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknlrelrrKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 654 VPQQAWIQ--NGTIKDNILFGSEY-----DEKKyQRVIEAcallpdLEMLpggDMAEIGEKGI-NLSGGQKHRVSLARAT 725
Cdd:COG1122 80 VFQNPDDQlfAPTVEEDVAFGPENlglprEEIR-ERVEEA------LELV---GLEHLADRPPhELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006289 726 YQDADIYILDDPLSAVDTHVGKHIFNKVvgpNGL-LSGKTRILVTHGIHFLPQV-DEIVVLGKGTILEKGSYSDLM 799
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELL---KRLnKEGKTVIIVTHDLDLVAELaDRVIVLDDGRIVADGTPREVF 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1250-1466 |
2.13e-23 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 98.92 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILeSAGGQIIIDGIDIASIGLHDLRGRLTI 1329
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDL-KPQQGEITLDGVPVSDLEKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1330 IPQDPILFSGNLRMNLdpfnkysdeeiwralelahlksfvaglqlgllhevtegGDNLSIGQRQLLCLGRAVLRKSKILV 1409
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 1410 LDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYG 1466
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
604-791 |
2.59e-23 |
|
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: 99.85 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG--------SIAYVPQQA----WIqngTIKDNILF 671
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvtgpgpDRGYVFQQDallpWL---TVLDNVAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 672 GSEY----DEKKYQRVIEAcallpdlemlpggdMAEIGEKGI------NLSGGQKHRVSLARATYQDADIYILDDPLSAV 741
Cdd:cd03293 97 GLELqgvpKAEARERAEEL--------------LELVGLSGFenayphQLSGGMRQRVALARALAVDPDVLLLDEPFSAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569006289 742 DTHVGKHIfnkvvgpNGLL------SGKTRILVTHGIH---FLPqvDEIVVLGK--GTILE 791
Cdd:cd03293 163 DALTREQL-------QEELldiwreTGKTVLLVTHDIDeavFLA--DRVVVLSArpGRIVA 214
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1250-1461 |
3.50e-23 |
|
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: 99.08 E-value: 3.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRP---ELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLfrilesaggqiiidgidiasIG-LHDLRG 1325
Cdd:cd03250 1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--------------------LGeLEKLSG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1326 RLTI------IPQDPILFSGNLRMNL---DPFNKysdEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLC 1396
Cdd:cd03250 61 SVSVpgsiayVSQEPWIQNGTIRENIlfgKPFDE---ERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 1397 LGRAVLRKSKILVLDEATAAVDLET-DSLIQTTIRNEFSQC-TVITIAHRLHTIMDSDKIMVLDSGK 1461
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1156-1473 |
3.92e-23 |
|
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: 105.51 E-value: 3.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1156 WLAIRLELVGNLIVFCSALllviyknsltgdtVGFVLS---NALNitqtlNWLVRMTSevetnIVAVERINEYINVDNEA 1232
Cdd:TIGR01842 248 YLAIDGEITPGMMIAGSIL-------------VGRALApidGAIG-----GWKQFSGA-----RQAYKRLNELLANYPSR 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1233 PwvtdkkPPADWPK-KGEIQFNNYQVRYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRI---------LE 1302
Cdd:TIGR01842 305 D------PAMPLPEpEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIwpptsgsvrLD 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1303 SAGGQIIIDGIDIASIGLhdlrgrltiIPQDPILFSGNLRMNLDPFNKYSD-EEIWRALELAHLKSFVAGLQLGLLHEVT 1381
Cdd:TIGR01842 379 GADLKQWDRETFGKHIGY---------LPQDVELFPGTVAENIARFGENADpEKIIEAAKLAGVHELILRLPDGYDTVIG 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1382 EGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETD-SLIQTTIRNEFSQCTVITIAHRLHTIMDSDKIMVLDSG 1460
Cdd:TIGR01842 450 PGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEqALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDG 529
|
330
....*....|...
gi 569006289 1461 KIVEYGSPEELLS 1473
Cdd:TIGR01842 530 RIARFGERDEVLA 542
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
604-793 |
3.97e-23 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 97.89 E-value: 3.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS-------------IAYVPQqawiqngtikdnil 670
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaslspkelarkIAYVPQ-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 671 fgseydekkyqrvieACALLpdlemlpggDMAEIGEKGIN-LSGGQKHRVSLARATYQDADIYILDDPLSAVDTHVGKHI 749
Cdd:cd03214 81 ---------------ALELL---------GLAHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 569006289 750 FNKVVGPNGlLSGKTRILVTHGIHFLPQV-DEIVVLGKGTILEKG 793
Cdd:cd03214 137 LELLRRLAR-ERGKTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
604-803 |
4.76e-23 |
|
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: 99.93 E-value: 4.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG------------SIAYVPQQAWI-QNGTIKDNI- 669
Cdd:COG4555 17 LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPDERGLyDRLTVRENIr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 670 LFGSEYDEKKYQRVIEACALLPDLEMLPGGDMAeIGEkginLSGGQKHRVSLARATYQDADIYILDDPLSAVDThVGKHI 749
Cdd:COG4555 97 YFAELYGLFDEELKKRIEELIELLGLEEFLDRR-VGE----LSTGMKKKVALARALVHDPKVLLLDEPTNGLDV-MARRL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 569006289 750 FNKVVGpNGLLSGKTRILVTHGIHFLPQV-DEIVVLGKGTILEKGSYSDLMDKKG 803
Cdd:COG4555 171 LREILR-ALKKEGKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
604-800 |
9.06e-23 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 99.35 E-value: 9.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-------------SIAYVPQQAWIQNG-TIKDNI 669
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAYVPQEPPAPFGlTVRELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 670 LFG--------SEYDEKKYQRVIEAcallpdLEMLpggDMAEIGEKGIN-LSGGQKHRVSLARATYQDADIYILDDPLSA 740
Cdd:COG1120 97 ALGryphlglfGRPSAEDREAVEEA------LERT---GLEHLADRPVDeLSGGERQRVLIARALAQEPPLLLLDEPTSH 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 741 VDTHVGKHIFNkvvgpngLL------SGKTRILVThgiHFLPQV----DEIVVLGKGTILEKGSYSDLMD 800
Cdd:COG1120 168 LDLAHQLEVLE-------LLrrlareRGRTVVMVL---HDLNLAaryaDRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1267-1415 |
1.23e-22 |
|
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: 95.79 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1267 LKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTIIPQDPILFSG-----NL 1341
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRltvreNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1342 RMNL---DPFNKYSDEEIWRALElahlksfvaglQLGLLHE----VTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEAT 1414
Cdd:pfam00005 81 RLGLllkGLSKREKDARAEEALE-----------KLGLGDLadrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 569006289 1415 A 1415
Cdd:pfam00005 150 A 150
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
272-563 |
1.34e-22 |
|
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: 99.93 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 272 ILKSFILKLAHDILLFLNPQLLKFLIGFVKDPDSYPWVGYIyAILMFSVTLIQSFFLQCYFQFCFVLGMTVRTTIIASVY 351
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWI-ALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 352 KKALTLSNLARRQYTIGETVNLMSVDSQKLMD-VTNYIHLLWSSVLQIALSIFFL----WRelgpsiLAGVGLMV--LLV 424
Cdd:cd07346 80 RHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNlVSSGLLQLLSDVLTLIGALVILfylnWK------LTLVALLLlpLYV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 425 PVNGVLATKIRKIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPS----FKEQVNSIRKKELRNLLRFSQLQTILIFIL 500
Cdd:cd07346 154 LILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEReierFREANRDLRDANLRAARLSALFSPLIGLLT 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006289 501 HLTPTLvsVITFSVYvLVdSQNVLNAEKAFTSITLFNILRFPLAMLPMVISSVIQASVSVDRL 563
Cdd:cd07346 234 ALGTAL--VLLYGGY-LV-LQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
586-791 |
3.71e-22 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 97.85 E-value: 3.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 586 AVQFSEASFTWDRDLEAT--IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG--------SIAYVP 655
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpDRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 656 QQA----WIqngTIKDNILFG-------SEYDEKKYQRVIEACALLPDLEMLPGgdmaeigekgiNLSGGQKHRVSLARA 724
Cdd:COG1116 87 QEPallpWL---TVLDNVALGlelrgvpKAERRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569006289 725 TYQDADIYILDDPLSAVDTHVGKHIfnkvvgpNGLL------SGKTRILVTHGIH---FLpqVDEIVVLGK--GTILE 791
Cdd:COG1116 153 LANDPEVLLMDEPFGALDALTRERL-------QDELlrlwqeTGKTVLFVTHDVDeavFL--ADRVVVLSArpGRIVE 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1255-1474 |
3.82e-22 |
|
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: 102.29 E-value: 3.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1255 YQVRYRPELDlVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAG---GQIIIDGIDIASIGLHDLRGRLTIIP 1331
Cdd:COG1123 270 YPVRGKGGVR-AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSgsiLFDGKDLTKLSRRSLRELRRRVQMVF 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1332 QDPILfSGNLRMN--------LDPFNKYSDEEIW-RALELahLKSFvaGLQLGLL----HEvteggdnLSIGQRQLLCLG 1398
Cdd:COG1123 349 QDPYS-SLNPRMTvgdiiaepLRLHGLLSRAERReRVAEL--LERV--GLPPDLAdrypHE-------LSGGQRQRVAIA 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1399 RAVLRKSKILVLDEATAAVDLetdsLIQTTIRNEFSQ------CTVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEEL 1471
Cdd:COG1123 417 RALALEPKLLILDEPTSALDV----SVQAQILNLLRDlqrelgLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEV 492
|
...
gi 569006289 1472 LSN 1474
Cdd:COG1123 493 FAN 495
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
604-793 |
6.61e-22 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 96.04 E-value: 6.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG----------------SIAYVPQQAwiqNG---- 663
Cdd:cd03257 21 LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirrkEIQMVFQDP---MSslnp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 664 --TIKDNI------LFGSEYDEKKYQRVIEACALLPD----LEMLPGGdmaeigekginLSGGQKHRVSLARATYQDADI 731
Cdd:cd03257 98 rmTIGEQIaeplriHGKLSKKEARKEAVLLLLVGVGLpeevLNRYPHE-----------LSGGQRQRVAIARALALNPKL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569006289 732 YILDDPLSAVDTHVGKHIFNkvvgpngLL------SGKTRILVTHGIHFLPQV-DEIVVLGKGTILEKG 793
Cdd:cd03257 167 LIADEPTSALDVSVQAQILD-------LLkklqeeLGLTLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1247-1477 |
6.76e-22 |
|
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: 101.75 E-value: 6.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1247 KGEIQFNNYQVRYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQiiidgidiASIGLHDLR-- 1324
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGS--------VRLDGADLSqw 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1325 -----GRLtI--IPQDPILFSGNLRMNLDPFNKYSDEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCL 1397
Cdd:COG4618 400 dreelGRH-IgyLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGL 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1398 GRAVLRKSKILVLDEATAAVDLETDSLIQTTIRNEFSQ-CTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELLSNMG 1476
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLARLA 558
|
.
gi 569006289 1477 P 1477
Cdd:COG4618 559 R 559
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
586-794 |
1.77e-21 |
|
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: 99.98 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 586 AVQFSEASFTWDRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMEN---VHGHITIKG------------- 649
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGrdllelsealrgr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 650 SIAYVPQQAWIQ-NG-TIKDNILFGSEYD----EKKYQRVIEAcallpdLEMLpggDMAEIGEKGIN-LSGGQKHRVSLA 722
Cdd:COG1123 84 RIGMVFQDPMTQlNPvTVGDQIAEALENLglsrAEARARVLEL------LEAV---GLERRLDRYPHqLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006289 723 RATYQDADIYILDDPLSAVDTHVGKHIFNKVVGPNGLLsGKTRILVTHGIHFLPQV-DEIVVLGKGTILEKGS 794
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRER-GTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGP 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1248-1444 |
2.28e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 100.27 E-value: 2.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1248 GEIQFNNYQVRyRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLtnclFRILesaggqiiidgidiA--------SIG 1319
Cdd:COG4178 361 GALALEDLTLR-TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTL----LRAI--------------AglwpygsgRIA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1320 LHDLrGRLTIIPQDPILFSGNLRMNL---DPFNKYSDEEIWRALELAHLKSFVaglqlGLLHEVTEGGDNLSIGQRQLLC 1396
Cdd:COG4178 422 RPAG-ARVLFLPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGLGHLA-----ERLDEEADWDQVLSLGEQQRLA 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 569006289 1397 LGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHR 1444
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1250-1474 |
3.26e-21 |
|
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: 99.21 E-value: 3.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQI---IIDGIDIASIGLHDLRGR 1326
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISgevLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1327 LTIIPQDPilfsgnlRMNLDPFN------------KYSDEEIW-RALELAHlksfvaglQLGLLHEVTEGGDNLSIGQRQ 1393
Cdd:COG1123 85 IGMVFQDP-------MTQLNPVTvgdqiaealenlGLSRAEARaRVLELLE--------AVGLERRLDRYPHQLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1394 LLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIR--NEFSQCTVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEE 1470
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEE 229
|
....
gi 569006289 1471 LLSN 1474
Cdd:COG1123 230 ILAA 233
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
604-793 |
3.38e-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: 93.35 E-value: 3.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-----------SIAYVPQQ-AWIQNGTIKDNILF 671
Cdd:cd03259 16 LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvtgvpperrNIGMVFQDyALFPHLTVAENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 672 G----SEYDEKKYQRVIEACALL---PDLEMLPGGdmaeigekginLSGGQKHRVSLARATYQDADIYILDDPLSAVDTH 744
Cdd:cd03259 96 GlklrGVPKAEIRARVRELLELVgleGLLNRYPHE-----------LSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 745 VG-------KHIFNKvvgpngllSGKTRILVTHGI-HFLPQVDEIVVLGKGTILEKG 793
Cdd:cd03259 165 LReelreelKELQRE--------LGITTIYVTHDQeEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
604-789 |
6.53e-21 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 92.94 E-value: 6.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISaMLGEMENV-HGHITIKG-----------------SIAYVPQQ-AWIQNGT 664
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVRVDGtdisklsekelaafrrrHIGFVFQSfNLLPDLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 665 IKDNILFGSEYDEKKyQRVIEACALlpdlEMLPGGDMAEIGEKGIN-LSGGQKHRVSLARATYQDADIYILDDPLSAVDT 743
Cdd:cd03255 99 ALENVELPLLLAGVP-KKERRERAE----ELLERVGLGDRLNHYPSeLSGGQQQRVAIARALANDPKIILADEPTGNLDS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 569006289 744 HVGKHIFNKVVGPNGlLSGKTRILVTHGIHFLPQVDEIVVLGKGTI 789
Cdd:cd03255 174 ETGKEVMELLRELNK-EAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
599-794 |
1.16e-20 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 91.70 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 599 DLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-------------SIAYVPQQAWIQNGTI 665
Cdd:cd03369 19 DLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 666 KDNILFGSEYDEKKYQRVIeacallpdlemlpggdmaEIGEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVDTHV 745
Cdd:cd03369 99 RSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 569006289 746 gKHIFNKVVgpNGLLSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGS 794
Cdd:cd03369 161 -DALIQKTI--REEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1250-1466 |
1.89e-20 |
|
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: 91.80 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELDLV--LKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILE--SAGGQIIIDGIDIASIGLHDLRG 1325
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKptSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1326 R-LTIIPQDPILfSGNLRMN-----LDPF---NKYSDEEIWRALELAHLKSFvaGLQLGLL----HEvteggdnLSIGQR 1392
Cdd:cd03257 82 KeIQMVFQDPMS-SLNPRMTigeqiAEPLrihGKLSKKEARKEAVLLLLVGV--GLPEEVLnrypHE-------LSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569006289 1393 QLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTT---IRNEFsQCTVITIAHRLHTI-MDSDKIMVLDSGKIVEYG 1466
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLlkkLQEEL-GLTLLFITHDLGVVaKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1250-1473 |
2.49e-20 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 92.17 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELDL--VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRL 1327
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1328 TIIPQDPILfSGNLRMNLD-----PFN----KYSDEEIWRALELAhlksfvaGLQLGLL----HEvteggdnLSIGQRQL 1394
Cdd:COG1124 82 QMVFQDPYA-SLHPRHTVDrilaePLRihglPDREERIAELLEQV-------GLPPSFLdrypHQ-------LSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1395 LCLGRAVLRKSKILVLDEATAAVDLETDSLIQ---TTIRNEFsQCTVITIAHRLHTI--MdSDKIMVLDSGKIVEYGSPE 1469
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILnllKDLREER-GLTYLFVSHDLAVVahL-CDRVAVMQNGRIVEELTVA 224
|
....
gi 569006289 1470 ELLS 1473
Cdd:COG1124 225 DLLA 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
604-800 |
3.51e-20 |
|
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: 96.13 E-value: 3.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG----------------SIAYVPQ---QAWIQNGT 664
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkdltklsrrslrelrrRVQMVFQdpySSLNPRMT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 665 IKDNI-----LFGSEYDEKKYQRV---IEACALLPD-LEMLPGGdmaeigekginLSGGQKHRVSLARATYQDADIYILD 735
Cdd:COG1123 361 VGDIIaeplrLHGLLSRAERRERVaelLERVGLPPDlADRYPHE-----------LSGGQRQRVAIARALALEPKLLILD 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006289 736 DPLSAVDTHVGKHIFNkvvgpngLL------SGKTRILVTHGIHFLPQV-DEIVVLGKGTILEKGSYSDLMD 800
Cdd:COG1123 430 EPTSALDVSVQAQILN-------LLrdlqreLGLTYLFISHDLAVVRYIaDRVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1256-1461 |
6.94e-20 |
|
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: 88.07 E-value: 6.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1256 QVRYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAggqiiidgidiasiglhdlrgrltiipqdpi 1335
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT------------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1336 lfSGNLRMNLDPFNKYSDEEIWRalelahlksfvaglQLGLLHEvteggdnLSIGQRQLLCLGRAVLRKSKILVLDEATA 1415
Cdd:cd00267 53 --SGEILIDGKDIAKLPLEELRR--------------RIGYVPQ-------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 569006289 1416 AVDLETDSLIQTTIRNEFSQ-CTVITIAHRLHTIMD-SDKIMVLDSGK 1461
Cdd:cd00267 110 GLDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1251-1461 |
8.03e-20 |
|
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: 89.45 E-value: 8.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1251 QFNNYQVRYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTII 1330
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1331 PQDP------------ILFSgnLRmNLdpfnKYSDEEIWRALELAhLKSFvaGLQlGLLHEVTEggdNLSIGQRQLLCLG 1398
Cdd:cd03225 81 FQNPddqffgptveeeVAFG--LE-NL----GLPEEEIEERVEEA-LELV--GLE-GLRDRSPF---TLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006289 1399 RAVLRKSKILVLDEATAAVDLETDSLIQTTIRnEFSQC--TVITIAHRLHTIMD-SDKIMVLDSGK 1461
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLK-KLKAEgkTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
587-799 |
9.56e-20 |
|
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: 90.05 E-value: 9.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 587 VQFSEASFTWdRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISaMLGEM-ENVHGHITIKG-------------SIA 652
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMK-MINRLiEPTSGEIFIDGedireqdpvelrrKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 653 YVPQQAwiqnG-----TIKDNI-----LFGSEyDEKKYQRVIEACALLpDLEmlPGGDMAEIGEKginLSGGQKHRVSLA 722
Cdd:cd03295 79 YVIQQI----GlfphmTVEENIalvpkLLKWP-KEKIRERADELLALV-GLD--PAEFADRYPHE---LSGGQQQRVGVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569006289 723 RATYQDADIYILDDPLSAVDTHVGKHIFNKVVGPNGLLsGKTRILVTHGI-HFLPQVDEIVVLGKGTILEKGSYSDLM 799
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQEL-GKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1266-1476 |
1.44e-19 |
|
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: 89.53 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHdLRGRLTIIPQDPILFSGN-LRMN 1344
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLPDERGLYDRLtVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1345 LD---PFNKYSDEEI-WRALELAHLksfvagLQLG-LLHEVTEGgdnLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDL 1419
Cdd:COG4555 95 IRyfaELYGLFDEELkKRIEELIEL------LGLEeFLDRRVGE---LSTGMKKKVALARALVHDPKVLLLDEPTNGLDV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006289 1420 ETdsliQTTIRNEFSQC-----TVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEELLSNMG 1476
Cdd:COG4555 166 MA----RRLLREILRALkkegkTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
604-788 |
2.93e-19 |
|
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: 86.14 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIkgsiayvpqqawiqngtikdnilFGSEYDEKKYQRV 683
Cdd:cd00267 15 LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI-----------------------DGKDIAKLPLEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 684 IEACALLPDLemlpggdmaeigekginlSGGQKHRVSLARATYQDADIYILDDPLSAVDTHVGKHIFNKVVGPNglLSGK 763
Cdd:cd00267 72 RRRIGYVPQL------------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELA--EEGR 131
|
170 180
....*....|....*....|....*.
gi 569006289 764 TRILVTHGIHFLPQV-DEIVVLGKGT 788
Cdd:cd00267 132 TVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
605-800 |
3.93e-19 |
|
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: 88.33 E-value: 3.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 605 QDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS----------------IAYVPQQ-AWIQNGTIKD 667
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrrMGMLFQSgALFDSLTVFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 668 NILFG----SEYDEKKYQRV----IEACALLPDLEMLPGgdmaeigekgiNLSGGQKHRVSLARATYQDADIYILDDPLS 739
Cdd:cd03261 97 NVAFPlrehTRLSEEEIREIvlekLEAVGLRGAEDLYPA-----------ELSGGMKKRVALARALALDPELLLYDEPTA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 740 AVDThVGKHIFNKVVgpnglLS-----GKTRILVTHGIHFLPQV-DEIVVLGKGTILEKGSYSDLMD 800
Cdd:cd03261 166 GLDP-IASGVIDDLI-----RSlkkelGLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1266-1474 |
4.83e-19 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 88.02 E-value: 4.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSL---TNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTIIPQDPILFS---- 1338
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLircINGLERPTSGSVLVDGTDLTLLSGKELRKARRRIGMIFQHFNLLSsrtv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1339 -GNLRMNLDPFNKYSDEEIWRALELAHLksfvaglqLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAV 1417
Cdd:cd03258 100 fENVALPLEIAGVPKAEIEERVLELLEL--------VGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1418 DLETDSLIQTTIR--NEFSQCTVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEELLSN 1474
Cdd:cd03258 172 DPETTQSILALLRdiNRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
586-793 |
7.78e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 88.40 E-value: 7.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 586 AVQFSEASFTWdRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS----------IAYVP 655
Cdd:PRK15056 6 GIVVNDVTVTW-RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 656 QQA---WIQNGTIKDNILFGS--------EYDEKKYQRVIEACALLpdlemlpggDMAEIGEKGI-NLSGGQKHRVSLAR 723
Cdd:PRK15056 85 QSEevdWSFPVLVEDVVMMGRyghmgwlrRAKKRDRQIVTAALARV---------DMVEFRHRQIgELSGGQKKRVFLAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569006289 724 ATYQDADIYILDDPLSAVDTHVGKHIFNkvvgpngLL-----SGKTRILVTHGIHFLPQVDEIVVLGKGTILEKG 793
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARIIS-------LLrelrdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
587-806 |
2.01e-18 |
|
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: 86.89 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 587 VQFSEASFTWDRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-SIAYVP---------- 655
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGiDISKLPlhtlrsrlsi 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 656 --QQAWIQNGTIKDNILFGSEYDEKKYQRVIEACALLPDLEMLPGGDMAEIGEKGINLSGGQKHRVSLARATYQDADIYI 733
Cdd:cd03288 100 ilQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006289 734 LDDPLSAVDTHVgKHIFNKVVgpNGLLSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGSYSDLMDKK-GVFA 806
Cdd:cd03288 180 MDEATASIDMAT-ENILQKVV--MTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFA 250
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
604-798 |
6.50e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 87.05 E-value: 6.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGeMENV-HGHITIKG-----------SIAYVPQQ-AWIQNGTIKDNIL 670
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG-LEDPtSGEILIGGrdvtdlppkdrNIAMVFQSyALYPHMTVYENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 671 FG--------SEYDekkyQRVIEACALLpDLEML----PGgdmaeigekgiNLSGGQKHRVSLARATYQDADIYILDDPL 738
Cdd:COG3839 98 FPlklrkvpkAEID----RRVREAAELL-GLEDLldrkPK-----------QLSGGQRQRVALGRALVREPKVFLLDEPL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006289 739 SAVD--------THVgKHIFNKvvgpngllSGKTRILVTHGihflpQV------DEIVVLGKGTILEKGSYSDL 798
Cdd:COG3839 162 SNLDaklrvemrAEI-KRLHRR--------LGTTTIYVTHD-----QVeamtlaDRIAVMNDGRIQQVGTPEEL 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
604-791 |
8.56e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 83.94 E-value: 8.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISaMLGEMENV-HGHITIKG-----------------SIAYVPQQA-WIQNGT 664
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVLIDGqdisslserelarlrrrHIGFVFQFFnLLPELT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 665 IKDNILFGSEYD----EKKYQRVIEAcallpdLEMLpggDMAEIGEKGIN-LSGGQKHRVSLARATYQDADIYILDDPLS 739
Cdd:COG1136 103 ALENVALPLLLAgvsrKERRERAREL------LERV---GLGDRLDHRPSqLSGGQQQRVAIARALVNRPKLILADEPTG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 569006289 740 AVDTHVGKHIFNkvvgpngLL------SGKTRILVTHGIHFLPQVDEIVVLGKGTILE 791
Cdd:COG1136 174 NLDSKTGEEVLE-------LLrelnreLGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1266-1466 |
9.11e-18 |
|
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: 82.48 E-value: 9.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTIIPQdpilfsgnlrmnl 1345
Cdd:cd03214 14 VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1346 dpfnkysdeeiwrALELahlksfvaglqLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDL----ET 1421
Cdd:cd03214 81 -------------ALEL-----------LGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIahqiEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 569006289 1422 DSLIQTTIRNEfsQCTVITIAHRL-HTIMDSDKIMVLDSGKIVEYG 1466
Cdd:cd03214 137 LELLRRLARER--GKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1250-1473 |
1.62e-17 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 83.60 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELdlVLKGITCNIKSTEKVGVVGRTGAGKSSLtnclFRILesaggqiiidgidiasIGLHDL-RGRLT 1328
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTL----LKAI----------------LGLLPPtSGTVR 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1329 IIPQDPILFSGNL---------------------RMNLDP----FNKYSDEE---IWRALELAHLKSFvAGLQLGllhev 1380
Cdd:COG1121 65 LFGKPPRRARRRIgyvpqraevdwdfpitvrdvvLMGRYGrrglFRRPSRADreaVDEALERVGLEDL-ADRPIG----- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1381 teggdNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRnEFSQ--CTVITIAHRLHTIMD-SDKIMVL 1457
Cdd:COG1121 139 -----ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLR-ELRRegKTILVVTHDLGAVREyFDRVLLL 212
|
250
....*....|....*.
gi 569006289 1458 DsGKIVEYGSPEELLS 1473
Cdd:COG1121 213 N-RGLVAHGPPEEVLT 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
606-788 |
2.18e-17 |
|
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: 81.46 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 606 DVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG---------------SIAYVPQQ-AWIQNGTIKDNI 669
Cdd:cd03229 18 DVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelpplrrRIGMVFQDfALFPHLTVLENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 670 LFGseydekkyqrvieacallpdlemlpggdmaeigekginLSGGQKHRVSLARATYQDADIYILDDPLSAVDThVGKHI 749
Cdd:cd03229 98 ALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDP-ITRRE 138
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 569006289 750 FNKVVGPNGLLSGKTRILVTHGIHFLPQV-DEIVVLGKGT 788
Cdd:cd03229 139 VRALLKSLQAQLGITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
605-783 |
2.47e-17 |
|
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: 82.14 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 605 QDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG------------SIAYVPQQ-AWIQNGTIKDNILF 671
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYLGHAdGLKPELTVRENLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 672 -----GSEYDEKKYQRVIEACALlPDLEMLPGGdmaeigekgiNLSGGQKHRVSLARATYQDADIYILDDPLSAVDTHvG 746
Cdd:COG4133 99 waalyGLRADREAIDEALEAVGL-AGLADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA-G 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 569006289 747 KHIFNKVVgpNGLL-SGKTRILVTHGIHFLPQVDEIVV 783
Cdd:COG4133 167 VALLAELI--AAHLaRGGAVLLTTHQPLELAAARVLDL 202
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1250-1473 |
2.61e-17 |
|
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: 83.17 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELdlVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTI 1329
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1330 IPQDPILfSGNL---------RMN-LDPFNKYSDEE---IWRALElahlksfvaglQLGLLH----EVTEggdnLSIGQR 1392
Cdd:COG1120 80 VPQEPPA-PFGLtvrelvalgRYPhLGLFGRPSAEDreaVEEALE-----------RTGLEHladrPVDE----LSGGER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1393 QLLCLGRAVLRKSKILVLDEATAAVDL----ETDSLIQTtiRNEFSQCTVITIAHRL-HTIMDSDKIMVLDSGKIVEYGS 1467
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRR--LARERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGP 221
|
....*.
gi 569006289 1468 PEELLS 1473
Cdd:COG1120 222 PEEVLT 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
604-789 |
3.02e-17 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 80.90 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGsiayvpQQAWIQNGTIKDNILFgseydekkyqrV 683
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG------KDIKKEPEEVKRRIGY-----------L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 684 IEACALLPDL---EMLpggdmaeigekgiNLSGGQKHRVSLARATYQDADIYILDDPLSAVDTHVGKHIFNKVVGPNGll 760
Cdd:cd03230 79 PEEPSLYENLtvrENL-------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKK-- 143
|
170 180 190
....*....|....*....|....*....|
gi 569006289 761 SGKTRILVTHGIHFLPQV-DEIVVLGKGTI 789
Cdd:cd03230 144 EGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1266-1471 |
3.65e-17 |
|
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: 82.23 E-value: 3.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILE-------SAGGQIIIDGIDIASIGLHDLRGRLTIIPQDPILFS 1338
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgapdEGEVLLDGKDIYDLDVDVLELRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1339 G----NLRMNLDPF----NKYSDEEIWRALELAHLKSFVAgLQLGLLHevteggdnLSIGQRQLLCLGRAVLRKSKILVL 1410
Cdd:cd03260 95 GsiydNVAYGLRLHgiklKEELDERVEEALRKAALWDEVK-DRLHALG--------LSGGQQQRLCLARALANEPEVLLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006289 1411 DEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEEL 1471
Cdd:cd03260 166 DEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
592-800 |
4.04e-17 |
|
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: 82.54 E-value: 4.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 592 ASFTWDRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS-------------IAYVPQQA 658
Cdd:COG1124 9 VSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRpvtrrrrkafrrrVQMVFQDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 659 -------WiqngTIKD------NILFGSEYDEkkyqRVIEACAL--LPD--LEMLPGgdmaeigekgiNLSGGQKHRVSL 721
Cdd:COG1124 89 yaslhprH----TVDRilaeplRIHGLPDREE----RIAELLEQvgLPPsfLDRYPH-----------QLSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 722 ARATYQDADIYILDDPLSAVDTHVGKHIFNkvvgpngLL------SGKTRILVTHGI----HFlpqVDEIVVLGKGTILE 791
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILN-------LLkdlreeRGLTYLFVSHDLavvaHL---CDRVAVMQNGRIVE 219
|
....*....
gi 569006289 792 KGSYSDLMD 800
Cdd:COG1124 220 ELTVADLLA 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1266-1463 |
5.20e-17 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 79.78 E-value: 5.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFrilesaggqiiidgidiasiGLHdlrgrltiiPQDpilfSGNLRMNL 1345
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILS--------------------GLY---------KPD----SGEILVDG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1346 DPFNKYSDEEIWRA-LELAHlksfvaglQLgllhevteggdnlSIGQRQLLCLGRAVLRKSKILVLDEATAAVDL-ETDS 1423
Cdd:cd03216 62 KEVSFASPRDARRAgIAMVY--------QL-------------SVGERQMVEIARALARNARLLILDEPTAALTPaEVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 569006289 1424 LIQtTIRNEFSQ-CTVITIAHRLHTIMD-SDKIMVLDSGKIV 1463
Cdd:cd03216 121 LFK-VIRRLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
604-792 |
8.32e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.05 E-value: 8.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGSIAYVP---------QQAWIQNGTIKDNILFGSE 674
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPgaergvvfqNEGLLPWRNVQDNVAFGLQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 675 Y-DEKKYQRVIEAcallpdLEMLPGGDMAEIGEKGI-NLSGGQKHRVSLARATYQDADIYILDDPLSAVDThvgkhiFNK 752
Cdd:PRK11248 97 LaGVEKMQRLEIA------HQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA------FTR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 569006289 753 VVGPNGLL-----SGKTRILVTHGIH---FLpqVDEIVVL--GKGTILEK 792
Cdd:PRK11248 165 EQMQTLLLklwqeTGKQVLLITHDIEeavFM--ATELVLLspGPGRVVER 212
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
584-801 |
9.50e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 82.54 E-value: 9.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 584 DKAVQFSEASFTWDRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSS---LISAMLGEMENVHGHITIKGsIAYVPQQAW- 659
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDG-ITLTAKTVWd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 660 --------IQN-------GTIKDNILFGSEYDEKKYQRVIEACA-LLPDLEMLPggdmaEIGEKGINLSGGQKHRVSLAR 723
Cdd:PRK13640 82 irekvgivFQNpdnqfvgATVGDDVAFGLENRAVPRPEMIKIVRdVLADVGMLD-----YIDSEPANLSGGQKQRVAIAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 724 ATYQDADIYILDDPLSAVDTHVGKHIFN---KVVGPNGLlsgkTRILVTHGIHFLPQVDEIVVLGKGTILEKGSYSDLMD 800
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKlirKLKKKNNL----TVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
.
gi 569006289 801 K 801
Cdd:PRK13640 233 K 233
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
585-742 |
9.83e-17 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 81.92 E-value: 9.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 585 KAVQFSEASFTWDRDLEAT-----IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG---------- 649
Cdd:cd03294 16 KAFKLLAKGKSKEEILKKTgqtvgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrke 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 650 -------SIAYVPQQ-AWIQNGTIKDNILFGSEYD-------EKKYQRVIEACALLPDLEMLPGgdmaeigekgiNLSGG 714
Cdd:cd03294 96 lrelrrkKISMVFQSfALLPHRTVLENVAFGLEVQgvpraerEERAAEALELVGLEGWEHKYPD-----------ELSGG 164
|
170 180
....*....|....*....|....*...
gi 569006289 715 QKHRVSLARATYQDADIYILDDPLSAVD 742
Cdd:cd03294 165 MQQRVGLARALAVDPDILLMDEAFSALD 192
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1189-1457 |
1.13e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 86.62 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1189 GFVLSNALNITQTLNWLVRMTSEVETNIVAVERINEYINVDNEAPWVTDKKPPADWPKKGEIQFNNYQVRYRPELDL-VL 1267
Cdd:PTZ00265 322 GSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYDTRKDVeIY 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1268 KGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILE-SAGGQIIIDGIDIASIGLHDLRGRLTIIPQDPILFSGNLRMNL- 1345
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDpTEGDIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIk 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1346 ------------------DPFNKYSDEEIWRAL------------------ELAHLKS---------------------F 1368
Cdd:PTZ00265 482 yslyslkdlealsnyyneDGNDSQENKNKRNSCrakcagdlndmsnttdsnELIEMRKnyqtikdsevvdvskkvlihdF 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1369 VAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRN---EFSQCTVItIAHRL 1445
Cdd:PTZ00265 562 VSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNlkgNENRITII-IAHRL 640
|
330
....*....|..
gi 569006289 1446 HTIMDSDKIMVL 1457
Cdd:PTZ00265 641 STIRYANTIFVL 652
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
604-800 |
1.25e-16 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 80.56 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS--------------IAYVPQ-QAWIQNGTIKDN 668
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEgRRIFPELTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 669 ILFGSE--YDEKKYQRVIEACALLPDL-EMLpggdmaeiGEKGINLSGGQKHRVSLARATYQDADIYILDDP---LSAVd 742
Cdd:cd03224 96 LLLGAYarRRAKRKARLERVYELFPRLkERR--------KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPsegLAPK- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 569006289 743 thVGKHIFNKVVGPNGllSGKTRILVTHGIHFLPQV-DEIVVLGKGTILEKGSYSDLMD 800
Cdd:cd03224 167 --IVEEIFEAIRELRD--EGVTILLVEQNARFALEIaDRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1266-1474 |
2.62e-16 |
|
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: 79.79 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILEsaggqiiidgidiASIGLHDLRGR-LTIIP------------- 1331
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLR-------------PTSGSVLFDGEdITGLPpheiarlgigrtf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1332 QDPILFSG-----NLRM----------NLDPFNKYSDEEIWRALELAHlksfvaglQLGLLHEVTEGGDNLSIGQRQLLC 1396
Cdd:cd03219 82 QIPRLFPEltvleNVMVaaqartgsglLLARARREEREARERAEELLE--------RVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1397 LGRAVLRKSKILVLDEATAAVDL-ETDSLIQtTIR--NEFSqCTVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEELL 1472
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPeETEELAE-LIRelRERG-ITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVR 231
|
..
gi 569006289 1473 SN 1474
Cdd:cd03219 232 NN 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
587-801 |
3.70e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 80.18 E-value: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 587 VQFSEASFTWDRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHI-------------TIKGSIAY 653
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfeKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 654 VPQQAWIQ--NGTIKDNILFGSE-----YDEKKyQRVIEAcalLPDLEMLPGGDmaeigEKGINLSGGQKHRVSLARATY 726
Cdd:PRK13648 88 VFQNPDNQfvGSIVKYDVAFGLEnhavpYDEMH-RRVSEA---LKQVDMLERAD-----YEPNALSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 727 QDADIYILDDPLSAVDTHVGKHIFNKVvgpNGLLSGK--TRILVTHGIHFLPQVDEIVVLGKGTILEKGSYSDLMDK 801
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLV---RKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
604-742 |
3.89e-16 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 79.53 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS----------------IAYVPQQ-AWIQNGTIK 666
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrrqIGMIFQQfNLIERLSVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 667 DNILFG------------SEYDEKKYQRvieACALLPDLEMLpggDMAEIgeKGINLSGGQKHRVSLARATYQDADIYIL 734
Cdd:cd03256 97 ENVLSGrlgrrstwrslfGLFPKEEKQR---ALAALERVGLL---DKAYQ--RADQLSGGQQQRVAIARALMQQPKLILA 168
|
....*...
gi 569006289 735 DDPLSAVD 742
Cdd:cd03256 169 DEPVASLD 176
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
606-800 |
3.96e-16 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 81.73 E-value: 3.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 606 DVNLDIKPGQLVAVVGTVGSGKSSLISAMLG-EMENvHGHITIKG------------SIAYVPQQ-AWIQNGTIKDNILF 671
Cdd:COG1118 20 DVSLEIASGELVALLGPSGSGKTTLLRIIAGlETPD-SGRIVLNGrdlftnlpprerRVGFVFQHyALFPHMTVAENIAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 672 GseydekkyqrvieacallpdLEMLPGGDmAEIGEK-----------GI------NLSGGQKHRVSLARATYQDADIYIL 734
Cdd:COG1118 99 G--------------------LRVRPPSK-AEIRARveellelvqleGLadrypsQLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 735 DDPLSAVDTHVGK-------HIFNKVvgpngllsGKTRILVTHgihflpQVDE-------IVVLGKGTILEKGSYSDLMD 800
Cdd:COG1118 158 DEPFGALDAKVRKelrrwlrRLHDEL--------GGTTVFVTH------DQEEaleladrVVVMNQGRIEQVGTPDEVYD 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
605-800 |
4.68e-16 |
|
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: 79.25 E-value: 4.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 605 QDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-SIAYVPQQAWI----------QNG------TIKD 667
Cdd:COG1127 22 DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqDITGLSEKELYelrrrigmlfQGGalfdslTVFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 668 NILFG----SEYDEK-KYQRVIEAcallpdLEM--LPG-GDM--AEigekginLSGGQKHRVSLARATYQDADIYILDDP 737
Cdd:COG1127 102 NVAFPlrehTDLSEAeIRELVLEK------LELvgLPGaADKmpSE-------LSGGMRKRVALARALALDPEILLYDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006289 738 LSAVDTHVGKHIFNKVVGPNGLLsGKTRILVTHGIHFLPQV-DEIVVLGKGTILEKGSYSDLMD 800
Cdd:COG1127 169 TAGLDPITSAVIDELIRELRDEL-GLTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEELLA 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
587-791 |
4.94e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 78.94 E-value: 4.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 587 VQFSEASFTWDRDLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG----------------S 650
Cdd:COG2884 2 IRFENVSKRYPGGREA-LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlkrreipylrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 651 IAYVPQQAW-IQNGTIKDNILFG---SEYDEKKYQ-RVIEAcallpdLEMLpggdmaEIGEKG----INLSGGQKHRVSL 721
Cdd:COG2884 81 IGVVFQDFRlLPDRTVYENVALPlrvTGKSRKEIRrRVREV------LDLV------GLSDKAkalpHELSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 722 ARATYQDADIYILDDPLSAVDTHVGKHI------FNKVvgpngllsGKTRILVTHGIHFLPQVDE-IVVLGKGTILE 791
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPETSWEImelleeINRR--------GTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
604-801 |
6.20e-16 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 78.92 E-value: 6.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-----------SIAYVPQQ-AWIQNGTIKDNILF 671
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatdvpvqerNVGFVFQHyALFRHMTVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 672 G-------SEYDEKKYQRVIEACALLPDLEMLPGGDMAEigekginLSGGQKHRVSLARATYQDADIYILDDPLSAVDTH 744
Cdd:cd03296 98 GlrvkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQ-------LSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569006289 745 VGKH-------IFNKVvgpngllsGKTRILVTHGIHFLPQV-DEIVVLGKGTILEKGSYSDLMDK 801
Cdd:cd03296 171 VRKElrrwlrrLHDEL--------HVTTVFVTHDQEEALEVaDRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
584-802 |
6.34e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 79.65 E-value: 6.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 584 DKAVQFSEASFTWDRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG------SIAYVPQQ 657
Cdd:PRK13632 5 SVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskeNLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 658 AWI--QN-------GTIKDNILFGSE---YDEKKYQRVIEACALLPDLEMLpggdmaeIGEKGINLSGGQKHRVSLARAT 725
Cdd:PRK13632 85 IGIifQNpdnqfigATVEDDIAFGLEnkkVPPKKMKDIIDDLAKKVGMEDY-------LDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 726 YQDADIYILDDPLSAVDTHvGKHIFNKVVGPNGLLSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGSYSDLMDKK 802
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPK-GKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1266-1471 |
7.65e-16 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 78.70 E-value: 7.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNC---LFRILESAGGQIIIDGIDIASIGLHDLRGRLTIIPQDPILFSG--- 1339
Cdd:cd03261 15 VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLivgLLRPDSGEVLIDGEDISGLSEAELYRLRRRMGMLFQSGALFDSltv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1340 --NLRMNLDPFNKYSDEEIwRALELAHLKsfvaglQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAV 1417
Cdd:cd03261 95 feNVAFPLREHTRLSEEEI-REIVLEKLE------AVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 569006289 1418 D----LETDSLIQTTirNEFSQCTVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEEL 1471
Cdd:cd03261 168 DpiasGVIDDLIRSL--KKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
603-793 |
7.85e-16 |
|
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: 78.07 E-value: 7.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 603 TIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-----------SIAYVPQQ-AWIQNGTIKDNIL 670
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkdrDIAMVFQNyALYPHMTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 671 FG--------SEYDEkkyqRVIEACALLpDLEMLpggdmaeIGEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVD 742
Cdd:cd03301 95 FGlklrkvpkDEIDE----RVREVAELL-QIEHL-------LDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569006289 743 THVGKHIFNKVVGPNGLLsGKTRILVTHG-IHFLPQVDEIVVLGKGTILEKG 793
Cdd:cd03301 163 AKLRVQMRAELKRLQQRL-GTTTIYVTHDqVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
587-788 |
1.52e-15 |
|
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: 75.18 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 587 VQFSEASFTW-DRDLeatIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITI--KGSIAYVPQqawiqng 663
Cdd:cd03221 1 IELENLSKTYgGKLL---LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWgsTVKIGYFEQ------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 664 tikdnilfgseydekkyqrvieacallpdlemlpggdmaeigekginLSGGQKHRVSLARATYQDADIYILDDPLSAVDt 743
Cdd:cd03221 71 -----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD- 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 569006289 744 hvgkhIFNKVVGPNGLLS-GKTRILVTHGIHFLPQV-DEIVVLGKGT 788
Cdd:cd03221 103 -----LESIEALEEALKEyPGTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
604-744 |
1.66e-15 |
|
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: 77.31 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSL---ISAMLGEMENVHGHITIKG----------SIAYVPQQ-AWIQNGTIKDNI 669
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLldaISGRVEGGGTTSGQILFNGqprkpdqfqkCVAYVRQDdILLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 670 LF-----GSEYDEKKYQRVIEACALLPDLEMLPGGdmaeiGEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVDTH 744
Cdd:cd03234 103 TYtailrLPRKSSDAIRKKRVEDVLLRDLALTRIG-----GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1266-1461 |
1.94e-15 |
|
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: 75.69 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILE--SAGGQIIIDGIDIASIGLHDLRGRLTIIPQDPILFSGnlrm 1343
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEpdSGSILIDGEDLTDLEDELPPLRRRIGMVFQDFALFPH---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1344 nldpfnkysdeeiwralelahlksfvaglqLGLLHEVTEGgdnLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDS 1423
Cdd:cd03229 91 ------------------------------LTVLENIALG---LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 569006289 1424 LIQTTIR--NEFSQCTVITIAHRLHTIMD-SDKIMVLDSGK 1461
Cdd:cd03229 138 EVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
596-794 |
2.52e-15 |
|
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: 76.84 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 596 WDRDLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLISAM-----LGEMENVHGHITIKGS---------------IAYVP 655
Cdd:cd03260 9 YYGDKHA-LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKdiydldvdvlelrrrVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 656 QQAWIQNGTIKDNILFG---SEYDEKKYQRVIEACAL----LPDLEmlpgGDMAeigeKGINLSGGQKHRVSLARATYQD 728
Cdd:cd03260 88 QKPNPFPGSIYDNVAYGlrlHGIKLKEELDERVEEALrkaaLWDEV----KDRL----HALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006289 729 ADIYILDDPLSAVDTHVGKHI------FNKVVgpngllsgkTRILVTHGIHflpQV----DEIVVLGKGTILEKGS 794
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIeeliaeLKKEY---------TIVIVTHNMQ---QAarvaDRTAFLLNGRLVEFGP 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
603-789 |
4.04e-15 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 75.76 E-value: 4.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 603 TIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG----------SIAYVPQQAWIQNG--TIKDNIL 670
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQDVDYQLFtdSVREELL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 671 FGSEYDEKKYQRVIEacaLLPDLEMLpggDMAEigEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVDTH----VG 746
Cdd:cd03226 95 LGLKELDAGNEQAET---VLKDLDLY---ALKE--RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKnmerVG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 569006289 747 KhIFNKVVGpngllSGKTRILVTHGIHFLPQV-DEIVVLGKGTI 789
Cdd:cd03226 167 E-LIRELAA-----QGKAVIVITHDYEFLAKVcDRVLLLANGAI 204
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
606-807 |
4.61e-15 |
|
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: 76.22 E-value: 4.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 606 DVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS-----------IAYVPQQ-AWIQNGTIKDNILFG- 672
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYKNIAYGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 673 ---SEYDEKKYQRVIEACALLPDLEMLpggdmaeiGEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVDTHVGKHI 749
Cdd:cd03299 97 kkrKVDKKEIERKVLEIAEMLGIDHLL--------NRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569006289 750 FN--KVVGPNgllSGKTRILVTHG-IHFLPQVDEIVVLGKGTILEKGsysdlmDKKGVFAK 807
Cdd:cd03299 169 REelKKIRKE---FGVTVLHVTHDfEEAWALADKVAIMLNGKLIQVG------KPEEVFKK 220
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1250-1444 |
5.50e-15 |
|
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: 74.11 E-value: 5.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVrYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLtnclFRILesaggqiiidgidiA--------SIGLH 1321
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSL----FRAL--------------AglwpwgsgRIGMP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1322 DlRGRLTIIPQDPILFSGNLRmnldpfnkysdEEI---WralelahlksfvaglqlgllhevtegGDNLSIGQRQLLCLG 1398
Cdd:cd03223 62 E-GEDLLFLPQRPYLPLGTLR-----------EQLiypW--------------------------DDVLSGGEQQRLAFA 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 569006289 1399 RAVLRKSKILVLDEATAAVDLETDSLIQTTIRNEFsqCTVITIAHR 1444
Cdd:cd03223 104 RLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG--ITVISVGHR 147
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
604-797 |
6.64e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.34 E-value: 6.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIkGS---IAYVPQQawiQ-----NGTIKDNIlfgSEY 675
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GEtvkIGYFDQH---QeeldpDKTVLDEL---RDG 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 676 DEKKyqRVIEACALLPDleMLPGGDMAE--IGekgiNLSGGQKHRVSLARATYQDADIYILDDP---LSaVDThvgKHIF 750
Cdd:COG0488 404 APGG--TEQEVRGYLGR--FLFSGDDAFkpVG----VLSGGEKARLALAKLLLSPPNVLLLDEPtnhLD-IET---LEAL 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 569006289 751 NkvvgpNGLLS--GkTRILVTHGIHFLPQV-DEIVVLGKGTILEK-GSYSD 797
Cdd:COG0488 472 E-----EALDDfpG-TVLLVSHDRYFLDRVaTRILEFEDGGVREYpGGYDD 516
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
602-805 |
7.59e-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: 76.43 E-value: 7.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 602 ATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLgEMENVHGHITIKG-------------SIAYVPQQAWIQNGTIKDN 668
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwrkAFGVIPQKVFIFSGTFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 669 ILFGSEYDEKKYQRVIEACALLPDLEMLPGGDMAEIGEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVDThVGKH 748
Cdd:cd03289 97 LDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-ITYQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 749 IFNKVVgpNGLLSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGSYSDLMDKKGVF 805
Cdd:cd03289 176 VIRKTL--KQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
606-794 |
1.19e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 77.43 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 606 DVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS-----------IAYVPQQ-AWIQNGTIKDNILFG- 672
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHyALFRHMTVFDNIAFGl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 673 ----------SEYDEKKYQRVieacallpdLEMLPGGDMAEigEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVD 742
Cdd:PRK10851 100 tvlprrerpnAAAIKAKVTQL---------LEMVQLAHLAD--RYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569006289 743 THVGKHI------------FnkvvgpngllsgkTRILVTHGIHFLPQV-DEIVVLGKGTILEKGS 794
Cdd:PRK10851 169 AQVRKELrrwlrqlheelkF-------------TSVFVTHDQEEAMEVaDRVVVMSQGNIEQAGT 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
604-801 |
1.27e-14 |
|
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: 74.97 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-SIAYVP----------QQ-AWIQNGTIKDNILF 671
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkDITNLPphkrpvntvfQNyALFPHLTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 672 G-----SEYDEKKyQRVIEAcallpdLEMLpggDMAEIGEKGIN-LSGGQKHRVSLARATYQDADIYILDDPLSAVDTHV 745
Cdd:cd03300 96 GlrlkkLPKAEIK-ERVAEA------LDLV---QLEGYANRKPSqLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006289 746 GKHI------FNKVVgpngllsGKTRILVTHGI-HFLPQVDEIVVLGKGTILEKGSYSDLMDK 801
Cdd:cd03300 166 RKDMqlelkrLQKEL-------GITFVFVTHDQeEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
592-785 |
1.66e-14 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 75.28 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 592 ASFTWDRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGSI--------AYVPQQ----AW 659
Cdd:COG4525 11 VRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVFQKdallPW 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 660 IqngTIKDNILFGSeydekKYQRVIEACALLPDLEMLPGGDMAEIGEKGI-NLSGGQKHRVSLARATYQDADIYILDDPL 738
Cdd:COG4525 91 L---NVLDNVAFGL-----RLRGVPKAERRARAEELLALVGLADFARRRIwQLSGGMRQRVGIARALAADPRFLLMDEPF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 569006289 739 SAVDTHVGKHIfnkvvgpNGLL------SGKTRILVTHGIhflpqvDEIVVLG 785
Cdd:COG4525 163 GALDALTREQM-------QELLldvwqrTGKGVFLITHSV------EEALFLA 202
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
964-1222 |
1.70e-14 |
|
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: 75.66 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 964 DNSPSQRDMR-----IGVFGALGIAQGIFLLSSSLWSIYACRNASKTLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDI 1038
Cdd:cd07346 27 DDVIPAGDLSlllwiALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1039 STVDDTLPQTLRSWLLCFFGIVSTLVMICmatpifiiiiiplsilYVSVQ----------VFYVATSRQLRRLDSVTK-- 1106
Cdd:cd07346 107 DAVQNLVSSGLLQLLSDVLTLIGALVILF----------------YLNWKltlvallllpLYVLILRYFRRRIRKASRev 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1107 ----SPIYSHFSETVSGLPVIRAFEHQQRFLANSEKQIDTNQKcvfSWITSNRWLAIRLELVGNLIVFCSALLLV----- 1177
Cdd:cd07346 171 reslAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRD---ANLRAARLSALFSPLIGLLTALGTALVLLyggyl 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 569006289 1178 IYKNSLT-GDTVGFVLSNALnITQTLNWLVRMTSEVETNIVAVERI 1222
Cdd:cd07346 248 VLQGSLTiGELVAFLAYLGM-LFGPIQRLANLYNQLQQALASLERI 292
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
604-794 |
1.73e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 76.68 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGeMENV-HGHITIKG-----------SIAYVPQqawiqNG------TI 665
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAG-FETPdSGRILLDGrdvtglppekrNVGMVFQ-----DYalfphlTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 666 KDNILFGSEY-----DEKKyQRVIEAcallpdLEMLpggDMAEIGEKGIN-LSGGQKHRVSLARATYQDADIYILDDPLS 739
Cdd:COG3842 95 AENVAFGLRMrgvpkAEIR-ARVAEL------LELV---GLEGLADRYPHqLSGGQQQRVALARALAPEPRVLLLDEPLS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569006289 740 AVDTHVG-------KHIFNKVvgpngllsGKTRILVTHGihflpQV------DEIVVLGKGTILEKGS 794
Cdd:COG3842 165 ALDAKLReemreelRRLQREL--------GITFIYVTHD-----QEealalaDRIAVMNDGRIEQVGT 219
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
599-745 |
2.44e-14 |
|
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: 73.48 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 599 DLEATIQDVNLDIK---PGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS-----------------IAYVPQQ- 657
Cdd:cd03297 5 DIEKRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkkinlppqqrkIGLVFQQy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 658 AWIQNGTIKDNILFGSEYDEKKYQRVIEAcallpdlEMLPGGDMAEIGEKGI-NLSGGQKHRVSLARATYQDADIYILDD 736
Cdd:cd03297 85 ALFPHLNVRENLAFGLKRKRNREDRISVD-------ELLDLLGLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDE 157
|
....*....
gi 569006289 737 PLSAVDTHV 745
Cdd:cd03297 158 PFSALDRAL 166
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
604-799 |
3.42e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 74.28 E-value: 3.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-------------SIAYVPQQAWIQNG-TIKDNI 669
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTPEGiTVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 670 LFG-----------SEYDEKKYQRVIEACALlpdlemlpggdmAEIGEKGI-NLSGGQKHRVSLARATYQDADIYILDDP 737
Cdd:PRK11231 98 AYGrspwlslwgrlSAEDNARVNQAMEQTRI------------NHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569006289 738 LSAVDthvgkhiFNKVVGPNGLL-----SGKTRILVthgIHFLPQV----DEIVVLGKGTILEKGSYSDLM 799
Cdd:PRK11231 166 TTYLD-------INHQVELMRLMrelntQGKTVVTV---LHDLNQAsrycDHLVVLANGHVMAQGTPEEVM 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
605-744 |
3.47e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 72.98 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 605 QDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG----------SIAYV-PQQAWIQNGTIKDNILFGS 673
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpdvaeACHYLgHRNAMKPALTVAENLEFWA 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006289 674 EYDEKKYQRVIEA-CAL-LPDLEMLPGGdmaeigekgiNLSGGQKHRVSLARATYQDADIYILDDPLSAVDTH 744
Cdd:PRK13539 99 AFLGGEELDIAAAlEAVgLAPLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
604-798 |
4.18e-14 |
|
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: 73.38 E-value: 4.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISaMLGEMEN-VHGHITIKG----------------SIAYVPQQ-AWIQNGTI 665
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIR-CINGLERpTSGSVLVDGtdltllsgkelrkarrRIGMIFQHfNLLSSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 666 KDNILF-----GSEYDEKKyQRVIEACALLpDLEmlpggDMAEIGEKgiNLSGGQKHRVSLARATYQDADIYILDDPLSA 740
Cdd:cd03258 100 FENVALpleiaGVPKAEIE-ERVLELLELV-GLE-----DKADAYPA--QLSGGQKQRVGIARALANNPKVLLCDEATSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 569006289 741 VDTHVGKHIFNKVVGPNGLLsGKTRILVTHGIHFLPQV-DEIVVLGKGTILEKGSYSDL 798
Cdd:cd03258 171 LDPETTQSILALLRDINREL-GLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEV 228
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
598-791 |
4.25e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.07 E-value: 4.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 598 RDLEATI-QDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKgsiayVPQQAWIQNGTIKDNILFGSEYD 676
Cdd:COG2401 39 RVVERYVlRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----VPDNQFGREASLIDAIGRKGDFK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 677 EKKYqrVIEACALlpdlemlpgGDMAEIGEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVDTHVGKHIFNKVvgp 756
Cdd:COG2401 114 DAVE--LLNAVGL---------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNL--- 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 569006289 757 nGLLS---GKTRILVTHG---IHFLpQVDEIVVLGKGTILE 791
Cdd:COG2401 180 -QKLArraGITLVVATHHydvIDDL-QPDLLIFVGYGGVPE 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
605-802 |
5.36e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.64 E-value: 5.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 605 QDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG--SIAYVPQQAWI-QNGTIKDNILFGseyDEKKYQ 681
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLdDDLTVLDTVLDG---DAELRA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 682 RVIEACALLPDLEMlPGGDMAEIGEK-----------------------GI----------NLSGGQKHRVSLARATYQD 728
Cdd:COG0488 92 LEAELEELEAKLAE-PDEDLERLAELqeefealggweaearaeeilsglGFpeedldrpvsELSGGWRRRVALARALLSE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 729 ADIYILDDP-----LSAVD---THVGKHifnkvvgPNGLlsgktrILVTHGIHFLPQV-DEIVVLGKGTILE-KGSYSDL 798
Cdd:COG0488 171 PDLLLLDEPtnhldLESIEwleEFLKNY-------PGTV------LVVSHDRYFLDRVaTRILELDRGKLTLyPGNYSAY 237
|
....
gi 569006289 799 MDKK 802
Cdd:COG0488 238 LEQR 241
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
607-806 |
8.28e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 72.86 E-value: 8.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 607 VNLDIKPGQLVAVVGTVGSGKSSLISAM--LGEMENVH---GHITIKGSIAYVPQQAWI-----------QN------GT 664
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCInlLEQPEAGTirvGDITIDTARSLSQQKGLIrqlrqhvgfvfQNfnlfphRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 665 IKDNILFGSEY--DEKKYQRVIEACALLpdlemlpggdmAEIGEKGIN------LSGGQKHRVSLARATYQDADIYILDD 736
Cdd:PRK11264 102 VLENIIEGPVIvkGEPKEEATARARELL-----------AKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006289 737 PLSAVDTHVGKHIFNKVvgpNGLLSGK-TRILVTHGIHFLPQV-DEIVVLGKGTILEKGsysdlmDKKGVFA 806
Cdd:PRK11264 171 PTSALDPELVGEVLNTI---RQLAQEKrTMVIVTHEMSFARDVaDRAIFMDQGRIVEQG------PAKALFA 233
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1266-1466 |
8.58e-14 |
|
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: 72.17 E-value: 8.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHdlRGRLTIIPQDPILFS-----GN 1340
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPhltvaEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1341 LRMNLDPFNKYSDEEIWRALELAhlksfvagLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLE 1420
Cdd:cd03259 93 IAFGLKLRGVPKAEIRARVRELL--------ELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 569006289 1421 TDSLIQTTIRNEFSQ--CTVITIAHRLHTIMD-SDKIMVLDSGKIVEYG 1466
Cdd:cd03259 165 LREELREELKELQRElgITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
604-794 |
1.08e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 73.54 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG---------------SIAYVPQQAWIQ--NGTIK 666
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkKVGLVFQYPEYQlfEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 667 DNILFG----SEYDEKKYQRVIEACALLpdlemlpGGDMAEIGEKG-INLSGGQKHRVSLARATYQDADIYILDDPLSAV 741
Cdd:PRK13637 103 KDIAFGpinlGLSEEEIENRVKRAMNIV-------GLDYEDYKDKSpFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 742 DTHVGKHIFNKVvgpnGLLSGK---TRILVTHGIHFLPQ-VDEIVVLGKGTILEKGS 794
Cdd:PRK13637 176 DPKGRDEILNKI----KELHKEynmTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1250-1493 |
1.26e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 72.72 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTI 1329
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1330 IPQDP------------ILFSGNLRMnLDPfnkysdEEIWR-ALELAHlksfVAGLQLGLLHEvtegGDNLSIGQRQLLC 1396
Cdd:PRK13632 88 IFQNPdnqfigatveddIAFGLENKK-VPP------KKMKDiIDDLAK----KVGMEDYLDKE----PQNLSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1397 LGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRN--EFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELLSN 1474
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
250 260
....*....|....*....|....*....
gi 569006289 1475 M---------GPF-YLMAKEagIESVNHT 1493
Cdd:PRK13632 233 KeilekakidSPFiYKLSKK--LKGIDPT 259
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
593-793 |
2.18e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 72.36 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 593 SFTWDRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGsIAYVPQQAW---------IQN- 662
Cdd:PRK13635 12 SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG-MVLSEETVWdvrrqvgmvFQNp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 663 ------GTIKDNILFGSEYD----EKKYQRVIEAcalLPDLEMLPGGDmaeigEKGINLSGGQKHRVSLARATYQDADIY 732
Cdd:PRK13635 91 dnqfvgATVQDDVAFGLENIgvprEEMVERVDQA---LRQVGMEDFLN-----REPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006289 733 ILDDPLSAVDThVGKHifnKVVGPNGLLSGKTRILV---THGIHFLPQVDEIVVLGKGTILEKG 793
Cdd:PRK13635 163 ILDEATSMLDP-RGRR---EVLETVRQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEEG 222
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1251-1462 |
2.61e-13 |
|
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: 70.64 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1251 QFNNYQVRYRPELdlVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLfrilesaggqiiidgidiasIGLHDL-RGRLTI 1329
Cdd:cd03235 1 EVEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAI--------------------LGLLKPtSGSIRV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1330 --------------IPQD-------PILFSGNLRMNLDP----FNKYSDEEIWRALELahLKsfvaglQLGLLHEVTEGG 1384
Cdd:cd03235 59 fgkplekerkrigyVPQRrsidrdfPISVRDVVLMGLYGhkglFRRLSKADKAKVDEA--LE------RVGLSELADRQI 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1385 DNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRnEFSQ--CTVITIAHRLHTIMDS-DKIMVLDSGK 1461
Cdd:cd03235 131 GELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLR-ELRRegMTILVVTHDLGLVLEYfDRVLLLNRTV 209
|
.
gi 569006289 1462 I 1462
Cdd:cd03235 210 V 210
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1266-1474 |
2.77e-13 |
|
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: 70.93 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAggqiiidgidIASIGL--HDLRGR---------LTIIPQDP 1334
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPR----------SGSIRFdgRDITGLppheraragIGYVPEGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1335 ILFSG-----NLRMNLDPFNKYSDEEIW-RALELahlksFVAglqlglLHEV--TEGGdNLSIGQRQLLCLGRAVLRKSK 1406
Cdd:cd03224 85 RIFPEltveeNLLLGAYARRRAKRKARLeRVYEL-----FPR------LKERrkQLAG-TLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569006289 1407 ILVLDEATAAvdletdslIQTTIRNEFSQC---------TVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEELLSN 1474
Cdd:cd03224 153 LLLLDEPSEG--------LAPKIVEEIFEAirelrdegvTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
604-793 |
4.15e-13 |
|
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: 70.25 E-value: 4.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGSIAYVPQ-QAWIQNG-TIKDNILF-GSEY--DEK 678
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGlGGGFNPElTGRENIYLnGRLLglSRK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 679 KYQRVIEACAllpdlemlpggDMAEIGE------KgiNLSGGQKHRVSLARATYQDADIYILDDPLSAVDTH----VGKH 748
Cdd:cd03220 118 EIDEKIDEII-----------EFSELGDfidlpvK--TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfqekCQRR 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 569006289 749 IFNKVVGpngllsGKTRILVTHGIHFLPQV-DEIVVLGKGTILEKG 793
Cdd:cd03220 185 LRELLKQ------GKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
604-798 |
5.84e-13 |
|
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: 69.84 E-value: 5.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG------------SIAYVPQQAWIQNG-TIKDNIL 670
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYCPQFDALFDElTVREHLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 671 F------GSEYDEKKYQ-RVIEACALLPDLEMLPGgdmaeigekgiNLSGGQKHRVSLARATYQDADIYILDDPLSAVDT 743
Cdd:cd03263 98 FyarlkgLPKSEIKEEVeLLLRVLGLTDKANKRAR-----------TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 569006289 744 HVGKHIFNKVvgpNGLLSGKTRILVTHGIH---FLpqVDEIVVLGKGTILEKGSYSDL 798
Cdd:cd03263 167 ASRRAIWDLI---LEVRKGRSIILTTHSMDeaeAL--CDRIAIMSDGKLRCIGSPQEL 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
599-795 |
5.85e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 72.56 E-value: 5.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 599 DLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-SIAYVP-----------QQAWIQNGTIK 666
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvDLSHVPpyqrpinmmfqSYALFPHMTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 667 DNILFGSEYDEKKYQRVIEACAllpdlEMLPGGDMAEI-GEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVDTHV 745
Cdd:PRK11607 110 QNIAFGLKQDKLPKAEIASRVN-----EMLGLVHMQEFaKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569006289 746 GKHIFNKVVgpnGLLS--GKTRILVTHGihflpQVDEIVVLGKGTILEKGSY 795
Cdd:PRK11607 185 RDRMQLEVV---DILErvGVTCVMVTHD-----QEEAMTMAGRIAIMNRGKF 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1250-1473 |
6.52e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 70.81 E-value: 6.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLT---NCLFRiLESAGGQIIIDGIDIASIglHDLRGR 1326
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAkllNGLLL-PEAGTITVGGMVLSEETV--WDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1327 LTIIPQDP------------ILFSgnLRMNLDPfnkySDEEIWR---ALELAHLKSFvaglqlgLLHEVTeggdNLSIGQ 1391
Cdd:PRK13635 83 VGMVFQNPdnqfvgatvqddVAFG--LENIGVP----REEMVERvdqALRQVGMEDF-------LNREPH----RLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1392 RQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIR--NEFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPE 1469
Cdd:PRK13635 146 KQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
....
gi 569006289 1470 ELLS 1473
Cdd:PRK13635 226 EIFK 229
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
605-789 |
7.27e-13 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 69.48 E-value: 7.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 605 QDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGSIAYVPQQAWIQ----------------NGTIKDN 668
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElrqkvgmvfqqfnlfpHLTVLEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 669 ILFGseydEKKYQRVIEACALLPDLEMLPGGDMAE-IGEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVDTHVGK 747
Cdd:cd03262 97 ITLA----PIKVKGMSKAEAEERALELLEKVGLADkADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 569006289 748 HIFNkvVGPNGLLSGKTRILVTHGIHFLPQV-DEIVVLGKGTI 789
Cdd:cd03262 173 EVLD--VMKDLAEEGMTMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
606-789 |
7.69e-13 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 67.84 E-value: 7.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 606 DVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGSIAYV--PQQAWiQNG--TIkdnilfgseydekkYQ 681
Cdd:cd03216 18 GVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFasPRDAR-RAGiaMV--------------YQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 682 rvieacallpdlemlpggdmaeigekginLSGGQKHRVSLARATYQDADIYILDDPLSAVDTHVGKHIFNKVvgpnGLL- 760
Cdd:cd03216 83 -----------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVI----RRLr 129
|
170 180 190
....*....|....*....|....*....|.
gi 569006289 761 -SGKTRILVTHGIHFLPQV-DEIVVLGKGTI 789
Cdd:cd03216 130 aQGVAVIFISHRLDEVFEIaDRVTVLRDGRV 160
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1266-1462 |
8.64e-13 |
|
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: 68.19 E-value: 8.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLfrilesaggqiiidgidiasiglhdlrgrLTIIPQDpilfSGNLRMNl 1345
Cdd:cd03230 15 ALDDISLTVEKGEIYGLLGPNGAGKTTLIKII-----------------------------LGLLKPD----SGEIKVL- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1346 dpfnkysDEEIWRALELAHLKSFVAGLQLGLLHEVTeGGDNL--SIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDS 1423
Cdd:cd03230 61 -------GKDIKKEPEEVKRRIGYLPEEPSLYENLT-VRENLklSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRR 132
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 569006289 1424 LIQTTIRNEFSQ-CTVITIAHRLHTIMD-SDKIMVLDSGKI 1462
Cdd:cd03230 133 EFWELLRELKKEgKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1264-1474 |
9.77e-13 |
|
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: 69.29 E-value: 9.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1264 DLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESaggQIIIDGIDIASI-GLHDLRGRLTIIPQDPILFSgnlr 1342
Cdd:cd03299 12 EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKP---DSGKILLNGKDItNLPPEKRDISYVPQNYALFP---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1343 mNLDPFN---------KYSDEEIWR-ALELAHLksfvaglqLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDE 1412
Cdd:cd03299 85 -HMTVYKniayglkkrKVDKKEIERkVLEIAEM--------LGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006289 1413 ATAAVDLET-DSLIQ--TTIRNEFSqCTVITIAHRLHTI-MDSDKIMVLDSGKIVEYGSPEELLSN 1474
Cdd:cd03299 156 PFSALDVRTkEKLREelKKIRKEFG-VTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
583-807 |
1.04e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 70.42 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 583 FDKAVQFSEASFTWDRDLE---ATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEM-----ENVHGHITIKGSIAYV 654
Cdd:PRK13645 3 FSKDIILDNVSYTYAKKTPfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIisetgQTIVGDYAIPANLKKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 655 ----------------PQQAWIQNgTIKDNILFG----SEYDEKKYQRVIEacalLPDLEMLPGgDMAEigEKGINLSGG 714
Cdd:PRK13645 83 kevkrlrkeiglvfqfPEYQLFQE-TIEKDIAFGpvnlGENKQEAYKKVPE----LLKLVQLPE-DYVK--RSPFELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 715 QKHRVSLARATYQDADIYILDDPLSAVDTHVGKHIFNKVVGPNGlLSGKTRILVTHGI-HFLPQVDEIVVLGKGTILEKG 793
Cdd:PRK13645 155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNK-EYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIG 233
|
250
....*....|....
gi 569006289 794 SYSDLMDKKGVFAK 807
Cdd:PRK13645 234 SPFEIFSNQELLTK 247
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
604-798 |
1.06e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 71.29 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS-----------IAYVPQQ-AWIQNGTIKDNILF 671
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvthrsiqqrdICMVFQSyALFPHMSLGENVGY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 672 GSEY-----DEKKyQRVIEACALLpdlemlpggDMAEIGEKGIN-LSGGQKHRVSLARATYQDADIYILDDPLSAVDTHV 745
Cdd:PRK11432 102 GLKMlgvpkEERK-QRVKEALELV---------DLAGFEDRYVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 569006289 746 GKHIFNKVVGPNGLLsGKTRILVTHGIHFLPQV-DEIVVLGKGTILEKGSYSDL 798
Cdd:PRK11432 172 RRSMREKIRELQQQF-NITSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1250-1474 |
1.14e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 69.68 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYrpELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRI--LESAGGQIIIDGIDIASI-----GLHD 1322
Cdd:PRK14258 8 IKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMneLESEVRVEGRVEFFNQNIyerrvNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1323 LRGRLTIIPQDPILFSGNLRMNLdpfnKYSDEEI-WR-ALEL-----AHLKSfvAGLQLGLLHEVTEGGDNLSIGQRQLL 1395
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNV----AYGVKIVgWRpKLEIddiveSALKD--ADLWDEIKHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1396 CLGRAVLRKSKILVLDEATAAVD----LETDSLIQT-TIRNEFsqcTVITIAHRLHTIMD-SDKIMVLDS-----GKIVE 1464
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSlRLRSEL---TMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVE 236
|
250
....*....|
gi 569006289 1465 YGSPEELLSN 1474
Cdd:PRK14258 237 FGLTKKIFNS 246
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
604-794 |
1.46e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 70.05 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITI-------------------KGSIAYVPQQAWIQNGT 664
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitagkknkklkplrkKVGIVFQFPEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 665 IKDNILFG------SEYD-EKKYQRVIEACALLPD-LEMLPggdmaeigekgINLSGGQKHRVSLARATYQDADIYILDD 736
Cdd:PRK13634 103 VEKDICFGpmnfgvSEEDaKQKAREMIELVGLPEElLARSP-----------FELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006289 737 PLSAVDTHVGKHI---FNKVVGPNGLlsgkTRILVTHGIHFLPQ-VDEIVVLGKGTILEKGS 794
Cdd:PRK13634 172 PTAGLDPKGRKEMmemFYKLHKEKGL----TTVLVTHSMEDAARyADQIVVMHKGTVFLQGT 229
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1267-1460 |
1.61e-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: 68.51 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1267 LKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDL----RGRLTIIPQDPILFSGNLR 1342
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1343 MNL---DPFNKYSDEEIwraLELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDL 1419
Cdd:cd03290 97 ENItfgSPFNKQRYKAV---TDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 569006289 1420 E-TDSLIQTTIRnEFSQ---CTVITIAHRLHTIMDSDKIMVLDSG 1460
Cdd:cd03290 174 HlSDHLMQEGIL-KFLQddkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
604-793 |
1.72e-12 |
|
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: 67.58 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVH--GHITIKG----------SIAYVPQqawiqngtikDNILF 671
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGrpldkrsfrkIIGYVPQ----------DDILH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 672 GseydekkYQRVIEAcallpdLEMlpggdMAEIgeKGInlSGGQKHRVSLARATYQDADIYILDDPLSAVDTHVGKHIFn 751
Cdd:cd03213 95 P-------TLTVRET------LMF-----AAKL--RGL--SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM- 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569006289 752 kvvgpnGLLS-----GKTRILVTH-----GIHFLpqvDEIVVLGKGTILEKG 793
Cdd:cd03213 152 ------SLLRrladtGRTIICSIHqpsseIFELF---DKLLLLSQGRVIYFG 194
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
604-742 |
1.85e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 71.76 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITI--KGSIAYVPQQAWIQNGTIKDNILF---GSEYDEK 678
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQRPYLPLGTLREALLYpatAEAFSDA 458
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006289 679 KYQRVIEACAlLPDLEmlpgGDMAEIGEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVD 742
Cdd:COG4178 459 ELREALEAVG-LGHLA----ERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
605-794 |
2.41e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 68.57 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 605 QDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGSIA--------YVPQQawiqngTIKDNILFG---- 672
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSallelgagFHPEL------TGRENIYLNgrll 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 673 ----SEYDEkKYQRVIeacallpdlemlpggDMAEIGEKgINL-----SGGQKHRVSLARATYQDADIYILDDPLSAVDT 743
Cdd:COG1134 117 glsrKEIDE-KFDEIV---------------EFAELGDF-IDQpvktySSGMRARLAFAVATAVDPDILLVDEVLAVGDA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 569006289 744 HVGK---HIFNKVVGpngllSGKTRILVTHGIHFLPQV-DEIVVLGKGTILEKGS 794
Cdd:COG1134 180 AFQKkclARIRELRE-----SGRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGD 229
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
976-1222 |
3.06e-12 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 69.13 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 976 VFGALGIAQGIFLLSSSLWSIYACRNASKTLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDI----STVDDTLPQTLRS 1051
Cdd:cd18557 41 ILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTsvlqSAVTDNLSQLLRN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1052 WLLCFFGIVS--------TLVMICMatpifiiiiiplSILYVSVQVFYVATSRQLRR--LDSVTKSPiySHFSETVSGLP 1121
Cdd:cd18557 121 ILQVIGGLIIlfilswklTLVLLLV------------IPLLLIASKIYGRYIRKLSKevQDALAKAG--QVAEESLSNIR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1122 VIRAF---EHQ-QRFLANSEKQIDTNQKCVFsWITSNRWLAIRLELVGNLIVFCSALLLVIYKNSLTGDTVGFVL----- 1192
Cdd:cd18557 187 TVRSFsaeEKEiRRYSEALDRSYRLARKKAL-ANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILytimv 265
|
250 260 270
....*....|....*....|....*....|.
gi 569006289 1193 -SNALNITQTLNWLVRMTSevetnivAVERI 1222
Cdd:cd18557 266 aSSVGGLSSLLADIMKALG-------ASERV 289
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
601-802 |
4.12e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.47 E-value: 4.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 601 EATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGsiAYVPQQAWI---------------QNGTI 665
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG--VPVPARARLararigvvpqfdnldLEFTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 666 KDNILFGSEYDEKKyQRVIEAcaLLPDLEmlpggDMAEIGEKG----INLSGGQKHRVSLARATYQDADIYILDDPLSAV 741
Cdd:PRK13536 132 RENLLVFGRYFGMS-TREIEA--VIPSLL-----EFARLESKAdarvSDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006289 742 DTHVGKHIFNKVvgpNGLLS-GKTRILVThgiHFLPQV----DEIVVLGKGTILEKGSYSDLMDKK 802
Cdd:PRK13536 204 DPHARHLIWERL---RSLLArGKTILLTT---HFMEEAerlcDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
604-804 |
4.22e-12 |
|
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: 67.57 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG--------------SIAYVPQQAWI-QNGTIKDN 668
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmhkrarlGIGYLPQEASIfRKLTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 669 ILFGSEYDEK-KYQRVIEACALLPDLEMLPGGDmaeigEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVD----- 742
Cdd:cd03218 96 ILAVLEIRGLsKKEREEKLEELLEEFHITHLRK-----SKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDpiavq 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006289 743 --THVGKHIFNKVVGpngllsgktrILVT-HGIH-FLPQVDEIVVLGKGTILEKGSYSDLMDKKGV 804
Cdd:cd03218 171 diQKIIKILKDRGIG----------VLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAANELV 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
604-742 |
5.03e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 67.87 E-value: 5.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-------------SIAYVPQQAwiqngtikdNIL 670
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHS---------SLS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 671 F---------------GSEYDEKkyQRVIEACALLPDLEMLPGGDMAEigekginLSGGQKHRVSLARA----TYQDAD- 730
Cdd:PRK13548 89 FpftveevvamgraphGLSRAED--DALVAAALAQVDLAHLAGRDYPQ-------LSGGEQQRVQLARVlaqlWEPDGPp 159
|
170
....*....|...
gi 569006289 731 -IYILDDPLSAVD 742
Cdd:PRK13548 160 rWLLLDEPTSALD 172
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1250-1472 |
5.05e-12 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 67.80 E-value: 5.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRY--RPeldlVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFR---------------------ILEsagg 1306
Cdd:COG1119 4 LELRNVTVRRggKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdlpptygndvrlfgerrggedVWE---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1307 qiiidgiDIASIGL------HDLRGRLTIIpqDPILfSGnLRMNLDPFNKYSDEEIWRALELAHLksfvaglqLGLLHEV 1380
Cdd:COG1119 76 -------LRKRIGLvspalqLRFPRDETVL--DVVL-SG-FFDSIGLYREPTDEQRERARELLEL--------LGLAHLA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1381 TEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRN--EFSQCTVITIAHRLHTIMDS-DKIMVL 1457
Cdd:COG1119 137 DRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLL 216
|
250
....*....|....*
gi 569006289 1458 DSGKIVEYGSPEELL 1472
Cdd:COG1119 217 KDGRVVAAGPKEEVL 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
587-802 |
5.49e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 68.27 E-value: 5.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 587 VQFSEASFTWDR----DLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHIT---------------- 646
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyEHQA-IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTvdditithktkdkyir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 647 -IKGSIAYVPQ--QAWIQNGTIKDNILFGSEYDEKKYQRVIE-ACALLPDLemlpgGDMAEIGEKG-INLSGGQKHRVSL 721
Cdd:PRK13646 82 pVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNyAHRLLMDL-----GFSRDVMSQSpFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 722 ARATYQDADIYILDDPLSAVDTHvGKHIFNKVVGPNGLLSGKTRILVTHGIHFLPQ-VDEIVVLGKGTILEKGSYSDLMD 800
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQ-SKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFK 235
|
..
gi 569006289 801 KK 802
Cdd:PRK13646 236 DK 237
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
586-787 |
6.91e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 67.37 E-value: 6.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 586 AVQFSEASFTWDRdlEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAmLGEMENVHGHITIKGSIAYVPQQAWIQNGTI 665
Cdd:PRK14258 7 AIKVNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNIYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 666 ------------KDNILFGSEYDEKKYQrvIEACALLPDLEM-------LPGGDM-----AEIGEKGINLSGGQKHRVSL 721
Cdd:PRK14258 84 nrlrrqvsmvhpKPNLFPMSVYDNVAYG--VKIVGWRPKLEIddivesaLKDADLwdeikHKIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006289 722 ARATYQDADIYILDDPLSAVDTHVGKHIfNKVVGPNGLLSGKTRILVTHGIHFLPQVDEIVVLGKG 787
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKV-ESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
590-802 |
9.69e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.80 E-value: 9.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 590 SEASFTWDRDLEATIQ---DVNLDIKPGQLVAVVGTVGSGKSSLISAM-----------------------LGEMENVHG 643
Cdd:PRK13651 6 KNIVKIFNKKLPTELKaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLnalllpdtgtiewifkdeknkkkTKEKEKVLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 644 HITIKGS--------------IAYVPQQAWIQ--NGTIKDNILFGS-------EYDEKKYQRVIEACALlpDLEMLPggd 700
Cdd:PRK13651 86 KLVIQKTrfkkikkikeirrrVGVVFQFAEYQlfEQTIEKDIIFGPvsmgvskEEAKKRAAKYIELVGL--DESYLQ--- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 701 maeigEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVDTHVGKHIFNKVVGPNglLSGKTRILVTHGI-HFLPQVD 779
Cdd:PRK13651 161 -----RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN--KQGKTIILVTHDLdNVLEWTK 233
|
250 260
....*....|....*....|....
gi 569006289 780 EIVVLGKGTILEKG-SYSDLMDKK 802
Cdd:PRK13651 234 RTIFFKDGKIIKDGdTYDILSDNK 257
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
604-799 |
1.05e-11 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 66.65 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEM-----ENVH------GHITI---KGSIAYV-P--QQAWIQNGTIK 666
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpptygNDVRlfgerrGGEDVwelRKRIGLVsPalQLRFPRDETVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 667 DNIL---FGS-----EYDEKKYQRVIEAcallpdLEMLpggDMAEIGEKGIN-LSGGQKHRVSLARATYQDADIYILDDP 737
Cdd:COG1119 99 DVVLsgfFDSiglyrEPTDEQRERAREL------LELL---GLAHLADRPFGtLSQGEQRRVLIARALVKDPELLILDEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006289 738 LSAVDTHvGKHIFNKVVGPNGLLSGKTRILVTHGIHFLPQ-VDEIVVLGKGTILEKGSYSDLM 799
Cdd:COG1119 170 TAGLDLG-ARELLLALLDKLAAEGAPTLVLVTHHVEEIPPgITHVLLLKDGRVVAAGPKEEVL 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1250-1473 |
1.06e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 67.06 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELD-LVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLT 1328
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1329 IIPQDPI-LFSG------------NLRMNLDPFNKYSDEeiwrALELAHLKSFVaglqlgllhevTEGGDNLSIGQRQLL 1395
Cdd:PRK13650 85 MVFQNPDnQFVGatveddvafgleNKGIPHEEMKERVNE----ALELVGMQDFK-----------EREPARLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1396 CLGRAVLRKSKILVLDEATAAVDLETD-SLIQT--TIRNEFsQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELL 1472
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRlELIKTikGIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELF 228
|
.
gi 569006289 1473 S 1473
Cdd:PRK13650 229 S 229
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
608-742 |
1.21e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.14 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 608 NLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG------SIAYVPQQAWIQNG------TIKDNILFG--- 672
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhtttPPSRRPVSMLFQENnlfshlTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006289 673 ----SEYDEKKYQRVIEACALLPDLEMLPGgdmaeigekgiNLSGGQKHRVSLARATYQDADIYILDDPLSAVD 742
Cdd:PRK10771 99 glklNAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
584-810 |
1.42e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 66.68 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 584 DKAVQFSEASFTWDRDLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGSIAYVPQQAWIQN- 662
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKA-LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 663 --------------GTIKDNILFG--------SEYDEkkyqRVIEACALLpdlemlpggDMAEIGEKG-INLSGGQKHRV 719
Cdd:PRK13647 81 vglvfqdpddqvfsSTVWDDVAFGpvnmgldkDEVER----RVEEALKAV---------RMWDFRDKPpYHLSYGQKKRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 720 SLARATYQDADIYILDDPLSAVDTHVGKHIFNKVVGPNGllSGKTRILVTHGIHFLPQ-VDEIVVLGKGTILEKGSYSDL 798
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHN--QGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLL 225
|
250
....*....|..
gi 569006289 799 MDKKGVFAKNWK 810
Cdd:PRK13647 226 TDEDIVEQAGLR 237
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
602-770 |
1.71e-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: 65.51 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 602 ATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG----------------SIAYVPQQA-WIQNGT 664
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgraipylrrKIGVVFQDFrLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 665 IKDNILFGSEYDEKKYQRVIEACALLPDLEMLPGG--DMAEigekgiNLSGGQKHRVSLARATYQDADIYILDDPLSAVD 742
Cdd:cd03292 95 VYENVAFALEVTGVPPREIRKRVPAALELVGLSHKhrALPA------ELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180
....*....|....*....|....*...
gi 569006289 743 THVGKHIFNKVVGPNglLSGKTRILVTH 770
Cdd:cd03292 169 PDTTWEIMNLLKKIN--KAGTTVVVATH 194
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
604-794 |
1.80e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 67.66 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-SIAYVPQQ-----------AWIQNGTIKDNILF 671
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqDITHVPAEnrhvntvfqsyALFPHMTVFENVAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 672 G--------SEYDEkkyqRVIEAcallpdLEMLPGGDMAEigEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVDT 743
Cdd:PRK09452 110 GlrmqktpaAEITP----RVMEA------LRMVQLEEFAQ--RKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDY 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569006289 744 HVGKHIFNKVVGPNGLLsGKTRILVTHGI-HFLPQVDEIVVLGKGTILEKGS 794
Cdd:PRK09452 178 KLRKQMQNELKALQRKL-GITFVFVTHDQeEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
598-803 |
1.91e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 64.86 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 598 RDLEATI------QDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEM--ENVHGHITIKGsiayvpqqawiqngtikDNI 669
Cdd:cd03217 4 KDLHVSVggkeilKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKG-----------------EDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 670 LFGSEYDEKK------YQRVIEacallpdlemLPGGDMAE-IGEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVD 742
Cdd:cd03217 67 TDLPPEERARlgiflaFQYPPE----------IPGVKNADfLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006289 743 THVGKHIFNKVvgpNGLLS-GKTRILVTHGIHFLPQV--DEIVVLGKGTILEKGSYS--DLMDKKG 803
Cdd:cd03217 137 IDALRLVAEVI---NKLREeGKSVLIITHYQRLLDYIkpDRVHVLYDGRIVKSGDKElaLEIEKKG 199
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1256-1474 |
2.38e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 67.75 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1256 QVRYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDL----RGRLTIIP 1331
Cdd:PRK10070 33 QILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1332 QDpilFSGNLRMNLDPFNKYSDEEIWRALELAHLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLD 1411
Cdd:PRK10070 113 QS---FALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMD 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1412 EATAAVdletDSLIQTTIRNEF------SQCTVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEELLSN 1474
Cdd:PRK10070 190 EAFSAL----DPLIRTEMQDELvklqakHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
604-799 |
3.22e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 67.17 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-------------SIAYVPQQAWIQ-NGTIKDNI 669
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASVPQDTSLSfEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 670 LFG-----------SEYDEKKYQRVIEAcallpdlemlpgGDMAEIGEKGI-NLSGGQKHRVSLARATYQDADIYILDDP 737
Cdd:PRK09536 99 EMGrtphrsrfdtwTETDRAAVERAMER------------TGVAQFADRPVtSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006289 738 LSAVDTHvgkHIFNKVVGPNGLL-SGKTRILVTHGIHFLPQ-VDEIVVLGKGTILEKGSYSDLM 799
Cdd:PRK09536 167 TASLDIN---HQVRTLELVRRLVdDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1250-1473 |
3.22e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 65.54 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTI 1329
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1330 IPQDPI-LFSGN---------LRMNLDPFNKYSdEEIWRALElahlksfvaglQLGLLHEVTEGGDNLSIGQRQLLCLGR 1399
Cdd:PRK13648 88 VFQNPDnQFVGSivkydvafgLENHAVPYDEMH-RRVSEALK-----------QVDMLERADYEPNALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006289 1400 AVLRKSKILVLDEATAAVDLETDSLIQTTIR--NEFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELLS 1473
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
606-799 |
3.30e-11 |
|
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: 66.66 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 606 DVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-----------------SIAYVPQQAwiq-ngTIKD 667
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargiflpphrrRIGYVFQEArlfphlSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 668 NILFG----------SEYDEkkyqrVIEACALLPDLEMLPGgdmaeigekgiNLSGGQKHRVSLARATYQDADIYILDDP 737
Cdd:COG4148 97 NLLYGrkrapraerrISFDE-----VVELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 738 LSAVDTHVGKHIfnkvvgpngL-----LSGKTRI---LVTHgihflpQVDEI-------VVLGKGTILEKGSYSDLM 799
Cdd:COG4148 161 LAALDLARKAEI---------LpylerLRDELDIpilYVSH------SLDEVarladhvVLLEQGRVVASGPLAEVL 222
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
654-807 |
3.77e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.13 E-value: 3.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 654 VPQQAWIQNGTIKDNILFGSEYDEKK-YQRVIEACALLPDLEMLPGGDMAEIGEKGINLSGGQKHRVSLARATYQDADIY 732
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGKEDATREdVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKIL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 733 ILDDPLSAVDTHVGKHIFNKVVGPNGlLSGKTRILVTHGIHFLPQVDEIVVLGK----GTILE-KGSYSDLMD-KKGVFA 806
Cdd:PTZ00265 1381 LLDEATSSLDSNSEKLIEKTIVDIKD-KADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSvQDGVYK 1459
|
.
gi 569006289 807 K 807
Cdd:PTZ00265 1460 K 1460
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
604-800 |
3.82e-11 |
|
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: 64.62 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS--------------IAYVPQqawiqnG------ 663
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarlgIGYVPE------Grrifps 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 664 -TIKDNILFGSEY--DEKKYQRVIE-ACALLPDL-EML--PGGdmaeigekgiNLSGGQKHRVSLARATYQDADIYILDD 736
Cdd:COG0410 93 lTVEENLLLGAYArrDRAEVRADLErVYELFPRLkERRrqRAG----------TLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569006289 737 P---LSAVdthVGKHIFNKVVGPNGllSGKTRILVTHGIHFLPQV-DEIVVLGKGTILEKGSYSDLMD 800
Cdd:COG0410 163 PslgLAPL---IVEEIFEIIRRLNR--EGVTILLVEQNARFALEIaDRAYVLERGRIVLEGTAAELLA 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1245-1488 |
4.40e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 65.59 E-value: 4.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1245 PKKGEIQFNNYQVRYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSS---LTNCLFRILESAGGQIIIDGIDIASIGLH 1321
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1322 DLRGRLTIIPQDPI-LFSGNLRMNLDPFNKYSdeeiwRALELAHLKSFVAGL--QLGLLHEVTEGGDNLSIGQRQLLCLG 1398
Cdd:PRK13640 81 DIREKVGIVFQNPDnQFVGATVGDDVAFGLEN-----RAVPRPEMIKIVRDVlaDVGMLDYIDSEPANLSGGQKQRVAIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1399 RAVLRKSKILVLDEATAAVDLETDSLIQTTIRN--EFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELLSNMg 1476
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKlkKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV- 234
|
250
....*....|..
gi 569006289 1477 pfyLMAKEAGIE 1488
Cdd:PRK13640 235 ---EMLKEIGLD 243
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
605-784 |
5.26e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.97 E-value: 5.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 605 QDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGemenVH----GHITIKGS--------------IAYVPQQ-AWIQNGTI 665
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSG----VYqpdsGEILLDGEpvrfrsprdaqaagIAIIHQElNLVPNLSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 666 KDNILFGSEY------DEKK-YQRVIEACALLpDLEMLPGgdmAEIGEkginLSGGQKHRVSLARATYQDADIYILDDP- 737
Cdd:COG1129 97 AENIFLGREPrrggliDWRAmRRRARELLARL-GLDIDPD---TPVGD----LSVAQQQLVEIARALSRDARVLILDEPt 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 569006289 738 --LSAVDThvgKHIFnKVVgpngllsgktRILVTHGI------HFLPQV----DEIVVL 784
Cdd:COG1129 169 asLTEREV---ERLF-RII----------RRLKAQGVaiiyisHRLDEVfeiaDRVTVL 213
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
604-794 |
5.46e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 65.01 E-value: 5.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG----------------SIAYVPQQAWIQNGTIKD 667
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfsklqgirklvGIVFQNPETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 668 NILFGSEydekkyqrviEACalLPDLEMLPGGDMAeIGEKGI---------NLSGGQKHRVSLARATYQDADIYILDDPL 738
Cdd:PRK13644 98 DLAFGPE----------NLC--LPPIEIRKRVDRA-LAEIGLekyrhrspkTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 569006289 739 SAVDTHVGKHIFNKVVGPNGllSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGS 794
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHE--KGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
607-805 |
7.11e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.50 E-value: 7.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 607 VNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-------------SIAYVPQQAWIQNGTIKDNILFGS 673
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGreigayglrelrrQFSMIPQDPVLFDGTVRQNVDPFL 1408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 674 EYDEKKYQRVIEACALLPDLEMLPGGDMAEIGEKGINLSGGQKHRVSLARATYQDADIYILDDPLSA-VDTHVGKHIFNK 752
Cdd:PTZ00243 1409 EASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILMDEATAnIDPALDRQIQAT 1488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 569006289 753 VVGPnglLSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGSYSDL-MDKKGVF 805
Cdd:PTZ00243 1489 VMSA---FSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIF 1539
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1250-1473 |
7.74e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 64.73 E-value: 7.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELDL-VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLT 1328
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1329 IIPQDP------ILFSGNLRMNLDPFNKYSDEEIWRALElahlksfvAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVL 1402
Cdd:PRK13642 85 MVFQNPdnqfvgATVEDDVAFGMENQGIPREEMIKRVDE--------ALLAVNMLDFKTREPARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006289 1403 RKSKILVLDEATAAVDLETDSLIQTTIR--NEFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELLS 1473
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHeiKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1267-1474 |
8.14e-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: 66.63 E-value: 8.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1267 LKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAggqiiidgidiASIGLHD-------------LRGRLTIIPQD 1333
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-----------GEIRFDGqdldglsrralrpLRRRMQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1334 PilFSG-NLRMN-----------LDPfnKYSDEE----IWRALElahlksfvaglQLGLL--------HEvteggdnLSI 1389
Cdd:COG4172 371 P--FGSlSPRMTvgqiiaeglrvHGP--GLSAAErrarVAEALE-----------EVGLDpaarhrypHE-------FSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1390 GQRQLLCLGRAVLRKSKILVLDEATAAVDLetdsliqtTIrnefsQCTVIT---------------IAHRLHTI--MdSD 1452
Cdd:COG4172 429 GQRQRIAIARALILEPKLLVLDEPTSALDV--------SV-----QAQILDllrdlqrehglaylfISHDLAVVraL-AH 494
|
250 260
....*....|....*....|..
gi 569006289 1453 KIMVLDSGKIVEYGSPEELLSN 1474
Cdd:COG4172 495 RVMVMKDGKVVEQGPTEQVFDA 516
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1250-1430 |
9.00e-11 |
|
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: 62.88 E-value: 9.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELdlVLKGITCNIKSTEKVGVVGRTGAGKSSLtnclFRI---LESAGGQIIIDGIDIASIGLHDLRGR 1326
Cdd:COG4133 3 LEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTL----LRIlagLLPPSAGEVLWNGEPIRDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1327 LTIIPQDPILFSG-----NLRM--NLDPFnKYSDEEIWRALElahlksfvaglQLGLLHEVTEGGDNLSIGQRQLLCLGR 1399
Cdd:COG4133 77 LAYLGHADGLKPEltvreNLRFwaALYGL-RADREAIDEALE-----------AVGLAGLADLPVRQLSAGQKRRVALAR 144
|
170 180 190
....*....|....*....|....*....|.
gi 569006289 1400 AVLRKSKILVLDEATAAVDLETDSLIQTTIR 1430
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAAGVALLAELIA 175
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
593-799 |
1.00e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 64.09 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 593 SFTWDRDLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG----------------------S 650
Cdd:COG4167 19 GLFRRQQFEA-VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhkleygdykyrckhirmifqdpN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 651 IAYVPQQawiQNGTIKDNIL-FGSEYDEKK-YQRVIEAcalLPDLEMLPggDMAEIGekgIN-LSGGQKHRVSLARATYQ 727
Cdd:COG4167 98 TSLNPRL---NIGQILEEPLrLNTDLTAEErEERIFAT---LRLVGLLP--EHANFY---PHmLSSGQKQRVALARALIL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 728 DADIYILDDPLSAVDTHVGKHIFNKvvgpngLLS-----GKTRILVTH--GI--HFlpqVDEIVVLGKGTILEKGSYSDL 798
Cdd:COG4167 167 QPKIIIADEALAALDMSVRSQIINL------MLElqeklGISYIYVSQhlGIvkHI---SDKVLVMHQGEVVEYGKTAEV 237
|
.
gi 569006289 799 M 799
Cdd:COG4167 238 F 238
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1250-1464 |
1.12e-10 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 63.15 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELDlVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILEsaggqiiidgidiASIG---------- 1319
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEER-------------PTSGqvlvngqdls 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1320 ------LHDLRGRLTIIPQDPILFSG-----NLRMNLDpFNKYSDEEIWRALELAhLKsfvaglQLGLLHEVTEGGDNLS 1388
Cdd:COG2884 68 rlkrreIPYLRRRIGVVFQDFRLLPDrtvyeNVALPLR-VTGKSRKEIRRRVREV-LD------LVGLSDKAKALPHELS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1389 IGQRQLLCLGRAVLRKSKILVLDEATAAVDLET-DSLIQttIRNEFSQ--CTVItIA-HRLHtIMDS--DKIMVLDSGKI 1462
Cdd:COG2884 140 GGEQQRVAIARALVNRPELLLADEPTGNLDPETsWEIME--LLEEINRrgTTVL-IAtHDLE-LVDRmpKRVLELEDGRL 215
|
..
gi 569006289 1463 VE 1464
Cdd:COG2884 216 VR 217
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
258-751 |
1.25e-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: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 258 SWLVKALFKTFYVvilKSFILKLAHDILLF-----------LNPQLLKFLIGfvKDPDSYPWVGYIYAILMFSVTLIQSF 326
Cdd:TIGR00954 80 DFLLKILIPRVFC---KETGLLILIAFLLVsrtylsvyvatLDGQIESSIVR--RSPRNFAWILFKWFLIAPPASFINSA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 327 --FLQCYFQFCFvlgmTVR-TTIIASVYKKALTLSNLARRQYTIGETVNLMSVDSQKLMDvtNYIHL---LWSSVLQIAL 400
Cdd:TIGR00954 155 ikYLLKELKLRF----RVRlTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCD--SVVELysnLTKPILDVIL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 401 SIFFLWRELGPSilaGVGLMVLLVPVNGVLATKIR----KIQVQNMKNK-DKRLKIMNEILSGIKILKYFAWEPSfKEQV 475
Cdd:TIGR00954 229 YSFKLLTALGSV---GPAGLFAYLFATGVVLTKLRppigKLTVEEQALEgEYRYVHSRLIMNSEEIAFYQGNKVE-KETV 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 476 NSIrkkeLRNLLRFSQLQTILIFILHLTPTLVSVITFSV--YVLVDSQNVLNAEKAFTSITL------FNILRFPLAMLP 547
Cdd:TIGR00954 305 MSS----FYRLVEHLNLIIKFRFSYGFLDNIVAKYTWSAvgLVAVSIPIFDKTHPAFLEMSEeelmqeFYNNGRLLLKAA 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 548 MVISSVIQASVSVDRLEQYLGSDD--LDLSAIRHVCHFDK-AVQFSEASFTWDRDL------------------------ 600
Cdd:TIGR00954 381 DALGRLMLAGRDMTRLAGFTARVDtlLQVLDDVKSGNFKRpRVEEIESGREGGRNSnlvpgrgiveyqdngikfeniplv 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 601 ----EATIQDVNLDIKPGQLVAVVGTVGSGKSSLISaMLGEMENVHG---HITIKGSIAYVPQQAWIQNGTIKDNILFGS 673
Cdd:TIGR00954 461 tpngDVLIESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIYPD 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 674 EYDEKKYQRVIEAcallpDLE-MLPGGDMAEIGEKGIN----------LSGGQKHRVSLARATYQDADIYILDDPLSAVD 742
Cdd:TIGR00954 540 SSEDMKRRGLSDK-----DLEqILDNVQLTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614
|
....*....
gi 569006289 743 THVGKHIFN 751
Cdd:TIGR00954 615 VDVEGYMYR 623
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
604-737 |
1.29e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.81 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS--------------IAYVP----QQAWIQNGTI 665
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVPedrkGEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 666 KDNILFGS--EY------DEKKYQRVIEacALLPDLEMLPGGDMAEIGekgiNLSGG--QKhrVSLARATYQDADIYILD 735
Cdd:COG1129 348 RENITLASldRLsrggllDRRRERALAE--EYIKRLRIKTPSPEQPVG----NLSGGnqQK--VVLAKWLATDPKVLILD 419
|
..
gi 569006289 736 DP 737
Cdd:COG1129 420 EP 421
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1266-1462 |
1.50e-10 |
|
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: 62.51 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCL----------FRILEsaggqiiIDGIDIASIGLHDLRGR-LTIIPQDP 1334
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILggldrptsgeVRVDG-------TDISKLSEKELAAFRRRhIGFVFQSF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1335 ILFSG-----NLRMNLDPFNKYSDEEIWRALELAHlksfvaglQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILV 1409
Cdd:cd03255 92 NLLPDltaleNVELPLLLAGVPKKERRERAEELLE--------RVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 569006289 1410 LDEATAAVDLETDSLIQTTIR--NEFSQCTVITIAHRLHTIMDSDKIMVLDSGKI 1462
Cdd:cd03255 164 ADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
596-791 |
1.60e-10 |
|
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: 62.84 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 596 WDRDLEATI-QDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-----------------SIAYVpQQ 657
Cdd:COG4181 19 GTGAGELTIlKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGqdlfaldedararlrarHVGFV-FQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 658 AW--IQNGTIKDNI-----LFGSEYDEKKYQRVIEACALLPDLEMLPGGdmaeigekginLSGGQKHRVSLARATYQDAD 730
Cdd:COG4181 98 SFqlLPTLTALENVmlpleLAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 731 IYILDDPLSAVDTHVGKHIFnkvvgpnGLL------SGKTRILVTHGIHFLPQVDEIVVLGKGTILE 791
Cdd:COG4181 167 ILFADEPTGNLDAATGEQII-------DLLfelnreRGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
603-770 |
1.80e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 63.26 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 603 TIQDVNLDIKPGQLVAVVGTVGSGKSSLISAmLGEMENVHGHITIKGSIAY---------------------VPQQAWIQ 661
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRS-INRMNDLNPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 662 NGTIKDNILFG----SEYDEKKYQRVIEacallpdlEMLPGGDMAE-----IGEKGINLSGGQKHRVSLARATYQDADIY 732
Cdd:PRK14239 99 PMSIYENVVYGlrlkGIKDKQVLDEAVE--------KSLKGASIWDevkdrLHDSALGLSGGQQQRVCIARVLATSPKII 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 569006289 733 ILDDPLSAVDTHVGKHIFNKVVgpnGLLSGKTRILVTH 770
Cdd:PRK14239 171 LLDEPTSALDPISAGKIEETLL---GLKDDYTMLLVTR 205
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1267-1473 |
2.12e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 63.33 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1267 LKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILE--SAGGQIIIDGIDIASIGLHDLRGRLTIIPQDP--ILFSGNLR 1342
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKpsSGRILFDGKPIDYSRKGLMKLRESVGMVFQDPdnQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1343 MNLD--PFN-KYSDEEIWRALELAHLKSFVAGLQlgllHEVTEGgdnLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDL 1419
Cdd:PRK13636 102 QDVSfgAVNlKLPEDEVRKRVDNALKRTGIEHLK----DKPTHC---LSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 1420 ETDSLIQTTIRNEFSQ--CTVITIAHRLHTI-MDSDKIMVLDSGKIVEYGSPEELLS 1473
Cdd:PRK13636 175 MGVSEIMKLLVEMQKElgLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
608-742 |
2.17e-10 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 62.46 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 608 NLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-SIAYVP----------QQawiQN----GTIKDNILFG 672
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqDLTALPpaerpvsmlfQE---NNlfphLTVAQNIGLG 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 673 SE----YDEKKYQRVIEACAL--LPDLEM-LPGgdmaeigekgiNLSGGQKHRVSLARATYQDADIYILDDPLSAVD 742
Cdd:COG3840 96 LRpglkLTAEQRAQVEQALERvgLAGLLDrLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1266-1475 |
2.92e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 64.65 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFrilesaggqiiidgidiasiGLHD-------LRGR------------ 1326
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILS--------------------GVYQpdsgeilLDGEpvrfrsprdaqa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1327 --LTIIPQDPILFSG-----NLRMNLDPFNKYS-DeeiWRALE---LAHLKSFvaGLQLGLLHEVteggDNLSIGQRQLL 1395
Cdd:COG1129 79 agIAIIHQELNLVPNlsvaeNIFLGREPRRGGLiD---WRAMRrraRELLARL--GLDIDPDTPV----GDLSVAQQQLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1396 CLGRAVLRKSKILVLDEATAAVDL-ETDSLIQtTIRNEFSQ-CTVITIAHRLHTIMD-SDKIMVLDSGKIVEYG-----S 1467
Cdd:COG1129 150 EIARALSRDARVLILDEPTASLTErEVERLFR-IIRRLKAQgVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGpvaelT 228
|
....*...
gi 569006289 1468 PEELLSNM 1475
Cdd:COG1129 229 EDELVRLM 236
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
606-793 |
3.01e-10 |
|
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: 61.74 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 606 DVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-SIAYVPQQAWIQNGTIKDNILFGSEYDEkkyQRVi 684
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvDVTAAPPADRPVSMLFQENNLFAHLTVE---QNV- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 685 eACALLPDLEMLP------GGDMAEIGEKGI------NLSGGQKHRVSLARATYQDADIYILDDPLSAVDTHVgKHIFNK 752
Cdd:cd03298 92 -GLGLSPGLKLTAedrqaiEVALARVGLAGLekrlpgELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL-RAEMLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 569006289 753 VVGPNGLLSGKTRILVTHgihflpQVDEI-------VVLGKGTILEKG 793
Cdd:cd03298 170 LVLDLHAETKMTVLMVTH------QPEDAkrlaqrvVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1250-1480 |
3.50e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 62.70 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYrPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIG-LHDLRGRLT 1328
Cdd:PRK13644 2 IRLENVSYSY-PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1329 IIPQDP-----------ILFSGNLRMNLDPFnkysdeEIWRALELAHLksfvaglQLGLLHEVTEGGDNLSIGQRQLLCL 1397
Cdd:PRK13644 81 IVFQNPetqfvgrtveeDLAFGPENLCLPPI------EIRKRVDRALA-------EIGLEKYRHRSPKTLSGGQGQCVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1398 GRAVLRKSKILVLDEATAAVDLETDSLIQTTIRNEFSQC-TVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELLSNMG 1476
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
....
gi 569006289 1477 PFYL 1480
Cdd:PRK13644 228 LQTL 231
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
604-787 |
3.66e-10 |
|
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: 61.53 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS---------IAYVPQQAWI-QNGTIKDNIL-FG 672
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarnrIGYLPEERGLyPKMKVIDQLVyLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 673 SEYDEKKYQRVIEACALLPDLEMlpgGDMAEigEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVDThVGKHIFNK 752
Cdd:cd03269 96 QLKGLKKEEARRRIDEWLERLEL---SEYAN--KRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVELLKD 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 569006289 753 VVgpNGLL-SGKTRILVTHGIHFLPQV-DEIVVLGKG 787
Cdd:cd03269 170 VI--RELArAGKTVILSTHQMELVEELcDRVLLLNKG 204
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
604-743 |
3.90e-10 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 60.25 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITI--KGSIAYVPQQAWIQNGTIKDNILFgseydekkyq 681
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpeGEDLLFLPQRPYLPLGTLREQLIY---------- 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006289 682 rvieacallpdlemlPGGDMaeigekginLSGGQKHRVSLARATYQDADIYILDDPLSAVDT 743
Cdd:cd03223 87 ---------------PWDDV---------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1252-1473 |
4.00e-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: 62.57 E-value: 4.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1252 FNNYQVRYRPeldlVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILEsaggqiiidgidiASIGLHDLRGRLTIIP 1331
Cdd:cd03291 42 FSNLCLVGAP----VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELE-------------PSEGKIKHSGRISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1332 QDPILFSGNLRMNLdPFNKYSDEEIWRALELA-HLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVL 1410
Cdd:cd03291 105 QFSWIMPGTIKENI-IFGVSYDEYRYKSVVKAcQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569006289 1411 DEATAAVDLETDSLIqttirneFSQC--------TVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELLS 1473
Cdd:cd03291 184 DSPFGYLDVFTEKEI-------FESCvcklmankTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQS 247
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
593-794 |
4.59e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 62.40 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 593 SFTWDRDLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS-IAY-------VPQQAWI--QN 662
Cdd:PRK13639 8 KYSYPDGTEA-LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpIKYdkkslleVRKTVGIvfQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 663 G-------TIKDNILFG------SEYDEKKyqRVIEAcallpdlemlpggdMAEIGEKGI------NLSGGQKHRVSLAR 723
Cdd:PRK13639 87 PddqlfapTVEEDVAFGplnlglSKEEVEK--RVKEA--------------LKAVGMEGFenkpphHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006289 724 ATYQDADIYILDDPLSAVDTHVGKHIFNKVVGPNGllSGKTRILVTHGIHFLP-QVDEIVVLGKGTILEKGS 794
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNK--EGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGT 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1246-1474 |
4.75e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 61.99 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1246 KKGEIQFNNYQVRYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILE------SAGGQIIIDGIDIASIG 1319
Cdd:PRK14246 5 KSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1320 LHDLRGRLTIIPQDPILFS-----GNLRMNLDPFNKYSDEEIWRALELAHLKsfvAGLQLGLLHEVTEGGDNLSIGQRQL 1394
Cdd:PRK14246 85 AIKLRKEVGMVFQQPNPFPhlsiyDNIAYPLKSHGIKEKREIKKIVEECLRK---VGLWKEVYDRLNSPASQLSGGQQQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1395 LCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEELLS 1473
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFT 241
|
.
gi 569006289 1474 N 1474
Cdd:PRK14246 242 S 242
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1266-1474 |
6.47e-10 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 61.02 E-value: 6.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLF--------RILesaggqiiidgidiasIGLHDL-------RGRLTII 1330
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVglvkpdsgKIL----------------LDGQDItklpmhkRARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1331 --PQDPILFSG-----NLRMNLDPFNKYSDEEIWRALELAHLksfvaglqLGLLHEVTEGGDNLSIGQRQLLCLGRAVLR 1403
Cdd:cd03218 79 ylPQEASIFRKltveeNILAVLEIRGLSKKEREEKLEELLEE--------FHITHLRKSKASSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006289 1404 KSKILVLDEATAAVDLETDSLIQTTIRN--EFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELLSN 1474
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIAVQDIQKIIKIlkDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1386-1475 |
6.99e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.51 E-value: 6.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1386 NLSIGQRQLLCLGRAVLRKSKILVLDEATaAV--DLETDSLIQtTIRNEFSQ-CTVITIAHRLHTIMD-SDKIMVLDSGK 1461
Cdd:COG3845 141 DLSVGEQQRVEILKALYRGARILILDEPT-AVltPQEADELFE-ILRRLAAEgKSIIFITHKLREVMAiADRVTVLRRGK 218
|
90
....*....|....*...
gi 569006289 1462 IVEYGSPEEL----LSNM 1475
Cdd:COG3845 219 VVGTVDTAETseeeLAEL 236
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
604-800 |
7.32e-10 |
|
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: 61.99 E-value: 7.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLG---EMENVHGHITIKGS-----------------IAYVPQQA----- 658
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEdllklsekelrkirgreIQMIFQDPmtsln 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 659 --WiqngTIKDNI-----LFGSEYDEKKYQRVIEAcallpdLEMLpggdmaeigekGIN------------LSGGQKHRV 719
Cdd:COG0444 101 pvM----TVGDQIaeplrIHGGLSKAEARERAIEL------LERV-----------GLPdperrldrypheLSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 720 SLARATYQDADIYILDDPLSAVDTHVGKHIFNkvvgpngLLS------GKTRILVTHGIHFLPQV-DEIVVLGKGTILEK 792
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILN-------LLKdlqrelGLAILFITHDLGVVAEIaDRVAVMYAGRIVEE 232
|
....*...
gi 569006289 793 GSYSDLMD 800
Cdd:COG0444 233 GPVEELFE 240
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
606-793 |
7.73e-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: 60.28 E-value: 7.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 606 DVNLDIKPGqLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS------------IAYVPQQ-AWIQNGTIKD----- 667
Cdd:cd03264 18 GVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrIGYLPQEfGVYPNFTVREfldyi 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 668 NILFGSEyDEKKYQRVIEACALLpdlemlpggDMAEIGEKGIN-LSGGQKHRVSLARATYQDADIYILDDPLSAVDThVG 746
Cdd:cd03264 97 AWLKGIP-SKEVKARVDEVLELV---------NLGDRAKKKIGsLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP-EE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 569006289 747 KHIFNKVVGpnGLLSGKTRILVTH---GIHFLpqVDEIVVLGKGTILEKG 793
Cdd:cd03264 166 RIRFRNLLS--ELGEDRIVILSTHiveDVESL--CNQVAVLNKGKLVFEG 211
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1266-1466 |
8.29e-10 |
|
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: 59.87 E-value: 8.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIaSIGLHDLRGRLTIIPQDPILFsGNLrmnl 1345
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGR-PLDKRSFRKIIGYVPQDDILH-PTL---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1346 dpfnkysdeEIWRALElahlksFVAGLQlgllhevteggdNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLI 1425
Cdd:cd03213 98 ---------TVRETLM------FAAKLR------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 569006289 1426 QTTIRNEFSQ-CTVITIAHRLHTIMDS--DKIMVLDSGKIVEYG 1466
Cdd:cd03213 151 MSLLRRLADTgRTIICSIHQPSSEIFElfDKLLLLSQGRVIYFG 194
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
593-794 |
9.00e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 61.18 E-value: 9.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 593 SFTWDRDLEAtiqdVNLDIKPGQLVAVVGTVGSGKSSLI---SAMLGEMENVHGHITIKGSI------------------ 651
Cdd:PRK09984 13 TFNQHQALHA----VDLNIHHGEMVALLGPSGSGKSTLLrhlSGLITGDKSAGSHIELLGRTvqregrlardirksrant 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 652 AYVPQQAWIQNG-TIKDNILFG------------SEYDEKKYQRVIEAcallpdlemLPGGDMAEIGEKGIN-LSGGQKH 717
Cdd:PRK09984 89 GYIFQQFNLVNRlSVLENVLIGalgstpfwrtcfSWFTREQKQRALQA---------LTRVGMVHFAHQRVStLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569006289 718 RVSLARATYQDADIYILDDPLSAVDTHVGKHIFNKVVGPNGlLSGKTRILVTHGIHF-LPQVDEIVVLGKGTILEKGS 794
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQ-NDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGS 236
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1387-1495 |
9.57e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 61.26 E-value: 9.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1387 LSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIR--NEFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVE 1464
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKelNKKYGITIILITHYMEEAVEADRIIVMDSGKVVM 224
|
90 100 110
....*....|....*....|....*....|.
gi 569006289 1465 YGSPEELLSNMGpfylMAKEAGIESVNHTEL 1495
Cdd:PRK13633 225 EGTPKEIFKEVE----MMKKIGLDVPQVTEL 251
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
604-800 |
1.01e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 60.49 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAM--LGEMEN----VHGhITIKGSIA----------YVPQQAWI-QNGTIK 666
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITSgdliVDG-LKVNDPKVderlirqeagMVFQQFYLfPHLTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 667 DNILFGSEYDEKKYQRVIEACALlpdlEMLPGGDMAE-IGEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVDTHV 745
Cdd:PRK09493 96 ENVMFGPLRVRGASKEEAEKQAR----ELLAKVGLAErAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 746 gKHIFNKVVgpNGLLS-GKTRILVTHGIHFLPQV-DEIVVLGKGTILEKGSYSDLMD 800
Cdd:PRK09493 172 -RHEVLKVM--QDLAEeGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIK 225
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
593-742 |
1.09e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 61.29 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 593 SFTWDRDLEA-TIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGSiAYVPQQAW---------IQN 662
Cdd:PRK13650 11 TFKYKEDQEKyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-LLTEENVWdirhkigmvFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 663 -------GTIKDNILFGSE-----YDEKKyQRVIEACALLpdlemlpggDMAEIGEKG-INLSGGQKHRVSLARATYQDA 729
Cdd:PRK13650 90 pdnqfvgATVEDDVAFGLEnkgipHEEMK-ERVNEALELV---------GMQDFKEREpARLSGGQKQRVAIAGAVAMRP 159
|
170
....*....|...
gi 569006289 730 DIYILDDPLSAVD 742
Cdd:PRK13650 160 KIIILDEATSMLD 172
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
604-801 |
1.10e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 61.79 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIK----------GSIAYVPQQAWIQN----------- 662
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkknnHELITNPYSKKIKNfkelrrrvsmv 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 663 ----------GTIKDNILFG------SEYDEKKYQRVIeacallpdLEMLpGGDMAEIGEKGINLSGGQKHRVSLARATY 726
Cdd:PRK13631 122 fqfpeyqlfkDTIEKDIMFGpvalgvKKSEAKKLAKFY--------LNKM-GLDDSYLERSPFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 727 QDADIYILDDPLSAVDTHvGKHIFNKVVgPNGLLSGKTRILVTHGI-HFLPQVDEIVVLGKGTILEKGS-YSDLMDK 801
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPK-GEHEMMQLI-LDAKANNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGTpYEIFTDQ 267
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
604-799 |
1.14e-09 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 60.53 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-SIAYVPQQAWIQNG--------------TIKDN 668
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeDITGLPPHEIARLGigrtfqiprlfpelTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 669 IL---------------FGSEYDE--KKYQRVIEACALLPDLEMLPGgdmaeigekgiNLSGGQKHRVSLARATYQDADI 731
Cdd:cd03219 96 VMvaaqartgsglllarARREEREarERAEELLERVGLADLADRPAG-----------ELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006289 732 YILDDP---LSAVDTHVGKHIFNKVVGpngllSGKTRILVTHGIHFLPQV-DEIVVLGKGTILEKGSYSDLM 799
Cdd:cd03219 165 LLLDEPaagLNPEETEELAELIRELRE-----RGITVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDEVR 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
587-801 |
1.21e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 61.29 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 587 VQFSEASFTWDRD---LEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIK--------------- 648
Cdd:PRK13643 2 IKFEKVNYTYQPNspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGdivvsstskqkeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 649 -----GSIAYVPQQAWIQNGTIKDnILFGSEYDEKKYQRVIEACAllPDLEMLpgGDMAEIGEKG-INLSGGQKHRVSLA 722
Cdd:PRK13643 82 vrkkvGVVFQFPESQLFEETVLKD-VAFGPQNFGIPKEKAEKIAA--EKLEMV--GLADEFWEKSpFELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 723 RATYQDADIYILDDPLSAVDTHVGKHIFNKVVGPNGllSGKTRILVTHGIHFLPQ-VDEIVVLGKGTILEKGSYSDLMDK 801
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQ--SGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1266-1474 |
1.22e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.88 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLH------DLRGRLTIIPQDPILFSG 1339
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFnyrdvlEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1340 NLRMNLDP---FNKYSDEEIWRALELAHLKSfvAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAA 1416
Cdd:PRK14271 116 SIMDNVLAgvrAHKLVPRKEFRGVAQARLTE--VGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 569006289 1417 VDLETDSLIQTTIRNEFSQCTVITIAHRL-HTIMDSDKIMVLDSGKIVEYGSPEELLSN 1474
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1269-1475 |
1.30e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 62.51 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1269 GITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDG----IDIASIGLhDLRGRLT----IIPQDPILFSGn 1340
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVgdewVDMTKPGP-DGRGRAKryigILHQEYDLYPH- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1341 lRMNLDPFNKYSDEEIwrALELAHLKSFVAGLQLGLLHEVTEG-----GDNLSIGQRQLLCLGRAVLRKSKILVLDEATA 1415
Cdd:TIGR03269 380 -RTVLDNLTEAIGLEL--PDELARMKAVITLKMVGFDEEKAEEildkyPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006289 1416 AVDLETDSLIQTTI---RNEFSQcTVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEELLSNM 1475
Cdd:TIGR03269 457 TMDPITKVDVTHSIlkaREEMEQ-TFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEEL 519
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
582-800 |
1.32e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 61.97 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 582 HFDKAVQFSEASFTWDRDLEAT-----IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGsiayvpq 656
Cdd:PRK10070 17 HPQRAFKYIEQGLSKEQILEKTglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 657 qawIQNGTIKDNILfgSEYDEKKYQRVIEACALLPDLEML---------PGGDMAEIGEKGIN----------------- 710
Cdd:PRK10070 90 ---VDIAKISDAEL--REVRRKKIAMVFQSFALMPHMTVLdntafgmelAGINAEERREKALDalrqvglenyahsypde 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 711 LSGGQKHRVSLARATYQDADIYILDDPLSAVDTHVGKHIFNKVVGPNGlLSGKTRILVTHGIHFLPQV-DEIVVLGKGTI 789
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQA-KHQRTIVFISHDLDEAMRIgDRIAIMQNGEV 243
|
250
....*....|.
gi 569006289 790 LEKGSYSDLMD 800
Cdd:PRK10070 244 VQVGTPDEILN 254
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1250-1474 |
1.36e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 61.63 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELDLV--LKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRiLESaggqiiidgidiASIG-------- 1319
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL-LER------------PTSGsvlvdgvd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1320 --------LHDLRGRLTIIPQDPILFS-----GN----LRMnldpfNKYSDEEIW-RALELahlksfvagLQL-GLLHEV 1380
Cdd:COG1135 69 ltalsereLRAARRKIGMIFQHFNLLSsrtvaENvalpLEI-----AGVPKAEIRkRVAEL---------LELvGLSDKA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1381 TEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLE-TDS---LIQtTIRNEFsQCTVITIAHRLHTIMD-SDKIM 1455
Cdd:COG1135 135 DAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPEtTRSildLLK-DINREL-GLTIVLITHEMDVVRRiCDRVA 212
|
250
....*....|....*....
gi 569006289 1456 VLDSGKIVEYGSPEELLSN 1474
Cdd:COG1135 213 VLENGRIVEQGPVLDVFAN 231
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1267-1474 |
1.76e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 60.83 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1267 LKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIA--SIGLHDLRGRLTIIPQDP---------- 1334
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQYPeyqlfeetie 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1335 --ILFsGNLRMNLdpfnkySDEEI----WRALELahlksfvaglqLGLLHEVTEGGD--NLSIGQRQLLCLGRAVLRKSK 1406
Cdd:PRK13637 103 kdIAF-GPINLGL------SEEEIenrvKRAMNI-----------VGLDYEDYKDKSpfELSGGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569006289 1407 ILVLDEATAAVDLETDSLIQTTIRN--EFSQCTVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEELLSN 1474
Cdd:PRK13637 165 ILILDEPTAGLDPKGRDEILNKIKElhKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVFKE 235
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
605-793 |
2.65e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 60.81 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 605 QDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITI-----------KGSIAYVPQQ-AWIQNGTIKDNILFG 672
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIgekrmndvppaERGVGMVFQSyALYPHLSVAENMSFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 673 ---SEYDEKKYQRVIEACAllpdlEMLPGGDMAEIGEKGinLSGGQKHRVSLARATYQDADIYILDDPLSAVD------- 742
Cdd:PRK11000 100 lklAGAKKEEINQRVNQVA-----EVLQLAHLLDRKPKA--LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvqm 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 569006289 743 ----THVGKHIfnkvvgpngllsGKTRILVTHG-IHFLPQVDEIVVLGKGTILEKG 793
Cdd:PRK11000 173 rieiSRLHKRL------------GRTMIYVTHDqVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1266-1474 |
2.84e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 59.54 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILE-----SAGGQIIIDGIDIASIGLHDLRGRLTIIPQ--DPI--- 1335
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQipNPIpnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1336 -LFSG---NLRMN-LDPFNKYSDEEIWRALELAHLKSFVAglqlgllHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVL 1410
Cdd:PRK14247 98 sIFENvalGLKLNrLVKSKKELQERVRWALEKAQLWDEVK-------DRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1411 DEATAAVDLETDSLIQTTIRNEFSQCTVITIAH------RLhtimdSDKIMVLDSGKIVEYGSPEELLSN 1474
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
604-742 |
3.06e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 59.31 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHI--------TIKGSIAYVPQQA----WiqnGTIKDNILF 671
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELlagtaplaEAREDTRLMFQDArllpW---KKVIDNVGL 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006289 672 GSEYD-EKKYQRVIEACALlpdlemlpgGDMAeiGEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVD 742
Cdd:PRK11247 105 GLKGQwRDAALQALAAVGL---------ADRA--NEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
607-800 |
3.18e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.22 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 607 VNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS--------------IAYVPQQAWI-QNGTIKDNILF 671
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLfPNLSVKENILF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 672 GSEYDEKKYQRVIEACALLP---DLEMLPGgdMAEIGEKGInlsggqkhrVSLARATYQDADIYILDDPLSAVDTHVGKH 748
Cdd:PRK15439 110 GLPKRQASMQKMKQLLAALGcqlDLDSSAG--SLEVADRQI---------VEILRGLMRDSRILILDEPTASLTPAETER 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 569006289 749 IFNKVvgpNGLLS-GKTRILVTHGIHFLPQV-DEIVVLGKGTILEKGSYSDLMD 800
Cdd:PRK15439 179 LFSRI---RELLAqGVGIVFISHKLPEIRQLaDRISVMRDGTIALSGKTADLST 229
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1263-1486 |
3.71e-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: 60.50 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1263 LDLVLKGITcnikstekvGVVGRTGAGKSSLTNCLfrilesaggqiiidgidiAsiGL-HDLRGRLTI------------ 1329
Cdd:COG4148 20 FTLPGRGVT---------ALFGPSGSGKTTLLRAI------------------A--GLeRPDSGRIRLggevlqdsargi 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1330 -IP----------QDPILFS-----GNLRmnldpfnkYSdeeIWRALELAHLKSF--VAGLqLGLLHEVTEGGDNLSIGQ 1391
Cdd:COG4148 71 fLPphrrrigyvfQEARLFPhlsvrGNLL--------YG---RKRAPRAERRISFdeVVEL-LGIGHLLDRRPATLSGGE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1392 RQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQ---TTIRNEFSqCTVITIAH------RLhtimdSDKIMVLDSGKI 1462
Cdd:COG4148 139 RQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILpylERLRDELD-IPILYVSHsldevaRL-----ADHVVLLEQGRV 212
|
250 260
....*....|....*....|....*.
gi 569006289 1463 VEYGSPEELLSN--MGPFyLMAKEAG 1486
Cdd:COG4148 213 VASGPLAEVLSRpdLLPL-AGGEEAG 237
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
604-785 |
4.39e-09 |
|
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: 61.57 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG------------SIAYVPQQAWI-QNGTIKDNIL 670
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldavrqSLGMCPQHNILfHHLTVAEHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 671 FGSEYDEKKYQRV-IEACALLPDLemlpgGDMAEIGEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVDTHVGKHI 749
Cdd:TIGR01257 1026 FYAQLKGRSWEEAqLEMEAMLEDT-----GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190
....*....|....*....|....*....|....*.
gi 569006289 750 FNKVVgpnGLLSGKTRILVTHgihflpQVDEIVVLG 785
Cdd:TIGR01257 1101 WDLLL---KYRSGRTIIMSTH------HMDEADLLG 1127
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1267-1471 |
4.44e-09 |
|
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: 58.54 E-value: 4.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1267 LKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESaggqiiidGIDIASIGLHD-------LRGRLTIIPQDPIL--- 1336
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKP--------TSGRATVAGHDvvrepreVRRRIGIVFQDLSVdde 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1337 FSG--NLRMNLDPFNKYSDEEIWRALELahLKSFvaglqlgllhEVTEGGDNL----SIGQRQLLCLGRAVLRKSKILVL 1410
Cdd:cd03265 88 LTGweNLYIHARLYGVPGAERRERIDEL--LDFV----------GLLEAADRLvktySGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569006289 1411 DEATAAVDLETDSLIQTTIR--NEFSQCTVITIAHrlhtIMD-----SDKIMVLDSGKIVEYGSPEEL 1471
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEklKEEFGMTILLTTH----YMEeaeqlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
604-793 |
4.73e-09 |
|
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: 58.15 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-SIAYVPQQAWIQNG------------TIKDNI- 669
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARRRLGfvsdstglydrlTARENLe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 670 ----LFGSEYDEKKyQRVIEACALLpdlemlpggDMAEIGEK-GINLSGGQKHRVSLARATYQDADIYILDDPLSAVDth 744
Cdd:cd03266 101 yfagLYGLKGDELT-ARLEELADRL---------GMEELLDRrVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD-- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 569006289 745 vgkhifnkVVGPNGLL--------SGKTRILVTHGIHFLPQV-DEIVVLGKGTILEKG 793
Cdd:cd03266 169 --------VMATRALRefirqlraLGKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
605-744 |
5.21e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.89 E-value: 5.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 605 QDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-SI-----AYVPQQAWI--QNGtIKD------NIL 670
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGePIrrqrdEYHQDLLYLghQPG-IKTeltaleNLR 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569006289 671 F----GSEYDEKKYQRVIEACALLpDLEMLPGGdmaeigekgiNLSGGQKHRVSLARATYQDADIYILDDPLSAVDTH 744
Cdd:PRK13538 97 FyqrlHGPGDDEALWEALAQVGLA-GFEDVPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1250-1462 |
5.37e-09 |
|
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: 58.19 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYrPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIAsiGLHD-----LR 1324
Cdd:cd03292 1 IEFINVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS--DLRGraipyLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1325 GRLTIIPQDPILFSgnlrmNLDPFnkysdEEIWRALELAHL------KSFVAGL-QLGLLHEVTEGGDNLSIGQRQLLCL 1397
Cdd:cd03292 78 RKIGVVFQDFRLLP-----DRNVY-----ENVAFALEVTGVppreirKRVPAALeLVGLSHKHRALPAELSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 1398 GRAVLRKSKILVLDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIMD--SDKIMVLDSGKI 1462
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDttRHRVIALERGKL 214
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
604-742 |
5.79e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 58.37 E-value: 5.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITI--------------KGSIAYVPQQAWI-QNGTIKDN 668
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllplharaRRGIGYLPQEASIfRRLSVYDN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006289 669 ILFGSEY--DEKKYQRVIEACALLPDLEMLPGGDmaeigEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVD 742
Cdd:PRK10895 99 LMAVLQIrdDLSAEQREDRANELMEEFHIEHLRD-----SMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
593-794 |
5.84e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 58.95 E-value: 5.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 593 SFTWDRDLEAT----IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGSIAYVPQQAW--------- 659
Cdd:PRK13633 11 SYKYESNEESTeklaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdirnkagmv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 660 IQN------GTI-KDNILFGSEY----DEKKYQRVIEAcallpdlemLPGGDMAEIGEKGIN-LSGGQKHRVSLARATYQ 727
Cdd:PRK13633 91 FQNpdnqivATIvEEDVAFGPENlgipPEEIRERVDES---------LKKVGMYEYRRHAPHlLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 728 DADIYILDDPLSAVDTHVGKHIFNKVVGPNGLlSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGS 794
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELNKK-YGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1245-1444 |
6.54e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 60.53 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1245 PKKGEIQFNNYQVRYR------PELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLtnclFRILEsaggqiiidgidiasi 1318
Cdd:TIGR00954 440 PGRGIVEYQDNGIKFEniplvtPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSL----FRILG---------------- 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1319 GLHDLR-GRLTI--------IPQDPILFSGNLR------MNLDPFNK--YSDEEIWRALELAHLKSFVAglQLGLLHEVT 1381
Cdd:TIGR00954 500 ELWPVYgGRLTKpakgklfyVPQRPYMTLGTLRdqiiypDSSEDMKRrgLSDKDLEQILDNVQLTHILE--REGGWSAVQ 577
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006289 1382 EGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRNefSQCTVITIAHR 1444
Cdd:TIGR00954 578 DWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHR 638
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
604-800 |
7.05e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 59.05 E-value: 7.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS------------IAYVPQQAWIQ-NGTIKDNIL 670
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharqrVGVVPQFDNLDpDFTVRENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 671 FGSEYDEKKYQRVIEACALLPDLEMLPGGDMAEIGEkginLSGGQKHRVSLARATYQDADIYILDDPLSAVDTHVGKHIF 750
Cdd:PRK13537 103 VFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMW 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 569006289 751 NKVvgPNGLLSGKTRILVThgiHFLPQV----DEIVVLGKGTILEKGSYSDLMD 800
Cdd:PRK13537 179 ERL--RSLLARGKTILLTT---HFMEEAerlcDRLCVIEEGRKIAEGAPHALIE 227
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
597-798 |
7.16e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 59.32 E-value: 7.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 597 DRDLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLI---------SAmlgemenvhGHITIKG----------------SI 651
Cdd:COG1135 15 GGPVTA-LDDVSLTIEKGEIFGIIGYSGAGKSTLIrcinllerpTS---------GSVLVDGvdltalserelraarrKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 652 AYVPQQ-AWIQNGTIKDNILFGSEYD----EKKYQRVIEacaLLpdlemlpggDMAEIGEKG----INLSGGQKHRVSLA 722
Cdd:COG1135 85 GMIFQHfNLLSSRTVAENVALPLEIAgvpkAEIRKRVAE---LL---------ELVGLSDKAdaypSQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 723 RATYQDADIYILDDPLSAVDTHVGKHIFNkvvgpngLLS------GKTRILVTHGIHFLPQV-DEIVVLGKGTILEKGSY 795
Cdd:COG1135 153 RALANNPKVLLCDEATSALDPETTRSILD-------LLKdinrelGLTIVLITHEMDVVRRIcDRVAVLENGRIVEQGPV 225
|
...
gi 569006289 796 SDL 798
Cdd:COG1135 226 LDV 228
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1266-1457 |
7.21e-09 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 57.24 E-value: 7.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILesAGGQIIIDGIDIASIGLhdLRGRLTIIPQDPILFSGNLRMNL 1345
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVL--RPTSGTVRRAGGARVAY--VPQRSEVPDSLPLTVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1346 ----DPFNKYSDE---EIWRALELAHLKSFvAGLQLgllhevteggDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVD 1418
Cdd:NF040873 83 warrGLWRRLTRDdraAVDDALERVGLADL-AGRQL----------GELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 569006289 1419 LETDSLIQTTIRNEFS-QCTVITIAHRLHTIMDSDKIMVL 1457
Cdd:NF040873 152 AESRERIIALLAEEHArGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1250-1474 |
7.42e-09 |
|
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: 58.08 E-value: 7.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYrPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTI 1329
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1330 IPQDPILF-----SGNLRMnLDPFNKYSDEEI-WRALELAHLksfvagLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLR 1403
Cdd:cd03295 80 VIQQIGLFphmtvEENIAL-VPKLLKWPKEKIrERADELLAL------VGLDPAEFADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006289 1404 KSKILVLDEATAAVDLET-DSLIQTTIR-NEFSQCTVITIAHRL-HTIMDSDKIMVLDSGKIVEYGSPEELLSN 1474
Cdd:cd03295 153 DPPLLLMDEPFGALDPITrDQLQEEFKRlQQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
606-815 |
7.93e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 58.69 E-value: 7.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 606 DVNLDIKPGQLVAVVGTVGSGKSSLI---SAML----GEMENVHGHIT----------IKGSIAYV---PQQAWIQNGTI 665
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMqhfNALLkpssGTITIAGYHITpetgnknlkkLRKKVSLVfqfPEAQLFENTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 666 KDNIL----FGSEYDEKKYQRV--IEACALLPDLemlpggdmaeIGEKGINLSGGQKHRVSLARATYQDADIYILDDPLS 739
Cdd:PRK13641 105 KDVEFgpknFGFSEDEAKEKALkwLKKVGLSEDL----------ISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569006289 740 AVDTHVGKHIFNKVVgpNGLLSGKTRILVTHGIHFLPQ-VDEIVVLGKGTILEKGSysdlmdKKGVFA-KNWktFMKH 815
Cdd:PRK13641 175 GLDPEGRKEMMQLFK--DYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHAS------PKEIFSdKEW--LKKH 242
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
576-783 |
1.03e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.80 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 576 AIRHVCHFDKAVQFSEASFTWDrDLEATIQDVNLDIKPGQL-----VAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS 650
Cdd:COG1245 324 PIEFEVHAPRREKEEETLVEYP-DLTKSYGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 651 IAYVPQqaWI---QNGTIKDNI--LFGSEYDEKKYQ-RVIEACALLPDLEMlpggdmaEIGEkginLSGGQKHRVSLARA 724
Cdd:COG1245 403 ISYKPQ--YIspdYDGTVEEFLrsANTDDFGSSYYKtEIIKPLGLEKLLDK-------NVKD----LSGGELQRVAIAAC 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006289 725 TYQDADIYILDDPLSAVD----THVGKHIFNKVVGpngllSGKTRILVTHGIHFLPQV-DEIVV 783
Cdd:COG1245 470 LSRDADLYLLDEPSAHLDveqrLAVAKAIRRFAEN-----RGKTAMVVDHDIYLIDYIsDRLMV 528
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1361-1463 |
1.19e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 57.79 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1361 ELAHLKSFVAGLQLGL---LHEVTEggdNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIqTTIRNEF---S 1434
Cdd:COG1101 123 RRELFRELLATLGLGLenrLDTKVG---LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALV-LELTEKIveeN 198
|
90 100 110
....*....|....*....|....*....|....*..
gi 569006289 1435 QCTVITIAHRLH--------TIMdsdkimvLDSGKIV 1463
Cdd:COG1101 199 NLTTLMVTHNMEqaldygnrLIM-------MHEGRII 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
698-799 |
1.23e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 57.67 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 698 GGDMAEIGEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVDTH-VGK--HIFNKVVGpngllSGKTRILVTHGIHF 774
Cdd:PRK10619 140 GIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElVGEvlRIMQQLAE-----EGKTMVVVTHEMGF 214
|
90 100
....*....|....*....|....*.
gi 569006289 775 LPQV-DEIVVLGKGTILEKGSYSDLM 799
Cdd:PRK10619 215 ARHVsSHVIFLHQGKIEEEGAPEQLF 240
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1266-1473 |
1.60e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 59.05 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLF----------RIL-------------------------ESAGGQIII 1310
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRgmdqyeptsgRIIyhvalcekcgyverpskvgepcpvcGGTLEPEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1311 DGIDIASIGLHDLRGRLTIIPQDPILFSGNLR-----MNLDPFNKYS-DEEIWRALELAHlksfvaglQLGLLHEVTEGG 1384
Cdd:TIGR03269 95 DFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTvldnvLEALEEIGYEgKEAVGRAVDLIE--------MVQLSHRITHIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1385 DNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRN--EFSQCTVITIAHRLHTIMD-SDKIMVLDSGK 1461
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIEDlSDKAIWLENGE 246
|
250
....*....|..
gi 569006289 1462 IVEYGSPEELLS 1473
Cdd:TIGR03269 247 IKEEGTPDEVVA 258
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
610-742 |
1.63e-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: 57.03 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 610 DIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-SIAYVPQQAWI-QNGTIKDnilFGSEYDEKKYQRVIEAC 687
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKAdYEGTVRD---LLSSITKDFYTHPYFKT 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 569006289 688 ALLPDLEMLPggdmaeIGEKGIN-LSGGQKHRVSLARATYQDADIYILDDPLSAVD 742
Cdd:cd03237 98 EIAKPLQIEQ------ILDREVPeLSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1268-1474 |
1.67e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.18 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1268 KGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQII---IDGIDIASIGLHDLRGRLTIIPQDPiLFSGNLRMN 1344
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwlgKDLLGMKDDEWRAVRSDIQMIFQDP-LASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1345 L-----DPFNKYSDEeiwraLELAHLKSFVAG--LQLGLL--------HEvteggdnLSIGQRQLLCLGRAVLRKSKILV 1409
Cdd:PRK15079 117 IgeiiaEPLRTYHPK-----LSRQEVKDRVKAmmLKVGLLpnlinrypHE-------FSGGQCQRIGIARALILEPKLII 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006289 1410 LDEATAAVDLEtdslIQTTIRNEFSQC------TVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEELLSN 1474
Cdd:PRK15079 185 CDEPVSALDVS----IQAQVVNLLQQLqremglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHN 252
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1258-1473 |
1.76e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 57.32 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1258 RYRPELdlVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRIL--ESAGGQIIIDGIDIASIGLHDLRGRLTIIPQDP- 1334
Cdd:PRK13638 10 RYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrpQKGAVLWQGKPLDYSKRGLLALRQQVATVFQDPe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1335 -----------ILFSgnLRmNLDpfnkYSDEEIWR----ALELAHLKSFvaglqlglLHEVTEGgdnLSIGQRQLLCLGR 1399
Cdd:PRK13638 88 qqifytdidsdIAFS--LR-NLG----VPEAEITRrvdeALTLVDAQHF--------RHQPIQC---LSHGQKKRVAIAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006289 1400 AVLRKSKILVLDEATAAVDLETDSLIQTTIRNEFSQCT-VITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEELLS 1473
Cdd:PRK13638 150 ALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNhVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
604-790 |
1.98e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 58.97 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISaMLGEMEN-VHGHITIKGS-IAYVPQQAWIQ-----------------NGT 664
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKpTSGTYRVAGQdVATLDADALAQlrrehfgfifqryhllsHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 665 IKDNILFGSEYDEK-KYQRVIEACALLPDLemlpgGDMAEIGEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVDT 743
Cdd:PRK10535 103 AAQNVEVPAVYAGLeRKQRLLRAQELLQRL-----GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 569006289 744 HVGKHIFNKVVGPNGllSGKTRILVTHGIHFLPQVDEIVVLGKGTIL 790
Cdd:PRK10535 178 HSGEEVMAILHQLRD--RGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
960-1222 |
2.28e-08 |
|
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: 57.48 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 960 QNGTDNSPSQRDMR-----IGVFGALGIAQGIFLLSSSLWSIYACRNASKTLHRQLLTNILRAPMSFFDTTPTGRIVNRF 1034
Cdd:cd18545 24 KIAIDEYIPNGDLSglliiALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1035 AGDISTVDDTLPQTLRSWLLCFFGIVSTLVM----------ICMATpifiiiiiplsilyvsVQVFYVAT------SRQL 1098
Cdd:cd18545 104 INDVNSLSDLLSNGLINLIPDLLTLVGIVIImfslnvrlalVTLAV----------------LPLLVLVVfllrrrARKA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1099 RRLDSVTKSPIYSHFSETVSGLPVIRAFEHQQRflaNSEKQIDTNQKCVFSWITsnrwlAIRLE-LVGNLIVFCSAL--- 1174
Cdd:cd18545 168 WQRVRKKISNLNAYLHESISGIRVIQSFAREDE---NEEIFDELNRENRKANMR-----AVRLNaLFWPLVELISALgta 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 569006289 1175 LLVIY--KNSLTGD-TVGFVLSNALNIT---QTLNWLVRMTSEVETNIVAVERI 1222
Cdd:cd18545 240 LVYWYggKLVLGGAiTVGVLVAFIGYVGrfwQPIRNLSNFYNQLQSAMASAERI 293
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
606-796 |
2.46e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 56.56 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 606 DVNLDIKPGQLVAVVGTVGSGKSSLISAM-LGEMENvHGHITIKGS-------------------IAYVPQQ--AWiQNG 663
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPR-SGTLNIAGNhfdfsktpsdkairelrrnVGMVFQQynLW-PHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 664 TIKDNIL------FGSEYDEKKYQrvieACALLPDLEMlpgGDMAEigEKGINLSGGQKHRVSLARATYQDADIYILDDP 737
Cdd:PRK11124 98 TVQQNLIeapcrvLGLSKDQALAR----AEKLLERLRL---KPYAD--RFPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006289 738 LSAVDthvgKHIFNKVVGPNGLLS--GKTRILVTHGIHFLPQVDEIVV-LGKGTILEKGSYS 796
Cdd:PRK11124 169 TAALD----PEITAQIVSIIRELAetGITQVIVTHEVEVARKTASRVVyMENGHIVEQGDAS 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
599-798 |
2.59e-08 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 56.22 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 599 DLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLISaMLGEM-------ENVHGH------ITIKGSIAYVPQQAWIQNG-T 664
Cdd:cd03265 12 DFEA-VRGVSFRVRRGEIFGLLGPNGAGKTTTIK-MLTTLlkptsgrATVAGHdvvrepREVRRRIGIVFQDLSVDDElT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 665 IKDNI-----LFGSEYDEKKyQRVIEACALLpdlemlpggDMAEIGEKGI-NLSGGQKHRVSLARATYQDADIYILDDPL 738
Cdd:cd03265 90 GWENLyiharLYGVPGAERR-ERIDELLDFV---------GLLEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006289 739 SAVDTHVGKHIFN---KVVGPNGLlsgkTRILVTHGIHFLPQV-DEIVVLGKGTILEKGSYSDL 798
Cdd:cd03265 160 IGLDPQTRAHVWEyieKLKEEFGM----TILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEEL 219
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
606-742 |
2.62e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 57.58 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 606 DVNLDIkPGQLV-AVVGTVGSGKSSLISAMLGEMENVHGHITIKGS-----------------IAYVPQQAWI-QNGTIK 666
Cdd:PRK11144 16 TVNLTL-PAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekgiclppekrrIGYVFQDARLfPHYKVR 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 667 DNILFG-SEYDEKKYQRVIEACALLPDLEMLPggdmaeigekgINLSGGQKHRVSLARATYQDADIYILDDPLSAVD 742
Cdd:PRK11144 95 GNLRYGmAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
598-742 |
2.72e-08 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 55.44 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 598 RDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG------------SIAYVPQQAWIQNG-T 664
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplaeqrdepheNILYLGHLPGLKPElS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 665 IKDNILFGSEyDEKKYQRVIEAcAL----LPDLEMLPGGdmaeigekgiNLSGGQKHRVSLARATYQDADIYILDDPLSA 740
Cdd:TIGR01189 90 ALENLHFWAA-IHGGAQRTIED-ALaavgLTGFEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
..
gi 569006289 741 VD 742
Cdd:TIGR01189 158 LD 159
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1266-1473 |
2.73e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 57.93 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTIIPQDPIL---FSGN-- 1340
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfeFDVRqv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1341 LRMN-------LDPFNKYSDEEIWRALELAHLKSFVAglqlgllHEVTEggdnLSIGQRQLLCLGRAVLRKSKILVLDEA 1413
Cdd:PRK09536 98 VEMGrtphrsrFDTWTETDRAAVERAMERTGVAQFAD-------RPVTS----LSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569006289 1414 TAAVDL----ETDSLIQTTIRNEFsqcTVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEELLS 1473
Cdd:PRK09536 167 TASLDInhqvRTLELVRRLVDDGK---TAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLT 228
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
598-807 |
2.87e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 57.50 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 598 RDLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG----------------SIAYVPQQAWIQ 661
Cdd:PRK11153 16 RTIHA-LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdltalsekelrkarrQIGMIFQHFNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 662 NG-TIKDNILFGSEYD----EKKYQRVIEacaLLpdlemlpggDMAEIGEKG----INLSGGQKHRVSLARATYQDADIY 732
Cdd:PRK11153 95 SSrTVFDNVALPLELAgtpkAEIKARVTE---LL---------ELVGLSDKAdrypAQLSGGQKQRVAIARALASNPKVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006289 733 ILDDPLSAVDTHVGKHIFNKVVGPNGLLsGKTRILVTHGIHFLPQV-DEIVVLGKGTILEKGSYSDlmdkkgVFAK 807
Cdd:PRK11153 163 LCDEATSALDPATTRSILELLKDINREL-GLTIVLITHEMDVVKRIcDRVAVIDAGRLVEQGTVSE------VFSH 231
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
599-740 |
3.16e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.28 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 599 DLEATIQDVNLDIKPGQL-----VAVVGTVGSGKSSLISAMLGEMENVHGHITIKGSIAYVPQqaWI---QNGTIKDNIL 670
Cdd:PRK13409 345 DLTKKLGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQ--YIkpdYDGTVEDLLR 422
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006289 671 F-GSEYDEKKYQrvieacallpdLEMLPGGDMAEIGEKGIN-LSGGQKHRVSLARATYQDADIYILDDPlSA 740
Cdd:PRK13409 423 SiTDDLGSSYYK-----------SEIIKPLQLERLLDKNVKdLSGGELQRVAIAACLSRDADLYLLDEP-SA 482
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1268-1471 |
3.45e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 57.35 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1268 KGITCNIKSTEKVGVVGRTGAGKSSLTNCLfrilesaggqiiidgidiasIGLHDL-RGRLTIipqdpilfsGNLRMNLD 1346
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMI--------------------AGLEDItSGDLFI---------GEKRMNDV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1347 P---------FNKYSdeeIWRALELAHLKSF---VAG----------------LQLGllHEVTEGGDNLSIGQRQLLCLG 1398
Cdd:PRK11000 71 PpaergvgmvFQSYA---LYPHLSVAENMSFglkLAGakkeeinqrvnqvaevLQLA--HLLDRKPKALSGGQRQRVAIG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1399 RAVLRKSKILVLDEATAAVdletDSLIQTTIRNEFS------QCTVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEEL 1471
Cdd:PRK11000 146 RTLVAEPSVFLLDEPLSNL----DAALRVQMRIEISrlhkrlGRTMIYVTHDQVEAMTlADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1250-1462 |
3.76e-08 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 55.61 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELdlVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIII--DGIDIASIGLHDLRGRL 1327
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIdgLKLTDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1328 TIIPQDPILFS-----GNLRMNLDPFNKYSDEE-IWRALELahLKsfvaglQLGLLHEVTEGGDNLSIGQRQLLCLGRAV 1401
Cdd:cd03262 79 GMVFQQFNLFPhltvlENITLAPIKVKGMSKAEaEERALEL--LE------KVGLADKADAYPAQLSGGQQQRVAIARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 1402 LRKSKILVLDEATAAVDLETDSLIQTTIRN-EFSQCTVITIAHRlhtiMD-----SDKIMVLDSGKI 1462
Cdd:cd03262 151 AMNPKVMLFDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTHE----MGfarevADRVIFMDDGRI 213
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
604-802 |
3.78e-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: 58.02 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITI-KG-SIAYVPQQAWI-QNGTIKDNILFG-------- 672
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGiKVGYLPQEPQLdPTKTVRENVEEGvaeikdal 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 673 SEYDE-------------------KKYQRVIEACA---LLPDLEM------LPGGDmAEIGekgiNLSGGQKHRVSLARA 724
Cdd:TIGR03719 101 DRFNEisakyaepdadfdklaaeqAELQEIIDAADawdLDSQLEIamdalrCPPWD-ADVT----KLSGGERRRVALCRL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 725 TYQDADIYILDDPLSAVDTH----VGKHIFNkvvgpnglLSGkTRILVTHGIHFLPQVDE-IVVLGKGT-ILEKGSYSDL 798
Cdd:TIGR03719 176 LLSKPDMLLLDEPTNHLDAEsvawLERHLQE--------YPG-TVVAVTHDRYFLDNVAGwILELDRGRgIPWEGNYSSW 246
|
....
gi 569006289 799 MDKK 802
Cdd:TIGR03719 247 LEQK 250
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
974-1179 |
4.33e-08 |
|
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: 56.63 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 974 IGVFGALGIAQGIFLLSSSLWSIYACRNASKTLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDTLPQTLRSWL 1053
Cdd:cd18544 44 ALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1054 LCFFGIVSTLVM----------ICMATpifiiiiiplsilyvsVQVFYVAT------SRQLRRLDSVTKSPIYSHFSETV 1117
Cdd:cd18544 124 GDLLLLIGILIAmfllnwrlalISLLV----------------LPLLLLATylfrkkSRKAYREVREKLSRLNAFLQESI 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569006289 1118 SGLPVIRAFEHQQRFLANSEKqidTNQKCVFSWITSNRWLAI-R--LELVGNLivfcsALLLVIY 1179
Cdd:cd18544 188 SGMSVIQLFNREKREFEEFDE---INQEYRKANLKSIKLFALfRplVELLSSL-----ALALVLW 244
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1266-1477 |
4.39e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.75 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRIL--ESAGGQIIIDGIDIASIGL-HDLRgrLTIIPQDPILFSgNLR 1342
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVppDSGTLEIGGNPCARLTPAKaHQLG--IYLVPQEPLLFP-NLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1343 MNldpfnkysdEEIW-----RALELAHLKSFVAGLQLGLLHEVTEGgdNLSIGQRQLLCLGRAVLRKSKILVLDEATAAV 1417
Cdd:PRK15439 103 VK---------ENILfglpkRQASMQKMKQLLAALGCQLDLDSSAG--SLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569006289 1418 D-LETDSLIQtTIRNEFSQ-CTVITIAHRLHTIMD-SDKIMVLDSGKIVEYG-----SPEELLSNMGP 1477
Cdd:PRK15439 172 TpAETERLFS-RIRELLAQgVGIVFISHKLPEIRQlADRISVMRDGTIALSGktadlSTDDIIQAITP 238
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
584-798 |
4.48e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 56.25 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 584 DKAVQFSEASFTWDRDLEAT-IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGSiAYVPQQAW--- 659
Cdd:PRK13642 2 NKILEVENLVFKYEKESDVNqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVWnlr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 660 ------IQN-------GTIKDNILFGSEYD----EKKYQRVIEACALLPDLEMLPggdmaeigEKGINLSGGQKHRVSLA 722
Cdd:PRK13642 81 rkigmvFQNpdnqfvgATVEDDVAFGMENQgiprEEMIKRVDEALLAVNMLDFKT--------REPARLSGGQKQRVAVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006289 723 RATYQDADIYILDDPLSAVDThVGKHIFNKVVGPNGLLSGKTRILVTHGIHFLPQVDEIVVLGKGTILEKGSYSDL 798
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDP-TGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
604-742 |
5.29e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 55.81 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISA---MLGEMENVH--GHITIKG---------------SIAYVPQQAwiqN- 662
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRClnrMNDLIPGARveGEILLDGediydpdvdvvelrrRVGMVFQKP---Np 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 663 --GTIKDNILFGseydekkyqrvieacalLPDLEMLPGGDMAEIGEK------------------GINLSGGQKHRVSLA 722
Cdd:COG1117 104 fpKSIYDNVAYG-----------------LRLHGIKSKSELDEIVEEslrkaalwdevkdrlkksALGLSGGQQQRLCIA 166
|
170 180
....*....|....*....|
gi 569006289 723 RATYQDADIYILDDPLSAVD 742
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALD 186
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1266-1473 |
5.74e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 55.96 E-value: 5.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTIIPQDP--ILFSGNLRM 1343
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1344 NL--DPFNKYSDEEiwralELAHLKSFVAGLqLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLE- 1420
Cdd:PRK13652 99 DIafGPINLGLDEE-----TVAHRVSSALHM-LGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQg 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 1421 TDSLIQttIRNEFSQ---CTVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEELLS 1473
Cdd:PRK13652 173 VKELID--FLNDLPEtygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFL 227
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
975-1222 |
6.06e-08 |
|
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: 55.87 E-value: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 975 GVFGALGIAQGIFLLSS------SLWSIYACRNASKTLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDTLPQT 1048
Cdd:cd18547 43 GLLRILLLLLGLYLLSAlfsylqNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1049 LRSWLLCFFGIVSTLVMICmatpifiiiiiplsilYVSVQ-----------VFYVAT----------SRQLRRLDSVTks 1107
Cdd:cd18547 123 LTQLISSILTIVGTLIMML----------------YISPLltlivlvtvplSLLVTKfiakrsqkyfRKQQKALGELN-- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1108 piySHFSETVSGLPVIRAFEHQQRFLAN----SEKQIDTNQKCVFSWITSNRWLAirleLVGNLIVFCSAL---LLVIyK 1180
Cdd:cd18547 185 ---GYIEEMISGQKVVKAFNREEEAIEEfdeiNEELYKASFKAQFYSGLLMPIMN----FINNLGYVLVAVvggLLVI-N 256
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 569006289 1181 NSLT-GDTVGFvLSNALNITQTLNWLVRMTSEVETNIVAVERI 1222
Cdd:cd18547 257 GALTvGVIQAF-LQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
604-742 |
6.31e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 55.42 E-value: 6.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS--------------IAYVPQQAWI-QNGTIKDN 668
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIGYLPQEASIfRKLTVEDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 669 I---LFGSEYDEKKYQRVIEAcaLLPDLEmlpggdmaeIGE----KGINLSGGQKHRVSLARATYQDADIYILDDPLSAV 741
Cdd:COG1137 99 IlavLELRKLSKKEREERLEE--LLEEFG---------ITHlrksKAYSLSGGERRRVEIARALATNPKFILLDEPFAGV 167
|
.
gi 569006289 742 D 742
Cdd:COG1137 168 D 168
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
974-1222 |
7.69e-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: 55.51 E-value: 7.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 974 IGVFgalgIAQGIFLLSSSLWSIYACRNASKTLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDTLPQTLRSWL 1053
Cdd:cd18552 46 IGLF----LLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1054 LCFFGIVSTL-VMIcmatpifiiiiiplsilYVSVQ-----------VFYVAT--SRQLRRL-----DSVTKspIYSHFS 1114
Cdd:cd18552 122 RDPLTVIGLLgVLF-----------------YLDWKltlialvvlplAALPIRriGKRLRKIsrrsqESMGD--LTSVLQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1115 ETVSGLPVIRAFEHQQRFLANSEKQIDTNQKcvfswiTSNRWLAIR------LELVGNL---IVFCSALLLVIYKNSLTG 1185
Cdd:cd18552 183 ETLSGIRVVKAFGAEDYEIKRFRKANERLRR------LSMKIARARalssplMELLGAIaiaLVLWYGGYQVISGELTPG 256
|
250 260 270
....*....|....*....|....*....|....*..
gi 569006289 1186 DTVGFVLSnALNITQTLNWLVRMTSEVETNIVAVERI 1222
Cdd:cd18552 257 EFISFITA-LLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
611-800 |
7.81e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 56.98 E-value: 7.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 611 IKPGQLVAVVGTVGSGKSSLISAMLGEMEN---VHGHITIKGSI----------AYVPQQ-AWIQNGTIKDNILFGSE-- 674
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPidakemraisAYVQQDdLFIPTLTVREHLMFQAHlr 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 675 -----YDEKKYQRVIEacaLLPDLEMLPGGDMAeIGEKGI--NLSGGQKHRVSLARATYQDADIYILDDPLSAVDT---- 743
Cdd:TIGR00955 128 mprrvTKKEKRERVDE---VLQALGLRKCANTR-IGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSfmay 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006289 744 ---HVGKHIFNKvvgpngllsGKTRILVTH--GIHFLPQVDEIVVLGKGTILEKGSYSDLMD 800
Cdd:TIGR00955 204 svvQVLKGLAQK---------GKTIICTIHqpSSELFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1282-1474 |
8.32e-08 |
|
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: 55.34 E-value: 8.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1282 VVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIG---LHDLRGR--------LTIIPQDPILfsGNLRMNLDPFNK 1350
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKkismvfqsFALLPHRTVL--ENVAFGLEVQGV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1351 YSDEEIWRALELAHLksfvAGLQlGLLHEVTeggDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVdletDSLIQTTIR 1430
Cdd:cd03294 133 PRAEREERAAEALEL----VGLE-GWEHKYP---DELSGGMQQRVGLARALAVDPDILLMDEAFSAL----DPLIRREMQ 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 569006289 1431 NEF------SQCTVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEELLSN 1474
Cdd:cd03294 201 DELlrlqaeLQKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1385-1471 |
8.39e-08 |
|
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: 54.94 E-value: 8.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1385 DNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRNeFSQCTVITIAHRLH----TIMDSDKIMVLDSG 1460
Cdd:cd03300 129 SQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKR-LQKELGITFVFVTHdqeeALTMSDRIAVMNKG 207
|
90
....*....|.
gi 569006289 1461 KIVEYGSPEEL 1471
Cdd:cd03300 208 KIQQIGTPEEI 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1250-1464 |
8.40e-08 |
|
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: 54.40 E-value: 8.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELD--LVLKGITCNIKSTEKVGVVGRTGAGKSSltncLFRI---LESaggqiiidgidiASIG----- 1319
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKST----LLRIiagLER------------PTSGevlvd 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1320 ---LHDLRGRLTIIPQDPILF-----SGN----LRMNLDPfNKYSDEEIWRALELAHLKSFVAGLQlgllHEvteggdnL 1387
Cdd:cd03293 65 gepVTGPGPDRGYVFQQDALLpwltvLDNvalgLELQGVP-KAEARERAEELLELVGLSGFENAYP----HQ-------L 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1388 SIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRN--EFSQCTVITIAHRLH-TIMDSDKIMVLDS--GKI 1462
Cdd:cd03293 133 SGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRI 212
|
..
gi 569006289 1463 VE 1464
Cdd:cd03293 213 VA 214
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1373-1474 |
9.50e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 55.00 E-value: 9.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1373 QLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVD-LETDSLIQ--TTIRNEFsQCTVITIAHRLHTIM 1449
Cdd:PRK11300 140 RVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNpKETKELDEliAELRNEH-NVTVLLIEHDMKLVM 218
|
90 100
....*....|....*....|....*.
gi 569006289 1450 D-SDKIMVLDSGKIVEYGSPEELLSN 1474
Cdd:PRK11300 219 GiSDRIYVVNQGTPLANGTPEEIRNN 244
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
604-784 |
1.08e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.33 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS-IAYVPQQAWIQN------------GTIKDNIL 670
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdISTLKPEIYRQQvsycaqtptlfgDTVYDNLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 671 F-----GSEYDEKKYQRVIEACALlpDLEMLpggdmaeigEKGIN-LSGGQKHRVSLARATYQDADIYILDDPLSAVDTH 744
Cdd:PRK10247 103 FpwqirNQQPDPAIFLDDLERFAL--PDTIL---------TKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 569006289 745 vGKHIFNKVVGPNGLLSGKTRILVTHGIHFLPQVDEIVVL 784
Cdd:PRK10247 172 -NKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1250-1474 |
1.19e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.22 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELDLVLKG---ITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILE----SAGGQIIIDGIDIASIGLHD 1322
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGldnISFELEEGSFVALVGHTGSGKSTLMQHFNALLKpssgTITIAGYHITPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1323 LRGRLTIIPQDP--ILFSGNLRMNLD--PFNKYSDEEIWRALELAHLKsfvaglQLGLLHEVTEGGD-NLSIGQRQLLCL 1397
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTVLKDVEfgPKNFGFSEDEAKEKALKWLK------KVGLSEDLISKSPfELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569006289 1398 GRAVLRKSKILVLDEATAAVDLET-DSLIQTTIRNEFSQCTVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEELLSN 1474
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSD 235
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1250-1477 |
1.40e-07 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 53.99 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRpelDLVLKgITCNIKSTEKVGVVGRTGAGKSSLTNCL--FRILESaggqiiidgidiasiglhdlrGRL 1327
Cdd:COG3840 2 LRLDDLTYRYG---DFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIagFLPPDS---------------------GRI 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1328 TIIPQD---------P--ILF-SGNL------RMN----LDPFNKYSDEEIWRALELAHlksfvaglQLGLLHEVTEGGD 1385
Cdd:COG3840 57 LWNGQDltalppaerPvsMLFqENNLfphltvAQNiglgLRPGLKLTAEQRAQVEQALE--------RVGLAGLLDRLPG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1386 NLSIGQRQLLCLGRAVLRKSKILVLDEATAAVD----LETDSLIQTTIRNEfsQCTVITIAHRLHTIMD-SDKIMVLDSG 1460
Cdd:COG3840 129 QLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRER--GLTVLMVTHDPEDAARiADRVLLVADG 206
|
250
....*....|....*..
gi 569006289 1461 KIVEYGSPEELLSNMGP 1477
Cdd:COG3840 207 RIAADGPTAALLDGEPP 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1267-1466 |
1.41e-07 |
|
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: 53.84 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1267 LKGITCNIK---STEKVGVVGRTGAGKSSLTNCLfrilesaggqiiidgidiasIGLHDLRGRlTIIPQDPILFSGNLRM 1343
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCI--------------------AGLEKPDGG-TIVLNGTVLFDSRKKI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1344 NLDP--------FNKYS-------DEEI---WRALELAHLKSFVAGL--QLGLLHEVTEGGDNLSIGQRQLLCLGRAVLR 1403
Cdd:cd03297 69 NLPPqqrkiglvFQQYAlfphlnvRENLafgLKRKRNREDRISVDELldLLGLDHLLNRYPAQLSGGEKQRVALARALAA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 1404 KSKILVLDEATAAVDLETDSLIQ---TTIRNEFsQCTVITIAHRLHTI-MDSDKIMVLDSGKIVEYG 1466
Cdd:cd03297 149 QPELLLLDEPFSALDRALRLQLLpelKQIKKNL-NIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1250-1466 |
1.53e-07 |
|
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: 53.91 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELDLV--LKGITCNIKSTEKVGVVGRTGAGKsslTNCLfRILESAggqiiidgiDIASIGLHDLRGRL 1327
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGK---TTTL-RMLAGL---------LEPDAGFATVDGFD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1328 TIipQDPILFSGNLRMNLDPFNKYSDEEIWRALE-------------LAHLKSFVAGLQLGLLHEVTEGGdnLSIGQRQL 1394
Cdd:cd03266 69 VV--KEPAEARRRLGFVSDSTGLYDRLTARENLEyfaglyglkgdelTARLEELADRLGMEELLDRRVGG--FSTGMRQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006289 1395 LCLGRAVLRKSKILVLDEATAAVD-LETDSLIQTTIRNEFSQCTVITIAHRLHTIMD-SDKIMVLDSGKIVEYG 1466
Cdd:cd03266 145 VAIARALVHDPPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
604-791 |
1.62e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.01 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG------------------------SIAYVPQQAW 659
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqmdeearaklrakhvgfvfqSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 660 IQNgtIKDNILFGSEYDEKKYQRVIEACALL---PDLEMLPGgdmaeigekgiNLSGGQKHRVSLARATYQDADIYILDD 736
Cdd:PRK10584 106 LEN--VELPALLRGESSRQSRNGAKALLEQLglgKRLDHLPA-----------QLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 569006289 737 PLSAVDTHVGKHIFNKVVGPNGLLsGKTRILVTHGIHFLPQVDEIVVLGKGTILE 791
Cdd:PRK10584 173 PTGNLDRQTGDKIADLLFSLNREH-GTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
595-778 |
1.95e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.31 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 595 TWDRDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS----------IAYVPQ-QAWIQNG 663
Cdd:PRK13543 18 AFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsrfMAYLGHlPGLKADL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 664 TIKDNILFGSEYDEKKYQRvieacallpdlemLPGGDMAEIGEKGI------NLSGGQKHRVSLARATYQDADIYILDDP 737
Cdd:PRK13543 98 STLENLHFLCGLHGRRAKQ-------------MPGSALAIVGLAGYedtlvrQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 569006289 738 LSAVDTHvGKHIFNKVVGPNgLLSGKTRILVTHGIHFLPQV 778
Cdd:PRK13543 165 YANLDLE-GITLVNRMISAH-LRGGGAALVTTHGAYAAPPV 203
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
598-799 |
2.14e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.06 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 598 RDLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEME--------NVHGHITIKGSI-------------AYVPQ 656
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPlaaidaprlarlrAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 657 QAWIQNGTIKDNILFGSEYDEKK-------YQRVIEACAL-LPDLEMLPGGDMAeigekgiNLSGGQKHRVSLARATYQ- 727
Cdd:PRK13547 91 AAQPAFAFSAREIVLLGRYPHARragalthRDGEIAWQALaLAGATALVGRDVT-------TLSGGELARVQFARVLAQl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 728 --------DADIYILDDPLSAVDTHVGKHIFNKVVGPN-----GLLSgktrilVTHGIHFLPQ-VDEIVVLGKGTILEKG 793
Cdd:PRK13547 164 wpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLArdwnlGVLA------IVHDPNLAARhADRIAMLADGAIVAHG 237
|
....*.
gi 569006289 794 SYSDLM 799
Cdd:PRK13547 238 APADVL 243
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1266-1473 |
2.37e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.10 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESaggqiiidgidIASIG-----LHDL--------RGRLTIIPQ 1332
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-----------QGEIWfdgqpLHNLnrrqllpvRHRIQVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1333 DPIlFSGNLRMNLDpfnkysdEEIWRALELaHLKSFVAGLQ----LGLLHEVteGGD---------NLSIGQRQLLCLGR 1399
Cdd:PRK15134 370 DPN-SSLNPRLNVL-------QIIEEGLRV-HQPTLSAAQReqqvIAVMEEV--GLDpetrhrypaEFSGGQRQRIAIAR 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 1400 AVLRKSKILVLDEATAAVDLETDSLIQTTIR--NEFSQCTVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEELLS 1473
Cdd:PRK15134 439 ALILKPSLIILDEPTSSLDKTVQAQILALLKslQQKHQLAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1266-1474 |
2.47e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 53.60 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLfRILE--SAGGQIIIDGIDIASIGL-------HDLRGRLTIIPQDPIL 1336
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLEqpEAGTIRVGDITIDTARSLsqqkgliRQLRQHVGFVFQNFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1337 F----------SGNLRMNLDPfnkySDEEIWRALELAhlksfvagLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSK 1406
Cdd:PRK11264 97 FphrtvleniiEGPVIVKGEP----KEEATARARELL--------AKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1407 ILVLDEATAAVDLETDSLIQTTIRNEFSQC-TVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEELLSN 1474
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1266-1463 |
2.50e-07 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 53.49 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILesaggqiiidgidiasiglHDLRGRLTIIPQDP----------- 1334
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLL-------------------QPTSGEVRVAGLVPwkrrkkflrri 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1335 -ILFS--GNLRMNLDPFNKYS-DEEIWRaLELAH----LKSFVAGLQLG-LLHEVTEggdNLSIGQRQLLCLGRAVLRKS 1405
Cdd:cd03267 97 gVVFGqkTQLWWDLPVIDSFYlLAAIYD-LPPARfkkrLDELSELLDLEeLLDTPVR---QLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569006289 1406 KILVLDEATAAVDLETDSLIQTTIR--NEFSQCTVITIAHRLHTIMD-SDKIMVLDSGKIV 1463
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKeyNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1266-1464 |
2.76e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 53.54 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRiLESAGGQII----IDGIDIASIGLHDLRGRLTIIPQDPI------ 1335
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVG-LESPSQGNVswrgEPLAKLNRAQRKAFRRDIQMVFQDSIsavnpr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1336 -----LFSGNLR--MNLDPfnkysDEEIWRALELAHLksfvAGLQLGLLHEVTEggdNLSIGQRQLLCLGRAVLRKSKIL 1408
Cdd:PRK10419 106 ktvreIIREPLRhlLSLDK-----AERLARASEMLRA----VDLDDSVLDKRPP---QLSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569006289 1409 VLDEATAAVDLetdsLIQTTI-------RNEF-SQCTVITiaHRLHTIMD-SDKIMVLDSGKIVE 1464
Cdd:PRK10419 174 ILDEAVSNLDL----VLQAGVirllkklQQQFgTACLFIT--HDLRLVERfCQRVMVMDNGQIVE 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1271-1473 |
2.77e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 53.05 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1271 TCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGgqiiidgidiASIGLHDLRGRLTIIPQDPI--------LFS---- 1338
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPAS----------GSLTLNGQDHTTTPPSRRPVsmlfqennLFShltv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1339 -GNLRMNLDPFNKYSDEEIWRALELAHlksfvaglQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAV 1417
Cdd:PRK10771 89 aQNIGLGLNPGLKLNAAQREKLHAIAR--------QMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006289 1418 D----LETDSLIQTTIRNEfsQCTVITIAHRLHtimDSDKI----MVLDSGKIVEYGSPEELLS 1473
Cdd:PRK10771 161 DpalrQEMLTLVSQVCQER--QLTLLMVSHSLE---DAARIaprsLVVADGRIAWDGPTDELLS 219
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
604-737 |
3.22e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.96 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG--------------SIAYVPQQAWI-QNGTIKDN 668
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditdwqtakimreAVAIVPEGRRVfSRMTVEEN 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569006289 669 ILFGSEY-DEKKYQ-RVIEACALLPDLemlpggdMAEIGEKGINLSGGQKHRVSLARATYQDADIYILDDP 737
Cdd:PRK11614 101 LAMGGFFaERDQFQeRIKWVYELFPRL-------HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1266-1474 |
3.64e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 53.12 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILEsaggqIIIDGIDIASIGLHD------------LRGRLTIIPQD 1333
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMND-----LIPGARVEGEILLDGediydpdvdvveLRRRVGMVFQK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1334 PILFSG----N----LRMNLDPFNKYSDEEIWRALELAhlksfvaglqlGLLHEV----TEGGDNLSIGQRQLLCLGRAV 1401
Cdd:COG1117 101 PNPFPKsiydNvaygLRLHGIKSKSELDEIVEESLRKA-----------ALWDEVkdrlKKSALGLSGGQQQRLCIARAL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569006289 1402 LRKSKILVLDEATAAVD-LETdSLIQTTIRNEFSQCTVITIAHRlhtiMD-----SDKIMVLDSGKIVEYGSPEELLSN 1474
Cdd:COG1117 170 AVEPEVLLMDEPTSALDpIST-AKIEELILELKKDYTIVIVTHN----MQqaarvSDYTAFFYLGELVEFGPTEQIFTN 243
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1264-1430 |
3.67e-07 |
|
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: 52.36 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1264 DLVLKGITCNIKSTEKVGVVGRTGAGKSSLtnclFRILeSAGGQIIIDGIDIASIGLHDLRGrltiIPQDPILFSGNL-- 1341
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTL----LRIL-AGLLRPDSGEVRWNGTPLAEQRD----EPHENILYLGHLpg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1342 -------RMNLD---PFNKYSDEEIWRALELAHLksfvAGLQLGLLHEvteggdnLSIGQRQLLCLGRAVLRKSKILVLD 1411
Cdd:TIGR01189 84 lkpelsaLENLHfwaAIHGGAQRTIEDALAAVGL----TGFEDLPAAQ-------LSAGQQRRLALARLWLSRRPLWILD 152
|
170
....*....|....*....
gi 569006289 1412 EATAAVDLETDSLIQTTIR 1430
Cdd:TIGR01189 153 EPTTALDKAGVALLAGLLR 171
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
604-742 |
3.75e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 53.25 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAM-----LGEMENVHGHITIKGSIAYVP---------------QQAWIQNG 663
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYAPdvdpvevrrrigmvfQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 664 TIKDNILFGSEYDEKK------YQRVIEACALLPDLEmlpggdmAEIGEKGINLSGGQKHRVSLARATYQDADIYILDDP 737
Cdd:PRK14243 106 SIYDNIAYGARINGYKgdmdelVERSLRQAALWDEVK-------DKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
....*
gi 569006289 738 LSAVD 742
Cdd:PRK14243 179 CSALD 183
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1387-1474 |
3.86e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 53.70 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1387 LSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDS-LIQTTIRNEFSQCTVITIAHRLHTIMD-SDKIMVLDSGKIVE 1464
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILK 256
|
90
....*....|
gi 569006289 1465 YGSPEELLSN 1474
Cdd:PRK13631 257 TGTPYEIFTD 266
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1266-1474 |
3.98e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 53.05 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLfRILESAGGQIIIDGIDIASIgLHDLRGRLTIIPQDPI-LFSGNLRMN 1344
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-NFLEKPSEGSIVVNGQTINL-VRDKDGQLKVADKNQLrLLRTRLTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1345 LDPFNKYSDEEIWRALELAHLKsfVAGLQLGLLHE----------VTEGGD-----NLSIGQRQLLCLGRAVLRKSKILV 1409
Cdd:PRK10619 98 FQHFNLWSHMTVLENVMEAPIQ--VLGLSKQEAREravkylakvgIDERAQgkypvHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1410 LDEATAAVDLEtdsLIQTTIR--NEFSQ--CTVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEELLSN 1474
Cdd:PRK10619 176 FDEPTSALDPE---LVGEVLRimQQLAEegKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1272-1466 |
4.11e-07 |
|
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: 52.50 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1272 CNIKSTEKVGVVGRTGAGKSSLTNCL--FRILESAGGQIIIDGIDIASIGlhdlRGRLTIIPQDPILFS-----GNLRMN 1344
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIagFETPQSGRVLINGVDVTAAPPA----DRPVSMLFQENNLFAhltveQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1345 LDPFNKYSDEEiWRALELAHLKSFVAGLQLGLlhevtegGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVD--LETD 1422
Cdd:cd03298 95 LSPGLKLTAED-RQAIEVALARVGLAGLEKRL-------PGELSGGERQRVALARVLVRDKPVLLLDEPFAALDpaLRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 569006289 1423 SL-IQTTIRNEfSQCTVITIAHRLHTIMD-SDKIMVLDSGKIVEYG 1466
Cdd:cd03298 167 MLdLVLDLHAE-TKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
600-799 |
4.43e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 53.25 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 600 LEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG----------------------SIAYVPQQ 657
Cdd:PRK15112 26 VEA-VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysyrsqrirmifqdpSTSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 658 --AWIQNGTIKDNILFGSEYDEKKYQRVIEACALLPD-LEMLPggDMaeigekginLSGGQKHRVSLARATYQDADIYIL 734
Cdd:PRK15112 105 riSQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDhASYYP--HM---------LAPGQKQRLGLARALILRPKVIIA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006289 735 DDPLSAVDTHVGKHIFNKVVGPNGlLSGKTRILVTHGIHFLPQV-DEIVVLGKGTILEKGSYSDLM 799
Cdd:PRK15112 174 DEALASLDMSMRSQLINLMLELQE-KQGISYIYVTQHLGMMKHIsDQVLVMHQGEVVERGSTADVL 238
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
605-787 |
4.47e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 54.26 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 605 QDVNLDIKPGQLVAVVGTVGSGKSSLISaML--------GEMEnVHGH-ITIKGsiayvPQQAwIQNG------------ 663
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMK-ILyglyqpdsGEIL-IDGKpVRIRS-----PRDA-IALGigmvhqhfmlvp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 664 --TIKDNILFGSE------YDEKKYQRVIEACA------LLPDlemlpggdmAEIGEkginLSGGQKHRVSLARATYQDA 729
Cdd:COG3845 94 nlTVAENIVLGLEptkggrLDRKAARARIRELSerygldVDPD---------AKVED----LSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006289 730 DIYILDDPlSAVDThvgkhifnkvvgP---NGLL--------SGKTRILVTHGihfLPQV----DEIVVLGKG 787
Cdd:COG3845 161 RILILDEP-TAVLT------------PqeaDELFeilrrlaaEGKSIIFITHK---LREVmaiaDRVTVLRRG 217
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
582-799 |
5.47e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 52.87 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 582 HFDKAVQFSEASFTW-DRDLeatIQDVNLDIKPGQLVAVVGTVGSGKSSLISaMLGEMEN-VHGHITIKGS--------- 650
Cdd:PRK10575 7 HSDTTFALRNVSFRVpGRTL---LHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQPpSEGEILLDAQpleswsska 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 651 ----IAYVPQQAWIQNG-TIKDNILFG--------SEYDEKKYQRVIEACALLpdlemlpggDMAEIGEKGIN-LSGGQK 716
Cdd:PRK10575 83 farkVAYLPQQLPAAEGmTVRELVAIGrypwhgalGRFGAADREKVEEAISLV---------GLKPLAHRLVDsLSGGER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 717 HRVSLARATYQDADIYILDDPLSAVDthVGKHIfnKVVGPNGLLS---GKTRILVTHGIHFLPQ-VDEIVVLGKGTILEK 792
Cdd:PRK10575 154 QRAWIAMLVAQDSRCLLLDEPTSALD--IAHQV--DVLALVHRLSqerGLTVIAVLHDINMAARyCDYLVALRGGEMIAQ 229
|
....*..
gi 569006289 793 GSYSDLM 799
Cdd:PRK10575 230 GTPAELM 236
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1266-1465 |
5.72e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 53.92 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSltncLFRILesaggqiiidgidiASIGLHD-----LRGRLTI--IPQDPILFS 1338
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKST----LLKIL--------------AGELEPDsgevsIPKGLRIgyLPQEPPLDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1339 G-----NLRMNLDPFNKYSDEeiWRALELAHLKSFVAGLQLGLLHE--VTEGG-------------------------DN 1386
Cdd:COG0488 75 DltvldTVLDGDAELRALEAE--LEELEAKLAEPDEDLERLAELQEefEALGGweaearaeeilsglgfpeedldrpvSE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1387 LSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRNefSQCTVITIAH-R--LHTImdSDKIMVLDSGKIV 1463
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN--YPGTVLVVSHdRyfLDRV--ATRILELDRGKLT 228
|
..
gi 569006289 1464 EY 1465
Cdd:COG0488 229 LY 230
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1250-1474 |
5.83e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 52.40 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELdlVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCL--FRILESAGGQIIIDGIDIASIGLHDLRGRL 1327
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITSGDLIVDGLKVNDPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1328 TIIPQDPILFS----------GNLRMNldPFNKYSDEEIWRALeLAHLksfvaGLQLGLLHEVTEggdnLSIGQRQLLCL 1397
Cdd:PRK09493 80 GMVFQQFYLFPhltalenvmfGPLRVR--GASKEEAEKQAREL-LAKV-----GLAERAHHYPSE----LSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1398 GRAVLRKSKILVLDEATAAVDLETDSLIQTTIR---NEFSQCTVIT----IAHRLHTimdsdKIMVLDSGKIVEYGSPEE 1470
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELRHEVLKVMQdlaEEGMTMVIVTheigFAEKVAS-----RLIFIDKGRIAEDGDPQV 222
|
....
gi 569006289 1471 LLSN 1474
Cdd:PRK09493 223 LIKN 226
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1267-1474 |
6.53e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 52.47 E-value: 6.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1267 LKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRI--LESAGGQIIIDGIDIASI-----GLHDLRGRLTIIPQDPILFSG 1339
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEVTITGSIVYNGHNIysprtDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1340 N--------LRMNLDPFNKYSDEEIWRALELAHLKSFVAGLqlglLHEVTEGgdnLSIGQRQLLCLGRAVLRKSKILVLD 1411
Cdd:PRK14239 101 SiyenvvygLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDR----LHDSALG---LSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006289 1412 EATAAVDLETDSLIQTTIRNEFSQCTVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEELLSN 1474
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQMFMN 237
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
604-742 |
6.62e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 52.42 E-value: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS--IAYVPQQAWIqNGTIKDNIlfgseydeKKYQ 681
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlrIGYVPQKLYL-DTTLPLTV--------NRFL 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006289 682 RV---IEACALLPDLEMLPGGDMAEIGEKgiNLSGGQKHRVSLARATYQDADIYILDDPLSAVD 742
Cdd:PRK09544 91 RLrpgTKKEDILPALKRVQAGHLIDAPMQ--KLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1250-1474 |
6.82e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 53.27 E-value: 6.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNN----YQVRYRPELdlVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRiLESAGGqiiidgidiasiglhdlrG 1325
Cdd:PRK11153 2 IELKNiskvFPQGGRTIH--ALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINL-LERPTS------------------G 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1326 RLTIIPQDPILFSGN-LR-------MNLDPFNKYSD----EEIWRALELAHL-KSFVAGLQLGLLHEV--TEGGD----N 1386
Cdd:PRK11153 61 RVLVDGQDLTALSEKeLRkarrqigMIFQHFNLLSSrtvfDNVALPLELAGTpKAEIKARVTELLELVglSDKADrypaQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1387 LSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIR--NEFSQCTVITIAHRlhtiMD-----SDKIMVLDS 1459
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKdiNRELGLTIVLITHE----MDvvkriCDRVAVIDA 216
|
250
....*....|....*
gi 569006289 1460 GKIVEYGSPEELLSN 1474
Cdd:PRK11153 217 GRLVEQGTVSEVFSH 231
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1267-1471 |
7.11e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 52.32 E-value: 7.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1267 LKGITCNIKSTEKVGVVGRTGAGKSSL-----------------TNCLFRILESAGGQIIIDGIDIASIGL----HDLRG 1325
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLlrhlsglitgdksagshIELLGRTVQREGRLARDIRKSRANTGYifqqFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1326 RLTIIPQDPILFSGNLRMNLDPFNKYSDEEIWRALElahlksfvAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKS 1405
Cdd:PRK09984 100 RLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQ--------ALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569006289 1406 KILVLDEATAAVDLETDSLIQTTIR--NEFSQCTVITIAHRL-HTIMDSDKIMVLDSGKIVEYGSPEEL 1471
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVdYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1258-1473 |
9.05e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 53.51 E-value: 9.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1258 RYRPELDLvLKGITCNIKSTEKVGVVGRTGAGKSSLTNCL-FRILESAGGQIIIDGIDIAsIGLHDLRGRLTIIPQDPIL 1336
Cdd:TIGR00955 33 RERPRKHL-LKNVSGVAKPGELLAVMGSSGAGKTTLMNALaFRSPKGVKGSGSVLLNGMP-IDAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1337 -----------FSGNLRMnldPFNKYSDE------EIWRALEL---AHLKSFVAGLQLGLlhevteggdnlSIGQRQLLC 1396
Cdd:TIGR00955 111 iptltvrehlmFQAHLRM---PRRVTKKEkrervdEVLQALGLrkcANTRIGVPGRVKGL-----------SGGERKRLA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1397 LGRAVLRKSKILVLDEATAAVD-LETDSLIQTTIRNEFSQCTVITIAHR-LHTIMDS-DKIMVLDSGKIVEYGSPEELLS 1473
Cdd:TIGR00955 177 FASELLTDPPLLFCDEPTSGLDsFMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELfDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1386-1474 |
1.03e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.77 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1386 NLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRNEFSQCTVITIAHR-LHTIMDSDKIMVLDSGKIVE 1464
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIE 228
|
90
....*....|
gi 569006289 1465 YGSPEELLSN 1474
Cdd:PRK14267 229 VGPTRKVFEN 238
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1266-1466 |
1.28e-06 |
|
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: 50.99 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILE----SAGGQIIIDGIDIASIGLH-DLRGRltiipqDPILFSGN 1340
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPpdsgTVTVRGRVSSLLGLGGGFNpELTGR------ENIYLNGR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1341 LrMNLDPfnKYSDEEIWRALELAHLKSFVaglqlgllhevteggD----NLSIGQRQLLCLGRAVLRKSKILVLDEATAA 1416
Cdd:cd03220 111 L-LGLSR--KEIDEKIDEIIEFSELGDFI---------------DlpvkTYSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569006289 1417 VDLETDSLIQTTIRNEFSQC-TVITIAHRLHTIMD-SDKIMVLDSGKIVEYG 1466
Cdd:cd03220 173 GDAAFQEKCQRRLRELLKQGkTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
974-1068 |
1.30e-06 |
|
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: 51.78 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 974 IGVFGALGIAQGIFLLSSSLWSIYACRNASKTLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDTLPQTLRSWL 1053
Cdd:cd18572 39 VLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFL 118
|
90
....*....|....*
gi 569006289 1054 LCFFGIVSTLVMICM 1068
Cdd:cd18572 119 RNLVQLVGGLAFMFS 133
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1266-1462 |
1.53e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 51.22 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNcLFRILESAGGQIIIDgidiASIGLHDLRGRLTIIPQDPILFsgnlrmnl 1345
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLR-LLAGLETPSAGELLA----GTAPLAEAREDTRLMFQDARLL-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1346 dPFNKYSD------EEIWRALELAHLKSfvaglqLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDL 1419
Cdd:PRK11247 94 -PWKKVIDnvglglKGQWRDAALQALAA------VGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 569006289 1420 ETDSLIQTTIRNEFSQ--CTVITIAHRL-HTIMDSDKIMVLDSGKI 1462
Cdd:PRK11247 167 LTRIEMQDLIESLWQQhgFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
602-796 |
1.58e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.33 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 602 ATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLG--EMENVHGHITIKGS--IAYVPQQawiqngTIKDNILFGSEY-- 675
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKdlLELSPED------RAGEGIFMAFQYpv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 676 ------DEKKYQRVIEACALLPDLEMLPGGDMAEIGEKGINL----------------SGGQKHRVSLARATYQDADIYI 733
Cdd:PRK09580 89 eipgvsNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALlkmpedlltrsvnvgfSGGEKKRNDILQMAVLEPELCI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006289 734 LDDPLSAVDTHVGKHIFNkvvGPNGLLSGK-TRILVTHGIHFLPQV--DEIVVLGKGTILEKGSYS 796
Cdd:PRK09580 169 LDESDSGLDIDALKIVAD---GVNSLRDGKrSFIIVTHYQRILDYIkpDYVHVLYQGRIVKSGDFT 231
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1266-1474 |
1.71e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 51.05 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDlRGRLTI--IPQDPILFS----- 1338
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA-RARRGIgyLPQEASIFRrlsvy 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1339 GNLRMNLDPFNKYSDEEIW-RALELAHlksfvaglQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAV 1417
Cdd:PRK10895 97 DNLMAVLQIRDDLSAEQREdRANELME--------EFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006289 1418 D----LETDSLIQtTIRNefSQCTVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEELLSN 1474
Cdd:PRK10895 169 DpisvIDIKRIIE-HLRD--SGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
604-807 |
1.98e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 51.39 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG---------------SIAYVPQQAWIQ--NGTIK 666
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpidysrkglmklreSVGMVFQDPDNQlfSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 667 DNILFGS---EYDEKKYQRVIEacallpdlEMLPGGDMAEIGEKGIN-LSGGQKHRVSLARATYQDADIYILDDPLSAVD 742
Cdd:PRK13636 102 QDVSFGAvnlKLPEDEVRKRVD--------NALKRTGIEHLKDKPTHcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006289 743 ThVGKHIFNKVVGPNGLLSGKTRILVTHGIHFLP-QVDEIVVLGKGTILEKGSYSDLMDKKGVFAK 807
Cdd:PRK13636 174 P-MGVSEIMKLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEKEMLRK 238
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
604-798 |
2.00e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.09 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG--------------SIAYVPQQ-AWIQNGTIKDN 668
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhklaaqlGIGIIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 669 ILFGSE----------YDEKKYQRVIEACALLPDLEMlpggdmaEIGEKGINLSGGQKHRVSLARATYQDADIYILDDPL 738
Cdd:PRK09700 101 LYIGRHltkkvcgvniIDWREMRVRAAMMLLRVGLKV-------DLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006289 739 SAVDTHVGKHIFNKVvgpNGLLS-GKTRILVTHGIHFLPQV-DEIVVLGKGTILEKGSYSDL 798
Cdd:PRK09700 174 SSLTNKEVDYLFLIM---NQLRKeGTAIVYISHKLAEIRRIcDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1265-1445 |
2.12e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 50.94 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1265 LVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFR---ILESAGGQiiidgidiASIGLHD------------LRGRLTI 1329
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGFRVE--------GKVTFHGknlyapdvdpveVRRRIGM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1330 IPQDPILFSGNLRMNLD---PFNKYS---DEEIWRALELAHLKSFVAglqlgllHEVTEGGDNLSIGQRQLLCLGRAVLR 1403
Cdd:PRK14243 96 VFQKPNPFPKSIYDNIAygaRINGYKgdmDELVERSLRQAALWDEVK-------DKLKQSGLSLSGGQQQRLCIARAIAV 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 569006289 1404 KSKILVLDEATAAVD----LETDSLIQTTIRnefsQCTVITIAHRL 1445
Cdd:PRK14243 169 QPEVILMDEPCSALDpistLRIEELMHELKE----QYTIIIVTHNM 210
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
977-1068 |
2.29e-06 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 51.32 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 977 FGALGIAQGIF-LLSSSLWSIYACRNASKtLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDD----TLPQTLRS 1051
Cdd:cd18577 53 FVYLGIGSFVLsYIQTACWTITGERQARR-IRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDgigeKLGLLIQS 131
|
90 100
....*....|....*....|....*
gi 569006289 1052 WLLCFFGIVS--------TLVMICM 1068
Cdd:cd18577 132 LSTFIAGFIIafiyswklTLVLLAT 156
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1266-1473 |
2.40e-06 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 50.54 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTIIPQDPIL-FSGN---- 1340
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTveev 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1341 LRMNLDPF---NKYSDEEIWRALELAHLksfvAGLQLGLLHEvteggdnLSIGQRQLLCLGRaVL-------RKSKILVL 1410
Cdd:PRK13548 97 VAMGRAPHglsRAEDDALVAAALAQVDL----AHLAGRDYPQ-------LSGGEQQRVQLAR-VLaqlwepdGPPRWLLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006289 1411 DEATAAVDLETDSLIQTTIRN--EFSQCTVITIAHRLH-TIMDSDKIMVLDSGKIVEYGSPEELLS 1473
Cdd:PRK13548 165 DEPTSALDLAHQHHVLRLARQlaHERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
532-804 |
2.46e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.90 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 532 SITLFnILRFPL----AMLPMVISsviqASVSVDRLEQY-LGSDDLDLSAIRHVCHFdKAVQFSEASFTWDrDLEATIQD 606
Cdd:PRK10522 269 SLTLL-FLRTPLlsavGALPTLLS----AQVAFNKLNKLaLAPYKAEFPRPQAFPDW-QTLELRNVTFAYQ-DNGFSVGP 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 607 VNLDIKPGQLVAVVGTVGSGKSSLisAML--GEMENVHGHITIKGS-IAYVPQQAWIQ--NGTIKDNILF-------GSE 674
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTL--AMLltGLYQPQSGEILLDGKpVTAEQPEDYRKlfSAVFTDFHLFdqllgpeGKP 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 675 YDEKKYQRVIEACALLPDLEmLPGGDMAEIgekgiNLSGGQKHRVSLARATYQDADIYILDDPLSAVDTHVgKHIFNKVV 754
Cdd:PRK10522 420 ANPALVEKWLERLKMAHKLE-LEDGRISNL-----KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF-RREFYQVL 492
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 569006289 755 GPNGLLSGKTRILVTHGIHFLPQVDEIVVLGKGTILE-KGSYSDLMDKKGV 804
Cdd:PRK10522 493 LPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDAASRDAV 543
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
976-1069 |
2.76e-06 |
|
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: 50.98 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 976 VFGALGiaqGIFLLSS--SLWSIYACRNAS----KTLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDTLPQT- 1048
Cdd:cd18573 43 FALALL---GVFVVGAaaNFGRVYLLRIAGerivARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNl 119
|
90 100 110
....*....|....*....|....*....|..
gi 569006289 1049 ---LRSWLLCFFGI-----VS---TLVMICMA 1069
Cdd:cd18573 120 sdgLRSLVSGVGGIgmmlyISpklTLVMLLVV 151
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
601-807 |
3.49e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 50.73 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 601 EATIQ---DVNLDIKPGQLVAVVGTVGSGKSSLiSAMLGEMEN-VHGHITIKGSIAYVPQQAWIQNGTIKDNILF----G 672
Cdd:PRK11308 25 ERLVKaldGVSFTLERGKTLAVVGESGCGKSTL-ARLLTMIETpTGGELYYQGQDLLKADPEAQKLLRQKIQIVFqnpyG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 673 SEYDEKKYQRVIEAcALLPD------------LEMlpggdMAEIGEKGIN-------LSGGQKHRVSLARATYQDADIYI 733
Cdd:PRK11308 104 SLNPRKKVGQILEE-PLLINtslsaaerrekaLAM-----MAKVGLRPEHydryphmFSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 734 LDDPLSAVDTHVGKHIFNkvvgpngLLS------GKTRILVTHGIHFLPQV-DEIVVLGKGTILEKGsysdlmDKKGVFA 806
Cdd:PRK11308 178 ADEPVSALDVSVQAQVLN-------LMMdlqqelGLSYVFISHDLSVVEHIaDEVMVMYLGRCVEKG------TKEQIFN 244
|
.
gi 569006289 807 K 807
Cdd:PRK11308 245 N 245
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1250-1466 |
3.78e-06 |
|
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: 49.50 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELdlVLKGITCNIkSTEKVGVVGRTGAGKSSLTNCLFRILEsAGGQIIIDGIDIASIGLHDLRGRLTI 1329
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTP-PSSGTIRIDGQDVLKQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1330 IPQDPILFSgnlRMNLDPFNKY-----------SDEEIWRALELahlksfvaglqLGLLHEVTEGGDNLSIGQRQLLCLG 1398
Cdd:cd03264 77 LPQEFGVYP---NFTVREFLDYiawlkgipskeVKARVDEVLEL-----------VNLGDRAKKKIGSLSGGMRRRVGIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006289 1399 RAVLRKSKILVLDEATAAVDLETdsliQTTIRNEFSQC----TVITIAHRLHTIMDS-DKIMVLDSGKIVEYG 1466
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEE----RIRFRNLLSELgedrIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
597-737 |
4.00e-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: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 597 DRDLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS--------------IAYVPQ----QA 658
Cdd:COG3845 268 DRGVPA-LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsprerrrlgVAYIPEdrlgRG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 659 WIQNGTIKDNILFGSeYDEKKYQR-------VIEACA--LLPDLEMLPGGDMAEIGekgiNLSGG--QKhrVSLARATYQ 727
Cdd:COG3845 347 LVPDMSVAENLILGR-YRRPPFSRggfldrkAIRAFAeeLIEEFDVRTPGPDTPAR----SLSGGnqQK--VILARELSR 419
|
170
....*....|
gi 569006289 728 DADIYILDDP 737
Cdd:COG3845 420 DPKLLIAAQP 429
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1387-1474 |
4.87e-06 |
|
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: 49.65 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1387 LSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIR---NEFSQCTVItIAHRLHTIMD-SDKIMVLDSGKI 1462
Cdd:cd03296 137 LSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRrlhDELHVTTVF-VTHDQEEALEvADRVVVMNKGRI 215
|
90
....*....|..
gi 569006289 1463 VEYGSPEELLSN 1474
Cdd:cd03296 216 EQVGTPDEVYDH 227
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1248-1475 |
5.70e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 50.01 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1248 GEIQFNNYQVRYRPELDLVLKGI---TCNIKSTEKVGVVGRTGAGKSS---LTNCLfrILESAGGQIIIDGIDIASIG-- 1319
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFEFKALnntSLTFKKNKVTCVIGTTGSGKSTmiqLTNGL--IISETGQTIVGDYAIPANLKki 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1320 --LHDLRGRLTIIPQDP--ILFSGNLRMNL--DPFNKYSD-EEIWRAL-ELAHLKSFVAglqlgllHEVTEGGDNLSIGQ 1391
Cdd:PRK13645 83 keVKRLRKEIGLVFQFPeyQLFQETIEKDIafGPVNLGENkQEAYKKVpELLKLVQLPE-------DYVKRSPFELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1392 RQLLCLGRAVLRKSKILVLDEATAAVDLE-TDSLIQTTIR-NEFSQCTVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSP 1468
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKgEEDFINLFERlNKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSP 235
|
....*..
gi 569006289 1469 EELLSNM 1475
Cdd:PRK13645 236 FEIFSNQ 242
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1267-1473 |
6.46e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 49.40 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1267 LKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIaSIGLHDLRG-RLTIIPQDPI---------- 1335
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSYRSqRIRMIFQDPStslnprqris 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1336 -LFSGNLRMNLDPFNKYSDEEIWRALElahlksfvaglQLGLLHE-VTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEA 1413
Cdd:PRK15112 108 qILDFPLRLNTDLEPEQREKQIIETLR-----------QVGLLPDhASYYPHMLAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006289 1414 TAAVDLETDS-LIQTTIR-NEFSQCTVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEELLS 1473
Cdd:PRK15112 177 LASLDMSMRSqLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
978-1222 |
6.84e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 49.82 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 978 GALGIAQGIFLLSSSLWSIYACRnasktlhRQLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDtlpqTLRSWLLCFF 1057
Cdd:cd18564 68 GLASYAGTYLTALVGQRVVLDLR-------RDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQD----LLVSGVLPLL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1058 GIVSTLV-MICMAtpifiiiiiplsiLYVSVQ----------VFYVATSRQLRRLDSVTK------SPIYSHFSETVSGL 1120
Cdd:cd18564 137 TNLLTLVgMLGVM-------------FWLDWQlalialavapLLLLAARRFSRRIKEASReqrrreGALASVAQESLSAI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1121 PVIRAF----EHQQRFLANSEKQIDTNQKcvfswitSNRwLAIRLELVGNLIVFCsALLLVIY-------KNSLT-GDTV 1188
Cdd:cd18564 204 RVVQAFgreeHEERRFARENRKSLRAGLR-------AAR-LQALLSPVVDVLVAV-GTALVLWfgawlvlAGRLTpGDLL 274
|
250 260 270
....*....|....*....|....*....|....*.
gi 569006289 1189 GFV--LSNALNITQTlnwLVRMTSEVETNIVAVERI 1222
Cdd:cd18564 275 VFLayLKNLYKPVRD---LAKLTGRIAKASASAERV 307
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1257-1474 |
6.88e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 49.69 E-value: 6.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1257 VRYR-PELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILE--SAGGQIIIDGIDIASIGLHDLRGRLTIIPQD 1333
Cdd:PRK13639 7 LKYSyPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKptSGEVLIKGEPIKYDKKSLLEVRKTVGIVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1334 P--ILFSGNLRMNL--DPFN-KYSDEEIWRALELAHLKSFVAGLQLGLLHevteggdNLSIGQRQLLCLGRAVLRKSKIL 1408
Cdd:PRK13639 87 PddQLFAPTVEEDVafGPLNlGLSKEEVEKRVKEALKAVGMEGFENKPPH-------HLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569006289 1409 VLDEATAAVDLETDSLIQTTIRNEFSQ-CTVITIAHRLHTI-MDSDKIMVLDSGKIVEYGSPEELLSN 1474
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNKEgITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1283-1473 |
7.37e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 49.24 E-value: 7.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1283 VGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTIIPQDPILFSG-NLR----------MNLdpFNKY 1351
Cdd:PRK11231 34 IGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRelvaygrspwLSL--WGRL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1352 SDEE---IWRALELAHLKSFVAglqlgllHEVTEggdnLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDL----ETDSL 1424
Cdd:PRK11231 112 SAEDnarVNQAMEQTRINHLAD-------RRLTD----LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDInhqvELMRL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569006289 1425 IQttirnEFSQC--TVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEELLS 1473
Cdd:PRK11231 181 MR-----ELNTQgkTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
578-800 |
7.46e-06 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 50.45 E-value: 7.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 578 RHVCHFdKAVQfseasftwdrdleatiqDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGeMENVHGHITIKG-SIAYVPQ 656
Cdd:COG4172 294 RTVGHV-KAVD-----------------GVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGqDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 657 QAW------IQ------NG------TIKDNI-----LFGSEYDEK-KYQRVIEAcallpdlemlpggdMAEIG------- 705
Cdd:COG4172 355 RALrplrrrMQvvfqdpFGslsprmTVGQIIaeglrVHGPGLSAAeRRARVAEA--------------LEEVGldpaarh 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 706 ----EkginLSGGQKHRVSLARATYQDADIYILDDPLSAVDTHVGKHIFNkvvgpngLLS------GKTRILVTHGIHFL 775
Cdd:COG4172 421 ryphE----FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILD-------LLRdlqrehGLAYLFISHDLAVV 489
|
250 260
....*....|....*....|....*.
gi 569006289 776 PQV-DEIVVLGKGTILEKGSYSDLMD 800
Cdd:COG4172 490 RALaHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
974-1222 |
7.87e-06 |
|
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: 49.37 E-value: 7.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 974 IGVFGALGIAQGIFLLSSSLWSIYACRNASKTLHRQLLTNILRAPMSFFDTTPTGRIVNRFaGDISTVDDTLPQTLRSWL 1053
Cdd:cd18570 45 SIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTTISLF 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1054 LCFFGIVSTLVMICMATPIFIIIIIPLSILYVSVQVFYVATSRQLRRLDSVTKSPIYSHFSETVSGLPVIRAFEHQQRFL 1133
Cdd:cd18570 124 LDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1134 ANSEKQIDTNQKCVFS---WITSNRWLAIRLELVGNLIVFCSALLLVIyKNSLT-GDTVGFvlsNAL--NITQTLNWLVR 1207
Cdd:cd18570 204 KKIEKKFSKLLKKSFKlgkLSNLQSSIKGLISLIGSLLILWIGSYLVI-KGQLSlGQLIAF---NALlgYFLGPIENLIN 279
|
250
....*....|....*
gi 569006289 1208 MTSEVETNIVAVERI 1222
Cdd:cd18570 280 LQPKIQEAKVAADRL 294
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1385-1471 |
9.43e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 49.72 E-value: 9.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1385 DNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRnEFSQCTVITIAHRLHTIMD----SDKIMVLDSG 1460
Cdd:PRK11432 135 DQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIR-ELQQQFNITSLYVTHDQSEafavSDTVIVMNKG 213
|
90
....*....|.
gi 569006289 1461 KIVEYGSPEEL 1471
Cdd:PRK11432 214 KIMQIGSPQEL 224
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
606-742 |
9.94e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.51 E-value: 9.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 606 DVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS--------------IAYVPQqawiqnG-------- 663
Cdd:NF033858 19 DVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGdmadarhrravcprIAYMPQ------Glgknlypt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 664 -TIKDNI-----LFGSEYDEKKyQRVIE---ACALLPDLEMlPGGdmaeigekgiNLSGGQKHRVSLARATYQDADIYIL 734
Cdd:NF033858 93 lSVFENLdffgrLFGQDAAERR-RRIDEllrATGLAPFADR-PAG----------KLSGGMKQKLGLCCALIHDPDLLIL 160
|
....*...
gi 569006289 735 DDPLSAVD 742
Cdd:NF033858 161 DEPTTGVD 168
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1387-1471 |
1.01e-05 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 49.45 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1387 LSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRN--EFSQCTVITIAHRLHTIMD-SDKIMVLDSGKIV 1463
Cdd:PRK11607 150 LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDilERVGVTCVMVTHDQEEAMTmAGRIAIMNRGKFV 229
|
....*...
gi 569006289 1464 EYGSPEEL 1471
Cdd:PRK11607 230 QIGEPEEI 237
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1388-1479 |
1.01e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 49.34 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1388 SIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQT---TIRNEFSQcTVITIAHRLHTIMDS-DKIMVLDSGKIV 1463
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTllnELKREFNT-AIIMITHDLGVVAGIcDKVLVMYAGRTM 241
|
90
....*....|....*.
gi 569006289 1464 EYGSPEELlsnmgpFY 1479
Cdd:PRK09473 242 EYGNARDV------FY 251
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
604-788 |
1.20e-05 |
|
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: 47.32 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLgemENVHGHITIKGSIAYVPQQAwiqngtikdnILFGSeydekkYQRV 683
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL---YASGKARLISFLPKFSRNKL----------IFIDQ------LQFL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 684 IEAcallpDLEMLPggdmaeIGEKGINLSGGQKHRVSLARATYQDAD--IYILDDPLSAVDTHVGKHIFNKVvgpNGLLS 761
Cdd:cd03238 72 IDV-----GLGYLT------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVI---KGLID 137
|
170 180
....*....|....*....|....*...
gi 569006289 762 -GKTRILVTHGIHFLPQVDEIVVLGKGT 788
Cdd:cd03238 138 lGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
979-1222 |
1.28e-05 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 48.97 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 979 ALGIAQGIFLLSSSLWSIYACRNASKTLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDTL----PQTLRSWLL 1054
Cdd:cd18542 47 GVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLafglVELVRAVLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1055 CFFGIVS--------TLVMICMATpifiiiiiplSILYVSVQVF------YVATSRQLRRLDSVTKspiyshfsETVSGL 1120
Cdd:cd18542 127 FIGALIImfsinwklTLISLAIIP----------FIALFSYVFFkkvrpaFEEIREQEGELNTVLQ--------ENLTGV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1121 PVIRAF---EHQ-QRFLANSEKQIDTNqkcvfswITSNRWLAIRLELvGNLIVFCSALLLVIY------KNSLT-GDTVG 1189
Cdd:cd18542 189 RVVKAFareDYEiEKFDKENEEYRDLN-------IKLAKLLAKYWPL-MDFLSGLQIVLVLWVggylviNGEITlGELVA 260
|
250 260 270
....*....|....*....|....*....|....*..
gi 569006289 1190 FVLsnalnITQTLNWLVRM----TSEVETNIVAVERI 1222
Cdd:cd18542 261 FIS-----YLWMLIWPVRQlgrlINDMSRASASAERI 292
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1387-1465 |
1.54e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.23 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1387 LSIGQRQLLCLGRAVLRKSKILVLDEATAAV-DLETDSLIQtTIRNEFSQ-CTVITIAHRLHTIMD-SDKIMVLDSGK-I 1462
Cdd:PRK10762 142 LSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFR-VIRELKSQgRGIVYISHRLKEIFEiCDDVTVFRDGQfI 220
|
...
gi 569006289 1463 VEY 1465
Cdd:PRK10762 221 AER 223
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1266-1472 |
1.70e-05 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 47.52 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLfrilesaggqiiidgidiasIGLHDLRgrltiIPQDPILFSGNLRMNL 1345
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI--------------------MGHPKYE-----VTEGEILFKGEDITDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1346 DPfnkysDEeiwRALELAHLkSF-----VAGLQLG-LLHEVTEGgdnLSIGQR------QLLCLgravlrKSKILVLDEA 1413
Cdd:cd03217 70 PP-----EE---RARLGIFL-AFqyppeIPGVKNAdFLRYVNEG---FSGGEKkrneilQLLLL------EPDLAILDEP 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006289 1414 TAAVDLETDSLIQTTI---RNEFSQCTVITIAHRLHTIMDSDKIMVLDSGKIVEYGSPEELL 1472
Cdd:cd03217 132 DSGLDIDALRLVAEVInklREEGKSVLIITHYQRLLDYIKPDRVHVLYDGRIVKSGDKELAL 193
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
606-740 |
1.71e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.16 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 606 DVNLDIKPGQLVAVVGTVGSGKSSLISAMLGemenVH------GHITIKGS--------------IAYVPQQ-AWIQNGT 664
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSG----VYphgtyeGEIIFEGEelqasnirdteragIAIIHQElALVKELS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 665 IKDNILFGSEY-------DEKKYQRvieACALLPDLEMlpggDMaEIGEKGINLSGGQKHRVSLARATYQDADIYILDDP 737
Cdd:PRK13549 99 VLENIFLGNEItpggimdYDAMYLR---AQKLLAQLKL----DI-NPATPVGNLGLGQQQLVEIAKALNKQARLLILDEP 170
|
...
gi 569006289 738 LSA 740
Cdd:PRK13549 171 TAS 173
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
606-798 |
1.81e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.20 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 606 DVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHIT-----------------IKGSIAYVPQQAWIQ--NGTIK 666
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRvddtlitstsknkdikqIRKKVGLVFQFPESQlfEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 667 DNILFGSE----YDEKKYQRVIEACALLpdlemlpgGDMAEIGEKG-INLSGGQKHRVSLARATYQDADIYILDDPLSAV 741
Cdd:PRK13649 105 KDVAFGPQnfgvSQEEAEALAREKLALV--------GISESLFEKNpFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569006289 742 DTHVGKH---IFNKVvgpngLLSGKTRILVTHGIHFLPQ-VDEIVVLGKGTILEKGSYSDL 798
Cdd:PRK13649 177 DPKGRKElmtLFKKL-----HQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
271-563 |
1.95e-05 |
|
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: 48.21 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 271 VILKSFILKLAHDILLFLNPQLLKFLIGFV---KDPDSYpwvgYIYAILMFSVTLIQSFFLqcYFQ--FCFVLGMTVRTT 345
Cdd:cd18570 3 LLILILLLSLLITLLGIAGSFFFQILIDDIipsGDINLL----NIISIGLILLYLFQSLLS--YIRsyLLLKLSQKLDIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 346 IIASVYKKALTL--SNLARRQytIGEtvnLMSvdsqKLMDVTNYIHLLWSSVLQIALSIFflwrelgpSILAGVGLM--- 420
Cdd:cd18570 77 LILGYFKHLLKLplSFFETRK--TGE---IIS----RFNDANKIREAISSTTISLFLDLL--------MVIISGIILffy 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 421 --------VLLVPVNGVLA----TKIRKIQVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFKEQVNSIRKKELRNLLR 488
Cdd:cd18570 140 nwklflitLLIIPLYILIIllfnKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFK 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569006289 489 FSQLQTILIFILHLTPTLVSVITF---SVYVLvdsQNVLNAEKAFTSITLFNILRFPLAMLPMVISSVIQASVSVDRL 563
Cdd:cd18570 220 LGKLSNLQSSIKGLISLIGSLLILwigSYLVI---KGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
610-803 |
1.98e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.80 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 610 DIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-SIAYVPQQawiqngtikdnilfgseydekkyqrvieaca 688
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQY------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 689 llpdlemlpggdmaeigekgINLSGGQKHRVSLARATYQDADIYILDDPLSAVDTHVGKHIfNKVVGPNGLLSGKTRILV 768
Cdd:cd03222 70 --------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNA-ARAIRRLSEEGKKTALVV 128
|
170 180 190
....*....|....*....|....*....|....*
gi 569006289 769 THGIHFLPQVDEIVVLGKGtilEKGSYSDLMDKKG 803
Cdd:cd03222 129 EHDLAVLDYLSDRIHVFEG---EPGVYGIASQPKG 160
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
604-741 |
2.35e-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: 48.67 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGemenVHGHITIKGSIAYVPQQ---------------------AWIQN 662
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSG----VYPHGTWDGEIYWSGSPlkasnirdteragiviihqelTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 663 GTIKDNILFGSEYDEK----KYQRVIEAC-ALLPDLEMLPGGDMAEIGEKGinlsGGQKHRVSLARATYQDADIYILDDP 737
Cdd:TIGR02633 93 LSVAENIFLGNEITLPggrmAYNAMYLRAkNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEP 168
|
....
gi 569006289 738 LSAV 741
Cdd:TIGR02633 169 SSSL 172
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
604-753 |
2.75e-05 |
|
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: 46.87 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGemeNVHGHITIKGSIAYVPQQAWIQNGTIKDNILFGSEYDEK----K 679
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHfptlT 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006289 680 YQRVIEACALLPDLEMLPGgdmaeigekginLSGGQKHRVSLARATYQDADIYILDDPLSAVDTHVGKHIFNKV 753
Cdd:cd03233 100 VRETLDFALRCKGNEFVRG------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCI 161
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
599-737 |
2.76e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.73 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 599 DLEATIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHI--TIKGSIAYVPQ--QAWIQNgtikDNILF--- 671
Cdd:PRK15064 330 DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwSENANIGYYAQdhAYDFEN----DLTLFdwm 405
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569006289 672 ---GSEYDEKKYQRVIEAcallpdlEMLPGGDmaEIGEKGINLSGGQKHRVSLARATYQDADIYILDDP 737
Cdd:PRK15064 406 sqwRQEGDDEQAVRGTLG-------RLLFSQD--DIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
960-1178 |
3.31e-05 |
|
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: 47.48 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 960 QNGTDNSPSQRDMRI-----GVFGALGIAQGIFLLSSSLWSIYACRNASKTLHRQLLTNILRAPMSFFDTTPTGRIVNRF 1034
Cdd:cd18546 23 RYGIDSGVRAGDLGVlllaaAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1035 AGDISTV----DDTLPQTLRSwLLCFFGIVSTLV-------MICMAtpifiiiiiplsilyvSVQVFYVATsRQLRRLDS 1103
Cdd:cd18546 103 TSDIDALsellQTGLVQLVVS-LLTLVGIAVVLLvldprlaLVALA----------------ALPPLALAT-RWFRRRSS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1104 V-------TKSPIYSHFSETVSGLPVIRAF----EHQQRFLANSEKQIDTNqkcvfswITSNRWLAIR---LELVGNLiv 1169
Cdd:cd18546 165 RayrrareRIAAVNADLQETLAGIRVVQAFrrerRNAERFAELSDDYRDAR-------LRAQRLVAIYfpgVELLGNL-- 235
|
....*....
gi 569006289 1170 fCSALLLVI 1178
Cdd:cd18546 236 -ATAAVLLV 243
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
606-750 |
3.85e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.19 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 606 DVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG-SIAYVPQQAWIQNG--------------TIKDNIL 670
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkEIDFKSSKEALENGismvhqelnlvlqrSVMDNMW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 671 FGsEY-------DEKKYQRVIEACALLPDLEMLPggdmaeiGEKGINLSGGQKHRVSLARATYQDADIYILDDPLSAVDT 743
Cdd:PRK10982 96 LG-RYptkgmfvDQDKMYRDTKAIFDELDIDIDP-------RAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTE 167
|
....*..
gi 569006289 744 HVGKHIF 750
Cdd:PRK10982 168 KEVNHLF 174
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1270-1462 |
3.87e-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: 47.90 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1270 ITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIG--LHDLRGRLTIIPQD-------PILFSGN 1340
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINGKPVDIRnpAQAIRAGIAMVPEDrkrhgivPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1341 lRMNLDPFNKYS-----DEE-----IWRALELAHLKSFVAGLQLGllhevteggdNLSIGQRQLLCLGRAVLRKSKILVL 1410
Cdd:TIGR02633 359 -NITLSVLKSFCfkmriDAAaelqiIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 569006289 1411 DEATAAVDLETDSLIQTTIrNEFSQ--CTVITIAHRLHTIMD-SDKIMVLDSGKI 1462
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLI-NQLAQegVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1265-1465 |
4.02e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 48.14 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1265 LVLKGITCNIKSTEKVGVVGRTGAGKSSltncLFRILesaggqiiidgidiasIG-LHDLRGRLTI--------IPQDpi 1335
Cdd:COG0488 329 TLLDDLSLRIDRGDRIGLIGPNGAGKST----LLKLL----------------AGeLEPDSGTVKLgetvkigyFDQH-- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1336 lfSGNLRMNLDPFnkysdEEIWRALELA---HLKSFVAGLQLgllhevteGGD-------NLSIGQRQLLCLGRAVLRKS 1405
Cdd:COG0488 387 --QEELDPDKTVL-----DELRDGAPGGteqEVRGYLGRFLF--------SGDdafkpvgVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569006289 1406 KILVLDEATAAVDLET-----DSLiqttirNEFsQCTVITIAH-R--LHTImdSDKIMVLDSGKIVEY 1465
Cdd:COG0488 452 NVLLLDEPTNHLDIETlealeEAL------DDF-PGTVLLVSHdRyfLDRV--ATRILEFEDGGVREY 510
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1250-1466 |
4.84e-05 |
|
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: 46.12 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELdlVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDL------ 1323
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIgylpee 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1324 RG---RLTIIPQdpILFSGNLR-MNLDPFNKYSDEEIWRaLELAHLKSFVAglqlgllhevteggDNLSIGQRQLLCLGR 1399
Cdd:cd03269 79 RGlypKMKVIDQ--LVYLAQLKgLKKEEARRRIDEWLER-LELSEYANKRV--------------EELSKGNQQKVQFIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569006289 1400 AVLRKSKILVLDEATAAVDLETDSLIQTTIRNEFSQ-CTVITIAHRLHTIMD-SDKIMVLDSGKIVEYG 1466
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1386-1461 |
5.11e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.62 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1386 NLSIGQRQLLCLGRAVLRKSKILVLDEATAAV-DLETDSL--IQTTIRNEFSQCtvITIAHRLHTIMD-SDKIMVLDSGK 1461
Cdd:PRK13549 143 NLGLGQQQLVEIAKALNKQARLLILDEPTASLtESETAVLldIIRDLKAHGIAC--IYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1385-1472 |
5.15e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 46.70 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1385 DNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDL----ETDSLIQTtirneFSQCTVITIAHRLHTI-MDS---DKIMV 1456
Cdd:PRK10575 146 DSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIahqvDVLALVHR-----LSQERGLTVIAVLHDInMAArycDYLVA 220
|
90
....*....|....*.
gi 569006289 1457 LDSGKIVEYGSPEELL 1472
Cdd:PRK10575 221 LRGGEMIAQGTPAELM 236
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1266-1473 |
5.52e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 46.52 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTIIPQDPILFSGNLRMNL 1345
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1346 DPFNKYSDEEI---WRALELAHLKSfvAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDL--E 1420
Cdd:PRK10253 102 VARGRYPHQPLftrWRKEDEEAVTK--AMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIshQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 1421 TDSLiqtTIRNEFSQCTVITIAHRLHTIMDSDK----IMVLDSGKIVEYGSPEELLS 1473
Cdd:PRK10253 180 IDLL---ELLSELNREKGYTLAAVLHDLNQACRyashLIALREGKIVAQGAPKEIVT 233
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1387-1464 |
7.06e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.21 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1387 LSIGQRQLLCLGRAVLRKSKILVLDEATAAVDL-ETDSLIQtTIRNEFSQCTVIT-IAHRLHTIMD-SDKIMVLDSGKIV 1463
Cdd:PRK11288 141 LSIGQRQMVEIAKALARNARVIAFDEPTSSLSArEIEQLFR-VIRELRAEGRVILyVSHRMEEIFAlCDAITVFKDGRYV 219
|
.
gi 569006289 1464 E 1464
Cdd:PRK11288 220 A 220
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1250-1474 |
7.88e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 46.27 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYRPELDlVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDLRGRLTI 1329
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1330 IPQDP--ILFS---------GNLRMNLDPfnKYSDEEIWRALELAHLKSFvaglqlgllheVTEGGDNLSIGQRQLLCLG 1398
Cdd:PRK13647 84 VFQDPddQVFSstvwddvafGPVNMGLDK--DEVERRVEEALKAVRMWDF-----------RDKPPYHLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1399 RAVLRKSKILVLDEATAAVDLE-TDSLiqTTIRNEFSQ--CTVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPeELLSN 1474
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRgQETL--MEILDRLHNqgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDK-SLLTD 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1387-1466 |
8.94e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 45.78 E-value: 8.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1387 LSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRnEFSQcTVIT---------IAHRLHTimdsdKIMVL 1457
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIR-ELAE-TGITqvivtheveVARKTAS-----RVVYM 214
|
....*....
gi 569006289 1458 DSGKIVEYG 1466
Cdd:PRK11124 215 ENGHIVEQG 223
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1266-1470 |
1.18e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 45.46 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILEsaggqiiidgidiASIGLHDLRGRLTiipqdPIL--------- 1336
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILE-------------PTSGRVEVNGRVS-----ALLelgagfhpe 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1337 FSG--NLRMNLDpFNKYSDEEIwRALeLAHLKSFvAGLqlgllhevtegGD-------NLSIGQRQLLCLGRAVLRKSKI 1407
Cdd:COG1134 103 LTGreNIYLNGR-LLGLSRKEI-DEK-FDEIVEF-AEL-----------GDfidqpvkTYSSGMRARLAFAVATAVDPDI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569006289 1408 LVLDEATAAVDLE-----TDSLiqttirNEFSQ--CTVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEE 1470
Cdd:COG1134 168 LLVDEVLAVGDAAfqkkcLARI------RELREsgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEE 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1278-1474 |
1.24e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.77 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1278 EKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIG---LHDLRGRLTIIPQDPIlfsgnlrMNLDPFNK--YS 1352
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY-------ASLDPRQTvgDS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1353 DEEIWRALELAHLKSF---VAGL--QLGLLHE-VTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQ 1426
Cdd:PRK10261 424 IMEPLRVHGLLPGKAAaarVAWLleRVGLLPEhAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQII 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569006289 1427 T---TIRNEFSqCTVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEELLSN 1474
Cdd:PRK10261 504 NlllDLQRDFG-IAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFEN 554
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1386-1470 |
1.34e-04 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 46.09 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1386 NLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLEtdslIQTTIRNEFSQ------CTVITIAH-RLHTIMDSDKIMVLD 1458
Cdd:PRK09452 144 QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK----LRKQMQNELKAlqrklgITFVFVTHdQEEALTMSDRIVVMR 219
|
90
....*....|..
gi 569006289 1459 SGKIVEYGSPEE 1470
Cdd:PRK09452 220 DGRIEQDGTPRE 231
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1250-1461 |
1.49e-04 |
|
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: 43.59 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1250 IQFNNYQVRYrpELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLtnclfrilesaggqiiidgidiasigLHDLRGRLTI 1329
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTL--------------------------LKLIAGELEP 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1330 IPQDPILFSGnlrmnldpfnkysdeeiwraLELAHLksfvaglqlgllhevteggDNLSIGQRQLLCLGRAVLRKSKILV 1409
Cdd:cd03221 53 DEGIVTWGST--------------------VKIGYF-------------------EQLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 569006289 1410 LDEATAAVDLETDSLIQTTIRNEfsQCTVITIAHRlHTIMDS--DKIMVLDSGK 1461
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEY--PGTVILVSHD-RYFLDQvaTKIIELEDGK 144
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
593-671 |
1.54e-04 |
|
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: 44.54 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 593 SFTWdRDLEATI----------QDVNLDIKPGQLVAVVGTVGSGKSSL--ISAMLGEMENVHGHITIKG---------SI 651
Cdd:cd03232 3 VLTW-KNLNYTVpvkggkrqllNNISGYVKPGTLTALMGESGAGKTTLldVLAGRKTAGVITGEILINGrpldknfqrST 81
|
90 100
....*....|....*....|.
gi 569006289 652 AYVPQQ-AWIQNGTIKDNILF 671
Cdd:cd03232 82 GYVEQQdVHSPNLTVREALRF 102
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
593-794 |
1.71e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 45.18 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 593 SFTWDRDLEAtIQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS-------------IAYVPQQA- 658
Cdd:PRK13652 10 CYSYSGSKEA-LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfVGLVFQNPd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 659 -WIQNGTIKDNILFGS---EYDEKKYQ-RVIEAcallpdLEMLPGGDMAEIGEKgiNLSGGQKHRVSLARATYQDADIYI 733
Cdd:PRK13652 89 dQIFSPTVEQDIAFGPinlGLDEETVAhRVSSA------LHMLGLEELRDRVPH--HLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006289 734 LDDPLSAVDTHVGKHIFNKVvgpNGLLS--GKTRILVTHGIHFLPQV-DEIVVLGKGTILEKGS 794
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFL---NDLPEtyGMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGT 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1267-1463 |
1.74e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.93 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1267 LKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGI--------DIASIGLHDLRGRLTIIPQDPILfs 1338
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhkLAAQLGIGIIYQELSVIDELTVL-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1339 GNLRMNLDPFNKYSDEEI--WRALElahLKSFVAGLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAA 1416
Cdd:PRK09700 99 ENLYIGRHLTKKVCGVNIidWREMR---VRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 569006289 1417 V-DLETDSL--IQTTIRNEFSqcTVITIAHRLHTIMD-SDKIMVLDSGKIV 1463
Cdd:PRK09700 176 LtNKEVDYLflIMNQLRKEGT--AIVYISHKLAEIRRiCDRYTVMKDGSSV 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1387-1471 |
1.87e-04 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 45.47 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1387 LSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIRN---EFsQCTVITIAHrlhtimD-------SDKIMV 1456
Cdd:COG3842 136 LSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRlqrEL-GITFIYVTH------DqeealalADRIAV 208
|
90
....*....|....*
gi 569006289 1457 LDSGKIVEYGSPEEL 1471
Cdd:COG3842 209 MNDGRIEQVGTPEEI 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
605-646 |
2.01e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 44.92 E-value: 2.01e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 569006289 605 QDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHIT 646
Cdd:PRK11701 23 RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH 64
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
604-789 |
2.05e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.69 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVH-GHITIKGS--------------IAYVP----------QQA 658
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKpvkirnpqqaiaqgIAMVPedrkrdgivpVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 659 WIQNGTIK--DNILFGSEYDEKKYQRVIEAcaLLPDLEMLPGGDMAEIGekgiNLSGGQKHRVSLARATYQDADIYILDD 736
Cdd:PRK13549 358 VGKNITLAalDRFTGGSRIDDAAELKTILE--SIQRLKVKTASPELAIA----RLSGGNQQKAVLAKCLLLNPKILILDE 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006289 737 PLSAVDthVG-KHIFNKVVGPngllsgktriLVTHGIHF------LPQV----DEIVVLGKGTI 789
Cdd:PRK13549 432 PTRGID--VGaKYEIYKLINQ----------LVQQGVAIivisseLPEVlglsDRVLVMHEGKL 483
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1266-1471 |
2.59e-04 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 45.07 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLtnclFRI---LESAGGQIIIDGIDIASiGLHDLRGRLTIIPQDPILF----- 1337
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTL----LRIiagLEHQTSGHIRFHGTDVS-RLHARDRKVGFVFQHYALFrhmtv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1338 SGNLRMNLD-------PFNKYSDEEIWRALELahlksfvagLQLGllHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVL 1410
Cdd:PRK10851 92 FDNIAFGLTvlprrerPNAAAIKAKVTQLLEM---------VQLA--HLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006289 1411 DEATAAVDLETDSLIQTTIRN--EFSQCTVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEEL 1471
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQlhEELKFTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQV 224
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
604-809 |
2.76e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 45.27 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGSIAYVPqqawIQNGTikDNILFGSEYdekkyqrv 683
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIA----ISSGL--NGQLTGIEN-------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 684 IEACALLPDL------EMLPGG-DMAEIGeKGIN-----LSGGQKHRVSLARATYQDADIYILDDPLSAVDTHVGKHIFN 751
Cdd:PRK13545 106 IELKGLMMGLtkekikEIIPEIiEFADIG-KFIYqpvktYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006289 752 KVvgpNGLL-SGKTRILVTHGihfLPQVDEIVV----LGKGTILEKGSYSDLMDKKGVFAKNW 809
Cdd:PRK13545 185 KM---NEFKeQGKTIFFISHS---LSQVKSFCTkalwLHYGQVKEYGDIKEVVDHYDEFLKKY 241
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1141-1465 |
3.05e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.48 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1141 DTNQKCVFSWITSNRWLAIRLELVGNLIVFCSALLLVIYKNSLT--GDTVGFVLSNalnitqtLNWLVRMTSEVETNIVA 1218
Cdd:TIGR00956 654 DDYLKLSFQYYNSHKWRNFGIIIGFTVFFFFVYILLTEFNKGAKqkGEILVFRRGS-------LKRAKKAGETSASNKND 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1219 VERINEYINVD--NEAPWVTDKKPpADWPKKGEIQF---NNYQVRYRPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSL 1293
Cdd:TIGR00956 727 IEAGEVLGSTDltDESDDVNDEKD-MEKESGEDIFHwrnLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTL 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1294 TNCL-----------------FRILESAGGQiiidgidiaSIGL---HDLR-GRLTIipQDPILFSGNLR----MNLDPF 1348
Cdd:TIGR00956 806 LNVLaervttgvitggdrlvnGRPLDSSFQR---------SIGYvqqQDLHlPTSTV--RESLRFSAYLRqpksVSKSEK 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1349 NKYSDEEIwRALELAHLKSFVAGLQlgllhevtegGDNLSIGQRQLLCLGRAVLRKSKILV-LDEATAAVDLETDSLIQT 1427
Cdd:TIGR00956 875 MEYVEEVI-KLLEMESYADAVVGVP----------GEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICK 943
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 569006289 1428 TIRN--EFSQCTVITIAHRLHTIMDS-DKIMVLDSGKIVEY 1465
Cdd:TIGR00956 944 LMRKlaDHGQAILCTIHQPSAILFEEfDRLLLLQKGGQTVY 984
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
604-794 |
3.68e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.08 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLgEMENVHGHITIKGSiayvPQQAW-----------IQ------NG--- 663
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTGLALL-RLINSQGEIWFDGQ----PLHNLnrrqllpvrhrIQvvfqdpNSsln 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 664 ---TIKDNILFGSEYDEK------KYQRVIEAcallpdlemlpggdMAEIG-------EKGINLSGGQKHRVSLARATYQ 727
Cdd:PRK15134 377 prlNVLQIIEEGLRVHQPtlsaaqREQQVIAV--------------MEEVGldpetrhRYPAEFSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569006289 728 DADIYILDDPLSAVDTHVGKHIFNKVVGpnglLSGKTR---ILVTHGIHFLPQV-DEIVVLGKGTILEKGS 794
Cdd:PRK15134 443 KPSLIILDEPTSSLDKTVQAQILALLKS----LQQKHQlayLFISHDLHVVRALcHQVIVLRQGEVVEQGD 509
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
1010-1066 |
3.75e-04 |
|
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: 44.22 E-value: 3.75e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 569006289 1010 LLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDTLPQTLRSWLLCFFGIVSTLVMI 1066
Cdd:cd18784 75 LFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFM 131
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
711-770 |
4.51e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 42.35 E-value: 4.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006289 711 LSGGQKHRVSLA----RATYQDADIYILDDPLSAVDTHVGKHIFNKVVGPngLLSGKTRILVTH 770
Cdd:cd03227 78 LSGGEKELSALAlilaLASLKPRPLYILDEIDRGLDPRDGQALAEAILEH--LVKGAQVIVITH 139
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
985-1066 |
4.76e-04 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, 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. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 44.07 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 985 GIFLLSSSLWSIY------ACRNASKTLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDI----STVDDTLPQTLRSWLL 1054
Cdd:cd18574 50 GLYLLQSLLTFAYisllsvVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVqefkSSFKQCVSQGLRSVTQ 129
|
90
....*....|..
gi 569006289 1055 CFFGIVStLVMI 1066
Cdd:cd18574 130 TVGCVVS-LYLI 140
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
974-1126 |
5.37e-04 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 43.63 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 974 IGVFgalgIAQGIFLLSSSLWSIYACRNASKTLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDD----TLPQTL 1049
Cdd:cd18576 43 LGLF----LLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDtlttTLAEFL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1050 RSWLLCFFGIVS--------TLVMICMatpifiiiiiplsilyvsVQVFYVAT---SRQLRRL-----DSVTKSpiYSHF 1113
Cdd:cd18576 119 RQILTLIGGVVLlffiswklTLLMLAT------------------VPVVVLVAvlfGRRIRKLskkvqDELAEA--NTIV 178
|
170
....*....|...
gi 569006289 1114 SETVSGLPVIRAF 1126
Cdd:cd18576 179 EETLQGIRVVKAF 191
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
1005-1222 |
5.66e-04 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 43.61 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1005 TLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDTLPQTLRswLLCFFGIVSTLVMICMATPIFIIIIIPLSILY 1084
Cdd:cd18589 70 RLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLS--LLMWYLARGLFLFIFMLWLSPKLALLTALGLP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1085 VSVQV------FYVATSRQLRrlDSVTKSPIYShfSETVSGLPVIRAFEHQ----QRFLANSEKQIDTNQK-----CVFS 1149
Cdd:cd18589 148 LLLLVpkfvgkFQQSLAVQVQ--KSLARANQVA--VETFSAMKTVRSFANEegeaQRYRQRLQKTYRLNKKeaaayAVSM 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006289 1150 WITSNRWLAIRlelVGnlIVFCSALLLVIYKNSlTGDTVGFVLSNaLNITQTLNWLVRMTSEVETNIVAVERI 1222
Cdd:cd18589 224 WTSSFSGLALK---VG--ILYYGGQLVTAGTVS-SGDLVTFVLYE-LQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1388-1474 |
5.92e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 43.80 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1388 SIGQRQLLCLGRAVLRKSKILVLDEATAAVDLEtdslIQTTIRN-------EFSQCTVItIAHRL----HTimdSDKIMV 1456
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVS----VQAQVLNlmmdlqqELGLSYVF-ISHDLsvveHI---ADEVMV 227
|
90
....*....|....*...
gi 569006289 1457 LDSGKIVEYGSPEELLSN 1474
Cdd:PRK11308 228 MYLGRCVEKGTKEQIFNN 245
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
311-562 |
6.15e-04 |
|
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: 43.54 E-value: 6.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 311 YIYAILMFSVTLIQSFF--LQCYFqfCFVLGMTVRTTIIASVYKKALTLSNlarrqytigETVNLMSVDSqkLM-----D 383
Cdd:cd18548 39 LRTGLLMLLLALLGLIAgiLAGYF--AAKASQGFGRDLRKDLFEKIQSFSF---------AEIDKFGTSS--LItrltnD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 384 VTNyIHLLWSSVLQIAL--------SIFFLWR---ELGPSILAGVGLMVLLVPVNGVLATKI-RKIQvqnmKNKDKRLKI 451
Cdd:cd18548 106 VTQ-VQNFVMMLLRMLVrapimligAIIMAFRinpKLALILLVAIPILALVVFLIMKKAIPLfKKVQ----KKLDRLNRV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 452 MNEILSGIKILKYFAWEP----SFKEQVNSIRKKELRNLLRFSQLQTILIFILHLTptLVSVITFSVYvLVDSQNVLNAE 527
Cdd:cd18548 181 VRENLTGIRVIRAFNREDyeeeRFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLA--IVAILWFGGH-LINAGSLQVGD 257
|
250 260 270
....*....|....*....|....*....|....*.
gi 569006289 528 -KAFTSItLFNILrFPLAMLPMVISSVIQASVSVDR 562
Cdd:cd18548 258 lVAFINY-LMQIL-MSLMMLSMVFVMLPRASASAKR 291
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1267-1463 |
6.37e-04 |
|
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: 44.05 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1267 LKGITCNIKSTEKVGVVGRTGAGKSSLTNCLF----------RILESAGGQIIIDGIDIASIGLHDLRGRLTIIPQDPIL 1336
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSgvyphgtwdgEIYWSGSPLKASNIRDTERAGIVIIHQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1337 ---FSGNlRMNLDPFNKYSDEEIWRALELahlksfVAGLQLGLLHEVTEGGDnLSIGQRQLLCLGRAVLRKSKILVLDEA 1413
Cdd:TIGR02633 97 eniFLGN-EITLPGGRMAYNAMYLRAKNL------LRELQLDADNVTRPVGD-YGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569006289 1414 TAAVDLETDSLIQTTIRN-EFSQCTVITIAHRLHTIMD-SDKIMVLDSGKIV 1463
Cdd:TIGR02633 169 SSSLTEKETEILLDIIRDlKAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
611-796 |
6.62e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 611 IKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG--SIAYVPQQAWIQNGTIKDNILFGS-EYD--EKKYQRVIE 685
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwQLAWVNQETPALPQPALEYVIDGDrEYRqlEAQLHDANE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 686 -------------------------ACALLPDLemlpGGDMAEIGEKGINLSGGQKHRVSLARATYQDADIYILDDPLSA 740
Cdd:PRK10636 104 rndghaiatihgkldaidawtirsrAASLLHGL----GFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNH 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 741 VDthvgkhiFNKVVGPNGLLSG--KTRILVTHGIHFL-PQVDEIVVLGKGTILE-KGSYS 796
Cdd:PRK10636 180 LD-------LDAVIWLEKWLKSyqGTLILISHDRDFLdPIVDKIIHIEQQSLFEyTGNYS 232
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
611-831 |
7.75e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 44.23 E-value: 7.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 611 IKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKG------------SIAYVPQQAWIqngtikDNILFGSEYdek 678
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGksiltnisdvhqNMGYCPQFDAI------DDLLTGREH--- 2032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 679 kyqrvieaCALLPDLEMLPGGDMAEIGEKGIN--------------LSGGQKHRVSLARATYQDADIYILDDPLSAVDTH 744
Cdd:TIGR01257 2033 --------LYLYARLRGVPAEEIEKVANWSIQslglslyadrlagtYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQ 2104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 745 VGKHIFNKVVGPngLLSGKTRILVTHGIHFLPQV-DEIVVLGKGTILEKGSYSDLMDKkgvFAKNWKTFMKHSGPEGEAT 823
Cdd:TIGR01257 2105 ARRMLWNTIVSI--IREGRAVVLTSHSMEECEALcTRLAIMVKGAFQCLGTIQHLKSK---FGDGYIVTMKIKSPKDDLL 2179
|
....*...
gi 569006289 824 VDNDSEEE 831
Cdd:TIGR01257 2180 PDLNPVEQ 2187
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1266-1463 |
9.20e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 43.94 E-value: 9.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTN---CLFRILESAGGQIIIDGIDIASIGLHDLR--------GRLTIIP--- 1331
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNilgCLDKPTSGTYRVAGQDVATLDADALAQLRrehfgfifQRYHLLShlt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1332 -----QDPILFSGNLRmnldpfnkysDEEIWRALELAhlksfvagLQLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSK 1406
Cdd:PRK10535 103 aaqnvEVPAVYAGLER----------KQRLLRAQELL--------QRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 569006289 1407 ILVLDEATAAVDLETDSLIQTTIRNEFSQC-TVITIAHRLHTIMDSDKIMVLDSGKIV 1463
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQLRDRGhTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
1280-1299 |
1.14e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 42.83 E-value: 1.14e-03
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
974-1145 |
1.19e-03 |
|
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: 42.78 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 974 IGVFGALGIAQGIFLLSSSLWSIYACRNASKTLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDTL-PQTLRSW 1052
Cdd:cd18541 43 ALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALgPGILYLV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1053 LLCFFGIVSTLVMIcmatpifiiiiiplsilYVSVQ-----------VFYVAT--SRQLRRL-DSVTKSpiYSHFS---- 1114
Cdd:cd18541 123 DALFLGVLVLVMMF-----------------TISPKltliallplplLALLVYrlGKKIHKRfRKVQEA--FSDLSdrvq 183
|
170 180 190
....*....|....*....|....*....|....*
gi 569006289 1115 ETVSGLPVIRAF----EHQQRFLANSEKQIDTNQK 1145
Cdd:cd18541 184 ESFSGIRVIKAFvqeeAEIERFDKLNEEYVEKNLR 218
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1266-1466 |
1.48e-03 |
|
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: 41.86 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1266 VLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIGLHDlRGrLTIIPQDPILFS-----GN 1340
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-RD-IAMVFQNYALYPhmtvyDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1341 LRMNLDpFNKYSDEEI-WRALELAHLksfvaglqLGLLHEVTEGGDNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVdl 1419
Cdd:cd03301 93 IAFGLK-LRKVPKDEIdERVREVAEL--------LQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNL-- 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 569006289 1420 etDSLIQTTIRNEFS------QCTVITIAHRLHTIMD-SDKIMVLDSGKIVEYG 1466
Cdd:cd03301 162 --DAKLRVQMRAELKrlqqrlGTTTIYVTHDQVEAMTmADRIAVMNDGQIQQIG 213
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
604-753 |
1.51e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 41.47 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 604 IQDVNLDIKPGQLVAVVGTVGSGKSSLISAMLGEMENVHGHITIKGS------IAYVPQQAWI-------QNGTIKDNIL 670
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlCTYQKQLCFVghrsginPYLTLRENCL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 671 FGSEYDEKKYQrVIEACAL--LPDLEMLPGGdmaeigekgiNLSGGQKHRVSLARATYQDADIYILDDPLSAVDTHVGKH 748
Cdd:PRK13540 97 YDIHFSPGAVG-ITELCRLfsLEHLIDYPCG----------LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
....*
gi 569006289 749 IFNKV 753
Cdd:PRK13540 166 IITKI 170
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
276-563 |
1.62e-03 |
|
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: 42.40 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 276 FILKLAHDILLFLNPQLLKFLIGFVKDPDSYPWVGYIYAILMFSVTLIQSFFLQCYFQFCFVLGMTVRTTIIASVYKKAL 355
Cdd:cd18541 5 ILFLILVDLLQLLIPRIIGRAIDALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 356 TLSNLARRQYTIGETVNLMSVDSQKLMDVTNY-IHLLWSSVLQIALSIFFLWReLGPSI-LAGVGLMVLLVPVNGVLATK 433
Cdd:cd18541 85 TLSPSFYQKNRTGDLMARATNDLNAVRMALGPgILYLVDALFLGVLVLVMMFT-ISPKLtLIALLPLPLLALLVYRLGKK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 434 IRK--IQVQnmknkdKRLKIMN----EILSGIKILKYFAWEPSFKEQVNSIRKKELRNLLRFSQLQTILIFILHLTPTLV 507
Cdd:cd18541 164 IHKrfRKVQ------EAFSDLSdrvqESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLS 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569006289 508 SVITFsvyvLVDSQNVLNAEkaftsITL-----FNI----LRFPLAMLPMVISSVIQASVSVDRL 563
Cdd:cd18541 238 FLIVL----WYGGRLVIRGT-----ITLgdlvaFNSylgmLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1263-1470 |
1.75e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 42.55 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1263 LDLVLKGITcnikstekvGVVGRTGAGKSSLTNCLF--------RIlesaggqiiidgidiaSIG---LHDLRGRLTIIP 1331
Cdd:PRK11144 19 LTLPAQGIT---------AIFGRSGAGKTSLINAISgltrpqkgRI----------------VLNgrvLFDAEKGICLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1332 ---------QDPILF-----SGNLRMNLDPFNKYSDEEIWRALELAH-LKSFVAglqlgllhevteggdNLSIGQRQLLC 1396
Cdd:PRK11144 74 ekrrigyvfQDARLFphykvRGNLRYGMAKSMVAQFDKIVALLGIEPlLDRYPG---------------SLSGGEKQRVA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1397 LGRAVLRKSKILVLDEATAAVD----------LETDSL-IQTTIrnefsqctvITIAHRLHTIMD-SDKIMVLDSGKIVE 1464
Cdd:PRK11144 139 IGRALLTAPELLLMDEPLASLDlprkrellpyLERLAReINIPI---------LYVSHSLDEILRlADRVVVLEQGKVKA 209
|
....*.
gi 569006289 1465 YGSPEE 1470
Cdd:PRK11144 210 FGPLEE 215
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
974-1065 |
3.01e-03 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 41.26 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 974 IGVFGALGIAQGIFLLSSSLWSIYACRNASKTLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDTLPQTLRSWL 1053
Cdd:cd18551 39 LALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLV 118
|
90
....*....|..
gi 569006289 1054 LCFFGIVSTLVM 1065
Cdd:cd18551 119 TGVLTVVGAVVL 130
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1387-1471 |
3.46e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 41.76 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1387 LSIGQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLIQTTIR---NEFSQcTVITIAHRLHTIMD-SDKIMVLDSGKI 1462
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlqKEMSM-GVIFITHDMGVVAEiADRVLVMYQGEA 247
|
....*....
gi 569006289 1463 VEYGSPEEL 1471
Cdd:PRK10261 248 VETGSVEQI 256
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1385-1464 |
4.19e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.31 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1385 DNLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDlETDS-----LIQttirnEFSQ--CTVITIAHRLHTIMD-SDKIMV 1456
Cdd:NF040905 138 TDIGVGKQQLVEIAKALSKDVKLLILDEPTAALN-EEDSaalldLLL-----ELKAqgITSIIISHKLNEIRRvADSITV 211
|
....*...
gi 569006289 1457 LDSGKIVE 1464
Cdd:NF040905 212 LRDGRTIE 219
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
1001-1191 |
4.68e-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: 40.87 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1001 NASKTLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVDDTLPQTL-RSWLLCFFGIVSTLVMICMATPIFIIIIIP 1079
Cdd:cd18554 76 KILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLmNIWLDMITIIIAICIMLVLNPKLTFVSLVI 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1080 LSILYVSVQVFYvATSRQLRRLDSVTKSPIYSHFSETVSGLPVIRAFEHQQRFLANSEKQidtNQKCVFSWITSNRWLAI 1159
Cdd:cd18554 156 FPFYILAVKYFF-GRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKR---NGHFLTRALKHTRWNAK 231
|
170 180 190
....*....|....*....|....*....|....*...
gi 569006289 1160 RLELV------GNLIVFCSALLLVIYKNSLTGDTVGFV 1191
Cdd:cd18554 232 TFSAVntitdlAPLLVIGFAAYLVIEGNLTVGTLVAFV 269
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1358-1473 |
4.71e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.94 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1358 RALELAH----------LKSFVaglqlgllHEVTEGgdnlsigQRQLLCLGRAVLRKSKILVLDEATAAVDLETDSLI-- 1425
Cdd:PRK15093 135 RAIELLHrvgikdhkdaMRSFP--------YELTEG-------ECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIfr 199
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 569006289 1426 QTTIRNEFSQCTVITIAHRLHTIMD-SDKIMVLDSGKIVEYGSPEELLS 1473
Cdd:PRK15093 200 LLTRLNQNNNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELVT 248
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1405-1473 |
4.88e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 40.30 E-value: 4.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006289 1405 SKILVLDEATAAVDLETDSLIQTTIRnEFSQC--TVITIAHRL-HTIMDSDKIMVLDSGKIVEYGSPEELLS 1473
Cdd:PRK03695 152 GQLLLLDEPMNSLDVAQQAALDRLLS-ELCQQgiAVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1006-1222 |
4.99e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 40.54 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1006 LHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDI----STVDDTLPQTLRSwllcFFGIVSTLV----------MICMATp 1071
Cdd:cd18550 74 LRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVggaqSVVTGTLTSVVSN----VVTLVATLVamlaldwrlaLLSLVL- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1072 ifiiiiiplsilyvsVQVFYVATSRQLRRLDSVTK------SPIYSHFSET--VSGLPVIRAF----EHQQRFLANSEKQ 1139
Cdd:cd18550 149 ---------------LPLFVLPTRRVGRRRRKLTReqqeklAELNSIMQETlsVSGALLVKLFgredDEAARFARRSREL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1140 IDTNQKCVfswiTSNRWLAIRLELVGNL---IVFCSALLLVIyKNSLT-GDTVGFVlsnAL--NITQTLNWLVRMTSEVE 1213
Cdd:cd18550 214 RDLGVRQA----LAGRWFFAALGLFTAIgpaLVYWVGGLLVI-GGGLTiGTLVAFT---ALlgRLYGPLTQLLNIQVDLM 285
|
....*....
gi 569006289 1214 TNIVAVERI 1222
Cdd:cd18550 286 TSLALFERI 294
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
591-743 |
5.11e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 41.63 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 591 EASFTWdRDLEATIQ----------DVNLDIKPGQLVAVVGTVGSGKSSLISAM----------LGEMEnVHGH---ITI 647
Cdd:TIGR00956 757 EDIFHW-RNLTYEVKikkekrvilnNVDGWVKPGTLTALMGASGAGKTTLLNVLaervttgvitGGDRL-VNGRpldSSF 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 648 KGSIAYVPQQ-AWIQNGTIKDNILFgSEY--------DEKKYQRVIEACALlpdLEMLPGGDmAEIGEKGINLSGGQKHR 718
Cdd:TIGR00956 835 QRSIGYVQQQdLHLPTSTVRESLRF-SAYlrqpksvsKSEKMEYVEEVIKL---LEMESYAD-AVVGVPGEGLNVEQRKR 909
|
170 180
....*....|....*....|....*.
gi 569006289 719 VSLA-RATYQDADIYILDDPLSAVDT 743
Cdd:TIGR00956 910 LTIGvELVAKPKLLLFLDEPTSGLDS 935
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
275-563 |
5.80e-03 |
|
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: 40.49 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 275 SFILKLAHDILLFLNPQLLKFLIGFVKDPDSYPWVgYIYAILMFSVTLIQSFFlQCYFQFCF-VLGMTVRTTIIASVYKK 353
Cdd:cd18542 4 AILALLLATALNLLIPLLIRRIIDSVIGGGLRELL-WLLALLILGVALLRGVF-RYLQGYLAeKASQKVAYDLRNDLYDH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 354 altLSNLARRQYTIGETVNLMS-----VDSQKLMdVTNYIHLLWSSVLQIALSIFFL----WRelgpsiLAGVglMVLLV 424
Cdd:cd18542 82 ---LQRLSFSFHDKARTGDLMSrctsdVDTIRRF-LAFGLVELVRAVLLFIGALIIMfsinWK------LTLI--SLAII 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 425 PVNGVLA----TKIRKIqvqnMKNKDKRLKIMN----EILSGIKILKYFAWEPS----FKEQVNSIRKKELRNLLRFSQL 492
Cdd:cd18542 150 PFIALFSyvffKKVRPA----FEEIREQEGELNtvlqENLTGVRVVKAFAREDYeiekFDKENEEYRDLNIKLAKLLAKY 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569006289 493 QTILIFILHLTPTLVSVI--------TFSVYVLVdsqnvlnaekAFTSitLFNILRFPLAMLPMVISSVIQASVSVDRL 563
Cdd:cd18542 226 WPLMDFLSGLQIVLVLWVggylvingEITLGELV----------AFIS--YLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| PilT |
COG2805 |
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ... |
616-647 |
6.95e-03 |
|
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures];
Pssm-ID: 442056 Cd Length: 342 Bit Score: 40.46 E-value: 6.95e-03
10 20 30
....*....|....*....|....*....|....
gi 569006289 616 LVAVVGTVGSGKSSLISAMLGEM-ENVHGHI-TI 647
Cdd:COG2805 127 LVLVTGPTGSGKSTTLAAMIDYInETRAKHIiTI 160
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
973-1192 |
7.05e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 40.21 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 973 RIGVFGALGIaqGIFLLSS--SLWSIY----ACRNASKTLHRQLLTNILRAPMSFFDTTPTGRIVNRFAGDISTVD---- 1042
Cdd:cd18778 38 LLLGLALLLL--GAYLLRAllNFLRIYlnhvAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVErlia 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1043 DTLPQTLRSwLLCFFGIV-------STLVMICMATPIFIIIIIplsilyvsvqVFYVATSRQLRRLDSVTKSPIYSHFSE 1115
Cdd:cd18778 116 DGIPQGITN-VLTLVGVAiilfsinPKLALLTLIPIPFLALGA----------WLYSKKVRPRYRKVREALGELNALLQD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1116 TVSGLPVIRAFEHQQ----RFLANSEKQIDTNQKCVFSWitsnrwlairlELVGNLIVFCSAL--LLVIY-------KNS 1182
Cdd:cd18778 185 NLSGIREIQAFGREEeeakRFEALSRRYRKAQLRAMKLW-----------AIFHPLMEFLTSLgtVLVLGfggrlvlAGE 253
|
250
....*....|.
gi 569006289 1183 LT-GDTVGFVL 1192
Cdd:cd18778 254 LTiGDLVAFLL 264
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
288-563 |
8.75e-03 |
|
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: 40.10 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 288 LNPQLLKFLI--GFVKDPdsyPWVGYIYAILMFSVTLIQSFFLqcYFQFCFV--LGMTVRTTIIASVYKKALTLSnLAR- 362
Cdd:cd18552 17 ALAWLLKPLLddIFVEKD---LEALLLVPLAIIGLFLLRGLAS--YLQTYLMayVGQRVVRDLRNDLFDKLLRLP-LSFf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 363 RQYTIGETVNLMSVDSQKLMD-VTNYIHLLWSSVLQIALSIFFL----WReLgpSILAGVGLMVLLVPVnGVLATKIRKI 437
Cdd:cd18552 91 DRNSSGDLISRITNDVNQVQNaLTSALTVLVRDPLTVIGLLGVLfyldWK-L--TLIALVVLPLAALPI-RRIGKRLRKI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 438 QVQNMKNKDKRLKIMNEILSGIKILKYFAWEPSFKEQVNSIRKKELRNLLRFSQLQTILIFILHltptLVSVITFSVYVL 517
Cdd:cd18552 167 SRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLME----LLGAIAIALVLW 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 569006289 518 VDSQNVLNAEK---AFTS-ITLFNILRFPLAMLPMVISSVIQASVSVDRL 563
Cdd:cd18552 243 YGGYQVISGELtpgEFISfITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1341-1487 |
8.76e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.56 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1341 LRMNLDPFN-KYSDEEIWRALELAHLksfvaglqlgLLHEVTEggdnLSIGQRQLLCLGRAVLRKSKILVLDEATAAVDL 1419
Cdd:PRK13409 421 LRSITDDLGsSYYKSEIIKPLQLERL----------LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 486
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006289 1420 ETDSLIQTTIRN--EFSQCTVITIAHRLHTI-MDSDKIMVLDsGKIVEYG---SPEELLSNMGPFYlmaKEAGI 1487
Cdd:PRK13409 487 EQRLAVAKAIRRiaEEREATALVVDHDIYMIdYISDRLMVFE-GEPGKHGhasGPMDMREGMNRFL---KELGI 556
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1240-1473 |
9.17e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 40.34 E-value: 9.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1240 PPADWPKkgeIQFNNYQVRYrPELDLVLKGITCNIKSTEKVGVVGRTGAGKSSLTNCLFRILESAGGQIIIDGIDIASIG 1319
Cdd:PRK10522 316 AFPDWQT---LELRNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1320 LHDLRGRLTIIPQDPILFSgnlRMnLDPFNKYSDEEI---WRA-LELAHlKSFVAGLQLGLLhevteggdNLSIGQRQLL 1395
Cdd:PRK10522 392 PEDYRKLFSAVFTDFHLFD---QL-LGPEGKPANPALvekWLErLKMAH-KLELEDGRISNL--------KLSKGQKKRL 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006289 1396 CLGRAVLRKSKILVLDEATAAVDletdsliqTTIRNEFSQC----------TVITIAHRLHTIMDSDKIMVLDSGKIVE- 1464
Cdd:PRK10522 459 ALLLALAEERDILLLDEWAADQD--------PHFRREFYQVllpllqemgkTIFAISHDDHYFIHADRLLEMRNGQLSEl 530
|
....*....
gi 569006289 1465 YGSPEELLS 1473
Cdd:PRK10522 531 TGEERDAAS 539
|
|
| |
